Header list of 1wil.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WIL TITLE SOLUTION STRUCTURE OF THE RING FINGER DOMAIN OF THE HUMAN KIAA1045 TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: KIAA1045 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RING FINGER 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 HH00656; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030609-29; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RING FINGER DOMAIN, KIAA1045 PROTEIN, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.MIYAMOTO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WIL 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1WIL 1 VERSN REVDAT 1 28-NOV-04 1WIL 0 JRNL AUTH K.MIYAMOTO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RING FINGER DOMAIN OF THE HUMAN JRNL TITL 2 KIAA1045 PROTEIN 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 1WIL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023620. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4MM RING FINGER DOMAIN U REMARK 210 -13C,15N; 20MM D-TRIS-HCL(PH7.0); REMARK 210 100MM NACL; 1MM D-DTT; 0.02% REMARK 210 NAN3; 0.1MM ZNCL2; 1O% 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 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.8996, 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 8 0.55 -69.71 REMARK 500 1 GLU A 16 54.22 -93.26 REMARK 500 1 CYS A 18 140.30 -34.49 REMARK 500 1 GLU A 27 176.43 -53.93 REMARK 500 1 CYS A 35 94.94 -46.19 REMARK 500 1 ARG A 46 -71.22 -63.75 REMARK 500 1 ILE A 50 -70.27 -100.35 REMARK 500 1 GLN A 51 43.07 38.95 REMARK 500 1 ASP A 53 90.27 -69.90 REMARK 500 1 GLU A 57 39.28 -94.44 REMARK 500 1 THR A 59 -73.28 -87.33 REMARK 500 1 THR A 64 150.64 -43.10 REMARK 500 1 CYS A 70 173.62 -50.78 REMARK 500 1 ILE A 76 40.64 -92.75 REMARK 500 1 LEU A 78 138.35 -37.58 REMARK 500 1 GLU A 83 113.48 -36.43 REMARK 500 2 VAL A 12 137.04 -173.92 REMARK 500 2 CYS A 35 32.56 -91.74 REMARK 500 2 THR A 36 36.33 34.01 REMARK 500 2 ARG A 37 136.02 -175.26 REMARK 500 2 HIS A 40 114.20 -39.30 REMARK 500 2 THR A 81 130.51 -36.44 REMARK 500 2 SER A 84 134.84 -36.82 REMARK 500 2 PRO A 86 85.56 -69.74 REMARK 500 2 SER A 88 117.30 -35.62 REMARK 500 3 PRO A 8 6.66 -69.76 REMARK 500 3 ARG A 9 93.85 -52.52 REMARK 500 3 GLU A 10 138.74 -173.29 REMARK 500 3 VAL A 12 140.85 -175.09 REMARK 500 3 HIS A 40 106.79 -59.76 REMARK 500 3 ASP A 41 -36.94 -38.88 REMARK 500 3 ALA A 62 -61.25 -107.48 REMARK 500 3 THR A 66 43.47 35.71 REMARK 500 3 ASP A 74 103.50 -57.26 REMARK 500 3 SER A 84 141.19 -37.88 REMARK 500 4 SER A 2 104.88 -49.17 REMARK 500 4 PRO A 8 6.97 -69.68 REMARK 500 4 GLU A 10 51.55 36.09 REMARK 500 4 VAL A 13 143.32 -34.23 REMARK 500 4 ASP A 15 -58.94 -126.91 REMARK 500 4 THR A 36 37.60 -81.95 REMARK 500 4 ARG A 37 111.83 -173.70 REMARK 500 4 TYR A 49 -70.31 -123.27 REMARK 500 4 SER A 54 -60.60 -96.13 REMARK 500 4 THR A 59 160.18 -39.52 REMARK 500 4 CYS A 70 -179.09 -50.81 REMARK 500 4 ASP A 74 37.15 -90.87 REMARK 500 4 ILE A 76 66.55 -110.76 REMARK 500 4 THR A 81 -39.26 -130.15 REMARK 500 4 PRO A 86 -173.42 -69.76 REMARK 500 REMARK 500 THIS ENTRY HAS 230 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 18 SG REMARK 620 2 CYS A 21 SG 118.2 REMARK 620 3 HIS A 40 ND1 111.6 99.6 REMARK 620 4 CYS A 43 SG 118.3 86.9 118.4 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 32 SG REMARK 620 2 CYS A 35 SG 115.2 REMARK 620 3 CYS A 70 SG 115.1 91.9 REMARK 620 4 CYS A 73 SG 128.8 110.5 84.6 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: HSK002001021.1 RELATED DB: TARGETDB DBREF 1WIL A 8 83 UNP Q9UPV7 K1045_HUMAN 150 225 SEQADV 1WIL GLY A 1 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 2 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 3 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL GLY A 4 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 5 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 6 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL GLY A 7 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 84 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL GLY A 85 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL PRO A 86 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 87 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL SER A 88 UNP Q9UPV7 CLONING ARTIFACT SEQADV 1WIL GLY A 89 UNP Q9UPV7 CLONING ARTIFACT SEQRES 1 A 89 GLY SER SER GLY SER SER GLY PRO ARG GLU PRO VAL VAL SEQRES 2 A 89 ASN ASP GLU MET CYS ASP VAL CYS GLU VAL TRP THR ALA SEQRES 3 A 89 GLU SER LEU PHE PRO CYS ARG VAL CYS THR ARG VAL PHE SEQRES 4 A 89 HIS ASP GLY CYS LEU ARG ARG MET GLY TYR ILE GLN GLY SEQRES 5 A 89 ASP SER ALA ALA GLU VAL THR GLU MET ALA HIS THR GLU SEQRES 6 A 89 THR GLY TRP SER CYS HIS TYR CYS ASP ASN ILE ASN LEU SEQRES 7 A 89 LEU LEU THR GLU GLU 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 ASP A 41 MET A 47 1 7 LINK SG CYS A 18 ZN ZN A 201 1555 1555 2.33 LINK SG CYS A 21 ZN ZN A 201 1555 1555 2.33 LINK SG CYS A 32 ZN ZN A 401 1555 1555 2.34 LINK SG CYS A 35 ZN ZN A 401 1555 1555 2.33 LINK ND1 HIS A 40 ZN ZN A 201 1555 1555 2.33 LINK SG CYS A 43 ZN ZN A 201 1555 1555 2.33 LINK SG CYS A 70 ZN ZN A 401 1555 1555 2.36 LINK SG CYS A 73 ZN ZN A 401 1555 1555 2.37 CISPEP 1 PHE A 30 PRO A 31 1 -0.01 CISPEP 2 PHE A 30 PRO A 31 2 -0.04 CISPEP 3 PHE A 30 PRO A 31 3 -0.07 CISPEP 4 PHE A 30 PRO A 31 4 0.11 CISPEP 5 PHE A 30 PRO A 31 5 -0.05 CISPEP 6 PHE A 30 PRO A 31 6 0.02 CISPEP 7 PHE A 30 PRO A 31 7 0.09 CISPEP 8 PHE A 30 PRO A 31 8 -0.04 CISPEP 9 PHE A 30 PRO A 31 9 0.03 CISPEP 10 PHE A 30 PRO A 31 10 0.01 CISPEP 11 PHE A 30 PRO A 31 11 0.02 CISPEP 12 PHE A 30 PRO A 31 12 0.03 CISPEP 13 PHE A 30 PRO A 31 13 0.04 CISPEP 14 PHE A 30 PRO A 31 14 -0.05 CISPEP 15 PHE A 30 PRO A 31 15 -0.03 CISPEP 16 PHE A 30 PRO A 31 16 0.07 CISPEP 17 PHE A 30 PRO A 31 17 0.09 CISPEP 18 PHE A 30 PRO A 31 18 0.07 CISPEP 19 PHE A 30 PRO A 31 19 -0.11 CISPEP 20 PHE A 30 PRO A 31 20 0.05 SITE 1 AC1 4 CYS A 18 CYS A 21 HIS A 40 CYS A 43 SITE 1 AC2 4 CYS A 32 CYS A 35 CYS A 70 CYS A 73 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