Header list of 2cqe.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 2CQE
TITLE SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN IN KIAA1064 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1064 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC-FINGER 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: C19ORF7;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041012-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CCCH ZINC-FINGER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SOMEYA,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 2CQE 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CQE 1 VERSN
REVDAT 1 19-NOV-05 2CQE 0
JRNL AUTH T.SOMEYA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN IN KIAA1064
JRNL TITL 2 PROTEIN
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 2CQE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024505.
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 : 1.34MM PROTEIN U-15N,13C; 20MM D
REMARK 210 -TRIS-HCL; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 0.05MM ZNCL2; 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 : 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 0.9295, 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 PRO A 431 80.38 -69.82
REMARK 500 1 ARG A 434 43.01 -100.15
REMARK 500 1 ALA A 448 -76.85 -81.14
REMARK 500 1 PRO A 452 1.50 -69.71
REMARK 500 1 HIS A 455 -77.87 -120.51
REMARK 500 1 TYR A 463 -25.09 -39.61
REMARK 500 1 ASP A 474 44.41 -104.18
REMARK 500 1 GLU A 484 -31.32 -39.95
REMARK 500 1 GLU A 485 -74.13 -80.01
REMARK 500 1 GLU A 505 160.18 -49.04
REMARK 500 1 LYS A 512 107.58 -169.33
REMARK 500 1 PRO A 516 -173.46 -69.69
REMARK 500 2 SER A 423 136.89 -34.88
REMARK 500 2 PRO A 431 -91.08 -69.77
REMARK 500 2 ALA A 448 -76.34 -80.18
REMARK 500 2 PRO A 452 0.26 -69.74
REMARK 500 2 HIS A 455 -75.85 -120.03
REMARK 500 2 ASP A 457 -35.53 -34.50
REMARK 500 2 THR A 466 -32.75 -132.93
REMARK 500 2 ASP A 474 46.92 -104.90
REMARK 500 2 GLU A 484 -29.44 -38.69
REMARK 500 2 GLU A 485 -75.77 -81.24
REMARK 500 2 ARG A 487 -36.50 -39.09
REMARK 500 2 LYS A 512 41.92 34.95
REMARK 500 3 SER A 423 117.65 -39.57
REMARK 500 3 ARG A 434 44.67 -105.53
REMARK 500 3 ALA A 446 -70.20 -41.56
REMARK 500 3 ALA A 448 -75.32 -79.93
REMARK 500 3 HIS A 455 -78.34 -113.17
REMARK 500 3 TYR A 463 -25.03 -39.67
REMARK 500 3 ASP A 474 42.70 -101.41
REMARK 500 3 LEU A 482 150.92 -40.98
REMARK 500 3 GLU A 485 -74.69 -80.16
REMARK 500 3 LYS A 512 43.37 -85.04
REMARK 500 3 LYS A 513 105.05 -47.22
REMARK 500 3 SER A 518 170.67 -58.46
REMARK 500 4 SER A 424 175.32 -58.28
REMARK 500 4 PRO A 431 2.57 -69.65
REMARK 500 4 ALA A 446 -75.61 -39.91
REMARK 500 4 ARG A 447 82.71 -67.69
REMARK 500 4 HIS A 455 -77.69 -122.57
REMARK 500 4 ASP A 457 -39.41 -34.73
REMARK 500 4 ASP A 474 44.47 -101.47
REMARK 500 4 GLU A 485 -77.00 -81.26
REMARK 500 4 LEU A 494 -73.87 -45.27
REMARK 500 4 ALA A 500 40.64 -84.30
REMARK 500 4 LYS A 506 148.01 -34.90
REMARK 500 4 GLU A 510 -75.50 -84.94
REMARK 500 4 PRO A 516 -179.08 -69.76
REMARK 500 5 SER A 424 110.06 -166.65
REMARK 500
REMARK 500 THIS ENTRY HAS 268 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 622 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 437 SG
REMARK 620 2 CYS A 445 SG 116.8
REMARK 620 3 CYS A 451 SG 97.8 116.5
REMARK 620 4 HIS A 455 NE2 114.8 118.4 86.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 822 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 460 SG
REMARK 620 2 CYS A 469 SG 109.7
REMARK 620 3 CYS A 475 SG 118.6 96.3
REMARK 620 4 HIS A 479 NE2 114.1 114.7 102.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 822
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101040.1 RELATED DB: TARGETDB
DBREF 2CQE A 429 513 UNP Q9UPT8 Q9UPT8_HUMAN 429 513
SEQADV 2CQE GLY A 422 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 423 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 424 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE GLY A 425 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 426 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 427 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE GLY A 428 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 514 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE GLY A 515 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE PRO A 516 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 517 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE SER A 518 UNP Q9UPT8 CLONING ARTIFACT
SEQADV 2CQE GLY A 519 UNP Q9UPT8 CLONING ARTIFACT
SEQRES 1 A 98 GLY SER SER GLY SER SER GLY GLU LEU PRO LYS LYS ARG
SEQRES 2 A 98 GLU LEU CYS LYS PHE TYR ILE THR GLY PHE CYS ALA ARG
SEQRES 3 A 98 ALA GLU ASN CYS PRO TYR MET HIS GLY ASP PHE PRO CYS
SEQRES 4 A 98 LYS LEU TYR HIS THR THR GLY ASN CYS ILE ASN GLY ASP
SEQRES 5 A 98 ASP CYS MET PHE SER HIS ASP PRO LEU THR GLU GLU THR
SEQRES 6 A 98 ARG GLU LEU LEU ASP LYS MET LEU ALA ASP ASP ALA GLU
SEQRES 7 A 98 ALA GLY ALA GLU ASP GLU LYS GLU VAL GLU GLU LEU LYS
SEQRES 8 A 98 LYS SER GLY PRO SER SER GLY
HET ZN A 622 1
HET ZN A 822 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 LYS A 461 THR A 466 1 6
HELIX 2 2 THR A 486 GLU A 499 1 14
LINK SG CYS A 437 ZN ZN A 622 1555 1555 2.37
LINK SG CYS A 445 ZN ZN A 622 1555 1555 2.33
LINK SG CYS A 451 ZN ZN A 622 1555 1555 2.34
LINK NE2 HIS A 455 ZN ZN A 622 1555 1555 2.33
LINK SG CYS A 460 ZN ZN A 822 1555 1555 2.33
LINK SG CYS A 469 ZN ZN A 822 1555 1555 2.33
LINK SG CYS A 475 ZN ZN A 822 1555 1555 2.33
LINK NE2 HIS A 479 ZN ZN A 822 1555 1555 2.33
SITE 1 AC1 4 CYS A 437 CYS A 445 CYS A 451 HIS A 455
SITE 1 AC2 4 CYS A 460 CYS A 469 CYS A 475 HIS A 479
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