Header list of 2csh.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 21-MAY-05 2CSH TITLE SOLUTION STRUCTURE OF TANDEM REPEAT OF THE ZF-C2H2 DOMAINS OF HUMAN TITLE 2 ZINC FINGER PROTEIN 297B COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZINC FINGER PROTEIN 297B; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ZF-C2H2 DOMAIN; COMPND 5 SYNONYM: ZNF-X, ZINC FINGER AND BTB DOMAIN CONTAINING PROTEIN 22B; 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 HH00161; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021021-05; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS ZF-C2H2 DOMAIN, ZINC FINGER PROTEIN 297B, ZINC FINGER AND BTB DOMAIN KEYWDS 2 CONTAINING PROTEIN 22B, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION 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 2CSH 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2CSH 1 VERSN REVDAT 1 21-NOV-05 2CSH 0 JRNL AUTH K.INOUE,K.SAITOH,F.HAYASHI,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF TANDEM REPEAT OF THE ZF-C2H2 DOMAINS JRNL TITL 2 OF HUMAN ZINC FINGER PROTEIN 297B 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 2CSH 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_1000024573. 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 U-15N, 13C-LABELED REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM REMARK 210 NACL; 0.02% NAN3; 0.1MM ZNCL2; REMARK 210 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 5.0.4, 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 LEU A 33 166.31 -44.56 REMARK 500 1 THR A 61 149.95 -36.71 REMARK 500 1 ALA A 97 39.23 37.85 REMARK 500 1 ALA A 104 161.22 -41.05 REMARK 500 2 THR A 61 134.30 -36.08 REMARK 500 2 ILE A 63 132.05 -35.45 REMARK 500 2 LYS A 96 152.83 -40.44 REMARK 500 2 GLU A 98 53.43 30.30 REMARK 500 2 GLN A 99 54.62 35.97 REMARK 500 2 THR A 102 46.65 -82.84 REMARK 500 2 SER A 105 141.62 -172.47 REMARK 500 2 PRO A 107 -177.66 -69.76 REMARK 500 3 SER A 5 128.17 -174.66 REMARK 500 3 ASP A 8 136.27 -38.97 REMARK 500 3 LEU A 35 77.85 -119.75 REMARK 500 3 PRO A 65 2.51 -69.76 REMARK 500 3 CYS A 68 173.31 -58.35 REMARK 500 3 CYS A 88 -35.15 -38.59 REMARK 500 3 ALA A 97 47.55 -85.72 REMARK 500 3 ASN A 100 98.53 -38.87 REMARK 500 3 GLU A 103 146.93 -35.65 REMARK 500 3 PRO A 107 -173.23 -69.75 REMARK 500 4 SER A 2 115.80 -169.21 REMARK 500 4 SER A 3 140.78 -170.40 REMARK 500 4 SER A 6 -42.56 -131.18 REMARK 500 4 GLU A 67 141.24 -172.00 REMARK 500 4 PHE A 81 -71.10 -61.84 REMARK 500 4 SER A 87 30.13 -86.27 REMARK 500 4 LYS A 96 164.11 -42.47 REMARK 500 4 THR A 101 140.47 -34.28 REMARK 500 4 THR A 102 102.83 -35.79 REMARK 500 5 SER A 2 146.51 -174.87 REMARK 500 5 LEU A 33 176.37 -49.03 REMARK 500 5 THR A 61 -176.90 -56.68 REMARK 500 5 LYS A 96 166.44 -47.73 REMARK 500 5 THR A 102 85.97 -59.29 REMARK 500 5 PRO A 107 7.90 -69.78 REMARK 500 5 SER A 108 131.72 -28.35 REMARK 500 6 SER A 2 141.21 -174.78 REMARK 500 6 ASP A 8 126.18 -170.56 REMARK 500 6 LEU A 33 170.30 -45.33 REMARK 500 6 THR A 61 121.90 -39.66 REMARK 500 6 CYS A 68 171.04 -53.36 REMARK 500 6 LYS A 90 -38.43 -34.40 REMARK 500 6 GLN A 99 42.31 -104.95 REMARK 500 7 LYS A 17 174.96 -59.01 REMARK 500 7 LEU A 33 45.61 -89.47 REMARK 500 7 LEU A 35 45.27 -97.15 REMARK 500 7 THR A 61 151.33 -40.46 REMARK 500 7 LYS A 64 70.71 -113.38 REMARK 500 REMARK 500 THIS ENTRY HAS 122 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 13 SG REMARK 620 2 CYS A 15 SG 110.5 REMARK 620 3 HIS A 28 ND1 106.9 107.1 REMARK 620 4 HIS A 32 NE2 106.6 107.5 118.