Header list of 1wyq.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYQ TITLE SOLUTION STRUCTURE OF THE SECOND CH DOMAIN OF HUMAN SPECTRIN BETA TITLE 2 CHAIN, BRAIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPECTRIN BETA CHAIN, BRAIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CH DOMAIN; COMPND 5 SYNONYM: SPECTRIN, NON-ERYTHROID BETA CHAIN 2, BETA-III SPECTRIN; 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: SPTBN2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-11; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS NPPSFA, STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WYQ 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WYQ 1 VERSN REVDAT 1 15-AUG-05 1WYQ 0 JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SECOND CH DOMAIN OF HUMAN SPECTRIN JRNL TITL 2 BETA CHAIN, BRAIN 2 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 1WYQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1000024161. 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 : 1.20MM CH DOMAIN U-15N,13C; 20MM REMARK 210 D-TRIS-HCL(PH 7.0); 100MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3; 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 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.9295, 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 : 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 : NULL 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 SER A 2 130.29 -172.83 REMARK 500 1 LYS A 9 45.64 -85.68 REMARK 500 1 THR A 32 -69.03 -132.80 REMARK 500 1 THR A 33 33.40 -88.16 REMARK 500 1 HIS A 46 -37.18 -35.83 REMARK 500 1 PRO A 50 3.02 -69.79 REMARK 500 1 LYS A 60 37.93 -90.53 REMARK 500 1 CYS A 61 -58.81 -122.63 REMARK 500 1 GLU A 77 -70.97 -61.24 REMARK 500 1 ASN A 90 95.23 -54.36 REMARK 500 1 TYR A 109 -73.24 -50.22 REMARK 500 1 MET A 113 179.55 -51.20 REMARK 500 1 LYS A 114 100.59 -54.07 REMARK 500 1 SER A 126 125.28 -173.65 REMARK 500 2 SER A 6 101.38 -49.88 REMARK 500 2 THR A 32 -68.28 -132.61 REMARK 500 2 HIS A 46 -33.34 -35.80 REMARK 500 2 PRO A 50 2.38 -69.80 REMARK 500 2 LEU A 67 -70.70 -69.24 REMARK 500 2 GLN A 68 -38.80 -38.14 REMARK 500 2 PRO A 86 0.30 -69.77 REMARK 500 2 ASN A 90 82.52 -58.56 REMARK 500 2 TYR A 109 -70.95 -59.49 REMARK 500 2 PRO A 124 -168.53 -69.76 REMARK 500 3 SER A 3 78.40 -115.12 REMARK 500 3 THR A 32 -68.53 -132.07 REMARK 500 3 PRO A 50 2.53 -69.73 REMARK 500 3 LYS A 60 -38.20 -34.70 REMARK 500 3 LYS A 76 -63.11 -106.99 REMARK 500 3 PRO A 86 0.31 -69.67 REMARK 500 3 ASN A 90 87.09 -61.95 REMARK 500 3 ASP A 95 94.49 -64.63 REMARK 500 3 TYR A 109 -72.16 -37.73 REMARK 500 3 MET A 113 154.01 -45.55 REMARK 500 4 THR A 32 -70.90 -122.85 REMARK 500 4 THR A 33 31.90 -89.68 REMARK 500 4 PRO A 50 3.63 -69.78 REMARK 500 4 LYS A 82 107.58 -49.67 REMARK 500 4 PRO A 86 0.40 -69.73 REMARK 500 4 ASN A 90 90.97 -56.35 REMARK 500 4 PRO A 94 -169.90 -69.73 REMARK 500 4 MET A 113 165.48 -46.66 REMARK 500 4 LYS A 114 101.81 -35.75 REMARK 500 4 PRO A 124 -175.59 -69.66 REMARK 500 5 THR A 32 -67.79 -128.22 REMARK 500 5 PRO A 50 2.66 -69.82 REMARK 500 5 LYS A 60 43.21 -92.75 REMARK 500 5 CYS A 61 -35.20 -133.10 REMARK 500 5 LYS A 76 -63.95 -108.93 REMARK 500 5 GLU A 77 -70.34 -61.76 REMARK 500 REMARK 500 THIS ENTRY HAS 240 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002300294.1 RELATED DB: TARGETDB DBREF 1WYQ A 8 121 UNP O15020 SPTN2_HUMAN 178 291 SEQADV 1WYQ GLY A 1 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 2 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 3 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ GLY A 4 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 5 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 6 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ GLY A 7 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 122 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ GLY A 123 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ PRO A 124 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 125 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ SER A 126 UNP O15020 CLONING ARTIFACT SEQADV 1WYQ GLY A 127 UNP O15020 CLONING ARTIFACT SEQRES 1 A 127 GLY SER SER GLY SER SER GLY ALA LYS ASP ALA LEU LEU SEQRES 2 A 127 LEU TRP CYS GLN MET LYS THR ALA GLY TYR PRO ASN VAL SEQRES 3 A 127 ASN VAL HIS ASN PHE THR THR SER TRP ARG ASP GLY LEU SEQRES 4 A 127 ALA PHE ASN ALA ILE VAL HIS LYS HIS ARG PRO ASP LEU SEQRES 5 A 127 LEU ASP PHE GLU SER LEU LYS LYS CYS ASN ALA HIS TYR SEQRES 6 A 127 ASN LEU GLN ASN ALA PHE ASN LEU ALA GLU LYS GLU LEU SEQRES 7 A 127 GLY LEU THR LYS LEU LEU ASP PRO GLU ASP VAL ASN VAL SEQRES 8 A 127 ASP GLN PRO ASP GLU LYS SER ILE ILE THR TYR VAL ALA SEQRES 9 A 127 THR TYR TYR HIS TYR PHE SER LYS MET LYS ALA LEU ALA SEQRES 10 A 127 VAL GLU GLY LYS SER GLY PRO SER SER GLY HELIX 1 1 LYS A 9 GLY A 22 1 14 HELIX 2 2 GLY A 38 ARG A 49 1 12 HELIX 3 3 ALA A 63 GLU A 77 1 15 HELIX 4 4 ASP A 95 MET A 113 1 19 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