Header list of 2csp.pdb file
Complete list - r 9 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 22-MAY-05 2CSP
TITLE SOLUTION STRUCTURE OF THE FNIII DOMAIN OF HUMAN RIM-BINDING PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIM BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FN3 DOMAIN;
COMPND 5 SYNONYM: RIM-BP2;
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: KAZUSA CDNA HG00364;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-13;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FN3 DOMAIN, RIM BINDING PROTEIN 2, RIM-BP2, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CSP 1 VERSN
REVDAT 1 22-NOV-05 2CSP 0
JRNL AUTH K.INOUE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FNIII DOMAIN OF HUMAN RIM-BINDING
JRNL TITL 2 PROTEIN 2
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 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CSP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024579.
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 : 1.09MM U-15N, 13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
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 0.9296, CYANA 2.0.17
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 : 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: 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 83.57 -68.97
REMARK 500 1 VAL A 8 110.20 -39.58
REMARK 500 1 GLN A 27 -75.73 -86.27
REMARK 500 1 ALA A 28 139.23 -175.77
REMARK 500 1 VAL A 30 -26.85 -38.16
REMARK 500 1 THR A 45 157.63 -37.27
REMARK 500 1 PRO A 46 15.00 -69.75
REMARK 500 1 SER A 50 -73.79 -82.59
REMARK 500 1 ALA A 62 -74.61 -108.55
REMARK 500 1 ILE A 71 43.64 -79.64
REMARK 500 1 SER A 77 136.83 -172.30
REMARK 500 1 VAL A 105 170.06 -54.98
REMARK 500 1 SER A 107 -178.04 -62.25
REMARK 500 1 ALA A 108 108.51 -55.78
REMARK 500 1 VAL A 109 104.93 -49.39
REMARK 500 1 ALA A 111 108.93 -59.77
REMARK 500 2 GLN A 27 -75.45 -93.11
REMARK 500 2 ALA A 28 135.20 -175.85
REMARK 500 2 VAL A 30 -34.62 -35.58
REMARK 500 2 THR A 45 157.70 -37.22
REMARK 500 2 PRO A 46 14.77 -69.76
REMARK 500 2 ALA A 62 -70.39 -108.77
REMARK 500 2 ARG A 66 108.71 -47.96
REMARK 500 2 ILE A 71 46.08 -77.56
REMARK 500 2 SER A 77 130.67 -173.14
REMARK 500 2 VAL A 105 163.43 -46.78
REMARK 500 2 SER A 107 178.09 -59.25
REMARK 500 2 VAL A 109 104.72 -53.76
REMARK 500 3 THR A 12 41.19 -100.65
REMARK 500 3 GLN A 27 -76.05 -90.90
REMARK 500 3 ALA A 28 134.25 -176.26
REMARK 500 3 VAL A 30 -28.25 -37.50
REMARK 500 3 THR A 45 157.87 -37.64
REMARK 500 3 PRO A 46 15.71 -69.79
REMARK 500 3 SER A 50 -73.34 -86.65
REMARK 500 3 ILE A 71 45.22 -77.70
REMARK 500 3 SER A 107 179.04 -57.12
REMARK 500 3 VAL A 109 104.96 -54.34
REMARK 500 3 HIS A 123 141.31 -38.68
REMARK 500 4 GLU A 9 148.37 -38.69
REMARK 500 4 GLN A 27 -75.44 -93.55
REMARK 500 4 ALA A 28 134.68 -175.69
REMARK 500 4 VAL A 30 -33.67 -38.86
REMARK 500 4 THR A 45 158.12 -37.25
REMARK 500 4 PRO A 46 16.11 -69.77
REMARK 500 4 SER A 50 -63.21 -94.67
REMARK 500 4 ALA A 62 -67.33 -121.29
REMARK 500 4 ILE A 71 46.09 -77.44
REMARK 500 4 SER A 77 130.16 -171.49
REMARK 500 4 GLU A 103 -174.67 -51.95
REMARK 500
REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000310.4 RELATED DB: TARGETDB
DBREF 2CSP A 8 124 UNP O15034 RIMB2_HUMAN 477 593
SEQADV 2CSP GLY A 1 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 2 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 3 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP GLY A 4 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 5 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 6 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP GLY A 7 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 125 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP GLY A 126 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP PRO A 127 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 128 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP SER A 129 UNP O15034 CLONING ARTIFACT
SEQADV 2CSP GLY A 130 UNP O15034 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY VAL GLU PHE SER THR LEU
SEQRES 2 A 130 PRO ALA GLY PRO PRO ALA PRO PRO GLN ASP VAL THR VAL
SEQRES 3 A 130 GLN ALA GLY VAL THR PRO ALA THR ILE ARG VAL SER TRP
SEQRES 4 A 130 ARG PRO PRO VAL LEU THR PRO THR GLY LEU SER ASN GLY
SEQRES 5 A 130 ALA ASN VAL THR GLY TYR GLY VAL TYR ALA LYS GLY GLN
SEQRES 6 A 130 ARG VAL ALA GLU VAL ILE PHE PRO THR ALA ASP SER THR
SEQRES 7 A 130 ALA VAL GLU LEU VAL ARG LEU ARG SER LEU GLU ALA LYS
SEQRES 8 A 130 GLY VAL THR VAL ARG THR LEU SER ALA GLN GLY GLU SER
SEQRES 9 A 130 VAL ASP SER ALA VAL ALA ALA VAL PRO PRO GLU LEU LEU
SEQRES 10 A 130 VAL PRO PRO THR PRO HIS PRO SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 82 GLU A 89 1 8
HELIX 2 2 PRO A 113 VAL A 118 1 6
SHEET 1 A 3 GLN A 22 VAL A 26 0
SHEET 2 A 3 THR A 34 ARG A 40 -1 O ARG A 40 N GLN A 22
SHEET 3 A 3 SER A 77 GLU A 81 -1 O THR A 78 N VAL A 37
SHEET 1 B 3 ARG A 66 VAL A 70 0
SHEET 2 B 3 VAL A 55 TYR A 61 -1 N TYR A 58 O VAL A 70
SHEET 3 B 3 THR A 94 SER A 99 -1 O LEU A 98 N GLY A 57
CISPEP 1 GLY A 16 PRO A 17 1 0.04
CISPEP 2 GLY A 16 PRO A 17 2 0.06
CISPEP 3 GLY A 16 PRO A 17 3 0.03
CISPEP 4 GLY A 16 PRO A 17 4 0.03
CISPEP 5 GLY A 16 PRO A 17 5 0.08
CISPEP 6 GLY A 16 PRO A 17 6 0.14
CISPEP 7 GLY A 16 PRO A 17 7 -0.05
CISPEP 8 GLY A 16 PRO A 17 8 0.06
CISPEP 9 GLY A 16 PRO A 17 9 0.08
CISPEP 10 GLY A 16 PRO A 17 10 0.13
CISPEP 11 GLY A 16 PRO A 17 11 0.09
CISPEP 12 GLY A 16 PRO A 17 12 0.07
CISPEP 13 GLY A 16 PRO A 17 13 0.03
CISPEP 14 GLY A 16 PRO A 17 14 0.08
CISPEP 15 GLY A 16 PRO A 17 15 0.12
CISPEP 16 GLY A 16 PRO A 17 16 0.14
CISPEP 17 GLY A 16 PRO A 17 17 0.09
CISPEP 18 GLY A 16 PRO A 17 18 -0.01
CISPEP 19 GLY A 16 PRO A 17 19 0.05
CISPEP 20 GLY A 16 PRO A 17 20 0.10
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 9 2 Bytes