Header list of 1wgr.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 28-MAY-04 1WGR
TITLE SOLUTION STRUCTURE OF THE RA DOMAIN OF HUMAN GRB7 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RA DOMAIN;
COMPND 5 SYNONYM: GRB7, GRB7 ADAPTER PROTEIN, EPIDERMAL GROWTH FACTOR RECEPTOR
COMPND 6 GRB-7, B47;
COMPND 7 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: IMS CDNA HEP10521;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-63;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RA DOMAIN, GRB7, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WGR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WGR 1 VERSN
REVDAT 1 28-NOV-04 1WGR 0
JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RA DOMAIN OF HUMAN GRB7 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023562.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.17MM RA DOMAIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.897, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 H HIS A 10 O VAL A 26 1.53
REMARK 500 O VAL A 73 H ALA A 77 1.59
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 5 128.54 179.51
REMARK 500 1 ALA A 28 97.63 -42.71
REMARK 500 1 HIS A 44 -76.81 64.96
REMARK 500 1 ALA A 45 93.22 51.51
REMARK 500 1 SER A 47 -51.64 172.77
REMARK 500 1 ASP A 48 177.45 57.27
REMARK 500 1 GLU A 49 172.16 -58.56
REMARK 500 1 TRP A 51 -173.30 63.64
REMARK 500 1 HIS A 59 -42.54 -166.23
REMARK 500 1 PHE A 93 92.97 179.78
REMARK 500 1 ALA A 94 -170.57 -175.44
REMARK 500 1 SER A 98 -58.40 -142.96
REMARK 500 1 SER A 99 107.05 56.67
REMARK 500 2 ALA A 28 98.12 -42.11
REMARK 500 2 ARG A 42 -58.10 177.74
REMARK 500 2 ALA A 43 -62.68 -145.76
REMARK 500 2 ALA A 45 87.22 61.95
REMARK 500 2 LEU A 46 67.51 -158.29
REMARK 500 2 ASP A 48 -50.04 -137.32
REMARK 500 2 GLU A 49 163.10 -45.22
REMARK 500 2 TRP A 51 168.42 63.78
REMARK 500 2 HIS A 59 -41.96 -167.39
REMARK 500 2 SER A 85 167.90 54.60
REMARK 500 2 PHE A 93 35.64 -90.06
REMARK 500 2 ALA A 94 -59.77 -124.57
REMARK 500 2 SER A 99 -57.60 -144.33
REMARK 500 3 SER A 2 -58.85 74.92
REMARK 500 3 SER A 5 103.59 -178.05
REMARK 500 3 SER A 6 -46.19 -165.83
REMARK 500 3 ARG A 8 155.24 -40.22
REMARK 500 3 ALA A 28 81.70 -62.30
REMARK 500 3 ARG A 42 85.80 178.52
REMARK 500 3 ALA A 43 174.83 64.71
REMARK 500 3 ALA A 45 -53.16 -142.03
REMARK 500 3 LEU A 46 123.87 63.10
REMARK 500 3 ASP A 48 -51.35 -152.62
REMARK 500 3 HIS A 59 -42.46 -166.40
REMARK 500 3 GLU A 67 -167.36 -70.66
REMARK 500 3 ASP A 84 56.21 -92.49
REMARK 500 3 ALA A 94 77.95 46.29
REMARK 500 3 SER A 98 93.56 44.68
REMARK 500 4 SER A 3 162.63 59.86
REMARK 500 4 SER A 5 119.19 -167.77
REMARK 500 4 SER A 6 91.36 41.21
REMARK 500 4 ARG A 8 156.93 -42.85
REMARK 500 4 ALA A 28 96.60 -44.77
REMARK 500 4 ARG A 42 52.60 -144.67
REMARK 500 4 ALA A 43 -59.98 -160.93
REMARK 500 4 HIS A 44 -65.01 -101.44
REMARK 500 4 ALA A 45 -172.69 56.96
REMARK 500
REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001618.1 RELATED DB: TARGETDB
DBREF 1WGR A 8 94 UNP Q14451 GRB7_HUMAN 100 186
SEQADV 1WGR GLY A 1 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 2 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 3 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR GLY A 4 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 5 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 6 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR GLY A 7 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 95 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR GLY A 96 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR PRO A 97 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 98 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR SER A 99 UNP Q14451 CLONING ARTIFACT
SEQADV 1WGR GLY A 100 UNP Q14451 CLONING ARTIFACT
SEQRES 1 A 100 GLY SER SER GLY SER SER GLY ARG PRO HIS VAL VAL LYS
SEQRES 2 A 100 VAL TYR SER GLU ASP GLY ALA CYS ARG SER VAL GLU VAL
SEQRES 3 A 100 ALA ALA GLY ALA THR ALA ARG HIS VAL CYS GLU MET LEU
SEQRES 4 A 100 VAL GLN ARG ALA HIS ALA LEU SER ASP GLU THR TRP GLY
SEQRES 5 A 100 LEU VAL GLU CYS HIS PRO HIS LEU ALA LEU GLU ARG GLY
SEQRES 6 A 100 LEU GLU ASP HIS GLU SER VAL VAL GLU VAL GLN ALA ALA
SEQRES 7 A 100 TRP PRO VAL GLY GLY ASP SER ARG PHE VAL PHE ARG LYS
SEQRES 8 A 100 ASN PHE ALA SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 32 VAL A 40 1 9
HELIX 2 2 VAL A 72 ALA A 78 1 7
SHEET 1 A 5 CYS A 21 VAL A 26 0
SHEET 2 A 5 HIS A 10 SER A 16 -1 N HIS A 10 O VAL A 26
SHEET 3 A 5 ARG A 86 PHE A 89 1 O PHE A 87 N TYR A 15
SHEET 4 A 5 LEU A 53 HIS A 57 -1 N CYS A 56 O ARG A 86
SHEET 5 A 5 LEU A 62 LEU A 66 -1 O ARG A 64 N GLU A 55
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 - r 2 2 Bytes