5nuh

Crystal structure of SIVmac239 Nef bound to an engineered Hck SH3 domain

Method: X-RAY DIFFRACTION D_max: 90.8 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein Nef

Simian immunodeficiency virus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 68–235	Not recorded	Tyrosine-protein kinase HCK,Tyrosine-protein kinase HCK × 1 （P08631）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol	Resolution 2.78 Å R-free 0.229
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 68–235	Not recorded	Tyrosine-protein kinase HCK,Tyrosine-protein kinase HCK × 1 （P08631）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol	Resolution 2.78 Å R-free 0.229

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 5NUH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3IK5 SIVmac239 Nef in complex with TCR zeta ITAM 1 polypeptide (A63-R80) Deposited 2009-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 95–235（141 aa） Fragment：core domain Chain C 95–235（141 aa） Fragment：core domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；15% PEG 3350, 0.2mM ammonmium fluoride, 0.1mM hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.05 Å R-free 0.184
3IK5 SIVmac239 Nef in complex with TCR zeta ITAM 1 polypeptide (A63-R80) Deposited 2009-08-05	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 95–235（141 aa） Fragment：core domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；15% PEG 3350, 0.2mM ammonmium fluoride, 0.1mM hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.05 Å R-free 0.184
3IK5 SIVmac239 Nef in complex with TCR zeta ITAM 1 polypeptide (A63-R80) Deposited 2009-08-05	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 95–235（141 aa） Fragment：core domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；15% PEG 3350, 0.2mM ammonmium fluoride, 0.1mM hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.05 Å R-free 0.184
3IOZ SIVmac239 Nef in complex with a TCR zeta polypeptide DP1 (L51-D93) Deposited 2009-08-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 95–235（141 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.2；277 K；15% PEG 3350, 0.15M KF, 0.1M hepes, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 3.70 Å R-free 0.329
3RWC Crystal structure of rhesus macaque MHC class I molecule Mamu-B*17-IW9 Deposited 2011-05-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 165–173（9 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.249
3RWC Crystal structure of rhesus macaque MHC class I molecule Mamu-B*17-IW9 Deposited 2011-05-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 165–173（9 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.249
3RWD rhesus macaque MHC class I molecule Mamu-B*17-IW11 Deposited 2011-05-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 165–175（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.277
3RWD rhesus macaque MHC class I molecule Mamu-B*17-IW11 Deposited 2011-05-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 165–175（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.277
3RWF Rhesus macaque MHC class I molecule Mamu-B*17-QW9 Deposited 2011-05-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 199–207（9 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.246
3RWG Rhesus macaque MHC class I molecule Mamu-B*17-MW9 Deposited 2011-05-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 195–203（9 aa）	Not recorded	XPE 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å R-free 0.237
5NUI Crystal structure of SIVmac239 Nef in an ExxxLM endocytic sorting motif bound state Deposited 2017-04-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 87–235（149 aa） Chain B 87–235（149 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；10% PEG 4000, 0.15 M ammonium sulfate, 0.1 M MES (pH 5.8)	Resolution 2.50 Å R-free 0.257

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q5QGG3_SIV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–172； UniProt 68–235 Author chain B； PDBConstruct 5–172； UniProt 68–235

Tyrosine-protein kinase HCK,Tyrosine-protein kinase HCK

Homo sapiens

UniProt P08631

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 78–90 Chain D； UniProt 96–138	Not recorded	Protein Nef × 1 （Q5QGG3）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol	Resolution 2.78 Å R-free 0.229
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 78–90 Chain C； UniProt 96–138	Not recorded	Protein Nef × 1 （Q5QGG3）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；12% PEG 3350, 0.15 M tri-lithium-citrat, 1% 1.6 hexandiol	Resolution 2.78 Å R-free 0.229

