HEADER SIGNALING PROTEIN/ANTAGONIST 06-APR-14 4P9V
TITLE GRB2 SH2 COMPLEXED WITH A PTYR-AC6CN-ASN TRIPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 53-163;
COMPND 5 SYNONYM: ADAPTER PROTEIN GRB2,PROTEIN ASH,SH2/SH3 ADAPTER GRB2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHQ-PTR-02K-ASN-NH2;
COMPND 9 CHAIN: B;
COMPND 10 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;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS GRB2 SH2, CATION-PI INTERACTION, SIGNALING PROTEIN-ANTAGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.CLEMENTS,S.F.MARTIN
REVDAT 8 15-NOV-23 4P9V 1 REMARK
REVDAT 7 27-SEP-23 4P9V 1 REMARK
REVDAT 6 27-NOV-19 4P9V 1 REMARK
REVDAT 5 27-SEP-17 4P9V 1 REMARK
REVDAT 4 09-AUG-17 4P9V 1 SOURCE JRNL REMARK
REVDAT 3 24-DEC-14 4P9V 1 DBREF
REVDAT 2 16-JUL-14 4P9V 1 JRNL
REVDAT 1 18-JUN-14 4P9V 0
JRNL AUTH J.M.MYSLINSKI,J.H.CLEMENTS,S.F.MARTIN
JRNL TITL PROTEIN-LIGAND INTERACTIONS: PROBING THE ENERGETICS OF A
JRNL TITL 2 PUTATIVE CATION-PI INTERACTION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 3164 2014
JRNL REFN ESSN 1464-3405
JRNL PMID 24856058
JRNL DOI 10.1016/J.BMCL.2014.04.114
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 10836
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 + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 560
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 730
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 858
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 56
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.72000
REMARK 3 B22 (A**2) : -0.72000
REMARK 3 B33 (A**2) : 1.45000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.726
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 891 ; 0.022 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1203 ; 2.192 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 101 ; 7.237 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 44 ;30.668 ;22.955
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 145 ;12.949 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;18.635 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 119 ; 0.443 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 700 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4P9V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11451
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 12.60
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 19.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3S8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 25.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M TRIS HYDROCHLORIDE, 30% W/V POLYETHYLENE GLYCOL 4000, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.35750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 20.96750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 20.96750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.53625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 20.96750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 20.96750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.17875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 20.96750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 20.96750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.53625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 20.96750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 20.96750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.17875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 54.35750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 54 N CG CD OE1 OE2
REMARK 470 MET A 55 SD CE
REMARK 470 LYS A 56 CD CE NZ
REMARK 470 GLN A 153 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 80 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 55 99.55 -26.39
REMARK 500 TRP A 121 -67.10 -127.43
REMARK 500 VAL A 122 -45.17 -135.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for PHQ-PTR-02K-ASN-NH2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S8O RELATED DB: PDB
REMARK 900 3S8O CONTAINS THE SAME PROTEIN COMPLEXED WITH A SIMILAR LIGAND
REMARK 900 RELATED ID: 4P9Z RELATED DB: PDB
DBREF 4P9V A 53 163 UNP P62993 GRB2_HUMAN 53 163
DBREF 4P9V B 1 5 PDB 4P9V 4P9V 1 5
SEQADV 4P9V HIS A 164 UNP P62993 EXPRESSION TAG
SEQADV 4P9V HIS A 165 UNP P62993 EXPRESSION TAG
SEQADV 4P9V HIS A 166 UNP P62993 EXPRESSION TAG
SEQADV 4P9V HIS A 167 UNP P62993 EXPRESSION TAG
SEQADV 4P9V HIS A 168 UNP P62993 EXPRESSION TAG
SEQADV 4P9V HIS A 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 B 5 PHQ PTR 02K ASN NH2
HET PHQ B 1 10
HET PTR B 2 16
HET 02K B 3 9
HET NH2 B 5 1
HET CL A 201 1
HETNAM PHQ BENZYL CHLOROCARBONATE
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 02K 1-AMINOCYCLOHEXANECARBOXYLIC ACID
HETNAM NH2 AMINO GROUP
HETNAM CL CHLORIDE ION
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PHQ C8 H7 CL O2
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 2 02K C7 H13 N O2
FORMUL 2 NH2 H2 N
FORMUL 3 CL CL 1-
FORMUL 4 HOH *56(H2 O)
HELIX 1 AA1 PRO A 66 LYS A 76 1 11
HELIX 2 AA2 SER A 127 HIS A 135 1 9
SHEET 1 AA1 3 PHE A 83 GLU A 87 0
SHEET 2 AA1 3 PHE A 95 PHE A 101 -1 O SER A 98 N LEU A 84
SHEET 3 AA1 3 ASP A 104 LYS A 109 -1 O PHE A 108 N LEU A 97
SHEET 1 AA2 3 LEU A 111 ARG A 112 0
SHEET 2 AA2 3 TYR A 118 PHE A 119 -1 O PHE A 119 N LEU A 111
SHEET 3 AA2 3 LYS A 124 PHE A 125 -1 O PHE A 125 N TYR A 118
LINK C1 PHQ B 1 N PTR B 2 1555 1555 1.35
LINK C PTR B 2 N 02K B 3 1555 1555 1.34
LINK C 02K B 3 N ASN B 4 1555 1555 1.39
LINK C ASN B 4 N NH2 B 5 1555 1555 1.30
SITE 1 AC1 3 SER A 139 GLN A 145 HOH A 327
SITE 1 AC2 16 ARG A 67 ARG A 78 ARG A 86 SER A 88
SITE 2 AC2 16 SER A 90 SER A 96 HIS A 107 PHE A 108
SITE 3 AC2 16 LYS A 109 LEU A 120 TRP A 121 HOH A 301
SITE 4 AC2 16 HOH A 307 HOH B 101 HOH B 102 HOH B 103
CRYST1 41.935 41.935 108.715 90.00 90.00 90.00 P 43 21 2 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 0.023846 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
