Header list of 1wjp.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 29-MAY-04 1WJP
TITLE SOLUTION STRUCTURE OF ZF-C2H2 DOMAINS FROM HUMAN ZINC FINGER PROTEIN
TITLE 2 295
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN 295;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-C2H2 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: KAZUSA CDNA FH04710;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040126-28;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZF-C2H2 DOMAIN, ZINC BINDING, NUCLEIC ACID BINDING, KIAA1227 PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WJP 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WJP 1 VERSN
REVDAT 1 29-NOV-04 1WJP 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF ZF-C2H2 DOMAINS FROM HUMAN ZINC FINGER
JRNL TITL 2 PROTEIN 295
JRNL REF TO BE PUBLISHED
JRNL REFN
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), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WJP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023649.
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 : 1.03MM ZF-C2H2 DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.01MM ZNCL2;
REMARK 210 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 0.901, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 10 -175.57 -69.82
REMARK 500 1 VAL A 11 129.22 -175.17
REMARK 500 1 ASN A 13 118.89 -167.68
REMARK 500 1 GLU A 15 118.33 -34.45
REMARK 500 1 PRO A 46 6.40 -69.74
REMARK 500 1 TYR A 47 -61.95 -102.72
REMARK 500 1 CYS A 72 82.97 -66.78
REMARK 500 1 MET A 76 52.82 35.04
REMARK 500 1 VAL A 92 -67.06 -98.29
REMARK 500 1 ASN A 97 -178.84 -49.93
REMARK 500 1 SER A 105 154.44 -40.12
REMARK 500 2 VAL A 11 134.15 -175.10
REMARK 500 2 ASN A 13 129.99 -170.02
REMARK 500 2 ASN A 23 45.81 70.63
REMARK 500 2 ALA A 42 -58.82 -29.80
REMARK 500 2 PRO A 46 5.93 -69.76
REMARK 500 2 TYR A 47 -61.01 -101.70
REMARK 500 2 CYS A 72 90.36 -65.02
REMARK 500 2 MET A 76 53.84 33.93
REMARK 500 2 VAL A 92 -66.10 -99.14
REMARK 500 2 ASN A 94 52.24 31.14
REMARK 500 2 MET A 98 106.12 -34.88
REMARK 500 2 PRO A 100 4.67 -69.73
REMARK 500 3 PRO A 46 5.73 -69.73
REMARK 500 3 CYS A 72 85.70 -66.65
REMARK 500 3 VAL A 92 -65.63 -99.12
REMARK 500 3 ASN A 96 44.93 -83.66
REMARK 500 3 MET A 98 138.01 -34.37
REMARK 500 3 PRO A 100 10.14 -69.77
REMARK 500 3 SER A 105 147.49 -34.64
REMARK 500 4 GLU A 15 113.60 -33.82
REMARK 500 4 ASN A 23 44.45 70.84
REMARK 500 4 PRO A 46 8.83 -69.84
REMARK 500 4 TYR A 47 -60.65 -109.31
REMARK 500 4 CYS A 72 85.14 -60.41
REMARK 500 4 MET A 76 55.01 38.12
REMARK 500 4 MET A 98 27.68 37.83
REMARK 500 4 ALA A 99 148.36 -34.70
REMARK 500 4 PRO A 100 96.85 -69.71
REMARK 500 5 SER A 3 -45.08 -130.82
REMARK 500 5 PRO A 46 6.52 -69.74
REMARK 500 5 TYR A 47 -60.04 -102.18
REMARK 500 5 SER A 49 41.66 74.53
REMARK 500 5 CYS A 72 80.61 -68.17
REMARK 500 5 MET A 76 54.83 32.68
REMARK 500 5 GLN A 95 -64.62 -90.12
REMARK 500 6 GLU A 15 133.37 -172.11
REMARK 500 6 ASN A 23 46.00 71.67
REMARK 500 6 CYS A 39 -9.66 -59.66
REMARK 500 6 PRO A 46 6.10 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 173 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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 19 SG