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 5NUH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AD5 SRC FAMILY KINASE HCK-AMP-PNP COMPLEX Deposited 1997-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions vapor diffusion - hanging drop and seeding；pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM AMP-PNP WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., vapor diffusion - hanging drop and seeding, temperature 292K	Resolution 2.60 Å R-free 0.307
1AD5 SRC FAMILY KINASE HCK-AMP-PNP COMPLEX Deposited 1997-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	X-RAY DIFFRACTION X-ray crystallization conditions vapor diffusion - hanging drop and seeding；pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM AMP-PNP WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., vapor diffusion - hanging drop and seeding, temperature 292K	Resolution 2.60 Å R-free 0.307
1BU1 SRC FAMILY KINASE HCK SH3 DOMAIN Deposited 1998-09-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 81–137（57 aa） Fragment：SH3 Chain B 81–137（57 aa） Fragment：SH3 Chain C 81–137（57 aa） Fragment：SH3 Chain D 81–137（57 aa） Fragment：SH3 Chain E 81–137（57 aa） Fragment：SH3 Chain F 81–137（57 aa） Fragment：SH3	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.3；294 K；HANGING DROPS (2UL) OF 4.3MG/ML PROTEIN WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 3.7 M SODIUM FORMATE, 2% PEG 3000, 100 MM BICINE (PH 9.3). THE MIXED DROPS WERE STORED AT 21 DEGREES, vapor diffusion - hanging drop, temperature 294K	Resolution 2.60 Å R-free 0.297
1QCF CRYSTAL STRUCTURE OF HCK IN COMPLEX WITH A SRC FAMILY-SELECTIVE TYROSINE KINASE INHIBITOR Deposited 1999-05-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：SH3-SH2-KINASE-HIGH AFFINITY TAIL	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	PP1 1-TER-BUTYL-3-P-TOLYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-YLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；PEG 10000, DIMETHYL SULFOXIDE, N-(2-HYDROXYETHYL)PIPERAZINE-N-(2- ETHANESULFONIC ACID), pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.257
2C0I Src family kinase Hck with bound inhibitor A-420983 Deposited 2005-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L1G N-(4-{4-AMINO-1-[4-(4-METHYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A-420983 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.30 Å R-free 0.274
2C0I Src family kinase Hck with bound inhibitor A-420983 Deposited 2005-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L1G N-(4-{4-AMINO-1-[4-(4-METHYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-420983 [100 MM STOCK SOLUTION OF THE BIS-MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-420983 CONCENTRATION OF 1 MM. HCK/A-420983 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.30 Å R-free 0.274
2C0O Src family kinase Hck with bound inhibitor A-770041 Deposited 2005-09-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L2G N-(4-{1-[4-(4-ACETYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-4-AMINO-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-770041 [100 MM STOCK SOLUTION IN DMSO) TO GIVE A FINAL A-770041 CONCENTRATION OF 1 MM. HCK/A-770041 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1,5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.85 Å R-free 0.273
2C0O Src family kinase Hck with bound inhibitor A-770041 Deposited 2005-09-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L2G N-(4-{1-[4-(4-ACETYLPIPERAZIN-1-YL)-TRANS-CYCLOHEXYL]-4-AMINO-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-770041 [100 MM STOCK SOLUTION IN DMSO) TO GIVE A FINAL A-770041 CONCENTRATION OF 1 MM. HCK/A-770041 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1,5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.85 Å R-free 0.273
2C0T Src family kinase Hck with bound inhibitor A-641359 Deposited 2005-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L3G N-(4-{4-AMINO-1-[1-(TETRAHYDRO-2H-PYRAN-4-YL)PIPERIDIN-4-YL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；CRYSTALLIZATION CONDITIONS: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-641359 [100 MM STOCK SOLUTION OF THE MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-641359 CONCENTRATION OF 1 MM. HCK/A-641359 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.15 Å R-free 0.253
2C0T Src family kinase Hck with bound inhibitor A-641359 Deposited 2005-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 80–525（446 aa） Fragment：SH3-SH2-SH1, RESIDUES 80-525	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	L3G N-(4-{4-AMINO-1-[1-(TETRAHYDRO-2H-PYRAN-4-YL)PIPERIDIN-4-YL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL}-2-METHOXYPHENYL)-1-METHYL-1H-INDOLE-2-CARBOXAMIDE × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；CRYSTALLIZATION CONDITIONS: HCK (10 MG/ML IN 150 MM NACL, 20 MM TRIS.HCL PH 8.0) WAS MIXED WITH A-641359 [100 MM STOCK SOLUTION OF THE MALEIC ACID SALT IN DMSO) TO GIVE A FINAL A-641359 CONCENTRATION OF 1 MM. HCK/A-641359 WAS THEN MIXED WITH RESERVOIR SOLUTION (12% PEG 6000, 3% 1, 5-DIAMINOPENTANE, 20% GLYCEROL, 200 MM CA(OAC)2, 100 MM TRIS.HCL PH 8.0) AND EQUILBRATED AGAINST THE RESERVOIR SOLUTION BY VAPOR DIFFUSION (SITTING DROPS) AT 277 K.	Resolution 2.15 Å R-free 0.253
2HCK SRC FAMILY KINASE HCK-QUERCETIN COMPLEX Deposited 1997-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL Chain B 79–526（448 aa） Fragment：SH3-SH2-KINASE-REGULATORY TAIL	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 QUE 3,5,7,3',4'-PENTAHYDROXYFLAVONE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；292 K；HANGING DROPS (1UL) OF 50MG/ML PROTEIN AND 10MM QUERCETIN WERE MIXED WITH EQUAL VOLUMES OF RESERVOIR BUFFER CONTAINING 150 MM CALCIUM ACETATE, 100MM CACODYLATE (PH 6.5), 7% PEG 8000 AND 16% V/V ETHYLENE GLYCOL. THE MIXED DROPS WERE THEN SEEDED AND STORED AT 19 DEGREES C., temperature 292K	Resolution 3.00 Å R-free 0.311
2HK5 Hck Kinase in Complex with Lck targetted Inhibitor PG-1009247 Deposited 2006-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 247–514（268 aa） Fragment：Kinase Domian (Residues 246-513)	Not recorded	1BM 3-{[2-(1H-BENZIMIDAZOL-1-YL)-6-{[2-(DIETHYLAMINO)ETHYL]AMINO}PYRIMIDIN-4-YL]AMINO}-4-METHYLPHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；288 K；0.5-3.0M Ammonium Sulfate or Sodium Formate or 18 - 28% PEG 10K + 0.1M HEPES or Tris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 2.00 Å R-free 0.250
2OI3 NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) Deposited 2007-01-10	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 60–140（81 aa） Fragment：SH3 domain, residues 60-140	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；298 K；Ionic strength (raw mmCIF value) 20mM KPO4, 20mM NaCl；Pressure 1 NMR sample composition 1.3mM Hck-SH3 U-13C, U-15N: 1.3mM PD1, 20mM KPO4, 20mM NaCl, pH 6.7, 93% H2O, 7% D2O \| 93% H2O/7% D2O	Resolution not provided
