HEADER HORMONE/GROWTH FACTOR 03-OCT-00 1FYR
TITLE DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF
TITLE 2 THE GRB2-SH2 AC-PYVNV COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR PEPTIDE;
COMPND 8 CHAIN: I, J, K, L;
COMPND 9 FRAGMENT: RESIDUES 1356-1359 (RESIDUES 0-3 IN COORDINATES);
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: THE SEQUENCE YVNV IS ALSO FOUND IN OTHER PROTEINS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 11 OCCURS NATURALLY IN HUMANS.
KEYWDS GRB2, SH2 DOMAIN, PHOSPHOPEPTIDE, MET, DOMAIN SWAPPING, DIMERIZATION,
KEYWDS 2 HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SCHIERING,E.CASALE,P.CACCIA,P.GIORDANO,C.BATTISTINI
REVDAT 5 15-NOV-23 1FYR 1 REMARK
REVDAT 4 09-AUG-23 1FYR 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1FYR 1 VERSN
REVDAT 2 01-APR-03 1FYR 1 JRNL
REVDAT 1 06-DEC-00 1FYR 0
JRNL AUTH N.SCHIERING,E.CASALE,P.CACCIA,P.GIORDANO,C.BATTISTINI
JRNL TITL DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL
JRNL TITL 2 STRUCTURE OF THE GRB2-SH2-AC-PYVNV COMPLEX.
JRNL REF BIOCHEMISTRY V. 39 13376 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11063574
JRNL DOI 10.1021/BI0012336
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 22403
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1100
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 22403
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3432
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.75000
REMARK 3 B22 (A**2) : 4.75000
REMARK 3 B33 (A**2) : -9.49000
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.290
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.800 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.460 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.840 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.420 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MASK
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 30.84
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012024.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-96
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22423
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25200
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: AMORE
REMARK 200 STARTING MODEL: 1GRI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.5M NACL, 0.1M MES/NAOH
REMARK 280 PH 5.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 91.73500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.80500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.80500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 137.60250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.80500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.80500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.86750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.80500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.80500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 137.60250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.80500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.80500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.86750
