Header list of 1x5m.pdb file
Complete list - r 2 2 Bytes
HEADER APOPTOSIS, SIGNALING PROTEIN 16-MAY-05 1X5M
TITLE SOLUTION STRUCTURE OF THE CORE DOMAIN OF CALCYCLIN BINDING PROTEIN;
TITLE 2 SIAH-INTERACTING PROTEIN (SIP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCYCLIN-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CS DOMAIN;
COMPND 5 SYNONYM: CACYBP, HCACYBP, SIAH-INTERACTING PROTEIN, S100A6-BINDING
COMPND 6 PROTEIN, PNAS-107;
COMPND 7 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: CACYBP, S100A6BP, SIP;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040329-62;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS CS DOMAIN, CALCYCLIN-BINDING PROTEIN/SIAH-INTERACTING PROTEIN/S100A6-
KEYWDS 2 BINDING PROTEIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, APOPTOSIS, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5M 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5M 1 VERSN
REVDAT 1 16-NOV-05 1X5M 0
JRNL AUTH X.R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CORE DOMAIN OF CALCYCLIN BINDING
JRNL TITL 2 PROTEIN; SIAH-INTERACTING PROTEIN (SIP)
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), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024408.
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 : 0.98MM 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_15N-SEPARATED_NOESY; 3D_13C
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 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, 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 : 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: 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 O LYS A 116 H GLU A 120 1.52
REMARK 500 O GLU A 115 H LYS A 119 1.53
REMARK 500 H VAL A 18 O SER A 69 1.54
REMARK 500 O VAL A 32 H CYS A 99 1.57
REMARK 500 O GLN A 50 H LEU A 61 1.58
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 95.41 66.45
REMARK 500 1 SER A 3 125.99 -171.80
REMARK 500 1 SER A 5 135.82 175.99
REMARK 500 1 SER A 6 159.17 178.27
REMARK 500 1 THR A 14 -153.27 38.61
REMARK 500 1 ASP A 29 78.18 -64.25
REMARK 500 1 LYS A 30 -54.69 170.53
REMARK 500 1 THR A 54 -165.62 -129.53
REMARK 500 1 ARG A 56 54.30 -142.50
REMARK 500 1 SER A 57 174.49 175.03
REMARK 500 1 PHE A 58 127.34 -171.53
REMARK 500 1 ASN A 64 90.92 41.00
REMARK 500 1 LEU A 65 -130.41 -126.40
REMARK 500 1 LYS A 68 -179.65 -171.69
REMARK 500 1 ASN A 76 97.87 84.19
REMARK 500 2 SER A 2 97.50 -165.90
REMARK 500 2 SER A 3 163.26 177.26
REMARK 500 2 SER A 5 98.17 177.34
REMARK 500 2 THR A 14 18.06 56.42
REMARK 500 2 SER A 21 -65.41 -91.61
REMARK 500 2 ASP A 29 77.35 -64.38
REMARK 500 2 LYS A 30 -54.50 171.26
REMARK 500 2 THR A 54 -164.68 -127.83
REMARK 500 2 ARG A 56 54.78 -141.30
REMARK 500 2 SER A 57 172.68 175.60
REMARK 500 2 PHE A 58 127.52 -170.39
REMARK 500 2 ASN A 64 89.96 40.23
REMARK 500 2 LEU A 65 -122.38 -121.30
REMARK 500 2 LYS A 68 -169.93 -169.71
REMARK 500 2 ASN A 76 86.92 84.61
REMARK 500 2 GLU A 104 -179.67 -67.44
REMARK 500 2 LYS A 121 99.15 -55.73
REMARK 500 2 SER A 125 86.27 70.51
REMARK 500 3 SER A 2 145.13 61.56
REMARK 500 3 SER A 5 143.66 65.03
REMARK 500 3 SER A 6 160.61 175.85
REMARK 500 3 ASP A 29 77.73 -64.53
REMARK 500 3 LYS A 30 -55.26 170.22
REMARK 500 3 THR A 54 -164.69 -128.46
REMARK 500 3 ARG A 56 55.21 -141.57
REMARK 500 3 SER A 57 173.88 175.01
REMARK 500 3 PHE A 58 127.91 -170.70
REMARK 500 3 ASN A 64 93.14 44.66
REMARK 500 3 LEU A 65 -135.06 -129.99
REMARK 500 3 ASN A 76 98.23 83.14
REMARK 500 3 LYS A 116 -70.04 -55.09
REMARK 500 3 LYS A 121 -71.27 -52.87
REMARK 500 3 SER A 125 96.25 58.95
REMARK 500 4 SER A 3 139.67 -175.07
REMARK 500 4 SER A 6 80.45 177.93
REMARK 500
REMARK 500 THIS ENTRY HAS 284 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000577 RELATED DB: TARGETDB
DBREF 1X5M A 8 121 UNP Q9HB71 CYBP_HUMAN 63 176
SEQADV 1X5M GLY A 1 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 2 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 3 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M GLY A 4 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 5 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 6 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M GLY A 7 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 122 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M GLY A 123 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M PRO A 124 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 125 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M SER A 126 UNP Q9HB71 CLONING ARTIFACT
SEQADV 1X5M GLY A 127 UNP Q9HB71 CLONING ARTIFACT
SEQRES 1 A 127 GLY SER SER GLY SER SER GLY VAL VAL ALA PRO ILE THR
SEQRES 2 A 127 THR GLY TYR THR VAL LYS ILE SER ASN TYR GLY TRP ASP
SEQRES 3 A 127 GLN SER ASP LYS PHE VAL LYS ILE TYR ILE THR LEU THR
SEQRES 4 A 127 GLY VAL HIS GLN VAL PRO THR GLU ASN VAL GLN VAL HIS
SEQRES 5 A 127 PHE THR GLU ARG SER PHE ASP LEU LEU VAL LYS ASN LEU
SEQRES 6 A 127 ASN GLY LYS SER TYR SER MET ILE VAL ASN ASN LEU LEU
SEQRES 7 A 127 LYS PRO ILE SER VAL GLU GLY SER SER LYS LYS VAL LYS
SEQRES 8 A 127 THR ASP THR VAL LEU ILE LEU CYS ARG LYS LYS VAL GLU
SEQRES 9 A 127 ASN THR ARG TRP ASP TYR LEU THR GLN VAL GLU LYS GLU
SEQRES 10 A 127 CYS LYS GLU LYS SER GLY PRO SER SER GLY
HELIX 1 1 THR A 112 GLU A 120 1 9
SHEET 1 A 4 VAL A 18 LYS A 19 0
SHEET 2 A 4 TYR A 70 ASN A 75 1 O SER A 71 N VAL A 18
SHEET 3 A 4 SER A 57 VAL A 62 -1 N LEU A 60 O MET A 72
SHEET 4 A 4 VAL A 49 PHE A 53 -1 N GLN A 50 O LEU A 61
SHEET 1 B 4 GLY A 24 SER A 28 0
SHEET 2 B 4 PHE A 31 THR A 37 -1 O TYR A 35 N GLY A 24
SHEET 3 B 4 THR A 94 ARG A 100 -1 O CYS A 99 N VAL A 32
SHEET 4 B 4 SER A 87 LYS A 91 -1 N LYS A 89 O LEU A 96
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