Header list of 1whh.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 28-MAY-04 1WHH TITLE SOLUTION STRUCTURE OF THE 2ND CAP-GLY DOMAIN IN MOUSE CLIP170-RELATED TITLE 2 59KDA PROTEIN CLIPR-59 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CLIPR-59; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CAP-GLY DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 1500005P14; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040223-85; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS MICROTUBULE BINDING, TRANS-GOLGI NETWORK, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WHH 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WHH 1 VERSN REVDAT 1 28-NOV-04 1WHH 0 JRNL AUTH K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE 2ND CAP-GLY DOMAIN IN MOUSE JRNL TITL 2 CLIP170-RELATED 59KDA PROTEIN CLIPR-59 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, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WHH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023585. 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 : 1MM PROTEIN, 20MM D-TRIS-HCL, PH REMARK 210 7.0, 100MM NACL, 1MM D-DTT, 0.02% REMARK 210 NAN3, 10% 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, CNS REMARK 210 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 SER A 2 121.17 62.32 REMARK 500 1 SER A 5 -63.11 -94.14 REMARK 500 1 LYS A 8 31.58 -157.01 REMARK 500 1 PRO A 13 88.97 -67.02 REMARK 500 1 SER A 17 109.32 -177.49 REMARK 500 1 LEU A 18 31.58 -153.80 REMARK 500 1 GLN A 19 31.75 -154.13 REMARK 500 1 GLN A 37 -71.42 -146.98 REMARK 500 1 PRO A 63 86.75 -55.83 REMARK 500 1 THR A 64 30.44 -157.30 REMARK 500 1 ASP A 68 48.49 -105.25 REMARK 500 1 ARG A 82 63.53 60.27 REMARK 500 1 HIS A 83 -46.02 -132.30 REMARK 500 2 SER A 3 -51.28 -120.49 REMARK 500 2 SER A 5 35.10 -167.79 REMARK 500 2 SER A 12 89.40 -161.93 REMARK 500 2 PRO A 13 108.60 -51.12 REMARK 500 2 SER A 14 -45.47 -145.86 REMARK 500 2 LEU A 15 -77.61 -116.87 REMARK 500 2 SER A 17 -168.53 -59.01 REMARK 500 2 GLN A 37 -72.83 -138.10 REMARK 500 2 LYS A 66 -47.33 -144.96 REMARK 500 2 ASP A 68 34.04 -98.42 REMARK 500 2 SER A 97 -173.97 -170.20 REMARK 500 2 SER A 100 175.45 58.57 REMARK 500 2 SER A 101 35.31 -168.48 REMARK 500 3 SER A 9 84.83 59.79 REMARK 500 3 SER A 11 -60.54 -141.39 REMARK 500 3 SER A 12 63.33 -165.98 REMARK 500 3 LEU A 15 73.98 -151.67 REMARK 500 3 SER A 17 37.80 -177.02 REMARK 500 3 LEU A 18 -67.82 -131.16 REMARK 500 3 GLN A 19 -178.24 60.43 REMARK 500 3 ALA A 24 79.80 59.77 REMARK 500 3 GLN A 37 -73.27 -140.28 REMARK 500 3 PRO A 52 -167.94 -70.67 REMARK 500 3 ASP A 68 36.51 -98.56 REMARK 500 3 ILE A 95 -61.88 -91.89 REMARK 500 3 SER A 97 -69.60 -155.06 REMARK 500 4 SER A 3 -47.45 -145.49 REMARK 500 4 LYS A 8 91.88 -60.56 REMARK 500 4 SER A 11 105.76 57.84 REMARK 500 4 PRO A 13 -169.39 -54.55 REMARK 500 4 SER A 14 -46.95 -150.60 REMARK 500 4 LEU A 15 32.06 -165.09 REMARK 500 4 LEU A 18 -48.66 -151.32 REMARK 500 4 GLU A 22 -44.42 -167.22 REMARK 500 4 LYS A 25 -48.55 -142.94 REMARK 500 4 VAL A 28 82.69 -67.85 REMARK 500 4 GLN A 37 -70.44 -144.36 REMARK 500 REMARK 500 THIS ENTRY HAS 257 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007015364.1 RELATED DB: TARGETDB DBREF 1WHH A 8 96 UNP Q9DB67 Q9DB67_MOUSE 19 107 SEQADV 1WHH GLY A 1 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 2 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 3 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH GLY A 4 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 5 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 6 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH GLY A 7 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 97 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH GLY A 98 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH PRO A 99 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 100 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH SER A 101 UNP Q9DB67 CLONING ARTIFACT SEQADV 1WHH GLY A 102 UNP Q9DB67 CLONING ARTIFACT SEQRES 1 A 102 GLY SER SER GLY SER SER GLY LYS SER PRO SER SER PRO SEQRES 2 A 102 SER LEU GLY SER LEU GLN GLN ARG GLU GLY ALA LYS ALA SEQRES 3 A 102 GLU VAL GLY ASP GLN VAL LEU VAL ALA GLY GLN LYS GLN SEQRES 4 A 102 GLY ILE VAL ARG PHE TYR GLY LYS THR ASP PHE ALA PRO SEQRES 5 A 102 GLY TYR TRP TYR GLY ILE GLU LEU ASP GLN PRO THR GLY SEQRES 6 A 102 LYS HIS ASP GLY SER VAL PHE GLY VAL ARG TYR PHE THR SEQRES 7 A 102 CYS ALA PRO ARG HIS GLY VAL PHE ALA PRO ALA SER ARG SEQRES 8 A 102 ILE GLN ARG ILE GLY SER GLY PRO SER SER GLY HELIX 1 1 PRO A 88 SER A 90 5 3 SHEET 1 A 5 GLY A 84 ALA A 87 0 SHEET 2 A 5 TYR A 54 GLU A 59 -1 N ILE A 58 O VAL A 85 SHEET 3 A 5 LYS A 38 LYS A 47 -1 N PHE A 44 O GLY A 57 SHEET 4 A 5 GLN A 31 VAL A 34 -1 N VAL A 32 O GLY A 40 SHEET 5 A 5 ILE A 92 ARG A 94 -1 O GLN A 93 N LEU A 33 SHEET 1 B 2 SER A 70 VAL A 71 0 SHEET 2 B 2 VAL A 74 ARG A 75 -1 O VAL A 74 N VAL A 71 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