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 91.73500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 PLEASE NOTE IT HAS NOT BEEN PROVEN THAT THE DOMAIN-
REMARK 300 SWAPPED DIMER HAS BIOLOGICAL SIGNIFICANCE.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L
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: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
REMARK 350 BIOMT1 1 0.000000 -1.000000 0.000000 38.80500
REMARK 350 BIOMT2 1 1.000000 0.000000 0.000000 -38.80500
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -45.86750
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 38.80500
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 38.80500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 45.86750
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
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 APPLY THE FOLLOWING TO CHAINS: C, D, K, L
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -77.61000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 183.47000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
REMARK 350 BIOMT1 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 1.000000 0.000000 0.000000 -77.61000
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 183.47000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J
REMARK 350 BIOMT1 1 0.000000 1.000000 0.000000 77.61000
REMARK 350 BIOMT2 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 183.47000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A 48
REMARK 465 SER A 49
REMARK 465 LYS A 50
REMARK 465 ASN A 51
REMARK 465 TYR A 52
REMARK 465 ILE A 53
REMARK 465 GLU A 54
REMARK 465 MET A 55
REMARK 465 LYS A 56
REMARK 465 PRO A 57
REMARK 465 GLN A 153
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 GLY B 48
REMARK 465 SER B 49
REMARK 465 LYS B 50
REMARK 465 ASN B 51
REMARK 465 TYR B 52
REMARK 465 ILE B 53
REMARK 465 GLU B 54
REMARK 465 GLN B 153
REMARK 465 VAL B 154
REMARK 465 PRO B 155
REMARK 465 GLN B 156
REMARK 465 GLN B 157
REMARK 465 PRO B 158
REMARK 465 THR B 159
REMARK 465 TYR B 160
REMARK 465 VAL B 161
REMARK 465 GLY C 48
REMARK 465 SER C 49
REMARK 465 LYS C 50
REMARK 465 ASN C 51
REMARK 465 TYR C 52
REMARK 465 ILE C 53
REMARK 465 GLU C 54
REMARK 465 GLN C 153
REMARK 465 VAL C 154
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 GLY D 48
REMARK 465 SER D 49
REMARK 465 LYS D 50
REMARK 465 ASN D 51
REMARK 465 TYR D 52
REMARK 465 ILE D 53
REMARK 465 GLU D 54
REMARK 465 MET D 55
REMARK 465 LYS D 56
REMARK 465 PRO D 57
REMARK 465 GLN D 153
REMARK 465 VAL D 154
REMARK 465 PRO D 155
REMARK 465 GLN D 156
REMARK 465 GLN D 157
REMARK 465 PRO D 158
REMARK 465 THR D 159
REMARK 465 TYR D 160
REMARK 465 VAL D 161
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 103 OD1
REMARK 480 ARG A 149 CD
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 PHE A 101 107.07 -164.81
REMARK 500 PRO B 59 10.14 -62.04
REMARK 500 PRO C 59 2.18 -65.39
REMARK 500 HIS C 135 29.94 -75.01
REMARK 500 ASN L 2 33.36 -95.68
