Header list of 2cpy.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-05 2CPY
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN 3 IN RNA BINDING MOTIF
TITLE 2 PROTEIN 12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-BINDING PROTEIN 12;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: RNA BINDING MOTIF PROTEIN 12, SH3/WW DOMAIN ANCHOR PROTEIN
COMPND 6 IN THE NUCLEUS, SWAN, HRIHFB2091;
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: RBM12;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040719-13;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CPY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CPY 1 VERSN
REVDAT 1 19-NOV-05 2CPY 0
JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN 3 IN RNA BINDING
JRNL TITL 2 MOTIF PROTEIN 12
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CPY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024489.
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 : 1.48MM 13C/15N-PROTEIN, 20MM D
REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL,
REMARK 210 1MM D-DTT, 0.02% NAN3, 10% 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9297, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 ASP A 538 135.97 -34.42
REMARK 500 1 VAL A 539 103.91 -40.35
REMARK 500 1 PRO A 631 169.65 -46.47
REMARK 500 1 PRO A 632 155.36 -46.15
REMARK 500 2 SER A 530 105.32 -56.38
REMARK 500 2 ARG A 599 -29.45 -37.60
REMARK 500 2 ALA A 633 -52.62 -124.43
REMARK 500 2 GLN A 634 42.68 -95.30
REMARK 500 3 SER A 533 99.57 -59.25
REMARK 500 3 VAL A 539 39.34 -84.71
REMARK 500 3 ASN A 540 157.15 -38.03
REMARK 500 3 SER A 541 99.34 -39.18
REMARK 500 3 PRO A 568 100.15 -44.64
REMARK 500 3 PRO A 639 38.03 -78.52
REMARK 500 4 PRO A 552 107.07 -47.44
REMARK 500 4 PRO A 631 165.82 -45.30
REMARK 500 4 LYS A 636 52.99 33.62
REMARK 500 5 PRO A 568 109.16 -47.62
REMARK 500 5 GLN A 634 47.35 73.11
REMARK 500 6 SER A 530 42.51 -97.11
REMARK 500 6 PRO A 568 92.66 -45.04
REMARK 500 6 GLN A 634 98.59 -49.25
REMARK 500 6 PRO A 639 163.10 -45.30
REMARK 500 7 SER A 530 86.02 -65.38
REMARK 500 7 SER A 541 47.87 -98.84
REMARK 500 7 PRO A 568 101.91 -47.92
REMARK 500 8 SER A 533 -55.68 -131.33
REMARK 500 8 ASP A 538 123.61 -172.34
REMARK 500 8 LYS A 543 94.74 -69.93
REMARK 500 8 ASP A 623 -38.15 -39.44
REMARK 500 8 ALA A 633 92.46 -68.46
REMARK 500 8 GLN A 634 91.32 -60.12
REMARK 500 9 ASP A 538 102.77 -59.15
REMARK 500 9 SER A 541 73.67 -118.81
REMARK 500 9 PHE A 553 36.39 -83.60
REMARK 500 9 GLN A 634 170.22 -57.89
REMARK 500 9 PRO A 639 36.86 -78.75
REMARK 500 9 SER A 640 117.79 -39.05
REMARK 500 10 SER A 531 106.53 -36.06
REMARK 500 10 SER A 534 42.14 -102.29
REMARK 500 10 ASP A 538 172.01 -53.69
REMARK 500 10 SER A 541 78.41 -112.92
REMARK 500 10 ASN A 581 33.05 -97.80
REMARK 500 10 ASP A 596 -39.20 -39.95
REMARK 500 10 PRO A 639 154.29 -45.48
REMARK 500 11 SER A 534 130.76 -34.68
REMARK 500 11 LYS A 543 97.58 -66.52
REMARK 500 11 PHE A 553 31.99 -87.48
REMARK 500 11 PRO A 568 109.53 -46.41
REMARK 500 12 LEU A 585 42.38 -81.84
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100747.2 RELATED DB: TARGETDB
DBREF 2CPY A 536 636 UNP Q9NTZ6 RBM12_HUMAN 536 636
SEQADV 2CPY GLY A 529 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 530 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 531 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY GLY A 532 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 533 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 534 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY GLY A 535 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 637 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY GLY A 638 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY PRO A 639 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 640 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY SER A 641 UNP Q9NTZ6 CLONING ARTIFACT
SEQADV 2CPY GLY A 642 UNP Q9NTZ6 CLONING ARTIFACT
SEQRES 1 A 114 GLY SER SER GLY SER SER GLY GLU GLY ASP VAL ASN SER
SEQRES 2 A 114 ALA LYS VAL CYS ALA HIS ILE THR ASN ILE PRO PHE SER
SEQRES 3 A 114 ILE THR LYS MET ASP VAL LEU GLN PHE LEU GLU GLY ILE
SEQRES 4 A 114 PRO VAL ASP GLU ASN ALA VAL HIS VAL LEU VAL ASP ASN
SEQRES 5 A 114 ASN GLY GLN GLY LEU GLY GLN ALA LEU VAL GLN PHE LYS
SEQRES 6 A 114 ASN GLU ASP ASP ALA ARG LYS SER GLU ARG LEU HIS ARG
SEQRES 7 A 114 LYS LYS LEU ASN GLY ARG GLU ALA PHE VAL HIS VAL VAL
SEQRES 8 A 114 THR LEU GLU ASP MET ARG GLU ILE GLU LYS ASN PRO PRO
SEQRES 9 A 114 ALA GLN GLY LYS SER GLY PRO SER SER GLY
HELIX 1 1 THR A 556 LEU A 564 1 9
HELIX 2 2 ASN A 594 GLU A 602 1 9
HELIX 3 3 ARG A 603 HIS A 605 5 3
HELIX 4 4 THR A 620 ASN A 630 1 11
SHEET 1 A 5 VAL A 574 VAL A 576 0
SHEET 2 A 5 ALA A 588 GLN A 591 -1 O LEU A 589 N HIS A 575
SHEET 3 A 5 CYS A 545 THR A 549 -1 N ILE A 548 O ALA A 588
SHEET 4 A 5 ARG A 612 VAL A 619 -1 O HIS A 617 N HIS A 547
SHEET 5 A 5 LYS A 607 LEU A 609 -1 N LEU A 609 O ARG A 612
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