Header list of 2cs3.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSLATION 20-MAY-05 2CS3 TITLE SOLUTION STRUCTURE OF THE ZF-C3HC4 DOMAIN OF HUMAN KIAA1865 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN C14ORF4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ZF-C3HC4 DOMAIN; COMPND 5 SYNONYM: MY039 PROTEIN; 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: KAZUSA CDNA FJ14303; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030609-19; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS ZF-C3HC4 DOMAIN, PROTEIN C14ORF4, MY039 PROTEIN, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 TRANSLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.INOUE,K.SAITOH,F.HAYASHI,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CS3 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2CS3 1 VERSN REVDAT 1 20-NOV-05 2CS3 0 JRNL AUTH K.INOUE,K.SAITOH,F.HAYASHI,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE ZF-C3HC4 DOMAIN OF HUMAN KIAA1865 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17 REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CS3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024560. 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 : 1.22MM U-15N, 13C-LABELED REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; REMARK 210 0.1MM ZNCL2; 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 : NMRPIPE 20031121, NMRVIEW 5.04, REMARK 210 KUJIRA 0.9296, 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, STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS 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 9 2.63 -69.76 REMARK 500 1 ASN A 12 86.80 -68.47 REMARK 500 1 GLU A 23 -64.34 -125.52 REMARK 500 1 THR A 28 -31.91 -34.65 REMARK 500 1 HIS A 29 -37.32 -33.61 REMARK 500 1 PRO A 44 19.66 -69.73 REMARK 500 1 CYS A 61 134.55 -36.39 REMARK 500 1 PRO A 62 3.38 -69.79 REMARK 500 1 ASN A 73 39.38 -98.43 REMARK 500 1 PHE A 78 140.49 -34.82 REMARK 500 1 ILE A 83 -35.83 -33.63 REMARK 500 1 SER A 92 41.64 -98.95 REMARK 500 2 SER A 3 142.51 -171.51 REMARK 500 2 GLU A 23 -75.26 -125.79 REMARK 500 2 THR A 28 -28.51 -37.60 REMARK 500 2 HIS A 29 -39.44 -39.37 REMARK 500 2 PHE A 30 150.96 -48.48 REMARK 500 2 HIS A 39 109.07 -51.46 REMARK 500 2 PRO A 44 20.11 -69.77 REMARK 500 2 CYS A 61 134.15 -34.77 REMARK 500 2 PRO A 62 4.77 -69.75 REMARK 500 2 ASN A 73 34.41 -91.42 REMARK 500 2 PHE A 78 137.58 -33.75 REMARK 500 2 ILE A 83 -37.86 -35.34 REMARK 500 3 SER A 8 145.79 -37.62 REMARK 500 3 ALA A 11 141.03 -171.22 REMARK 500 3 ASN A 12 95.73 -61.53 REMARK 500 3 LEU A 16 108.82 -44.57 REMARK 500 3 CYS A 18 155.33 -48.69 REMARK 500 3 GLU A 23 -61.04 -128.16 REMARK 500 3 THR A 28 -38.95 -29.41 REMARK 500 3 PHE A 30 151.73 -48.55 REMARK 500 3 PRO A 44 19.92 -69.81 REMARK 500 3 CYS A 61 134.87 -36.37 REMARK 500 3 PRO A 62 4.76 -69.70 REMARK 500 3 LYS A 66 47.76 33.71 REMARK 500 3 ASN A 73 32.88 -84.04 REMARK 500 3 TRP A 76 104.89 -42.26 REMARK 500 3 PHE A 78 150.62 -34.21 REMARK 500 3 GLN A 80 -36.29 -34.02 REMARK 500 3 ILE A 83 -36.08 -38.02 REMARK 500 3 PRO A 90 -172.24 -69.73 REMARK 500 4 CYS A 17 144.76 -174.80 REMARK 500 4 GLU A 23 -74.89 -129.73 REMARK 500 4 THR A 28 -30.42 -34.62 REMARK 500 4 HIS A 29 -39.08 -37.19 REMARK 500 4 PRO A 44 20.27 -69.81 REMARK 500 4 CYS A 61 134.92 -34.22 REMARK 500 4 PRO A 62 4.75 -69.70 REMARK 500 4 LEU A 69 154.24 -36.06 REMARK 500 REMARK 500 THIS ENTRY HAS 247 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 200 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 18 SG REMARK 620 2 CYS A 21 SG 109.7 REMARK 620 3 CYS A 42 SG 114.1 114.2 REMARK 620 4 CYS A 45 SG 107.9 104.9 105.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 400 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 33 SG REMARK 620 2 HIS A 39 ND1 116.8 REMARK 620 3 CYS A 61 SG 111.7 105.7 REMARK 620 4 CYS A 67 SG 111.8 107.7 101.9 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 200 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002001832 RELATED DB: TARGETDB DBREF 2CS3 A 8 87 UNP Q9H1B7 CN004_HUMAN 705 784 SEQADV 2CS3 GLY A 1 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 2 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 3 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 GLY A 4 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 5 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 6 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 GLY A 7 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 88 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 GLY A 89 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 PRO A 90 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 91 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 SER A 92 UNP Q9H1B7 CLONING ARTIFACT SEQADV 2CS3 GLY A 93 UNP Q9H1B7 CLONING ARTIFACT SEQRES 1 A 93 GLY SER SER GLY SER SER GLY SER PRO MET ALA ASN SER SEQRES 2 A 93 GLY PRO LEU CYS CYS THR ILE CYS HIS GLU ARG LEU GLU SEQRES 3 A 93 ASP THR HIS PHE VAL GLN CYS PRO SER VAL PRO SER HIS SEQRES 4 A 93 LYS PHE CYS PHE PRO CYS SER ARG GLU SER ILE LYS ALA SEQRES 5 A 93 GLN GLY ALA THR GLY GLU VAL TYR CYS PRO SER GLY GLU SEQRES 6 A 93 LYS CYS PRO LEU VAL GLY SER ASN VAL PRO TRP ALA PHE SEQRES 7 A 93 MET GLN GLY GLU ILE ALA THR ILE LEU SER GLY PRO SER SEQRES 8 A 93 SER GLY HET ZN A 200 1 HET ZN A 400 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 CYS A 42 ALA A 55 1 14 HELIX 2 2 MET A 79 SER A 88 1 10 SHEET 1 A 2 VAL A 31 GLN A 32 0 SHEET 2 A 2 LYS A 40 PHE A 41 -1 O PHE A 41 N VAL A 31 LINK SG CYS A 18 ZN ZN A 200 1555 1555 2.32 LINK SG CYS A 21 ZN ZN A 200 1555 1555 2.32 LINK SG CYS A 33 ZN ZN A 400 1555 1555 2.31 LINK ND1 HIS A 39 ZN ZN A 400 1555 1555 2.04 LINK SG CYS A 42 ZN ZN A 200 1555 1555 2.27 LINK SG CYS A 45 ZN ZN A 200 1555 1555 2.27 LINK SG CYS A 61 ZN ZN A 400 1555 1555 2.35 LINK SG CYS A 67 ZN ZN A 400 1555 1555 2.35 SITE 1 AC1 4 CYS A 18 CYS A 21 CYS A 42 CYS A 45 SITE 1 AC2 4 CYS A 33 HIS A 39 CYS A 61 CYS A 67 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 9 2 Bytes