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 ACE I -1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE J -1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE K -1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE L -1
DBREF 1FYR A 50 161 UNP P29354 GRB2_HUMAN 50 161
DBREF 1FYR B 50 161 UNP P29354 GRB2_HUMAN 50 161
DBREF 1FYR C 50 161 UNP P29354 GRB2_HUMAN 50 161
DBREF 1FYR D 50 161 UNP P29354 GRB2_HUMAN 50 161
DBREF 1FYR I 0 3 UNP P08581 MET_HUMAN 1356 1359
DBREF 1FYR J 0 3 UNP P08581 MET_HUMAN 1356 1359
DBREF 1FYR K 0 3 UNP P08581 MET_HUMAN 1356 1359
DBREF 1FYR L 0 3 UNP P08581 MET_HUMAN 1356 1359
SEQADV 1FYR GLY A 48 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR SER A 49 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR GLY B 48 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR SER B 49 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR GLY C 48 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR SER C 49 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR GLY D 48 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR SER D 49 UNP P08581 CLONING ARTIFACT
SEQADV 1FYR PTR I 0 UNP P08581 TYR 1356 MODIFIED RESIDUE
SEQADV 1FYR PTR J 0 UNP P08581 TYR 1356 MODIFIED RESIDUE
SEQADV 1FYR PTR K 0 UNP P08581 TYR 1356 MODIFIED RESIDUE
SEQADV 1FYR PTR L 0 UNP P08581 TYR 1356 MODIFIED RESIDUE
SEQRES 1 A 114 GLY SER LYS ASN TYR ILE GLU MET LYS PRO HIS PRO TRP
SEQRES 2 A 114 PHE PHE GLY LYS ILE PRO ARG ALA LYS ALA GLU GLU MET
SEQRES 3 A 114 LEU SER LYS GLN ARG HIS ASP GLY ALA PHE LEU ILE ARG
SEQRES 4 A 114 GLU SER GLU SER ALA PRO GLY ASP PHE SER LEU SER VAL
SEQRES 5 A 114 LYS PHE GLY ASN ASP VAL GLN HIS PHE LYS VAL LEU ARG
SEQRES 6 A 114 ASP GLY ALA GLY LYS TYR PHE LEU TRP VAL VAL LYS PHE
SEQRES 7 A 114 ASN SER LEU ASN GLU LEU VAL ASP TYR HIS ARG SER THR
SEQRES 8 A 114 SER VAL SER ARG ASN GLN GLN ILE PHE LEU ARG ASP ILE
SEQRES 9 A 114 GLU GLN VAL PRO GLN GLN PRO THR TYR VAL
SEQRES 1 B 114 GLY SER LYS ASN TYR ILE GLU MET LYS PRO HIS PRO TRP
SEQRES 2 B 114 PHE PHE GLY LYS ILE PRO ARG ALA LYS ALA GLU GLU MET
SEQRES 3 B 114 LEU SER LYS GLN ARG HIS ASP GLY ALA PHE LEU ILE ARG
SEQRES 4 B 114 GLU SER GLU SER ALA PRO GLY ASP PHE SER LEU SER VAL
SEQRES 5 B 114 LYS PHE GLY ASN ASP VAL GLN HIS PHE LYS VAL LEU ARG
SEQRES 6 B 114 ASP GLY ALA GLY LYS TYR PHE LEU TRP VAL VAL LYS PHE
SEQRES 7 B 114 ASN SER LEU ASN GLU LEU VAL ASP TYR HIS ARG SER THR
SEQRES 8 B 114 SER VAL SER ARG ASN GLN GLN ILE PHE LEU ARG ASP ILE
SEQRES 9 B 114 GLU GLN VAL PRO GLN GLN PRO THR TYR VAL
SEQRES 1 C 114 GLY SER LYS ASN TYR ILE GLU MET LYS PRO HIS PRO TRP
SEQRES 2 C 114 PHE PHE GLY LYS ILE PRO ARG ALA LYS ALA GLU GLU MET
SEQRES 3 C 114 LEU SER LYS GLN ARG HIS ASP GLY ALA PHE LEU ILE ARG
SEQRES 4 C 114 GLU SER GLU SER ALA PRO GLY ASP PHE SER LEU SER VAL
SEQRES 5 C 114 LYS PHE GLY ASN ASP VAL GLN HIS PHE LYS VAL LEU ARG
SEQRES 6 C 114 ASP GLY ALA GLY LYS TYR PHE LEU TRP VAL VAL LYS PHE
SEQRES 7 C 114 ASN SER LEU ASN GLU LEU VAL ASP TYR HIS ARG SER THR
SEQRES 8 C 114 SER VAL SER ARG ASN GLN GLN ILE PHE LEU ARG ASP ILE
SEQRES 9 C 114 GLU GLN VAL PRO GLN GLN PRO THR TYR VAL
