Header list of 1va1.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 07-FEB-04 1VA1
TITLE SOLUTION STRUCTURE OF TRANSCRIPTION FACTOR SP1 DNA BINDING DOMAIN
TITLE 2 (ZINC FINGER 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR SP1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER 1;
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: SP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEVSP1
KEYWDS C2H2 TYPE ZINC FINGER, TRANSCRIPTION FACTOR, DNA-BINDING PROTEIN,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 31
MDLTYP MINIMIZED AVERAGE
AUTHOR S.OKA,Y.SHIRAISHI,T.YOSHIDA,T.OHKUBO,Y.SUGIURA,Y.KOBAYASHI
REVDAT 3 02-MAR-22 1VA1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1VA1 1 VERSN
REVDAT 1 08-FEB-05 1VA1 0
JRNL AUTH S.OKA,Y.SHIRAISHI,T.YOSHIDA,T.OHKUBO,Y.SUGIURA,Y.KOBAYASHI
JRNL TITL NMR STRUCTURE OF TRANSCRIPTION FACTOR SP1 DNA BINDING DOMAIN
JRNL REF BIOCHEMISTRY V. 43 16027 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15609997
JRNL DOI 10.1021/BI048438P
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,
REMARK 3 WARREN (CNS), BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VA1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000006394.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10MM TRIS-D, 50MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM SP1 DNA-BINDING DOMAIN U
REMARK 210 -15N/13C; 10MM TRIS-D; 50MM NACL;
REMARK 210 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.4
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 31
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 CYS A 539 96.25 -66.11
REMARK 500 2 LYS A 535 158.22 60.64
REMARK 500 2 HIS A 540 30.55 -97.61
REMARK 500 2 GLN A 542 83.07 -62.58
REMARK 500 2 LYS A 546 -164.98 -100.10
REMARK 500 2 THR A 562 36.33 -97.31
REMARK 500 3 GLN A 536 -178.65 60.07
REMARK 500 3 CYS A 539 91.43 -65.31
REMARK 500 3 GLU A 564 -48.35 -146.58
REMARK 500 4 PRO A 531 98.74 -50.90
REMARK 500 4 HIS A 540 51.03 -115.96
REMARK 500 4 CYS A 544 -174.97 -68.75
REMARK 500 5 CYS A 544 -168.94 -107.79
REMARK 500 5 THR A 562 30.62 -97.78
REMARK 500 5 GLU A 564 -79.32 63.02
REMARK 500 6 LYS A 535 157.37 62.53
REMARK 500 6 GLN A 536 126.04 63.26
REMARK 500 6 HIS A 540 33.87 -96.80
REMARK 500 6 GLU A 564 -47.35 -146.24
REMARK 500 7 LYS A 535 -178.53 60.07
REMARK 500 7 CYS A 539 86.29 -59.91
REMARK 500 8 CYS A 539 97.02 -68.90
REMARK 500 9 LYS A 546 -172.42 -67.92
REMARK 500 10 LYS A 535 92.25 43.48
REMARK 500 11 LYS A 535 158.22 60.64
REMARK 500 11 HIS A 540 30.55 -97.61
REMARK 500 11 GLN A 542 83.07 -62.58
REMARK 500 11 LYS A 546 -164.98 -100.10
REMARK 500 11 THR A 562 36.33 -97.31
REMARK 500 12 GLN A 542 89.35 -58.89
REMARK 500 12 VAL A 547 87.00 57.12
REMARK 500 12 GLU A 564 32.32 -161.58
REMARK 500 13 GLN A 536 131.02 -172.91
REMARK 500 13 CYS A 539 98.49 -62.14
REMARK 500 13 CYS A 544 -165.72 -115.79
REMARK 500 13 VAL A 547 86.53 53.71
REMARK 500 14 HIS A 540 35.96 -96.65
REMARK 500 15 CYS A 539 93.15 -64.04
REMARK 500 15 CYS A 544 -168.16 -110.70
REMARK 500 15 LYS A 546 -171.45 -60.76
REMARK 500 15 THR A 562 -178.28 56.06
REMARK 500 16 ASP A 530 98.91 60.60
REMARK 500 16 CYS A 544 -165.16 -119.08
REMARK 500 17 CYS A 544 -167.03 -64.91
REMARK 500 17 VAL A 547 82.96 54.17
REMARK 500 17 GLU A 564 165.14 60.11
REMARK 500 18 PRO A 531 108.32 -51.87
REMARK 500 18 GLU A 564 -45.95 -155.83
REMARK 500 19 CYS A 544 -166.01 -64.98
REMARK 500 19 VAL A 547 99.31 57.04
REMARK 500
REMARK 500 THIS ENTRY HAS 88 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 100 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 539 SG
REMARK 620 2 CYS A 544 SG 121.8
REMARK 620 3 HIS A 557 NE2 89.5 129.2
REMARK 620 4 HIS A 561 NE2 88.9 120.9 95.9
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 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VA2 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, ZINC FINGER 2 DOMAIN
REMARK 900 RELATED ID: 1VA3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, ZINC FINGER 3 DOMAIN
DBREF 1VA1 A 530 565 UNP P08047 SP1_HUMAN 619 654
SEQADV 1VA1 MET A 1 UNP P08047 INITIATING METHIONINE
SEQRES 1 A 37 MET ASP PRO GLY LYS LYS LYS GLN HIS ILE CYS HIS ILE
SEQRES 2 A 37 GLN GLY CYS GLY LYS VAL TYR GLY LYS THR SER HIS LEU
SEQRES 3 A 37 ARG ALA HIS LEU ARG TRP HIS THR GLY GLU ARG
HET ZN A 100 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 LYS A 550 GLY A 563 1 14
SHEET 1 A 2 HIS A 537 ILE A 538 0
SHEET 2 A 2 VAL A 547 TYR A 548 -1 O TYR A 548 N HIS A 537
LINK ZN ZN A 100 SG CYS A 539 1555 1555 2.30
LINK ZN ZN A 100 SG CYS A 544 1555 1555 2.31
LINK ZN ZN A 100 NE2 HIS A 557 1555 1555 2.01
LINK ZN ZN A 100 NE2 HIS A 561 1555 1555 2.02
SITE 1 AC1 4 CYS A 539 CYS A 544 HIS A 557 HIS A 561
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