Header list of 2cpt.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN TRANSPORT 19-MAY-05 2CPT
TITLE SOLUTION STRUCTURE OF MIT DOMAIN FROM HUMAN SKD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VACUOLAR SORTING PROTEIN 4B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MIT DOMAIN;
COMPND 5 SYNONYM: SKD1 PROTEIN;
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: VPS4B, SKD1, VPS42;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040607-08;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS MIT, SKD1, HELIX BUNDLE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL 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 2CPT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CPT 1 VERSN
REVDAT 1 19-NOV-05 2CPT 0
JRNL AUTH T.SUETAKE,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF MIT DOMAIN FROM HUMAN SKD1
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 2CPT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024486.
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 : 1.11MM 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 2.0.17
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: 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 5 99.81 -45.74
REMARK 500 1 SER A 6 120.74 -172.11
REMARK 500 1 SER A 10 104.55 -57.71
REMARK 500 1 GLU A 55 37.76 -83.16
REMARK 500 1 ALA A 56 -177.72 -65.28
REMARK 500 1 GLN A 57 -63.87 -127.97
REMARK 500 1 ASP A 59 -38.55 -38.94
REMARK 500 1 GLU A 77 -39.73 -39.28
REMARK 500 1 LYS A 89 137.94 -37.55
REMARK 500 1 GLU A 104 151.70 -35.17
REMARK 500 1 LYS A 105 165.46 -43.76
REMARK 500 1 ASN A 107 161.10 -43.85
REMARK 500 1 SER A 116 92.66 -50.11
REMARK 500 2 SER A 6 122.27 -174.08
REMARK 500 2 SER A 9 42.26 -92.13
REMARK 500 2 SER A 12 155.77 -40.78
REMARK 500 2 HIS A 50 -39.89 -39.84
REMARK 500 2 GLU A 55 35.45 -84.00
REMARK 500 2 GLN A 57 -72.02 -100.84
REMARK 500 2 GLN A 63 -37.17 -37.75
REMARK 500 2 LEU A 79 -32.56 -38.10
REMARK 500 2 LYS A 88 94.19 -52.46
REMARK 500 2 ALA A 90 105.94 -51.15
REMARK 500 2 VAL A 94 76.90 -113.96
REMARK 500 2 PRO A 99 -166.90 -69.82
REMARK 500 2 ALA A 102 105.40 -50.84
REMARK 500 2 PRO A 114 -178.40 -69.70
REMARK 500 3 SER A 3 42.08 39.37
REMARK 500 3 SER A 6 98.57 -61.23
REMARK 500 3 GLU A 55 39.67 -83.10
REMARK 500 3 ALA A 56 161.37 -47.17
REMARK 500 3 GLU A 87 173.49 -49.77
REMARK 500 3 LYS A 89 97.69 -38.16
REMARK 500 3 GLN A 91 75.91 -66.68
REMARK 500 3 VAL A 94 135.64 -37.88
REMARK 500 3 GLU A 96 91.32 -68.47
REMARK 500 3 PRO A 99 -175.35 -69.72
REMARK 500 3 ASP A 110 136.19 -171.74
REMARK 500 3 PRO A 114 -177.64 -69.78
REMARK 500 4 SER A 3 152.87 -47.75
REMARK 500 4 GLU A 55 38.88 -82.65
REMARK 500 4 LYS A 92 144.90 -38.92
REMARK 500 5 SER A 12 154.40 -47.22
REMARK 500 5 ALA A 56 155.99 -41.86
REMARK 500 5 GLN A 57 -64.01 -108.77
REMARK 500 5 GLN A 91 98.06 -60.96
REMARK 500 6 GLU A 55 40.01 -82.21
REMARK 500 6 GLN A 57 -67.21 -125.29
REMARK 500 6 LYS A 60 -70.43 -58.27
REMARK 500 6 LEU A 79 -30.59 -36.06
REMARK 500
REMARK 500 THIS ENTRY HAS 189 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000811.1 RELATED DB: TARGETDB
DBREF 2CPT A 8 111 UNP O75351 VPS4B_HUMAN 1 104
SEQADV 2CPT GLY A 1 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 2 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 3 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT GLY A 4 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 5 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 6 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT GLY A 7 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 112 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT GLY A 113 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT PRO A 114 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 115 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT SER A 116 UNP O75351 CLONING ARTIFACT
SEQADV 2CPT GLY A 117 UNP O75351 CLONING ARTIFACT
SEQRES 1 A 117 GLY SER SER GLY SER SER GLY MET SER SER THR SER PRO
SEQRES 2 A 117 ASN LEU GLN LYS ALA ILE ASP LEU ALA SER LYS ALA ALA
SEQRES 3 A 117 GLN GLU ASP LYS ALA GLY ASN TYR GLU GLU ALA LEU GLN
SEQRES 4 A 117 LEU TYR GLN HIS ALA VAL GLN TYR PHE LEU HIS VAL VAL
SEQRES 5 A 117 LYS TYR GLU ALA GLN GLY ASP LYS ALA LYS GLN SER ILE
SEQRES 6 A 117 ARG ALA LYS CYS THR GLU TYR LEU ASP ARG ALA GLU LYS
SEQRES 7 A 117 LEU LYS GLU TYR LEU LYS ASN LYS GLU LYS LYS ALA GLN
SEQRES 8 A 117 LYS PRO VAL LYS GLU GLY GLN PRO SER PRO ALA ASP GLU
SEQRES 9 A 117 LYS GLY ASN ASP SER ASP GLY SER GLY PRO SER SER GLY
HELIX 1 1 SER A 12 GLY A 32 1 21
HELIX 2 2 ASN A 33 TYR A 54 1 22
HELIX 3 3 GLY A 58 GLU A 87 1 30
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