Header list of 1wry.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-OCT-04 1WRY
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH3 DOMAIN-BINDING GLUTAMIC ACID-RICH-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3BGR DOMAIN;
COMPND 5 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 STM03594;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040517-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3BGR LIKE PROTEIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,K.MIYAMOTO,T.NAGASHIMA,F.HAYASHI,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WRY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WRY 1 VERSN
REVDAT 1 29-APR-05 1WRY 0
JRNL AUTH K.INOUE,K.MIYAMOTO,T.NAGASHIMA,F.HAYASHI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN-BINDING GLUTAMIC
JRNL TITL 2 ACID-RICH-LIKE PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WRY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023928.
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 : 1.10MM SH3BGR U-15N,13C; 20MM D
REMARK 210 -TRIS-HCL; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 10% 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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.8992, 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 : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 O PHE A 33 HD21 ASN A 37 1.50
REMARK 500 O ASN A 78 H SER A 80 1.53
REMARK 500 O LEU A 34 H ILE A 39 1.54
REMARK 500 O ALA A 92 H ALA A 97 1.56
REMARK 500 O ARG A 93 H ASN A 96 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 2 140.77 -172.93
REMARK 500 1 MET A 8 85.92 38.86
REMARK 500 1 SER A 20 109.52 -54.99
REMARK 500 1 ALA A 48 -74.11 -74.21
REMARK 500 1 PRO A 66 -166.79 -75.04
REMARK 500 1 THR A 68 135.47 -177.84
REMARK 500 1 TYR A 70 162.14 56.30
REMARK 500 1 GLU A 79 -59.82 65.73
REMARK 500 1 SER A 80 -39.81 -145.81
REMARK 500 1 TYR A 86 -36.08 -37.88
REMARK 500 1 VAL A 115 89.28 41.28
REMARK 500 1 SER A 119 100.42 53.32
REMARK 500 2 SER A 2 -58.14 -167.53
REMARK 500 2 SER A 6 104.59 176.73
REMARK 500 2 SER A 16 125.63 -38.53
REMARK 500 2 SER A 17 54.06 85.07
REMARK 500 2 ALA A 48 57.05 -98.15
REMARK 500 2 ASN A 49 93.40 169.43
REMARK 500 2 GLU A 79 -62.02 65.92
REMARK 500 2 SER A 80 -38.30 -143.51
REMARK 500 2 TYR A 86 -37.79 -39.90
REMARK 500 2 ALA A 97 25.46 -153.70
REMARK 500 2 SER A 116 101.88 53.36
REMARK 500 3 SER A 3 99.06 -58.25
REMARK 500 3 SER A 5 105.90 -175.08
REMARK 500 3 ALA A 15 65.54 -113.88
REMARK 500 3 SER A 16 138.43 -37.65
REMARK 500 3 SER A 20 100.03 -173.05
REMARK 500 3 ALA A 47 50.32 -91.09
REMARK 500 3 ALA A 48 -67.49 -175.12
REMARK 500 3 THR A 68 144.23 -170.28
REMARK 500 3 GLU A 79 -76.38 62.82
REMARK 500 3 SER A 80 12.95 -141.40
REMARK 500 3 ALA A 97 37.78 -147.84
REMARK 500 3 VAL A 115 102.39 -40.74
REMARK 500 3 SER A 119 78.18 60.63
REMARK 500 4 SER A 2 107.43 -165.86
REMARK 500 4 MET A 8 85.34 -162.78
REMARK 500 4 ALA A 15 63.65 -115.60
REMARK 500 4 SER A 16 128.28 -37.74
REMARK 500 4 SER A 17 39.48 83.33
