Header list of 1fhs.pdb file
Complete list - t 27 2 Bytes
HEADER SH2 DOMAIN 12-JUN-97 1FHS
TITLE THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY DOMAIN-2
TITLE 2 OF THE GROWTH FACTOR RECEPTOR BOUND PROTEIN-2, NMR, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR BOUND PROTEIN-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: GRB2;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE-60
KEYWDS GRB2, SH2 DOMAIN, PROTEIN NMR, SOLUTION STRUCTURES
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR M.M.SENIOR,A.F.FREDERICK,S.BLACK,L.M.PERKINS,O.WILSON,M.E.SNOW,Y.-
AUTHOR 2 S.WANG
REVDAT 3 27-OCT-21 1FHS 1 REMARK
REVDAT 2 24-FEB-09 1FHS 1 VERSN
REVDAT 1 17-JUN-98 1FHS 0
JRNL AUTH M.M.SENIOR,A.F.FREDERICK,S.BLACK,N.J.MURGOLO,L.M.PERKINS,
JRNL AUTH 2 O.WILSON,M.E.SNOW,Y.S.WANG
JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY
JRNL TITL 2 DOMAIN-2 OF THE GROWTH FACTOR RECEPTOR-BOUND PROTEIN-2.
JRNL REF J.BIOMOL.NMR V. 11 153 1998
JRNL REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE GENERATED FROM
REMARK 3 SOLUTION NMR DATA USING DISTANT GEOMETRY AND SIMULATED ANNEALING
REMARK 3 CALCULATION FOLLOWED BY RESTRAINED ENERGY MINIMIZATION. A FAMILY
REMARK 3 OF 18 STRUCTURES WERE SELECTED FROM TOTAL OF 100 STRUCTURES.
REMARK 4
REMARK 4 1FHS 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_1000173290.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.3
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DG/SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HE ARG A 35 HG SER A 45 1.28
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 LYS A 5 94.11 39.08
REMARK 500 1 LYS A 13 42.28 31.10
REMARK 500 1 ALA A 17 -81.19 -56.32
REMARK 500 1 GLU A 21 -87.46 -40.40
REMARK 500 1 HIS A 28 -156.97 -76.10
REMARK 500 1 GLU A 38 -90.65 -38.60
REMARK 500 1 ALA A 40 150.23 -42.58
REMARK 500 1 PRO A 41 -116.30 -70.67
REMARK 500 1 PHE A 50 40.60 -92.60
REMARK 500 1 ASN A 52 -35.04 72.07
REMARK 500 1 ASP A 53 -163.63 -171.45
REMARK 500 1 ASP A 62 -129.74 74.79
REMARK 500 1 ALA A 64 36.01 -143.83
REMARK 500 1 LEU A 69 -83.49 -61.59
REMARK 500 1 VAL A 71 -82.75 -137.93
REMARK 500 1 PHE A 74 140.13 -170.04
REMARK 500 1 LEU A 80 -70.83 -72.10
REMARK 500 1 VAL A 81 -35.65 -37.98
REMARK 500 1 HIS A 84 39.13 -89.50
REMARK 500 1 SER A 88 -153.59 43.14
REMARK 500 1 VAL A 89 44.51 -153.99
REMARK 500 1 SER A 90 124.48 179.55
REMARK 500 1 GLN A 93 -148.69 -160.67
REMARK 500 1 ILE A 100 31.53 -71.95
REMARK 500 1 VAL A 103 149.00 -33.98
REMARK 500 1 GLN A 105 -156.54 36.59
REMARK 500 1 THR A 108 143.87 60.22
REMARK 500 1 TYR A 109 124.29 65.27