2OJ2 NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) Deposited 2007-01-12	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 60–140（81 aa） Fragment：SH3	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；298 K；Ionic strength (raw mmCIF value) 20mM KPO4, 20mM NaCl；Pressure 1 NMR sample composition 1.3mM Hck-SH3 U-13C, U-15N: 1.3mM PD1, 20mM KPO4, 20mM NaCl, pH=6.7 \| 93% H2O/7% D2O	Resolution not provided
3HCK NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures Deposited 1997-03-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 140–245（106 aa） Fragment：SH2, RESIDUES 119 - 224 OF HUMAN HCK	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.4；301 K	Resolution not provided
3NHN Crystal structure of the SRC-family kinase HCK SH3-SH2-linker regulatory region Deposited 2010-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 72–256（185 aa） Fragment：UNP residues 72-256, Hck-SH3-SH2-Linker fragment	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；25% (v/v) polyethylene glycol 3,350, 0.15 M KSCN, 0.05 M NaCl, and 1:100 dilution of Hck-SH3-SH2-linker crystal seeds (grown in 25% v/v polyethylene glycol 3,350, 0.1 M Tris pH 8.5, 0.2 M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.61 Å R-free 0.176
3RBB HIV-1 NEF protein in complex with engineered HCK SH3 domain Deposited 2011-03-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 79–138（60 aa）	Mutation：E90Y, A91S, I92P, H93F, H94S, E95W	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Hepes, 8% ethylene glycol, 22% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.35 Å R-free 0.245
3RBB HIV-1 NEF protein in complex with engineered HCK SH3 domain Deposited 2011-03-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 79–138（60 aa）	Mutation：E90Y, A91S, I92P, H93F, H94S, E95W	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1 M Hepes, 8% ethylene glycol, 22% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.35 Å R-free 0.245
3REA HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 79–138（60 aa）	Mutation：E90V, A91S, I92W, H93S, H94P, E95D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Tris buffer, 5% ethylne glycol, 10% PEG 8000, 0.2 M MgCl2, 15 mM MnCl2, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 2.00 Å R-free 0.205
3REA HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 79–138（60 aa）	Mutation：E90V, A91S, I92W, H93S, H94P, E95D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Tris buffer, 5% ethylne glycol, 10% PEG 8000, 0.2 M MgCl2, 15 mM MnCl2, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 2.00 Å R-free 0.205
3REB HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 79–138（60 aa）	Mutation：E90V, A91S, I92W, H93S, H94P, E95D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Hepes, 0.05 M sodium citrate, 15% isopropanol, 30% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 3.45 Å R-free 0.243
3REB HIV-1 Nef protein in complex with engineered Hck-SH3 domain Deposited 2011-04-04	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 79–138（60 aa）	Mutation：E90V, A91S, I92W, H93S, H94P, E95D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；285 K；100 mM Hepes, 0.05 M sodium citrate, 15% isopropanol, 30% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K	Resolution 3.45 Å R-free 0.243
3VRY Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	B43 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；21% PEG 6000, 180mM calcium acetate, 18% glycerol, 100mM Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.48 Å R-free 0.281
3VRY Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	B43 4-Amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl-cyclopentane × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；21% PEG 6000, 180mM calcium acetate, 18% glycerol, 100mM Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.48 Å R-free 0.281
3VRZ Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VRZ 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.22 Å R-free 0.267
3VRZ Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VRZ 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-benzylurea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.22 Å R-free 0.267
3VS0 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VS0 N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.93 Å R-free 0.295
3VS0 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VS0 N-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.93 Å R-free 0.295
3VS1 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSA 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.46 Å R-free 0.281
3VS1 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSA 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.46 Å R-free 0.281
3VS2 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSB 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.61 Å R-free 0.279
3VS2 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSB 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.61 Å R-free 0.279
3VS3 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.17 Å R-free 0.279
3VS3 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.17 Å R-free 0.279
3VS4 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSF 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.75 Å R-free 0.265
3VS4 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1 VSF 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.75 Å R-free 0.265
3VS5 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSG 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.85 Å R-free 0.309
3VS5 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSG 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.85 Å R-free 0.309
3VS6 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 CL CHLORIDE ION × 1 VSH tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.37 Å R-free 0.280
3VS6 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 CL CHLORIDE ION × 1 VSH tert-butyl {4-[4-amino-1-(propan-2-yl)-1H-pyrazolo[3,4-d]pyrimidin-3-yl]-2-methoxyphenyl}carbamate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.37 Å R-free 0.280
3VS7 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	KS1 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.00 Å R-free 0.290
3VS7 Crystal structure of HCK complexed with a pyrazolo-pyrimidine inhibitor 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine Deposited 2012-04-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q528E, Q529E, Q530I Non-standard monomer：Yes (specific site not provided by mmCIF)	KS1 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；0.1M Tris, 0.1M calcium acetate, 20% glycerol, 21% PEG6000, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.00 Å R-free 0.290
4HCK HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES Deposited 1998-03-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 72–143（72 aa） Fragment：SH3 DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.25；298 K	Resolution not provided
