Header list of 1wis.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WIS TITLE SOLUTION STRUCTURE OF THE FIFTH FNIII DOMAIN FROM HUMAN KIAA1514 TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: KIAA1514 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FNIII 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 FH00815; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-48; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS FNIII DOMAIN, KIAA1514, SIDEKICK-2, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.SUETAKE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WIS 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WIS 1 VERSN REVDAT 1 19-JUL-05 1WIS 0 JRNL AUTH T.SUETAKE,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FIFTH FNIII DOMAIN FROM HUMAN JRNL TITL 2 KIAA1514 PROTEIN 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 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WIS 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_1000023624. 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 : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.93MM 13C, 15N-LABELED PROTEIN; REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM REMARK 210 D-DTT; 0.02% NAN3 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2002045, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.860, CYANA 1.0.7 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, 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 H SER A 49 O VAL A 99 1.52 REMARK 500 REMARK 500 REMARK: NULL 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 2 90.54 -166.62 REMARK 500 1 SER A 10 88.65 -166.23 REMARK 500 1 SER A 11 -59.01 176.58 REMARK 500 1 PRO A 18 -161.97 -74.92 REMARK 500 1 THR A 22 -166.34 -120.22 REMARK 500 1 THR A 46 137.08 -174.16 REMARK 500 1 ARG A 50 141.91 -170.62 REMARK 500 1 GLU A 62 167.52 -46.77 REMARK 500 1 ILE A 69 -44.10 -136.06 REMARK 500 1 ASN A 74 74.98 55.24 REMARK 500 1 GLU A 75 65.23 176.11 REMARK 500 1 VAL A 102 -71.44 -78.56 REMARK 500 1 SER A 122 80.09 -174.72 REMARK 500 2 SER A 3 87.73 58.03 REMARK 500 2 ILE A 9 -164.30 43.45 REMARK 500 2 SER A 11 -56.06 -130.93 REMARK 500 2 PRO A 18 -161.49 -74.93 REMARK 500 2 THR A 22 -165.77 -109.96 REMARK 500 2 THR A 46 123.89 -174.38 REMARK 500 2 SER A 47 155.50 -49.32 REMARK 500 2 ILE A 69 -45.14 -135.09 REMARK 500 2 ASN A 74 81.86 38.35 REMARK 500 2 GLU A 75 66.01 171.44 REMARK 500 2 ARG A 95 -167.58 -126.72 REMARK 500 2 VAL A 102 -75.12 -80.86 REMARK 500 2 SER A 105 172.18 -59.35 REMARK 500 2 ARG A 112 145.30 -38.63 REMARK 500 2 SER A 123 107.94 -166.75 REMARK 500 3 SER A 2 102.31 56.72 REMARK 500 3 THR A 8 57.64 -109.78 REMARK 500 3 ILE A 9 -65.99 -130.36 REMARK 500 3 SER A 10 83.06 53.84 REMARK 500 3 PRO A 18 -165.39 -75.01 REMARK 500 3 THR A 22 -166.93 -124.67 REMARK 500 3 THR A 46 139.55 -173.86 REMARK 500 3 VAL A 59 97.89 -42.95 REMARK 500 3 GLU A 62 96.51 64.98 REMARK 500 3 ASN A 74 78.61 64.79 REMARK 500 3 GLU A 75 69.00 165.30 REMARK 500 3 PRO A 84 -169.05 -75.01 REMARK 500 3 ARG A 95 -167.61 -126.52 REMARK 500 3 VAL A 102 -74.81 -65.58 REMARK 500 4 SER A 10 -58.96 -170.40 REMARK 500 4 PRO A 18 -161.16 -75.08 REMARK 500 4 THR A 22 -166.05 -120.55 REMARK 500 4 THR A 46 115.29 -169.81 REMARK 500 4 VAL A 59 107.22 -42.98 REMARK 500 4 VAL A 60 78.89 -102.31 REMARK 500 4 ILE A 69 -44.12 -134.70 REMARK 500 4 ASN A 74 84.50 45.78 REMARK 500 REMARK 500 THIS ENTRY HAS 299 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002101486.3 RELATED DB: TARGETDB DBREF 1WIS A 8 118 GB 7959295 BAA96038 660 770 SEQADV 1WIS GLY A 1 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 2 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 3 GB 7959295 CLONING ARTIFACT SEQADV 1WIS GLY A 4 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 5 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 6 GB 7959295 CLONING ARTIFACT SEQADV 1WIS GLY A 7 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 119 GB 7959295 CLONING ARTIFACT SEQADV 1WIS GLY A 120 GB 7959295 CLONING ARTIFACT SEQADV 1WIS PRO A 121 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 122 GB 7959295 CLONING ARTIFACT SEQADV 1WIS SER A 123 GB 7959295 CLONING ARTIFACT SEQADV 1WIS GLY A 124 GB 7959295 CLONING ARTIFACT SEQRES 1 A 124 GLY SER SER GLY SER SER GLY THR ILE SER SER GLY VAL SEQRES 2 A 124 PRO PRO GLU LEU PRO GLY PRO PRO THR ASN LEU GLY ILE SEQRES 3 A 124 SER ASN ILE GLY PRO ARG SER VAL THR LEU GLN PHE ARG SEQRES 4 A 124 PRO GLY TYR ASP GLY LYS THR SER ILE SER ARG TRP LEU SEQRES 5 A 124 VAL GLU ALA GLN VAL GLY VAL VAL GLY GLU GLY GLU GLU SEQRES 6 A 124 TRP LEU LEU ILE HIS GLN LEU SER ASN GLU PRO ASP ALA SEQRES 7 A 124 ARG SER MET GLU VAL PRO ASP LEU ASN PRO PHE THR CYS SEQRES 8 A 124 TYR SER PHE ARG MET ARG GLN VAL ASN ILE VAL GLY THR SEQRES 9 A 124 SER PRO PRO SER GLN PRO SER ARG LYS ILE GLN THR LEU SEQRES 10 A 124 GLN SER GLY PRO SER SER GLY SHEET 1 A 3 THR A 22 SER A 27 0 SHEET 2 A 3 VAL A 34 ARG A 39 -1 O THR A 35 N SER A 27 SHEET 3 A 3 SER A 80 VAL A 83 -1 O VAL A 83 N VAL A 34 SHEET 1 B 3 LEU A 67 SER A 73 0 SHEET 2 B 3 ARG A 50 ALA A 55 -1 N VAL A 53 O HIS A 70 SHEET 3 B 3 ARG A 97 VAL A 99 -1 O ARG A 97 N LEU A 52 SHEET 1 C 2 CYS A 91 TYR A 92 0 SHEET 2 C 2 ILE A 114 GLN A 115 -1 O ILE A 114 N TYR A 92 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