Header list of 2cr6.pdb file
Complete list - r 9 2 Bytes
HEADER CONTRACTILE PROTEIN 20-MAY-05 2CR6
TITLE SOLUTION STRUCTURE OF THE IG DOMAIN (2998-3100) OF HUMAN OBSCURIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA1556 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IG;
COMPND 5 SYNONYM: OBSCURIN;
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: KIAA1556;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040202-82;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS IG-FOLD, KIAA1556 PROTEIN, IMMUNOGLOBULIN DOMAIN, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.NAGASHIMA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CR6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CR6 1 VERSN
REVDAT 1 20-NOV-05 2CR6 0
JRNL AUTH K.NAGASHIMA,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE IG DOMAIN (2998-3100) OF HUMAN
JRNL TITL 2 OBSCURIN
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 2CR6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024533.
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 : 1.21MM 13C,15N-LABELED PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 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 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TRSION 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 LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: SPECTROMETER_ID 1 FOR 3D_15N_SEPARATED_NOESY;
REMARK 210 SPECTROMETER_ID 2 FOR 3D_13C_SEPARATED_NOESY
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 ARG A 12 -176.70 -59.10
REMARK 500 1 ILE A 16 95.82 -64.42
REMARK 500 1 LEU A 20 171.43 -52.66
REMARK 500 1 GLU A 21 -75.63 -116.87
REMARK 500 1 ASP A 22 164.10 179.25
REMARK 500 1 ASN A 41 42.02 -104.68
REMARK 500 1 GLU A 43 158.73 178.13
REMARK 500 1 ASP A 50 -79.10 67.40
REMARK 500 1 LYS A 51 40.97 -151.00
REMARK 500 1 ASN A 57 -169.32 -164.87
REMARK 500 1 LEU A 74 92.62 -67.87
REMARK 500 1 GLN A 76 71.16 56.96
REMARK 500 1 SER A 82 109.01 -51.62
REMARK 500 1 ALA A 89 96.19 -165.29
REMARK 500 1 ALA A 97 99.74 -69.64
REMARK 500 1 SER A 105 -168.94 -73.32
REMARK 500 1 PHE A 107 81.93 52.79
REMARK 500 1 SER A 108 -75.02 -125.56
REMARK 500 2 ILE A 16 97.76 -60.55
REMARK 500 2 LEU A 20 176.07 -55.46
REMARK 500 2 GLU A 21 -75.77 -122.65
REMARK 500 2 ASP A 22 162.23 179.91
REMARK 500 2 GLU A 43 159.76 179.35
REMARK 500 2 ASP A 50 -78.80 67.69
REMARK 500 2 LYS A 51 40.99 -150.84
REMARK 500 2 ASN A 57 -169.54 -162.14
REMARK 500 2 GLN A 76 63.23 60.29
REMARK 500 2 SER A 82 108.09 -51.23
REMARK 500 2 ALA A 89 95.72 -163.59
REMARK 500 2 SER A 95 109.09 -161.02
REMARK 500 2 PHE A 107 -73.13 -88.29
REMARK 500 2 SER A 108 -178.92 -176.23
REMARK 500 2 ARG A 109 -67.64 -128.14
REMARK 500 2 PRO A 112 -178.97 -69.75
REMARK 500 3 ILE A 16 97.20 -61.48
REMARK 500 3 GLU A 21 -76.42 -116.06
REMARK 500 3 ASP A 22 163.51 179.53
REMARK 500 3 ASN A 41 33.91 -96.53
REMARK 500 3 GLU A 43 159.59 179.17
REMARK 500 3 ASP A 50 -77.07 68.32
REMARK 500 3 LYS A 51 40.73 -153.37
REMARK 500 3 GLN A 76 70.29 51.87
REMARK 500 3 SER A 82 105.15 -51.53
REMARK 500 3 TYR A 86 78.36 -105.08
REMARK 500 3 ALA A 89 98.76 -168.63
REMARK 500 3 ARG A 93 114.18 -172.94
REMARK 500 3 GLU A 102 171.69 -56.99
REMARK 500 3 PHE A 107 37.97 -159.06
REMARK 500 4 ILE A 16 96.56 -59.82
REMARK 500 4 GLU A 21 -76.25 -112.14
REMARK 500
REMARK 500 THIS ENTRY HAS 293 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001528 RELATED DB: TARGETDB
DBREF 2CR6 A 8 109 UNP Q9HCL6 Q9HCL6_HUMAN 274 375