4LUD Crystal Structure of HCK in complex with the fluorescent compound SKF86002 Deposited 2013-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 SK8 6-(4-fluorophenyl)-5-(pyridin-4-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole × 1 GOL GLYCEROL × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.85 Å R-free 0.261
4LUD Crystal Structure of HCK in complex with the fluorescent compound SKF86002 Deposited 2013-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 SK8 6-(4-fluorophenyl)-5-(pyridin-4-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole × 1 GOL GLYCEROL × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 2.85 Å R-free 0.261
4LUE Crystal Structure of HCK in complex with 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (resulting from displacement of SKF86002) Deposited 2013-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, soaked with 2mM inhibitor in DMSO., pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 3.04 Å R-free 0.256
4LUE Crystal Structure of HCK in complex with 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (resulting from displacement of SKF86002) Deposited 2013-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 81–526（446 aa） Fragment：UNP residues 81-526	Mutation：Q502E/Q503E/Q504I Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 2 IMD IMIDAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；288 K；0.1M Tris, 0.1M Calcium Acetate, 20% Glycerol, 24% PEG 6000, 2mM SKF86002, soaked with 2mM inhibitor in DMSO., pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 288K	Resolution 3.04 Å R-free 0.256
4ORZ HIV-1 Nef protein in complex with single domain antibody sdAb19 and an engineered Hck SH3 domain Deposited 2014-02-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 77–138（62 aa） Fragment：SH3 domain, UNP residues 77-138	Mutation：E90Y, A91S, I92P, H93F, H94S, E95W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；About 0.1 micro L of protein solution at 10 mg/ml concentration was mixed with 0.1 micro L of reservoir solution from a 70 L reservoir in 96-well Hampton 3553 crystallization plates. Initial crystals of NefSF2 sdAb19 SH3B6 could be obtained in 0.2 M potassium formate and 20% polyethylene glycol (PEG) 3350. Crystal conditions were optimized to 0.2 M potassium formate, 17.5% polyethylene glycol (PEG) 3350 and 0.35 M ammonium chloride grown by hanging-drop vapor diffusion in Linbro crystallization plates. , pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.236
4U5W Crystal Structure of HIV-1 Nef-SF2 Core Domain in Complex with the Src Family Kinase Hck SH3-SH2 Tandem Regulatory Domains Deposited 2014-07-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 72–242（171 aa） Fragment：SH3-SH2 domain, UNP residues 72-242 Chain D 72–242（171 aa） Fragment：SH3-SH2 domain, UNP residues 72-242	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 IOD IODIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277.15 K；0.09 M ADA, pH 6.5, 10.8% (v/v) 2-methyl-2,4-pentanediol, 100 mM NaI	Resolution 1.86 Å R-free 0.195
5H09 Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-ethyl2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanoate Deposited 2016-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP RESIDUES 81-526	Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	OOO ethyl (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-4-methyl-pentanoate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350	Resolution 1.95 Å R-free 0.223
5H0B Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanoic acid Deposited 2016-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP RESIDUES 81-526	Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	OOQ (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]azaniumyl]-4-methyl-pentanoate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350	Resolution 1.65 Å R-free 0.205
5H0E Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-4-methylpentanamide Deposited 2016-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP RESIDUES 81-526	Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	OOS (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-4-methyl-pentanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25M ammonium formate, 12-22% PEG 3350	Resolution 2.10 Å R-free 0.226
5H0G Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-N,4-dimethylpentanamide Deposited 2016-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP RESIDUES 81-526	Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	OOU (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-~{N},4-dimethyl-pentanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350	Resolution 1.80 Å R-free 0.224
5H0H Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor (S)-2-(((1r,4S)-4-(4-amino-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclohexyl)amino)-N,N,4-trimethylpentanamide Deposited 2016-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa） Fragment：UNP RESIDUES 81-526	Mutation：Q523E, Q524E, Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	OOV (2~{S})-2-[[4-[4-azanyl-5-(4-phenoxyphenyl)pyrrolo[2,3-d]pyrimidin-7-yl]cyclohexyl]amino]-~{N},~{N},4-trimethyl-pentanamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.22-0.25 M ammonium formate, 12-22 % PEG 3350	Resolution 1.72 Å R-free 0.224
5HCK HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-03-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 72–143（72 aa） Fragment：SH3 DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.25；298 K	Resolution not provided
5ZJ6 Crystal structure of HCK kinase complexed with a pyrrolo-pyrimidine inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine Deposited 2018-03-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 242–521（280 aa） Chain B 242–521（280 aa）	Not recorded	VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；288 K；0.1 M Tris-HCl (pH 8.5) 25 % (v/v) PEG 10,000	Resolution 1.70 Å R-free 0.240
8F2P Nef SF2 dimerization mutant bound to Hck SH3 Deposited 2022-11-08	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 77–140（64 aa） Fragment：Hck SH3 domain (UNP residues 77-140)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；0.1 M sodium chloride, 0.1 M sodium acetate, pH 4.6, 12% v/v MPD	Resolution 2.63 Å R-free 0.252
9BYJ Crystal Structure of Hck in complex with the Src-family kinase inhibitor A-419259 Deposited 2024-05-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–526（446 aa）	Mutation：Q523E,Q524E,Q525I Non-standard monomer：Yes (specific site not provided by mmCIF)	VSE 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine × 1 EDO 1,2-ETHANEDIOL × 6 DMS DIMETHYL SULFOXIDE × 2 SCN THIOCYANATE ION × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10 mM Tris-HCl, pH 8.3, 75 mM NaCl, 5% glycerol, 2 mM TCEP, 0.1 M sodium thiocyanate, 10% w/v PEG 3350, 0.095 mM 7-[trans-4-(4-Methyl-1-piperazinyl)cyclohexyl]-5-(4-phenoxyphenyl)-7H-Pyrrolo[2,3-d]pyrimidin-4-amine, 0.5 mM N~2~-{[2-(2,4-difluorophenoxy)pyridin-3-yl]methyl}-N~4~-isopropylpyrimidine-2,4-diamine,1 % DMSO	Resolution 1.80 Å R-free 0.219

