Header list of 1ghu.pdb file
Complete list - b 23 2 Bytes
HEADER SRC HOMOLOGY 2 DOMAIN 05-AUG-96 1GHU
TITLE NMR SOLUTION STRUCTURE OF GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2
TITLE 2 (GRB2) SH2 DOMAIN, 24 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRB2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-KT
KEYWDS SRC HOMOLOGY 2 DOMAIN, GRB2, SH2
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR K.H.THORNTON,W.T.MUELLER,P.MCCONNELL,G.ZHU,A.R.SALTIEL,V.THANABAL
REVDAT 4 23-FEB-22 1GHU 1 REMARK
REVDAT 3 24-FEB-09 1GHU 1 VERSN
REVDAT 2 01-APR-03 1GHU 1 JRNL
REVDAT 1 27-JAN-97 1GHU 0
JRNL AUTH K.H.THORNTON,W.T.MUELLER,P.MCCONNELL,G.ZHU,A.R.SALTIEL,
JRNL AUTH 2 V.THANABAL
JRNL TITL NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE GROWTH
JRNL TITL 2 FACTOR RECEPTOR-BOUND PROTEIN 2 SRC HOMOLOGY 2 DOMAIN.
JRNL REF BIOCHEMISTRY V. 35 11852 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8794768
JRNL DOI 10.1021/BI952615S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GHU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173579.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-24
REMARK 465 RES C SSSEQI
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 GLU A 159
REMARK 465 PHE A 160
REMARK 465 ILE A 161
REMARK 465 VAL A 162
REMARK 465 THR A 163
REMARK 465 ASP A 164
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 3 HIS A 107 CG HIS A 107 CD2 0.054
REMARK 500
REMARK 500 REMARK: NULL
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 1 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 HIS A 79 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 HIS A 107 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 1 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 HIS A 135 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 HIS A 79 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 PHE A 101 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 HIS A 107 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 HIS A 135 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 2 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 HIS A 79 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 HIS A 107 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 HIS A 135 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 3 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 HIS A 79 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 HIS A 107 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 HIS A 135 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 4 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 HIS A 79 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 5 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 HIS A 107 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 HIS A 135 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 5 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 243 ANGLE DEVIATIONS.
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 1 SER A 90 -34.11 103.39
REMARK 500 1 ALA A 115 -94.25 -89.03
REMARK 500 1 TRP A 121 -74.07 -92.03
REMARK 500 1 VAL A 122 -64.98 -147.24
REMARK 500 1 ASN A 143 -77.71 -160.32
REMARK 500 2 PHE A 62 -87.27 -116.49
REMARK 500 2 LYS A 64 73.42 67.14
REMARK 500 2 SER A 90 -22.21 84.98
REMARK 500 2 PHE A 101 -140.03 -89.23
REMARK 500 2 ASN A 103 58.72 -140.04
REMARK 500 2 ALA A 115 -79.15 78.53
REMARK 500 2 VAL A 122 -90.68 60.75
REMARK 500 3 TRP A 60 -44.35 -156.59
REMARK 500 3 PHE A 62 -71.91 -118.83
REMARK 500 3 LYS A 64 71.03 63.35
REMARK 500 3 ALA A 115 -83.11 -86.62
REMARK 500 3 TRP A 121 -86.17 -84.04
REMARK 500 3 VAL A 122 -61.02 -139.88
REMARK 500 3 ASN A 129 -58.56 167.32
REMARK 500 3 ARG A 142 -66.64 91.88
REMARK 500 4 LYS A 64 69.68 66.85
REMARK 500 4 GLU A 89 -72.00 74.45
REMARK 500 4 ASN A 103 45.38 -149.31
REMARK 500 4 ASP A 113 -65.42 -100.64
REMARK 500 4 LEU A 120 -61.63 -104.77
REMARK 500 4 TRP A 121 -82.04 -83.90
REMARK 500 4 VAL A 122 -58.78 -136.67
REMARK 500 5 SER A 59 115.27 75.39
REMARK 500 5 PHE A 62 -73.88 -105.60
REMARK 500 5 LYS A 64 -13.15 76.32
REMARK 500 5 GLU A 89 -89.78 72.65
REMARK 500 5 SER A 90 61.46 -152.55
REMARK 500 5 ALA A 115 -78.98 -88.72
REMARK 500 5 TRP A 121 -71.34 -76.82
REMARK 500 5 VAL A 122 -52.41 -156.47
REMARK 500 6 TRP A 60 -47.15 -130.71
REMARK 500 6 PHE A 62 -92.50 -99.84
REMARK 500 6 LYS A 64 69.97 64.69
REMARK 500 6 ASN A 103 -18.90 75.23
REMARK 500 6 ALA A 115 -84.14 -84.60
REMARK 500 6 TRP A 121 -84.74 -83.57
REMARK 500 6 VAL A 122 -55.97 -141.02
REMARK 500 6 ARG A 142 -78.79 86.65
REMARK 500 7 PHE A 62 -80.03 -121.30
REMARK 500 7 ASN A 103 -13.35 70.76
REMARK 500 7 ALA A 115 -70.37 -82.29
REMARK 500 7 LEU A 120 -32.88 -134.67
REMARK 500 7 TRP A 121 -76.60 -114.19
REMARK 500 7 VAL A 122 -73.57 -130.05
REMARK 500 7 SER A 141 -113.25 -105.94
REMARK 500
REMARK 500 THIS ENTRY HAS 154 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 6 PHE A 83 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GHU A 60 158 UNP P62993 GRB2_HUMAN 60 158
SEQRES 1 A 107 GLY SER TRP PHE PHE GLY LYS ILE PRO ARG ALA LYS ALA
SEQRES 2 A 107 GLU GLU MET LEU SER LYS GLN ARG HIS ASP GLY ALA PHE
SEQRES 3 A 107 LEU ILE ARG GLU SER GLU SER ALA PRO GLY ASP PHE SER
SEQRES 4 A 107 LEU SER VAL LYS PHE GLY ASN ASP VAL GLN HIS PHE LYS
SEQRES 5 A 107 VAL LEU ARG ASP GLY ALA GLY LYS TYR PHE LEU TRP VAL
SEQRES 6 A 107 VAL LYS PHE ASN SER LEU ASN GLU LEU VAL ASP TYR HIS
SEQRES 7 A 107 ARG SER THR SER VAL SER ARG ASN GLN GLN ILE PHE LEU
SEQRES 8 A 107 ARG ASP ILE GLU GLN VAL PRO GLN GLN PRO GLU PHE ILE
SEQRES 9 A 107 VAL THR ASP
HELIX 1 1 ARG A 67 LYS A 76 1 10
HELIX 2 2 LEU A 128 HIS A 135 1 8
SHEET 1 A 3 PHE A 83 GLU A 87 0
SHEET 2 A 3 PHE A 95 PHE A 101 -1 N SER A 98 O LEU A 84
SHEET 3 A 3 ASP A 104 VAL A 110 -1 N VAL A 110 O PHE A 95
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes