Header list of 1wlm.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-JUN-04 1WLM
TITLE SOLUTION STRUCTURE OF MOUSE CGI-38 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN CGI-38;
COMPND 3 CHAIN: A;
COMPND 4 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 2700055K07;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020902-43;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CGI-38, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.KOBAYASHI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WLM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WLM 1 VERSN
REVDAT 1 12-JUL-05 1WLM 0
JRNL AUTH N.KOBAYASHI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF MOUSE CGI-38 PROTEIN
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, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WLM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023712.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.23MM CGI-38 PROTEIN U-13C,
REMARK 210 15N; 20MM PHOSPHATE BUFFER NA
REMARK 210 (PH6.0); 100MM NACL; 1MM D-DTT;
REMARK 210 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.902, 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 VIOLATIONS, 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 SER A 98 H ALA A 102 1.51
REMARK 500 O ASN A 41 H LEU A 45 1.58
REMARK 500 O ASN A 78 H PHE A 82 1.59
REMARK 500 O PHE A 21 H ALA A 25 1.60
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 3 138.25 61.81
REMARK 500 1 SER A 6 145.47 61.73
REMARK 500 1 ALA A 9 159.77 171.35
REMARK 500 1 SER A 11 113.58 -161.99
REMARK 500 1 ALA A 15 71.41 63.40
REMARK 500 1 LEU A 17 -73.31 -55.85
REMARK 500 1 ASP A 29 105.85 -43.01
REMARK 500 1 LYS A 55 -78.03 -75.18
REMARK 500 1 LYS A 70 -164.67 -75.59
REMARK 500 1 LYS A 95 -135.96 -60.94
REMARK 500 1 ILE A 110 -65.47 -92.42
REMARK 500 1 ALA A 116 161.73 -43.65
REMARK 500 1 ILE A 118 118.52 61.34
REMARK 500 1 LYS A 122 123.69 -175.02
REMARK 500 1 ALA A 123 -179.35 176.97
REMARK 500 1 LYS A 124 113.52 -168.39
REMARK 500 1 ARG A 131 177.48 171.49
REMARK 500 1 LEU A 132 108.35 173.29
REMARK 500 1 SER A 136 101.00 52.37
REMARK 500 1 SER A 149 -56.58 -171.77
REMARK 500 2 SER A 3 109.96 -175.61
REMARK 500 2 SER A 6 164.40 -47.30
REMARK 500 2 ILE A 14 -151.71 -104.55
REMARK 500 2 ALA A 15 73.76 176.00
REMARK 500 2 LEU A 17 -72.42 -52.48
REMARK 500 2 HIS A 27 119.26 -39.01
REMARK 500 2 ASP A 29 105.55 -167.80
REMARK 500 2 ALA A 32 126.99 -39.53
REMARK 500 2 ALA A 52 75.38 -105.96
REMARK 500 2 LYS A 55 -76.16 -77.58
REMARK 500 2 LYS A 70 -168.11 -100.97
REMARK 500 2 LYS A 95 -148.88 -60.19
REMARK 500 2 LYS A 97 177.79 -49.03
REMARK 500 2 ILE A 110 -62.98 -98.51
REMARK 500 2 ALA A 111 115.82 -39.38
REMARK 500 2 PRO A 115 -158.51 -75.03
REMARK 500 2 ALA A 116 -176.69 73.41
REMARK 500 2 ASN A 117 79.57 -111.73
REMARK 500 2 ILE A 118 117.55 60.69
REMARK 500 2 LYS A 143 154.41 67.81
REMARK 500 2 GLU A 144 -57.42 177.27
REMARK 500 2 ARG A 145 130.72 -38.85
REMARK 500 2 SER A 146 111.71 -174.99
REMARK 500 3 SER A 2 -58.24 -128.36
REMARK 500 3 MET A 8 99.93 50.62
REMARK 500 3 SER A 11 110.36 -165.83
REMARK 500 3 ILE A 14 -71.68 -46.05
REMARK 500 3 ALA A 15 71.29 69.77
REMARK 500 3 LEU A 17 -81.96 -57.88
REMARK 500 3 HIS A 27 103.59 -39.06
REMARK 500
REMARK 500 THIS ENTRY HAS 507 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007015745.1 RELATED DB: TARGETDB
DBREF 1WLM A 8 145 UNP Q9CRB6 CG38_MOUSE 1 138
SEQADV 1WLM GLY A 1 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 2 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 3 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM GLY A 4 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 5 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 6 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM GLY A 7 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 146 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM GLY A 147 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM PRO A 148 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 149 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM SER A 150 UNP Q9CRB6 CLONING ARTIFACT
SEQADV 1WLM GLY A 151 UNP Q9CRB6 CLONING ARTIFACT
SEQRES 1 A 151 GLY SER SER GLY SER SER GLY MET ALA ALA SER THR ASP
SEQRES 2 A 151 ILE ALA GLY LEU GLU GLU SER PHE ARG LYS PHE ALA ILE
SEQRES 3 A 151 HIS GLY ASP PRO LYS ALA SER GLY GLN GLU MET ASN GLY
SEQRES 4 A 151 LYS ASN TRP ALA LYS LEU CYS LYS ASP CYS LYS VAL ALA
SEQRES 5 A 151 ASP GLY LYS ALA VAL THR GLY THR ASP VAL ASP ILE VAL
SEQRES 6 A 151 PHE SER LYS VAL LYS ALA LYS SER ALA ARG VAL ILE ASN
SEQRES 7 A 151 TYR GLU GLU PHE LYS LYS ALA LEU GLU GLU LEU ALA THR
SEQRES 8 A 151 LYS ARG PHE LYS GLY LYS SER LYS GLU GLU ALA PHE ASP
SEQRES 9 A 151 ALA ILE CYS GLN LEU ILE ALA GLY LYS GLU PRO ALA ASN
SEQRES 10 A 151 ILE GLY VAL THR LYS ALA LYS THR GLY GLY ALA VAL ASP
SEQRES 11 A 151 ARG LEU THR ASP THR SER LYS TYR THR GLY SER HIS LYS
SEQRES 12 A 151 GLU ARG SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 16 ILE A 26 1 11
HELIX 2 2 GLY A 39 CYS A 49 1 11
HELIX 3 3 THR A 58 LYS A 70 1 13
HELIX 4 4 TYR A 79 LEU A 89 1 11
HELIX 5 5 LEU A 89 PHE A 94 1 6
HELIX 6 6 SER A 98 ALA A 111 1 14
SHEET 1 A 2 GLU A 36 ASN A 38 0
SHEET 2 A 2 VAL A 76 ASN A 78 -1 O ILE A 77 N MET A 37
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