39 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HCK_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–13； UniProt 78–90 Author chain C； PDBConstruct 18–60； UniProt 96–138 Author chain D； PDBConstruct 1–13； UniProt 78–90 Author chain D； PDBConstruct 18–60； UniProt 96–138

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5nuh
Deposition date deposition_date	2017-04-30
Structure title title	Crystal structure of SIVmac239 Nef bound to an engineered Hck SH3 domain
Keywords keywords	SIV, Virus, Nef, SH3, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	23.98 Å
Radius of gyration Rg (electron density) rg_electron	22.88 Å
Forward intensity I(0) i0	28056100.00
Molecular weight molecular_weight	42317.0 kDa
Excluded volume excluded_volume	53428 Å³
Envelope volume envelope_volume	64038 Å³
Hydration-shell volume shell_volume	24122 Å³
Envelope diameter envelope_diameter	93.7 Å
Shell Rg shell_rg	29.02 Å
Envelope Rg envelope_rg	23.30 Å
Shape Rg shape_rg	22.85 Å
Total Rg total_rg	23.75 Å
Total atoms total_atoms	3009
Residues n_residues	366
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	90.8 Å
Rg (real space) rg_real	24.00 Å
Rg uncertainty (real space) rg_real_error	0.93 Å
I(0) (real space) i0_real	2.8060e+07
I(0) uncertainty (real space) i0_real_error	4.5080e+05
Rg (reciprocal space) rg_reciprocal	24.00 Å
I(0) (reciprocal space) i0_reciprocal	28060000.0000
Solution quality estimate total_estimate	0.8193
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.8 Å
Skewness Skewness skewness	0.432
Kurtosis Kurtosis kurtosis	0.092
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6696000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.603; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.838; Smooth: 0.998