REMARK 500 1 GLN A 111 114.31 57.90
REMARK 500 2 HIS A 7 153.12 -37.35
REMARK 500 2 TRP A 9 16.65 49.25
REMARK 500 2 LYS A 13 47.66 25.89
REMARK 500 2 ALA A 17 -72.13 -54.72
REMARK 500 2 GLU A 21 -81.88 -55.53
REMARK 500 2 LYS A 25 33.48 -72.07
REMARK 500 2 GLU A 38 -91.52 -41.08
REMARK 500 2 ALA A 40 102.58 -41.44
REMARK 500 2 PHE A 50 -104.33 -79.76
REMARK 500 2 ASP A 62 140.11 179.15
REMARK 500 2 ALA A 64 45.00 -142.98
REMARK 500 2 LYS A 66 -140.69 71.53
REMARK 500 2 TRP A 70 -41.41 -135.53
REMARK 500 2 VAL A 71 -83.05 -138.33
REMARK 500 2 HIS A 84 36.59 -83.05
REMARK 500 2 SER A 86 -78.20 -89.93
REMARK 500 2 THR A 87 39.48 -170.02
REMARK 500 2 SER A 88 140.98 -177.22
REMARK 500 2 SER A 90 -69.40 -138.94
REMARK 500 2 ARG A 91 6.90 -60.99
REMARK 500 2 ASN A 92 -11.97 70.86
REMARK 500
REMARK 500 THIS ENTRY HAS 583 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 42 ASP A 43 5 -45.03
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FHS A 2 112 UNP P62993 GRB2_HUMAN 53 163
SEQRES 1 A 112 GLY ILE GLU MET LYS PRO HIS PRO TRP PHE PHE GLY LYS
SEQRES 2 A 112 ILE PRO ARG ALA LYS ALA GLU GLU MET LEU SER LYS GLN
SEQRES 3 A 112 ARG HIS ASP GLY ALA PHE LEU ILE ARG GLU SER GLU SER
SEQRES 4 A 112 ALA PRO GLY ASP PHE SER LEU SER VAL LYS PHE GLY ASN
SEQRES 5 A 112 ASP VAL GLN HIS PHE LYS VAL LEU ARG ASP GLY ALA GLY
SEQRES 6 A 112 LYS TYR PHE LEU TRP VAL VAL LYS PHE ASN SER LEU ASN
SEQRES 7 A 112 GLU LEU VAL ASP TYR HIS ARG SER THR SER VAL SER ARG
SEQRES 8 A 112 ASN GLN GLN ILE PHE LEU ARG ASP ILE GLU GLN VAL PRO
SEQRES 9 A 112 GLN GLN PRO THR TYR VAL GLN ALA
HELIX 1 1 ARG A 16 LYS A 25 1 10
HELIX 2 2 LEU A 77 SER A 86 1 10
SHEET 1 A 3 PHE A 32 GLU A 36 0
SHEET 2 A 3 PHE A 44 LYS A 49 -1 N SER A 47 O LEU A 33
SHEET 3 A 3 VAL A 54 VAL A 59 -1 N VAL A 59 O PHE A 44
CISPEP 1 PRO A 8 TRP A 9 1 -15.56
CISPEP 2 GLN A 106 PRO A 107 2 -5.93
CISPEP 3 HIS A 28 ASP A 29 5 -0.12
CISPEP 4 ALA A 40 PRO A 41 6 -4.92
CISPEP 5 PRO A 104 GLN A 105 6 3.99
CISPEP 6 GLY A 1 ILE A 2 8 -0.05
CISPEP 7 ALA A 40 PRO A 41 8 -0.39
CISPEP 8 GLY A 1 ILE A 2 10 0.38
CISPEP 9 SER A 88 VAL A 89 10 -8.50
CISPEP 10 PRO A 6 HIS A 7 11 11.52
CISPEP 11 GLY A 12 LYS A 13 11 0.79
CISPEP 12 GLY A 12 LYS A 13 12 -6.45
CISPEP 13 ASP A 29 GLY A 30 13 7.07
CISPEP 14 GLN A 111 ALA A 112 14 4.38
CISPEP 15 GLY A 1 ILE A 2 15 -0.31
CISPEP 16 GLY A 63 ALA A 64 15 7.09
CISPEP 17 PRO A 104 GLN A 105 15 12.17
CISPEP 18 ARG A 27 HIS A 28 16 13.56
CISPEP 19 ASP A 62 GLY A 63 16 7.70
CISPEP 20 GLY A 1 ILE A 2 17 -0.49
CISPEP 21 GLY A 12 LYS A 13 17 -6.66
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 - t 27 2 Bytes