REMARK 620 2 CYS A 22 SG 112.0
REMARK 620 3 HIS A 35 NE2 99.5 92.9
REMARK 620 4 CYS A 39 SG 117.3 119.4 110.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 CYS A 48 SG 118.1
REMARK 620 3 HIS A 61 NE2 111.8 90.7
REMARK 620 4 CYS A 65 SG 118.3 118.2 90.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 72 SG
REMARK 620 2 CYS A 75 SG 107.7
REMARK 620 3 HIS A 88 NE2 116.5 90.7
REMARK 620 4 HIS A 93 NE2 111.6 116.9 112.1
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 AUTHOR 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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001201.1 RELATED DB: TARGETDB
DBREF 1WJP A 8 101 UNP Q9ULJ3 ZN295_HUMAN 713 806
SEQADV 1WJP GLY A 1 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 2 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 3 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP GLY A 4 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 5 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 6 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP GLY A 7 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 102 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP GLY A 103 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP PRO A 104 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 105 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP SER A 106 UNP Q9ULJ3 CLONING ARTIFACT
SEQADV 1WJP GLY A 107 UNP Q9ULJ3 CLONING ARTIFACT
SEQRES 1 A 107 GLY SER SER GLY SER SER GLY ALA SER PRO VAL GLU ASN
SEQRES 2 A 107 LYS GLU VAL TYR GLN CYS ARG LEU CYS ASN ALA LYS LEU
SEQRES 3 A 107 SER SER LEU LEU GLU GLN GLY SER HIS GLU ARG LEU CYS
SEQRES 4 A 107 ARG ASN ALA ALA VAL CYS PRO TYR CYS SER LEU ARG PHE
SEQRES 5 A 107 PHE SER PRO GLU LEU LYS GLN GLU HIS GLU SER LYS CYS
SEQRES 6 A 107 GLU TYR LYS LYS LEU THR CYS LEU GLU CYS MET ARG THR
SEQRES 7 A 107 PHE LYS SER SER PHE SER ILE TRP ARG HIS GLN VAL GLU
SEQRES 8 A 107 VAL HIS ASN GLN ASN ASN MET ALA PRO THR SER GLY PRO
SEQRES 9 A 107 SER SER GLY
HET ZN A 301 1
HET ZN A 501 1
HET ZN A 701 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
HELIX 1 1 SER A 28 ALA A 42 1 15
HELIX 2 2 SER A 54 CYS A 65 1 12
HELIX 3 3 TYR A 67 LYS A 69 5 3
HELIX 4 4 SER A 81 VAL A 92 1 12
SHEET 1 A 2 THR A 71 CYS A 72 0
SHEET 2 A 2 ARG A 77 THR A 78 -1 O ARG A 77 N CYS A 72
LINK SG CYS A 19 ZN ZN A 301 1555 1555 2.36
LINK SG CYS A 22 ZN ZN A 301 1555 1555 2.32
LINK NE2 HIS A 35 ZN ZN A 301 1555 1555 2.37
LINK SG CYS A 39 ZN ZN A 301 1555 1555 2.32
LINK SG CYS A 45 ZN ZN A 501 1555 1555 2.33
LINK SG CYS A 48 ZN ZN A 501 1555 1555 2.33
LINK NE2 HIS A 61 ZN ZN A 501 1555 1555 2.37
LINK SG CYS A 65 ZN ZN A 501 1555 1555 2.33
LINK SG CYS A 72 ZN ZN A 701 1555 1555 2.35
LINK SG CYS A 75 ZN ZN A 701 1555 1555 2.34
LINK NE2 HIS A 88 ZN ZN A 701 1555 1555 2.33
LINK NE2 HIS A 93 ZN ZN A 701 1555 1555 2.34
SITE 1 AC1 4 CYS A 19 CYS A 22 HIS A 35 CYS A 39
SITE 1 AC2 5 CYS A 45 TYR A 47 CYS A 48 HIS A 61
SITE 2 AC2 5 CYS A 65
SITE 1 AC3 4 CYS A 72 CYS A 75 HIS A 88 HIS A 93
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