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 40 SG REMARK 620 2 CYS A 43 SG 102.6 REMARK 620 3 HIS A 56 NE2 105.4 105.1 REMARK 620 4 HIS A 60 NE2 108.7 114.4 119.1 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 68 SG REMARK 620 2 CYS A 71 SG 103.1 REMARK 620 3 HIS A 84 NE2 107.3 105.0 REMARK 620 4 CYS A 88 SG 111.8 111.6 116.9 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 300 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 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: HSK002000403 RELATED DB: TARGETDB DBREF 2CSH A 8 104 UNP O43298 Z297B_HUMAN 370 466 SEQADV 2CSH GLY A 1 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 2 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 3 UNP O43298 CLONING ARTIFACT SEQADV 2CSH GLY A 4 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 5 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 6 UNP O43298 CLONING ARTIFACT SEQADV 2CSH GLY A 7 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 105 UNP O43298 CLONING ARTIFACT SEQADV 2CSH GLY A 106 UNP O43298 CLONING ARTIFACT SEQADV 2CSH PRO A 107 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 108 UNP O43298 CLONING ARTIFACT SEQADV 2CSH SER A 109 UNP O43298 CLONING ARTIFACT SEQADV 2CSH GLY A 110 UNP O43298 CLONING ARTIFACT SEQRES 1 A 110 GLY SER SER GLY SER SER GLY ASP LYS LEU TYR PRO CYS SEQRES 2 A 110 GLN CYS GLY LYS SER PHE THR HIS LYS SER GLN ARG ASP SEQRES 3 A 110 ARG HIS MET SER MET HIS LEU GLY LEU ARG PRO TYR GLY SEQRES 4 A 110 CYS GLY VAL CYS GLY LYS LYS PHE LYS MET LYS HIS HIS SEQRES 5 A 110 LEU VAL GLY HIS MET LYS ILE HIS THR GLY ILE LYS PRO SEQRES 6 A 110 TYR GLU CYS ASN ILE CYS ALA LYS ARG PHE MET TRP ARG SEQRES 7 A 110 ASP SER PHE HIS ARG HIS VAL THR SER CYS THR LYS SER SEQRES 8 A 110 TYR GLU ALA ALA LYS ALA GLU GLN ASN THR THR GLU ALA SEQRES 9 A 110 SER GLY PRO SER SER GLY HET ZN A 200 1 HET ZN A 300 1 HET ZN A 400 1 HETNAM ZN ZINC ION FORMUL 2 ZN 3(ZN 2+) HELIX 1 1 HIS A 21 LEU A 33 1 13 HELIX 2 2 LYS A 50 LYS A 58 1 9 HELIX 3 3 TRP A 77 ALA A 97 1 21 SHEET 1 A 2 TYR A 11 PRO A 12 0 SHEET 2 A 2 SER A 18 PHE A 19 -1 O PHE A 19 N TYR A 11 SHEET 1 B 2 TYR A 38 GLY A 39 0 SHEET 2 B 2 LYS A 46 PHE A 47 -1 O PHE A 47 N TYR A 38 SHEET 1 C 2 TYR A 66 GLU A 67 0 SHEET 2 C 2 ARG A 74 PHE A 75 -1 O PHE A 75 N TYR A 66 LINK SG CYS A 13 ZN ZN A 200 1555 1555 2.35 LINK SG CYS A 15 ZN ZN A 200 1555 1555 2.30 LINK ND1 HIS A 28 ZN ZN A 200 1555 1555 2.05 LINK NE2 HIS A 32 ZN ZN A 200 1555 1555 2.04 LINK SG CYS A 40 ZN ZN A 300 1555 1555 2.35 LINK SG CYS A 43 ZN ZN A 300 1555 1555 2.35 LINK NE2 HIS A 56 ZN ZN A 300 1555 1555 2.05 LINK NE2 HIS A 60 ZN ZN A 300 1555 1555 2.05 LINK SG CYS A 68 ZN ZN A 400 1555 1555 2.35 LINK SG CYS A 71 ZN ZN A 400 1555 1555 2.35 LINK NE2 HIS A 84 ZN ZN A 400 1555 1555 2.05 LINK SG CYS A 88 ZN ZN A 400 1555 1555 2.05 SITE 1 AC1 4 CYS A 13 CYS A 15 HIS A 28 HIS A 32 SITE 1 AC2 4 CYS A 40 CYS A 43 HIS A 56 HIS A 60 SITE 1 AC3 4 CYS A 68 CYS A 71 HIS A 84 CYS A 88 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