Header list of 1x4s.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 14-MAY-05 1X4S
TITLE SOLUTION STRUCTURE OF ZINC FINGER HIT DOMAIN IN PROTEIN FON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER HIT DOMAIN CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER HIT DOMAIN;
COMPND 5 SYNONYM: PROTEIN FON;
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: ZNHIT2, C11ORF5;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040906-13;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ZINC FINGER HIT DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1X4S 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1X4S 1 VERSN
REVDAT 2 01-JAN-08 1X4S 1 JRNL
REVDAT 1 14-NOV-05 1X4S 0
JRNL AUTH F.HE,T.UMEHARA,K.TSUDA,M.INOUE,T.KIGAWA,T.MATSUDA,T.YABUKI,
JRNL AUTH 2 M.AOKI,E.SEKI,T.TERADA,M.SHIROUZU,A.TANAKA,S.SUGANO,Y.MUTO,
JRNL AUTH 3 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE ZINC FINGER HIT DOMAIN IN PROTEIN
JRNL TITL 2 FON
JRNL REF PROTEIN SCI. V. 16 1577 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17656577
JRNL DOI 10.1110/PS.062635107
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X4S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024378.
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 : 0.8MM U-15, 13C; 20MM D-TRIS
REMARK 210 -HCL(PH 7.0); 100MM NACL; 100UM
REMARK 210 ZNCL2; 1MM D-DTT; 0.02% NAN3
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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.863, 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
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 5 159.35 -39.27
REMARK 500 1 CYS A 14 108.28 -48.62
REMARK 500 1 ALA A 19 126.00 -33.33
REMARK 500 1 GLU A 21 46.38 -83.17
REMARK 500 1 PRO A 24 98.61 -69.73
REMARK 500 1 ALA A 25 89.47 -63.01
REMARK 500 1 PRO A 30 4.12 -69.74
REMARK 500 1 ASN A 33 54.98 35.75
REMARK 500 1 THR A 47 39.10 -98.31
REMARK 500 1 ASN A 51 53.62 -97.16
REMARK 500 1 PHE A 52 -54.33 -134.27
REMARK 500 1 PRO A 56 0.85 -69.76
REMARK 500 1 SER A 58 146.88 -37.90
REMARK 500 2 CYS A 14 99.08 -42.23
REMARK 500 2 PHE A 16 -34.24 -133.38
REMARK 500 2 ALA A 19 115.01 -34.03
REMARK 500 2 GLU A 21 43.24 -93.65
REMARK 500 2 PRO A 30 5.48 -69.80
REMARK 500 2 ASN A 33 54.62 32.67
REMARK 500 2 CYS A 48 36.86 -83.30
REMARK 500 2 GLU A 50 -39.06 -34.11
REMARK 500 3 CYS A 14 104.30 -36.49
REMARK 500 3 ALA A 19 134.20 -30.17
REMARK 500 3 GLU A 21 40.22 -86.86
REMARK 500 3 ALA A 25 87.94 -67.86
REMARK 500 3 PRO A 30 6.94 -69.76
REMARK 500 3 ASN A 33 54.94 33.95
REMARK 500 3 THR A 47 40.62 -100.33
REMARK 500 3 PRO A 56 2.85 -69.79
REMARK 500 4 ALA A 11 -177.69 -67.37
REMARK 500 4 CYS A 14 97.24 -41.73
REMARK 500 4 ALA A 19 125.64 -33.59
REMARK 500 4 GLU A 21 41.00 -91.61
REMARK 500 4 PRO A 30 7.47 -69.79
REMARK 500 4 ASN A 33 54.98 31.91
REMARK 500 4 ALA A 49 35.23 -83.27
REMARK 500 4 PHE A 52 104.05 -53.45
REMARK 500 5 MET A 8 41.93 -102.36
REMARK 500 5 PRO A 10 83.38 -69.82
REMARK 500 5 ALA A 11 136.09 -174.79
REMARK 500 5 CYS A 14 102.33 -49.76
REMARK 500 5 PHE A 16 -37.70 -39.70
REMARK 500 5 VAL A 22 120.17 -37.52
REMARK 500 5 PRO A 24 91.03 -69.78
REMARK 500 5 ALA A 25 94.62 -60.87
REMARK 500 5 PRO A 30 5.98 -69.73
REMARK 500 5 ASN A 33 55.00 31.21
REMARK 500 5 THR A 47 41.28 -102.85
REMARK 500 5 ASN A 51 37.78 -93.62
REMARK 500 5 PRO A 56 2.25 -69.76
REMARK 500
REMARK 500 THIS ENTRY HAS 180 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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 114.7
REMARK 620 3 CYS A 37 SG 113.7 106.0
REMARK 620 4 CYS A 41 SG 105.6 105.9 110.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 29 SG
REMARK 620 2 CYS A 32 SG 101.7
REMARK 620 3 HIS A 45 NE2 105.5 106.0
REMARK 620 4 CYS A 48 SG 113.0 112.3 116.9
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001004088.1 RELATED DB: TARGETDB
DBREF 1X4S A 8 53 UNP Q9UHR6 ZNHI2_HUMAN 1 46
SEQADV 1X4S GLY A 1 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 2 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 3 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S GLY A 4 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 5 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 6 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S GLY A 7 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 54 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S GLY A 55 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S PRO A 56 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 57 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S SER A 58 UNP Q9UHR6 EXPRESSION TAG
SEQADV 1X4S GLY A 59 UNP Q9UHR6 EXPRESSION TAG
SEQRES 1 A 59 GLY SER SER GLY SER SER GLY MET GLU PRO ALA GLY PRO
SEQRES 2 A 59 CYS GLY PHE CYS PRO ALA GLY GLU VAL GLN PRO ALA ARG
SEQRES 3 A 59 TYR THR CYS PRO ARG CYS ASN ALA PRO TYR CYS SER LEU
SEQRES 4 A 59 ARG CYS TYR ARG THR HIS GLY THR CYS ALA GLU ASN PHE
SEQRES 5 A 59 TYR SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 LEU A 39 THR A 44 1 6
HELIX 2 2 ALA A 49 ASN A 51 5 3
SHEET 1 A 2 GLY A 12 PRO A 13 0
SHEET 2 A 2 PRO A 24 ALA A 25 -1
SHEET 1 B 2 TYR A 27 THR A 28 0
SHEET 2 B 2 PRO A 35 TYR A 36 -1
LINK SG CYS A 14 ZN ZN A 201 1555 1555 2.25
LINK SG CYS A 17 ZN ZN A 201 1555 1555 2.26
LINK SG CYS A 29 ZN ZN A 401 1555 1555 2.36
LINK SG CYS A 32 ZN ZN A 401 1555 1555 2.35
LINK SG CYS A 37 ZN ZN A 201 1555 1555 2.32
LINK SG CYS A 41 ZN ZN A 201 1555 1555 2.35
LINK NE2 HIS A 45 ZN ZN A 401 1555 1555 2.03
LINK SG CYS A 48 ZN ZN A 401 1555 1555 2.26
SITE 1 AC1 4 CYS A 14 CYS A 17 CYS A 37 CYS A 41
SITE 1 AC2 4 CYS A 29 CYS A 32 HIS A 45 CYS A 48
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