REMARK 500 4 ALA A 48 -86.12 -81.73
REMARK 500 4 GLU A 79 -59.79 66.50
REMARK 500 4 SER A 80 -37.99 -145.78
REMARK 500 4 SER A 116 143.05 61.10
REMARK 500 4 SER A 119 -59.67 72.71
REMARK 500 5 SER A 3 128.39 -178.82
REMARK 500 5 MET A 8 85.61 61.21
REMARK 500 5 ALA A 15 64.69 -119.53
REMARK 500 5 SER A 16 122.32 -38.38
REMARK 500
REMARK 500 THIS ENTRY HAS 253 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003589 RELATED DB: TARGETDB
DBREF 1WRY A 8 115 UNP O75368 SH3L1_HUMAN 1 108
SEQADV 1WRY GLY A 1 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 2 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 3 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY GLY A 4 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 5 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 6 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY GLY A 7 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 116 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY GLY A 117 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY PRO A 118 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 119 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY SER A 120 UNP O75368 CLONING ARTIFACT
SEQADV 1WRY GLY A 121 UNP O75368 CLONING ARTIFACT
SEQRES 1 A 121 GLY SER SER GLY SER SER GLY MET VAL ILE ARG VAL TYR
SEQRES 2 A 121 ILE ALA SER SER SER GLY SER THR ALA ILE LYS LYS LYS
SEQRES 3 A 121 GLN GLN ASP VAL LEU GLY PHE LEU GLU ALA ASN LYS ILE
SEQRES 4 A 121 GLY PHE GLU GLU LYS ASP ILE ALA ALA ASN GLU GLU ASN
SEQRES 5 A 121 ARG LYS TRP MET ARG GLU ASN VAL PRO GLU ASN SER ARG
SEQRES 6 A 121 PRO ALA THR GLY TYR PRO LEU PRO PRO GLN ILE PHE ASN
SEQRES 7 A 121 GLU SER GLN TYR ARG GLY ASP TYR ASP ALA PHE PHE GLU
SEQRES 8 A 121 ALA ARG GLU ASN ASN ALA VAL TYR ALA PHE LEU GLY LEU
SEQRES 9 A 121 THR ALA PRO PRO GLY SER LYS GLU ALA GLU VAL SER GLY
SEQRES 10 A 121 PRO SER SER GLY
HELIX 1 1 SER A 20 ASN A 37 1 18
HELIX 2 2 ASN A 49 VAL A 60 1 12
HELIX 3 3 TYR A 86 ASN A 95 1 10
HELIX 4 4 ALA A 97 LEU A 102 1 6
HELIX 5 5 SER A 110 VAL A 115 1 6
SHEET 1 A 4 PHE A 41 ASP A 45 0
SHEET 2 A 4 ILE A 10 ILE A 14 1 N ILE A 14 O LYS A 44
SHEET 3 A 4 GLN A 75 ASN A 78 -1 O GLN A 75 N TYR A 13
SHEET 4 A 4 GLN A 81 ASP A 85 -1 O GLY A 84 N ILE A 76
CISPEP 1 PRO A 73 PRO A 74 1 0.08
CISPEP 2 PRO A 73 PRO A 74 2 0.02
CISPEP 3 PRO A 73 PRO A 74 3 -0.05
CISPEP 4 PRO A 73 PRO A 74 4 0.04
CISPEP 5 PRO A 73 PRO A 74 5 0.03
CISPEP 6 PRO A 73 PRO A 74 6 0.06
CISPEP 7 PRO A 73 PRO A 74 7 0.00
CISPEP 8 PRO A 73 PRO A 74 8 -0.04
CISPEP 9 PRO A 73 PRO A 74 9 0.00
CISPEP 10 PRO A 73 PRO A 74 10 0.03
CISPEP 11 PRO A 73 PRO A 74 11 0.01
CISPEP 12 PRO A 73 PRO A 74 12 0.03
CISPEP 13 PRO A 73 PRO A 74 13 0.03
CISPEP 14 PRO A 73 PRO A 74 14 -0.01
CISPEP 15 PRO A 73 PRO A 74 15 -0.05
CISPEP 16 PRO A 73 PRO A 74 16 0.03
CISPEP 17 PRO A 73 PRO A 74 17 -0.01
CISPEP 18 PRO A 73 PRO A 74 18 0.02
CISPEP 19 PRO A 73 PRO A 74 19 -0.01
CISPEP 20 PRO A 73 PRO A 74 20 0.07
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