Header list of 2csk.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN TRANSPORT 22-MAY-05 2CSK
TITLE SOLUTION STRUCTURE OF PX DOMAIN FROM HUMAN SNX12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SORTING NEXIN 12;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PX 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: SNX12;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040308-51;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS SNX12, PX DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SUETAKE,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSK 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CSK 1 VERSN
REVDAT 1 22-NOV-05 2CSK 0
JRNL AUTH T.SUETAKE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF PX DOMAIN FROM HUMAN SNX12
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 2CSK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024576.
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 : 0.54MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D10-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 : 900 MHZ; 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 0.927, 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 VIOLATION, 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 O ILE A 108 H ALA A 112 1.49
REMARK 500 O PHE A 16 H GLU A 32 1.53
REMARK 500 O ASP A 55 H TRP A 58 1.56
REMARK 500 O GLU A 105 HD21 ASN A 109 1.57
REMARK 500 O GLU A 98 H GLN A 102 1.58
REMARK 500 O GLU A 99 H GLY A 103 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 -60.22 -142.58
REMARK 500 1 SER A 3 172.54 60.31
REMARK 500 1 SER A 8 133.67 61.87
REMARK 500 1 ASN A 17 63.83 65.17
REMARK 500 1 ALA A 26 28.85 45.99
REMARK 500 1 GLU A 64 40.32 -88.81
REMARK 500 1 ARG A 65 -67.28 -90.14
REMARK 500 1 ASP A 66 104.05 172.91
REMARK 500 1 SER A 67 36.91 -179.50
REMARK 500 1 LYS A 68 28.22 42.06
REMARK 500 1 ALA A 78 124.54 179.07
REMARK 500 1 LEU A 79 88.32 -170.91
REMARK 500 1 LYS A 80 65.89 -172.54
REMARK 500 1 PHE A 85 -46.39 -133.19
REMARK 500 1 LEU A 127 -90.82 -107.86
REMARK 500 1 ARG A 134 129.24 -37.90
REMARK 500 1 LYS A 140 -62.00 70.16
REMARK 500 1 SER A 141 80.10 40.14
REMARK 500 1 SER A 145 88.93 40.31
REMARK 500 2 SER A 5 94.67 -169.72
REMARK 500 2 ASN A 17 68.38 66.98
REMARK 500 2 ALA A 26 -35.47 176.23
REMARK 500 2 ARG A 27 -164.36 -55.77
REMARK 500 2 GLU A 62 -35.10 -39.84
REMARK 500 2 ASP A 66 105.20 -176.62
REMARK 500 2 SER A 67 123.07 171.15
REMARK 500 2 LYS A 77 152.51 177.01
REMARK 500 2 ALA A 78 82.17 56.47
REMARK 500 2 GLN A 82 112.72 -174.17
REMARK 500 2 ARG A 86 119.95 -172.00
REMARK 500 2 ILE A 91 89.14 39.60
REMARK 500 2 PHE A 92 -64.84 -152.42
REMARK 500 2 GLN A 128 -54.58 77.34
REMARK 500 2 ASN A 135 41.33 -109.14
REMARK 500 2 SER A 141 -71.71 -73.58
REMARK 500 3 SER A 5 -60.40 -90.56
REMARK 500 3 SER A 6 111.01 59.00
REMARK 500 3 ASN A 17 65.08 68.78
REMARK 500 3 ARG A 25 -57.19 170.87
REMARK 500 3 ARG A 27 177.99 -56.30
REMARK 500 3 SER A 54 -32.58 -37.45
REMARK 500 3 GLU A 64 43.32 -86.97
REMARK 500 3 ASP A 66 49.61 173.47
REMARK 500 3 SER A 67 -147.01 -123.55
REMARK 500 3 LEU A 79 81.10 63.84
REMARK 500 3 ASP A 88 -32.30 169.13
REMARK 500 3 GLU A 89 -54.36 -126.82
REMARK 500 3 ILE A 91 86.40 39.45
REMARK 500 3 PHE A 92 -43.05 -165.49
REMARK 500 3 GLN A 128 -55.57 75.12
REMARK 500
REMARK 500 THIS ENTRY HAS 367 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003053 RELATED DB: TARGETDB
DBREF 2CSK A 8 140 UNP Q9UMY4 SNX12_HUMAN 27 159
SEQADV 2CSK GLY A 1 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 2 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 3 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK GLY A 4 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 5 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 6 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK GLY A 7 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 141 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK GLY A 142 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK PRO A 143 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 144 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK SER A 145 UNP Q9UMY4 CLONING ARTIFACT
SEQADV 2CSK GLY A 146 UNP Q9UMY4 CLONING ARTIFACT
SEQRES 1 A 146 GLY SER SER GLY SER SER GLY SER ASN PHE LEU GLU ILE
SEQRES 2 A 146 ASP ILE PHE ASN PRO GLN THR VAL GLY VAL GLY ARG ALA
SEQRES 3 A 146 ARG PHE THR THR TYR GLU VAL ARG MET ARG THR ASN LEU
SEQRES 4 A 146 PRO ILE PHE LYS LEU LYS GLU SER CYS VAL ARG ARG ARG
SEQRES 5 A 146 TYR SER ASP PHE GLU TRP LEU LYS ASN GLU LEU GLU ARG
SEQRES 6 A 146 ASP SER LYS ILE VAL VAL PRO PRO LEU PRO GLY LYS ALA
SEQRES 7 A 146 LEU LYS ARG GLN LEU PRO PHE ARG GLY ASP GLU GLY ILE
SEQRES 8 A 146 PHE GLU GLU SER PHE ILE GLU GLU ARG ARG GLN GLY LEU
SEQRES 9 A 146 GLU GLN PHE ILE ASN LYS ILE ALA GLY HIS PRO LEU ALA
SEQRES 10 A 146 GLN ASN GLU ARG CYS LEU HIS MET PHE LEU GLN GLU GLU
SEQRES 11 A 146 ALA ILE ASP ARG ASN TYR VAL PRO GLY LYS SER GLY PRO
SEQRES 12 A 146 SER SER GLY
HELIX 1 1 ARG A 52 GLU A 64 1 13
HELIX 2 2 GLU A 93 HIS A 114 1 22
HELIX 3 3 HIS A 114 GLU A 120 1 7
HELIX 4 4 GLU A 120 LEU A 127 1 8
SHEET 1 A 3 GLU A 12 VAL A 21 0
SHEET 2 A 3 PHE A 28 ARG A 36 -1 O GLU A 32 N PHE A 16
SHEET 3 A 3 GLU A 46 ARG A 51 -1 O VAL A 49 N VAL A 33
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