HEADER SIGNALING PROTEIN/PEPTIDE 11-AUG-09 3IN7
TITLE CRYSTAL STRUCTURE OF THE GRB2 SH2 DOMAIN IN COMPLEX WITH A
TITLE 2 CYCLOPROPYL-CONSTRAINED AC-PY-Q-N-NH2 TRIPEPTIDE MIMIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: ADAPTER PROTEIN GRB2, SH2/SH3 ADAPTER GRB2, PROTEIN ASH;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GRB2, ASH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-60
KEYWDS LIGAND PREORGANIZATION, PEPTIDE MIMICS, GOLGI APPARATUS, HOST-VIRUS
KEYWDS 2 INTERACTION, PHOSPHOPROTEIN, SH2 DOMAIN, SH3 DOMAIN, SIGNALING
KEYWDS 3 PROTEIN-PSEUDOPEPTIDE LIGAND COMPLEX, SIGNALING PROTEIN-PEPTIDE
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.CLEMENTS
REVDAT 5 06-SEP-23 3IN7 1 REMARK SEQADV
REVDAT 4 01-NOV-17 3IN7 1 REMARK
REVDAT 3 13-JUL-11 3IN7 1 VERSN
REVDAT 2 01-DEC-09 3IN7 1 JRNL
REVDAT 1 17-NOV-09 3IN7 0
JRNL AUTH J.E.DELORBE,J.H.CLEMENTS,M.G.TERESK,A.P.BENFIELD,H.R.PLAKE,
JRNL AUTH 2 L.E.MILLSPAUGH,S.F.MARTIN
JRNL TITL THERMODYNAMIC AND STRUCTURAL EFFECTS OF CONFORMATIONAL
JRNL TITL 2 CONSTRAINTS IN PROTEIN-LIGAND INTERACTIONS. ENTROPIC
JRNL TITL 3 PARADOXY ASSOCIATED WITH LIGAND PREORGANIZATION.
JRNL REF J.AM.CHEM.SOC. V. 131 16758 2009
JRNL REFN ISSN 0002-7863
JRNL PMID 19886660
JRNL DOI 10.1021/JA904698Q
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.P.BENFIELD,M.G.TERESK,H.R.PLAKE,J.E.DELORBE,
REMARK 1 AUTH 2 L.E.MILLSPAUGH,S.F.MARTIN
REMARK 1 TITL LIGAND PREORGANIZATION MAY BE ACCOMPANIED BY ENTROPIC
REMARK 1 TITL 2 PENALTIES IN PROTEIN-LIGAND INTERACTIONS
REMARK 1 REF ANGEW.CHEM.INT.ED.ENGL. V. 45 6830 2006
REMARK 1 REFN ISSN 1433-7851
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.6
REMARK 3 NUMBER OF REFLECTIONS : 14090
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.200
REMARK 3 FREE R VALUE TEST SET COUNT : 709
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1643
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.47500
REMARK 3 B22 (A**2) : 7.85700
REMARK 3 B33 (A**2) : 6.61800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.413 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.268 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.881 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.766 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 20.71
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CPYQN.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CPYQN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000054621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : BLUE MAX-FLUX CONFOCAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19967
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 71.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 6.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2HUW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LIGAND IN LYOPHILIZED POWDER FORM WAS
REMARK 280 DISSOLVED IN A 7.6 MG/ML SOLUTION OF GRB2 SH2 IN WATER SUCH TO
REMARK 280 GIVE A PROTEIN/LIGAND MOLAR RATIO OF 1.7:1. 3.5 UL OF THIS
REMARK 280 SOLUTION WAS MIXED WITH 3.5 UL OF 0.1 M HEPES, 20% W/V PEG MW10,
REMARK 280 000, PH 7.5 TO CREATE THE HANGING DROP, WHICH YIELDED CRYSTALS
REMARK 280 OF THE PROTEIN-LIGAND COMPLEX IN THE PRESENCE OF THE ABOVE-
REMARK 280 MENTIONED SOLUTION AFTER TWO WEEKS AT ROOM TEMPERATURE., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.19200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.36250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.97750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.36250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.97750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ILE A 53
REMARK 465 GLU A 54
REMARK 465 VAL A 154
REMARK 465 PRO A 155
REMARK 465 GLN A 156
REMARK 465 GLN A 157
REMARK 465 PRO A 158
REMARK 465 THR A 159
REMARK 465 TYR A 160
REMARK 465 VAL A 161
REMARK 465 GLN A 162
REMARK 465 ALA A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 HIS A 167
REMARK 465 HIS A 168
REMARK 465 HIS A 169
REMARK 465 ILE C 53
REMARK 465 GLU C 54
REMARK 465 PRO C 155
REMARK 465 GLN C 156
REMARK 465 GLN C 157
REMARK 465 PRO C 158
REMARK 465 THR C 159
REMARK 465 TYR C 160
REMARK 465 VAL C 161
REMARK 465 GLN C 162
REMARK 465 ALA C 163
REMARK 465 HIS C 164
REMARK 465 HIS C 165
REMARK 465 HIS C 166
REMARK 465 HIS C 167
REMARK 465 HIS C 168
REMARK 465 HIS C 169
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 121 -92.43 -121.88
