Header list of 1wfz.pdb file
Complete list - r 2 2 Bytes
HEADER METAL TRANSPORT 27-MAY-04 1WFZ
TITLE SOLUTION STRUCTURE OF IRON-SULFUR CLUSTER PROTEIN U (ISCU)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITROGEN FIXATION CLUSTER-LIKE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ISCU;
COMPND 5 SYNONYM: IRON-SULFUR CLUSTER PROTEIN U;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 2300003J05;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020826-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS IRON-SULFUR CLUSTER BIOSYNTHESIS, THREE CONSERVED CYS, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAKANISHI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WFZ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WFZ 1 VERSN
REVDAT 1 27-NOV-04 1WFZ 0
JRNL AUTH T.NAKANISHI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF IRON-SULFUR CLUSTER PROTEIN U (ISCU)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023538.
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 : 1.12MM ISCU DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL;
REMARK 210 10MM D-DTT; 0.02% NAN3; 0.01MM
REMARK 210 ZNCL2; 90% H2O, 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 : XWINNMR 2.6, NMRPIPE 20030801,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.870,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : NULL
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, 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 SER A 3 95.92 -69.15
REMARK 500 1 GLU A 8 38.16 37.63
REMARK 500 1 ASN A 9 140.25 -34.44
REMARK 500 1 PRO A 10 -164.45 -69.70
REMARK 500 1 ASP A 17 101.25 -54.25
REMARK 500 1 SER A 61 -33.84 -34.95
REMARK 500 1 HIS A 101 -37.24 -38.91
REMARK 500 1 ALA A 113 -71.24 -60.34
REMARK 500 2 SER A 2 41.77 -95.07
REMARK 500 2 GLU A 8 101.35 -42.84
REMARK 500 2 PRO A 10 -179.76 -69.70
REMARK 500 2 ASN A 12 78.11 -62.55
REMARK 500 2 CYS A 59 177.18 -59.90
REMARK 500 2 SER A 61 -34.10 -34.82
REMARK 500 2 HIS A 101 -37.39 -37.77
REMARK 500 2 ALA A 113 -70.44 -53.19
REMARK 500 2 ALA A 115 -70.32 -45.80
REMARK 500 2 SER A 123 -175.05 -174.26
REMARK 500 2 PRO A 127 -173.10 -69.75
REMARK 500 3 VAL A 13 112.36 -38.74
REMARK 500 3 SER A 15 118.64 -169.67
REMARK 500 3 SER A 61 -30.16 -36.98
REMARK 500 3 SER A 65 -37.00 -39.79
REMARK 500 3 SER A 129 81.32 -65.89
REMARK 500 4 ARG A 11 -68.39 -95.16
REMARK 500 4 SER A 61 -33.81 -35.19
REMARK 500 4 ALA A 90 -37.78 -36.04
REMARK 500 4 HIS A 101 -31.87 -38.11
REMARK 500 4 LYS A 124 -43.75 -132.60
REMARK 500 5 PRO A 10 -168.70 -69.74
REMARK 500 5 SER A 15 118.12 -32.20
REMARK 500 5 ASP A 17 101.21 -55.11
REMARK 500 5 SER A 61 -37.75 -35.05
REMARK 500 5 ALA A 90 -37.38 -38.15
REMARK 500 5 SER A 125 100.91 -39.48
REMARK 500 6 SER A 5 127.47 -170.43
REMARK 500 6 SER A 15 140.55 -172.06
REMARK 500 6 SER A 61 -34.07 -35.22
REMARK 500 6 SER A 65 -32.43 -38.59
REMARK 500 6 SER A 67 -29.17 -39.60
REMARK 500 6 HIS A 101 -36.72 -37.84
REMARK 500 6 ALA A 113 -72.01 -58.37
REMARK 500 6 LYS A 124 45.30 -85.18
REMARK 500 6 PRO A 127 86.46 -69.76
REMARK 500 7 PRO A 10 -175.04 -69.71
REMARK 500 7 ASN A 12 89.78 -66.16
REMARK 500 7 SER A 61 -32.49 -34.90
REMARK 500 7 ALA A 64 -70.15 -65.70
REMARK 500 7 HIS A 101 -27.24 -38.44
REMARK 500 7 ALA A 113 -74.53 -58.68
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 33 SG
REMARK 620 2 ASP A 35 OD2 102.8
REMARK 620 3 CYS A 59 SG 117.3 110.0
REMARK 620 4 HIS A 101 NE2 101.9 113.0 111.5
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMK001001342.1 RELATED DB: TARGETDB
DBREF 1WFZ A 8 124 UNP Q9D7P6 NIFUN_MOUSE 45 161
SEQADV 1WFZ GLY A 1 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 2 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 3 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ GLY A 4 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 5 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 6 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ GLY A 7 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 125 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ GLY A 126 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ PRO A 127 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 128 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ SER A 129 UNP Q9D7P6 CLONING ARTIFACT
SEQADV 1WFZ GLY A 130 UNP Q9D7P6 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY GLU ASN PRO ARG ASN VAL
SEQRES 2 A 130 GLY SER LEU ASP LYS THR SER LYS ASN VAL GLY THR GLY
SEQRES 3 A 130 LEU VAL GLY ALA PRO ALA CYS GLY ASP VAL MET LYS LEU
SEQRES 4 A 130 GLN ILE GLN VAL ASP GLU LYS GLY LYS ILE VAL ASP ALA
SEQRES 5 A 130 ARG PHE LYS THR PHE GLY CYS GLY SER ALA ILE ALA SER
SEQRES 6 A 130 SER SER LEU ALA THR GLU TRP VAL LYS GLY LYS THR VAL
SEQRES 7 A 130 GLU GLU ALA LEU THR ILE LYS ASN THR ASP ILE ALA LYS
SEQRES 8 A 130 GLU LEU CYS LEU PRO PRO VAL LYS LEU HIS CYS SER MET
SEQRES 9 A 130 LEU ALA GLU ASP ALA ILE LYS ALA ALA LEU ALA ASP TYR
SEQRES 10 A 130 LYS LEU LYS GLN GLU SER LYS SER GLY PRO SER SER GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLY A 60 VAL A 73 1 14
HELIX 2 2 VAL A 78 ALA A 81 1 4
HELIX 3 3 ASN A 86 GLU A 92 1 7
HELIX 4 4 CYS A 102 GLN A 121 5 20
SHEET 1 A 3 VAL A 23 ALA A 30 0
SHEET 2 A 3 ASP A 35 VAL A 43 -1 O LEU A 39 N GLY A 26
SHEET 3 A 3 ILE A 49 PHE A 57 -1 O LYS A 55 N LYS A 38
LINK SG CYS A 33 ZN ZN A 201 1555 1555 2.33
LINK OD2 ASP A 35 ZN ZN A 201 1555 1555 2.07
LINK SG CYS A 59 ZN ZN A 201 1555 1555 2.28
LINK NE2 HIS A 101 ZN ZN A 201 1555 1555 2.09
SITE 1 AC1 5 CYS A 33 ASP A 35 CYS A 59 HIS A 101
SITE 2 AC1 5 CYS A 102
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