SEQRES 1 D 114 GLY SER LYS ASN TYR ILE GLU MET LYS PRO HIS PRO TRP
SEQRES 2 D 114 PHE PHE GLY LYS ILE PRO ARG ALA LYS ALA GLU GLU MET
SEQRES 3 D 114 LEU SER LYS GLN ARG HIS ASP GLY ALA PHE LEU ILE ARG
SEQRES 4 D 114 GLU SER GLU SER ALA PRO GLY ASP PHE SER LEU SER VAL
SEQRES 5 D 114 LYS PHE GLY ASN ASP VAL GLN HIS PHE LYS VAL LEU ARG
SEQRES 6 D 114 ASP GLY ALA GLY LYS TYR PHE LEU TRP VAL VAL LYS PHE
SEQRES 7 D 114 ASN SER LEU ASN GLU LEU VAL ASP TYR HIS ARG SER THR
SEQRES 8 D 114 SER VAL SER ARG ASN GLN GLN ILE PHE LEU ARG ASP ILE
SEQRES 9 D 114 GLU GLN VAL PRO GLN GLN PRO THR TYR VAL
SEQRES 1 I 5 ACE PTR VAL ASN VAL
SEQRES 1 J 5 ACE PTR VAL ASN VAL
SEQRES 1 K 5 ACE PTR VAL ASN VAL
SEQRES 1 L 5 ACE PTR VAL ASN VAL
MODRES 1FYR PTR I 0 TYR O-PHOSPHOTYROSINE
MODRES 1FYR PTR J 0 TYR O-PHOSPHOTYROSINE
MODRES 1FYR PTR K 0 TYR O-PHOSPHOTYROSINE
MODRES 1FYR PTR L 0 TYR O-PHOSPHOTYROSINE
HET ACE I -1 3
HET PTR I 0 16
HET ACE J -1 3
HET PTR J 0 16
HET ACE K -1 3
HET PTR K 0 16
HET ACE L -1 3
HET PTR L 0 16
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 5 ACE 4(C2 H4 O)
FORMUL 5 PTR 4(C9 H12 N O6 P)
FORMUL 9 HOH *182(H2 O)
HELIX 1 1 PRO A 66 LYS A 76 1 11
HELIX 2 2 SER A 127 HIS A 135 1 9
HELIX 3 3 PRO B 66 LYS B 76 1 11
HELIX 4 4 SER B 127 THR B 138 1 12
HELIX 5 5 PRO C 66 SER C 75 1 10
HELIX 6 6 SER C 127 HIS C 135 1 9
HELIX 7 7 PRO D 66 SER D 75 1 10
HELIX 8 8 SER D 127 HIS D 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 N SER A 96 O ARG A 86
SHEET 3 A 4 ASP A 104 ARG A 112 -1 O ASP A 104 N PHE A 101
SHEET 4 A 4 TYR A 118 PHE A 119 -1 O PHE A 119 N LEU A 111
SHEET 1 B 3 PHE B 83 GLU B 87 0
SHEET 2 B 3 PHE B 95 PHE B 101 -1 N SER B 96 O ARG B 86
SHEET 3 B 3 ASP B 104 LYS B 109 -1 O ASP B 104 N PHE B 101
SHEET 1 C 2 LEU B 111 ARG B 112 0
SHEET 2 C 2 TYR B 118 PHE B 119 -1 O PHE B 119 N LEU B 111
SHEET 1 D 4 PHE C 61 LYS C 64 0
SHEET 2 D 4 PHE C 83 GLU C 87 1 O ILE C 85 N PHE C 62
SHEET 3 D 4 PHE C 95 PHE C 101 -1 N SER C 96 O ARG C 86
SHEET 4 D 4 ASP C 104 LYS C 109 -1 O ASP C 104 N PHE C 101
SHEET 1 E 2 LEU C 111 ARG C 112 0
SHEET 2 E 2 TYR C 118 PHE C 119 -1 O PHE C 119 N LEU C 111
SHEET 1 F 4 ARG C 149 ASP C 150 0
SHEET 2 F 4 ALA D 82 GLU D 87 1 N PHE D 83 O ARG C 149
SHEET 3 F 4 PHE D 95 PHE D 101 -1 N SER D 96 O ARG D 86
SHEET 4 F 4 ASP D 104 LYS D 109 -1 O ASP D 104 N PHE D 101
SHEET 1 G 2 LEU D 111 ARG D 112 0
SHEET 2 G 2 TYR D 118 PHE D 119 -1 O PHE D 119 N LEU D 111
LINK C ACE I -1 N PTR I 0 1555 1555 1.33
LINK C PTR I 0 N VAL I 1 1555 1555 1.33
LINK C ACE J -1 N PTR J 0 1555 1555 1.34
LINK C PTR J 0 N VAL J 1 1555 1555 1.46
LINK C ACE K -1 N PTR K 0 1555 1555 1.34
LINK C PTR K 0 N VAL K 1 1555 1555 1.43
LINK C ACE L -1 N PTR L 0 1555 1555 1.34
LINK C PTR L 0 N VAL L 1 1555 1555 1.36
SITE 1 AC1 1 ARG A 67
SITE 1 AC2 2 ARG B 67 HOH J1039
SITE 1 AC3 1 ARG C 67
SITE 1 AC4 2 ARG D 67 HOH L1031
CRYST1 77.610 77.610 183.470 90.00 90.00 90.00 P 43 21 2 32
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 0.012885 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005450 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
