Header list of 1wff.pdb file
Complete list - v 10 2 Bytes
HEADER METAL BINDING PROTEIN 26-MAY-04 1WFF
TITLE SOLUTION STRUCTURE OF THE ZF-AN1 DOMAIN FROM MOUSE RIKEN CDNA
TITLE 2 2810002D23 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIKEN CDNA 2810002D23 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-AN1 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 1700043I15;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030324-18;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZF-AN1 DOMAIN, ZINC BINDING, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,K.IZUMI,M.YOSHIDA,T.YAMAZAKI,M.INOUE,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 10-NOV-21 1WFF 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WFF 1 VERSN
REVDAT 1 26-NOV-04 1WFF 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,K.IZUMI,M.YOSHIDA,T.YAMAZAKI,M.INOUE,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE ZF-AN1 DOMAIN FROM MOUSE RIKEN
JRNL TITL 2 CDNA 2810002D23 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DELTA 4.2, CYANA 2.0.17
REMARK 3 AUTHORS : JEOL (DELTA), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023518.
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 : 1.18MM ZF-AN1 DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.1MM 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 : ECA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
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 RESTRAINTED MOLECULAR 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 LYS A 15 144.51 -175.13
REMARK 500 1 PRO A 17 87.85 -69.74
REMARK 500 1 LYS A 22 118.30 -170.05
REMARK 500 1 HIS A 27 134.42 -171.92
REMARK 500 1 CYS A 28 140.76 -32.88
REMARK 500 1 THR A 35 -43.44 -133.25
REMARK 500 1 THR A 39 54.60 71.88
REMARK 500 1 CYS A 61 151.74 -40.15
REMARK 500 1 TYR A 63 132.07 -38.36
REMARK 500 1 TYR A 65 41.04 -106.38
REMARK 500 1 ARG A 71 -57.80 -131.99
REMARK 500 1 ASN A 77 155.59 -44.57
REMARK 500 2 SER A 6 148.79 -171.37
REMARK 500 2 HIS A 9 128.33 -173.32
REMARK 500 2 LYS A 15 108.21 -171.48
REMARK 500 2 ILE A 24 126.09 -33.95
REMARK 500 2 CYS A 28 150.56 -38.60
REMARK 500 2 THR A 39 -36.50 -35.15
REMARK 500 2 CYS A 61 153.99 -45.37
REMARK 500 2 TYR A 63 153.80 -40.16
REMARK 500 2 SER A 67 48.60 -86.18
REMARK 500 2 ALA A 68 117.87 -167.42
REMARK 500 2 GLU A 75 54.68 32.34
REMARK 500 2 ASN A 77 135.10 -173.42
REMARK 500 2 PRO A 78 99.81 -69.71
REMARK 500 2 PRO A 82 91.59 -69.76
REMARK 500 2 SER A 84 108.48 -161.86
REMARK 500 3 LEU A 11 135.28 -171.23
REMARK 500 3 GLN A 19 42.37 -104.52
REMARK 500 3 LYS A 21 -75.16 -102.13
REMARK 500 3 CYS A 28 151.89 -34.60
REMARK 500 3 CYS A 61 151.29 -36.02
REMARK 500 3 ASP A 64 86.27 -67.72
REMARK 500 3 LYS A 66 175.28 -48.13
REMARK 500 3 LEU A 73 178.81 -54.47
REMARK 500 3 PRO A 78 -177.71 -69.82
REMARK 500 4 ILE A 24 142.24 -38.34
REMARK 500 4 CYS A 28 150.19 -39.25
REMARK 500 4 TYR A 65 107.18 -37.43
REMARK 500 4 ALA A 68 -52.96 -127.67
REMARK 500 4 TYR A 72 141.68 -39.37
REMARK 500 4 PRO A 78 -179.67 -69.75
REMARK 500 5 ILE A 24 126.89 -38.90
REMARK 500 5 HIS A 27 140.00 -171.80
REMARK 500 5 CYS A 28 145.76 -37.24
REMARK 500 5 TYR A 72 150.23 -39.14
REMARK 500 5 PRO A 82 -174.42 -69.84
REMARK 500 6 SER A 5 143.90 -174.16
REMARK 500 6 HIS A 10 138.50 -172.30
REMARK 500 6 CYS A 28 154.24 -38.88
REMARK 500
REMARK 500 THIS ENTRY HAS 191 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 28 SG
REMARK 620 2 CYS A 31 SG 102.8
REMARK 620 3 CYS A 50 SG 115.1 116.7
REMARK 620 4 HIS A 53 ND1 117.2 112.2 93.5
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 43 SG
REMARK 620 2 CYS A 45 SG 112.7
REMARK 620 3 HIS A 59 NE2 90.9 118.1
REMARK 620 4 CYS A 61 SG 94.7 117.6 116.1
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 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: MMT007011622.1 RELATED DB: TARGETDB
DBREF 1WFF A 8 79 GB 38085001 XP_132758 735 806
SEQADV 1WFF GLY A 1 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 2 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 3 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF GLY A 4 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 5 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 6 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF GLY A 7 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF ASN A 62 GB 38085001 THR 789 ENGINEERED MUTATION
SEQADV 1WFF SER A 80 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF GLY A 81 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF PRO A 82 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 83 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF SER A 84 GB 38085001 CLONING ARTIFACT
SEQADV 1WFF GLY A 85 GB 38085001 CLONING ARTIFACT
SEQRES 1 A 85 GLY SER SER GLY SER SER GLY ILE HIS HIS LEU PRO PRO
SEQRES 2 A 85 VAL LYS ALA PRO LEU GLN THR LYS LYS LYS ILE MET LYS
SEQRES 3 A 85 HIS CYS PHE LEU CYS GLY LYS LYS THR GLY LEU ALA THR
SEQRES 4 A 85 SER PHE GLU CYS ARG CYS GLY ASN ASN PHE CYS ALA SER
SEQRES 5 A 85 HIS ARG TYR ALA GLU ALA HIS GLY CYS ASN TYR ASP TYR
SEQRES 6 A 85 LYS SER ALA GLY ARG ARG TYR LEU GLU GLU ALA ASN PRO
SEQRES 7 A 85 VAL 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 ALA A 56 GLY A 60 5 5
SHEET 1 A 2 PHE A 41 GLU A 42 0
SHEET 2 A 2 ASN A 48 PHE A 49 -1 O PHE A 49 N PHE A 41
LINK SG CYS A 28 ZN ZN A 201 1555 1555 2.36
LINK SG CYS A 31 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 43 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 45 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 50 ZN ZN A 201 1555 1555 2.33
LINK ND1 HIS A 53 ZN ZN A 201 1555 1555 2.33
LINK NE2 HIS A 59 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 61 ZN ZN A 401 1555 1555 2.34
SITE 1 AC1 4 CYS A 28 CYS A 31 CYS A 50 HIS A 53
SITE 1 AC2 4 CYS A 43 CYS A 45 HIS A 59 CYS A 61
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 - v 10 2 Bytes