SEQADV 2CR6 GLY A 1 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 2 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 3 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 GLY A 4 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 5 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 6 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 GLY A 7 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 110 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 GLY A 111 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 PRO A 112 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 113 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 SER A 114 UNP Q9HCL6 CLONING ARTIFACT
SEQADV 2CR6 GLY A 115 UNP Q9HCL6 CLONING ARTIFACT
SEQRES 1 A 115 GLY SER SER GLY SER SER GLY LEU VAL GLN GLY ARG ARG
SEQRES 2 A 115 VAL HIS ILE ILE GLU ASP LEU GLU ASP VAL ASP VAL GLN
SEQRES 3 A 115 GLU GLY SER SER ALA THR PHE ARG CYS ARG ILE SER PRO
SEQRES 4 A 115 ALA ASN TYR GLU PRO VAL HIS TRP PHE LEU ASP LYS THR
SEQRES 5 A 115 PRO LEU HIS ALA ASN GLU LEU ASN GLU ILE ASP ALA GLN
SEQRES 6 A 115 PRO GLY GLY TYR HIS VAL LEU THR LEU ARG GLN LEU ALA
SEQRES 7 A 115 LEU LYS ASP SER GLY THR ILE TYR PHE GLU ALA GLY ASP
SEQRES 8 A 115 GLN ARG ALA SER ALA ALA LEU ARG VAL THR GLU LYS PRO
SEQRES 9 A 115 SER VAL PHE SER ARG SER GLY PRO SER SER GLY
SHEET 1 A 4 HIS A 15 ILE A 17 0
SHEET 2 A 4 ALA A 31 SER A 38 -1 O SER A 38 N HIS A 15
SHEET 3 A 4 TYR A 69 LEU A 74 -1 O HIS A 70 N CYS A 35
SHEET 4 A 4 ASN A 60 ILE A 62 -1 O GLU A 61 N THR A 73
SHEET 1 B 5 ASP A 22 GLN A 26 0
SHEET 2 B 5 ALA A 96 THR A 101 1 O ARG A 99 N VAL A 23
SHEET 3 B 5 GLY A 83 ALA A 89 -1 N ILE A 85 O ALA A 96
SHEET 4 B 5 HIS A 46 LEU A 49 -1 N PHE A 48 O TYR A 86
SHEET 5 B 5 PRO A 53 LEU A 54 -1 O LEU A 54 N TRP A 47
SHEET 1 C 4 ASP A 22 GLN A 26 0
SHEET 2 C 4 ALA A 96 THR A 101 1 O ARG A 99 N VAL A 23
SHEET 3 C 4 GLY A 83 ALA A 89 -1 N ILE A 85 O ALA A 96
SHEET 4 C 4 GLN A 92 ARG A 93 -1 O GLN A 92 N ALA A 89
CISPEP 1 SER A 38 PRO A 39 1 -0.01
CISPEP 2 GLU A 43 PRO A 44 1 0.04
CISPEP 3 SER A 38 PRO A 39 2 -0.04
CISPEP 4 GLU A 43 PRO A 44 2 -0.06
CISPEP 5 SER A 38 PRO A 39 3 0.03
CISPEP 6 GLU A 43 PRO A 44 3 0.03
CISPEP 7 SER A 38 PRO A 39 4 -0.05
CISPEP 8 GLU A 43 PRO A 44 4 0.07
CISPEP 9 SER A 38 PRO A 39 5 0.02
CISPEP 10 GLU A 43 PRO A 44 5 0.01
CISPEP 11 SER A 38 PRO A 39 6 -0.02
CISPEP 12 GLU A 43 PRO A 44 6 0.06
CISPEP 13 SER A 38 PRO A 39 7 -0.01
CISPEP 14 GLU A 43 PRO A 44 7 -0.03
CISPEP 15 SER A 38 PRO A 39 8 0.00
CISPEP 16 GLU A 43 PRO A 44 8 -0.02
CISPEP 17 SER A 38 PRO A 39 9 0.01
CISPEP 18 GLU A 43 PRO A 44 9 0.00
CISPEP 19 SER A 38 PRO A 39 10 -0.02
CISPEP 20 GLU A 43 PRO A 44 10 0.02
CISPEP 21 SER A 38 PRO A 39 11 -0.06
CISPEP 22 GLU A 43 PRO A 44 11 0.03
CISPEP 23 SER A 38 PRO A 39 12 -0.01
CISPEP 24 GLU A 43 PRO A 44 12 0.02
CISPEP 25 SER A 38 PRO A 39 13 0.02
CISPEP 26 GLU A 43 PRO A 44 13 -0.03
CISPEP 27 SER A 38 PRO A 39 14 -0.09
CISPEP 28 GLU A 43 PRO A 44 14 -0.03
CISPEP 29 SER A 38 PRO A 39 15 -0.05
CISPEP 30 GLU A 43 PRO A 44 15 0.04
CISPEP 31 SER A 38 PRO A 39 16 -0.03
CISPEP 32 GLU A 43 PRO A 44 16 -0.01
CISPEP 33 SER A 38 PRO A 39 17 -0.06
CISPEP 34 GLU A 43 PRO A 44 17 -0.06
CISPEP 35 SER A 38 PRO A 39 18 0.01
CISPEP 36 GLU A 43 PRO A 44 18 0.01
CISPEP 37 SER A 38 PRO A 39 19 0.02
CISPEP 38 GLU A 43 PRO A 44 19 -0.12
CISPEP 39 SER A 38 PRO A 39 20 -0.10
CISPEP 40 GLU A 43 PRO A 44 20 0.00
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