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Protein Nef
Molecular weight formula_weight	20221.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3064

GAMATPWRNPAEEREKLAYRKQNMDDIDEEDDDLVGVSVRPKVPLRTMSYKLAIDMSHFIKEKGGLEGIYYSARRHRILDIYLEKEEGIIPDWQDYTSGPGIRYPKTFGWLWKLVPVNVSDEAQEDEEHYLMHPAQTSQWDDPWGEVLAWKFDPTLAYTYEAYVRYPEEFGS

来源 Source

来源生物 organism	Simian immunodeficiency virus
通用名 common_name	SIV
NCBI Class编号 ncbi_taxonomy_id	11723
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Tyrosine-protein kinase HCK,Tyrosine-protein kinase HCK
Molecular weight formula_weight	6994.8 kDa
EC 编号 ec_number	2.7.10.2,2.7.10.2
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

MEDIIVVALYDYEGWWGDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	55

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d5nuha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.102 — Regulatory factor Nef
Superfamily Superfamily superfamily	d.102.1 — Regulatory factor Nef
Family Family family	d.102.1.0 — automated matches

Domain ID domain_id	d5nuhb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.102 — Regulatory factor Nef
Superfamily Superfamily superfamily	d.102.1 — Regulatory factor Nef
Family Family family	d.102.1.0 — automated matches

Domain ID domain_id	d5nuhc_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

Domain ID domain_id	d5nuhd_
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.1 — SH3-domain

CATH v4.4 (4 domains)

Domain ID domain_id	5nuhA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	62 — Nef Regulatory Factor
Homologous superfamily homologous superfamily	10 — Nef Regulatory Factor

Domain ID domain_id	5nuhB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	62 — Nef Regulatory Factor
Homologous superfamily homologous superfamily	10 — Nef Regulatory Factor

Domain ID domain_id	5nuhC00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	5nuhD00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

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8. Citations (1)

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Unit-cell length a length_a	104.000 Å
Unit-cell length b length_b	104.000 Å
Unit-cell length c length_c	53.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	2.780 Å
Low-resolution limit resolution_low	45.680 Å
R factor r_factor	0.1940
R_work r_work	0.1920
R_free r_free	0.2290

fit	/app/data/saxs_computation/nu/5nuh/5nuh.fit
pddf	/app/data/pr_computation/nu/5nuh/5nuh.pr.out
profile	/app/data/saxs_computation/nu/5nuh/5nuh.dat

Crystal structure of SIVmac239 Nef bound to an engineered Hck SH3 domain

1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein Nef

State in the Current Structure

Other States of the Same Protein in the Database

Tyrosine-protein kinase HCK,Tyrosine-protein kinase HCK

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)