Header list of 2cri.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSPORT PROTEIN 20-MAY-05 2CRI TITLE SOLUTION STRUCTURE OF THE MSP DOMAIN OF MOUSE VAMP-ASSOCIATED PROTEINA COMPND MOL_ID: 1; COMPND 2 MOLECULE: VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: MSP (RESIDUES 1-147); COMPND 5 SYNONYM: VAMP- ASSOCIATED PROTEIN A, VAMP-A, VAP-A, 33 KDA VAMP- COMPND 6 ASSOCIATED PROTEIN, VAP-33; COMPND 7 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: VAPA, VAP33; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040329-04; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS VAP-A, VAP-33, BETA SANDWITCH FOLD, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSPORT KEYWDS 4 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CRI 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CRI 1 VERSN REVDAT 1 20-NOV-05 2CRI 0 JRNL AUTH H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE MSP DOMAIN OF MOUSE JRNL TITL 2 VAMP-ASSOCIATED PROTEINA 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 2CRI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024544. 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 : 120 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.52MM 13C,15N-LABELED PROTEIN; REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM REMARK 210 NACL; 1MM 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; 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 0.9296, 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 : 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 : 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 21 -75.29 -76.56 REMARK 500 1 PRO A 28 -177.25 -69.77 REMARK 500 1 ASP A 69 151.73 -41.71 REMARK 500 1 ASP A 84 95.76 -68.92 REMARK 500 1 LYS A 92 -64.47 -99.86 REMARK 500 1 HIS A 93 148.31 -37.97 REMARK 500 1 ILE A 106 97.20 -47.51 REMARK 500 1 ASN A 134 87.35 -52.61 REMARK 500 1 LYS A 138 141.49 -39.54 REMARK 500 1 SER A 142 35.04 -94.23 REMARK 500 1 SER A 146 157.68 -46.14 REMARK 500 2 SER A 21 -75.62 -77.99 REMARK 500 2 ALA A 55 67.15 -115.41 REMARK 500 2 ASP A 69 149.86 -36.90 REMARK 500 2 TYR A 85 101.31 -57.03 REMARK 500 2 GLU A 89 57.43 -108.96 REMARK 500 2 LYS A 90 42.53 -93.71 REMARK 500 2 LYS A 92 117.14 -172.37 REMARK 500 2 SER A 107 -61.26 -106.93 REMARK 500 2 LYS A 138 109.17 -37.52 REMARK 500 3 HIS A 11 54.48 -95.98 REMARK 500 3 SER A 21 -76.47 -82.73 REMARK 500 3 PHE A 29 30.65 -92.13 REMARK 500 3 LYS A 46 150.45 -45.54 REMARK 500 3 ASP A 84 105.74 -59.35 REMARK 500 3 LYS A 90 51.04 39.78 REMARK 500 3 ILE A 106 99.63 -50.52 REMARK 500 3 PRO A 133 0.06 -69.75 REMARK 500 3 ASN A 140 32.67 38.86 REMARK 500 4 SER A 21 -74.66 -80.58 REMARK 500 4 LYS A 46 135.28 -39.87 REMARK 500 4 SER A 65 147.48 -172.02 REMARK 500 4 LYS A 92 -55.78 -131.30 REMARK 500 4 SER A 107 -65.24 -102.28 REMARK 500 4 PRO A 133 -168.74 -69.76 REMARK 500 4 PRO A 144 0.26 -69.76 REMARK 500 4 SER A 145 139.91 -35.58 REMARK 500 5 LYS A 10 47.34 -102.09 REMARK 500 5 SER A 21 -76.34 -67.06 REMARK 500 5 ALA A 55 79.89 -108.58 REMARK 500 5 ASP A 84 92.40 -64.63 REMARK 500 5 TYR A 85 104.28 -59.53 REMARK 500 5 LYS A 92 -63.90 -129.42 REMARK 500 5 ASN A 105 65.48 -117.75 REMARK 500 5 LEU A 139 -69.21 -126.27 REMARK 500 5 SER A 146 173.58 -48.66 REMARK 500 6 SER A 21 -75.70 -70.23 REMARK 500 6 PRO A 28 -174.50 -69.69 REMARK 500 6 SER A 43 -177.77 -61.89 REMARK 500 6 ILE A 106 52.13 34.44 REMARK 500 REMARK 500 THIS ENTRY HAS 175 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007116377.1 RELATED DB: TARGETDB DBREF 2CRI A 8 141 UNP Q9WV55 VAPA_MOUSE 1 134 SEQADV 2CRI GLY A 1 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 2 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 3 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI GLY A 4 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 5 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 6 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI GLY A 7 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 142 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI GLY A 143 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI PRO A 144 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 145 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI SER A 146 UNP Q9WV55 CLONING ARTIFACT SEQADV 2CRI GLY A 147 UNP Q9WV55 CLONING ARTIFACT SEQRES 1 A 147 GLY SER SER GLY SER SER GLY MET ALA LYS HIS GLU GLN SEQRES 2 A 147 ILE LEU VAL LEU ASP PRO PRO SER ASP LEU LYS PHE LYS SEQRES 3 A 147 GLY PRO PHE THR ASP VAL VAL THR THR ASN LEU LYS LEU SEQRES 4 A 147 GLN ASN PRO SER ASP ARG LYS VAL CYS PHE LYS VAL LYS SEQRES 5 A 147 THR THR ALA PRO ARG ARG TYR CYS VAL ARG PRO ASN SER SEQRES 6 A 147 GLY ILE ILE ASP PRO GLY SER ILE VAL THR VAL SER VAL SEQRES 7 A 147 MET LEU GLN PRO PHE ASP TYR ASP PRO ASN GLU LYS SER SEQRES 8 A 147 LYS HIS LYS PHE MET VAL GLN THR ILE PHE ALA PRO PRO SEQRES 9 A 147 ASN ILE SER ASP MET GLU ALA VAL TRP LYS GLU ALA LYS SEQRES 10 A 147 PRO ASP GLU LEU MET ASP SER LYS LEU ARG CYS VAL PHE SEQRES 11 A 147 GLU MET PRO ASN GLU ASN ASP LYS LEU ASN ASP SER GLY SEQRES 12 A 147 PRO SER SER GLY HELIX 1 1 ASP A 108 ALA A 116 1 9 SHEET 1 A 4 VAL A 16 ASP A 18 0 SHEET 2 A 4 THR A 35 GLN A 40 -1 O LYS A 38 N ASP A 18 SHEET 3 A 4 ILE A 73 LEU A 80 -1 O VAL A 78 N THR A 35 SHEET 4 A 4 TYR A 59 ARG A 62 -1 N CYS A 60 O MET A 79 SHEET 1 B 5 ASP A 22 LYS A 26 0 SHEET 2 B 5 MET A 122 GLU A 131 1 O GLU A 131 N PHE A 25 SHEET 3 B 5 PHE A 95 PHE A 101 -1 N PHE A 95 O LEU A 126 SHEET 4 B 5 VAL A 47 THR A 53 -1 N CYS A 48 O ILE A 100 SHEET 5 B 5 SER A 65 ILE A 67 -1 O GLY A 66 N PHE A 49 CISPEP 1 ASP A 18 PRO A 19 1 0.00 CISPEP 2 GLY A 27 PRO A 28 1 0.07 CISPEP 3 ARG A 62 PRO A 63 1 0.01 CISPEP 4 ASP A 18 PRO A 19 2 0.04 CISPEP 5 GLY A 27 PRO A 28 2 0.04 CISPEP 6 ARG A 62 PRO A 63 2 0.02 CISPEP 7 ASP A 18 PRO A 19 3 0.07 CISPEP 8 GLY A 27 PRO A 28 3 0.03 CISPEP 9 ARG A 62 PRO A 63 3 -0.02 CISPEP 10 ASP A 18 PRO A 19 4 0.07 CISPEP 11 GLY A 27 PRO A 28 4 0.03 CISPEP 12 ARG A 62 PRO A 63 4 -0.01 CISPEP 13 ASP A 18 PRO A 19 5 -0.01 CISPEP 14 GLY A 27 PRO A 28 5 0.11 CISPEP 15 ARG A 62 PRO A 63 5 -0.02 CISPEP 16 ASP A 18 PRO A 19 6 0.10 CISPEP 17 GLY A 27 PRO A 28 6 0.01 CISPEP 18 ARG A 62 PRO A 63 6 -0.03 CISPEP 19 ASP A 18 PRO A 19 7 0.06 CISPEP 20 GLY A 27 PRO A 28 7 0.13 CISPEP 21 ARG A 62 PRO A 63 7 -0.02 CISPEP 22 ASP A 18 PRO A 19 8 -0.02 CISPEP 23 GLY A 27 PRO A 28 8 0.02 CISPEP 24 ARG A 62 PRO A 63 8 -0.07 CISPEP 25 ASP A 18 PRO A 19 9 0.00 CISPEP 26 GLY A 27 PRO A 28 9 0.06 CISPEP 27 ARG A 62 PRO A 63 9 0.03 CISPEP 28 ASP A 18 PRO A 19 10 0.03 CISPEP 29 GLY A 27 PRO A 28 10 0.05 CISPEP 30 ARG A 62 PRO A 63 10 -0.02 CISPEP 31 ASP A 18 PRO A 19 11 0.03 CISPEP 32 GLY A 27 PRO A 28 11 0.08 CISPEP 33 ARG A 62 PRO A 63 11 -0.02 CISPEP 34 ASP A 18 PRO A 19 12 -0.03 CISPEP 35 GLY A 27 PRO A 28 12 0.09 CISPEP 36 ARG A 62 PRO A 63 12 -0.08 CISPEP 37 ASP A 18 PRO A 19 13 -0.02 CISPEP 38 GLY A 27 PRO A 28 13 0.05 CISPEP 39 ARG A 62 PRO A 63 13 -0.02 CISPEP 40 ASP A 18 PRO A 19 14 0.02 CISPEP 41 GLY A 27 PRO A 28 14 0.08 CISPEP 42 ARG A 62 PRO A 63 14 0.03 CISPEP 43 ASP A 18 PRO A 19 15 -0.04 CISPEP 44 GLY A 27 PRO A 28 15 0.05 CISPEP 45 ARG A 62 PRO A 63 15 0.06 CISPEP 46 ASP A 18 PRO A 19 16 -0.02 CISPEP 47 GLY A 27 PRO A 28 16 0.07 CISPEP 48 ARG A 62 PRO A 63 16 0.04 CISPEP 49 ASP A 18 PRO A 19 17 0.08 CISPEP 50 GLY A 27 PRO A 28 17 0.04 CISPEP 51 ARG A 62 PRO A 63 17 -0.05 CISPEP 52 ASP A 18 PRO A 19 18 0.09 CISPEP 53 GLY A 27 PRO A 28 18 0.09 CISPEP 54 ARG A 62 PRO A 63 18 0.05 CISPEP 55 ASP A 18 PRO A 19 19 0.00 CISPEP 56 GLY A 27 PRO A 28 19 0.02 CISPEP 57 ARG A 62 PRO A 63 19 0.06 CISPEP 58 ASP A 18 PRO A 19 20 -0.03 CISPEP 59 GLY A 27 PRO A 28 20 0.02 CISPEP 60 ARG A 62 PRO A 63 20 -0.06 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