REMARK 500 LYS C 56 111.21 61.04
REMARK 500 TRP C 121 -86.46 -118.87
REMARK 500 ASN C 143 -60.47 -96.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N~2~-({(1R,2R,3S)-2-(METHYLCARBAMOYL)-3-[4-
REMARK 630 (PHOSPHONOOXY)PHENYL]CYCLOPROPYL}CARBONYL)-D-GLUTAMINYL-D-
REMARK 630 ASPARTAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 AYQ A 1
REMARK 630 AYQ C 1
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: AY0 GLN ASN NH2
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AYQ A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AYQ C 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HUW RELATED DB: PDB
REMARK 900 RELATED ID: 3C7I RELATED DB: PDB
REMARK 900 RELATED ID: 3IMD RELATED DB: PDB
REMARK 900 RELATED ID: 3IMJ RELATED DB: PDB
REMARK 900 RELATED ID: 3IN8 RELATED DB: PDB
DBREF 3IN7 A 53 163 UNP P62993 GRB2_HUMAN 53 163
DBREF 3IN7 C 53 163 UNP P62993 GRB2_HUMAN 53 163
SEQADV 3IN7 HIS A 164 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS A 165 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS A 166 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS A 167 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS A 168 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS A 169 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 164 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 165 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 166 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 167 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 168 UNP P62993 EXPRESSION TAG
SEQADV 3IN7 HIS C 169 UNP P62993 EXPRESSION TAG
SEQRES 1 A 117 ILE GLU MET LYS PRO HIS PRO TRP PHE PHE GLY LYS ILE
SEQRES 2 A 117 PRO ARG ALA LYS ALA GLU GLU MET LEU SER LYS GLN ARG
SEQRES 3 A 117 HIS ASP GLY ALA PHE LEU ILE ARG GLU SER GLU SER ALA
SEQRES 4 A 117 PRO GLY ASP PHE SER LEU SER VAL LYS PHE GLY ASN ASP
SEQRES 5 A 117 VAL GLN HIS PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS
SEQRES 6 A 117 TYR PHE LEU TRP VAL VAL LYS PHE ASN SER LEU ASN GLU
SEQRES 7 A 117 LEU VAL ASP TYR HIS ARG SER THR SER VAL SER ARG ASN
SEQRES 8 A 117 GLN GLN ILE PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN
SEQRES 9 A 117 GLN PRO THR TYR VAL GLN ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 117 ILE GLU MET LYS PRO HIS PRO TRP PHE PHE GLY LYS ILE
SEQRES 2 C 117 PRO ARG ALA LYS ALA GLU GLU MET LEU SER LYS GLN ARG
SEQRES 3 C 117 HIS ASP GLY ALA PHE LEU ILE ARG GLU SER GLU SER ALA
SEQRES 4 C 117 PRO GLY ASP PHE SER LEU SER VAL LYS PHE GLY ASN ASP
SEQRES 5 C 117 VAL GLN HIS PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS
SEQRES 6 C 117 TYR PHE LEU TRP VAL VAL LYS PHE ASN SER LEU ASN GLU
SEQRES 7 C 117 LEU VAL ASP TYR HIS ARG SER THR SER VAL SER ARG ASN
SEQRES 8 C 117 GLN GLN ILE PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN
SEQRES 9 C 117 GLN PRO THR TYR VAL GLN ALA HIS HIS HIS HIS HIS HIS
HET AYQ A 1 38
HET AYQ C 1 38
HETNAM AYQ N~2~-({(1R,2R,3S)-2-(METHYLCARBAMOYL)-3-[4-
HETNAM 2 AYQ (PHOSPHONOOXY)PHENYL]CYCLOPROPYL}CARBONYL)-D-
HETNAM 3 AYQ GLUTAMINYL-D-ASPARTAMIDE
FORMUL 3 AYQ 2(C21 H29 N6 O10 P)
FORMUL 5 HOH *119(H2 O)
HELIX 1 1 PRO A 66 SER A 75 1 10
HELIX 2 2 SER A 127 HIS A 135 1 9
HELIX 3 3 PRO C 66 LYS C 76 1 11
HELIX 4 4 SER C 127 HIS C 135 1 9
SHEET 1 A 4 PHE A 83 GLU A 87 0
SHEET 2 A 4 PHE A 95 PHE A 101 -1 O SER A 96 N ARG A 86
SHEET 3 A 4 ASP A 104 ARG A 112 -1 O PHE A 108 N LEU A 97
SHEET 4 A 4 TYR A 118 PHE A 119 -1 O PHE A 119 N LEU A 111
SHEET 1 B 6 PHE C 61 GLY C 63 0
SHEET 2 B 6 PHE C 83 GLU C 87 1 O ILE C 85 N PHE C 62
SHEET 3 B 6 PHE C 95 PHE C 101 -1 O SER C 96 N ARG C 86
SHEET 4 B 6 ASP C 104 ARG C 112 -1 O PHE C 108 N LEU C 97
SHEET 5 B 6 TYR C 118 PHE C 119 -1 O PHE C 119 N LEU C 111
SHEET 6 B 6 LYS C 124 PHE C 125 -1 O PHE C 125 N TYR C 118
SITE 1 AC1 17 HOH A 17 HOH A 22 ARG A 67 ARG A 86
SITE 2 AC1 17 SER A 88 SER A 90 SER A 96 GLN A 106
SITE 3 AC1 17 HIS A 107 PHE A 108 LYS A 109 LEU A 120
SITE 4 AC1 17 TRP A 121 ARG A 142 ASN A 143 HOH A 183
SITE 5 AC1 17 HOH A 193
SITE 1 AC2 14 HOH C 18 HOH C 39 ARG C 67 ARG C 86
SITE 2 AC2 14 SER C 88 SER C 90 SER C 96 HIS C 107
SITE 3 AC2 14 PHE C 108 LYS C 109 LEU C 120 TRP C 121
SITE 4 AC2 14 HOH C 170 HOH C 178
CRYST1 40.384 63.955 92.725 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024762 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010785 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
