Header list of 1yvc.pdb file
Complete list - 2 20 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-FEB-05 1YVC TITLE SOLUTION STRUCTURE OF THE CONSERVED PROTEIN FROM THE GENE LOCUS TITLE 2 MMP0076 OF METHANOCOCCUS MARIPALUDIS. NORTHEAST STRUCTURAL GENOMICS TITLE 3 TARGET MRR5. COMPND MOL_ID: 1; COMPND 2 MOLECULE: MRR5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: GENE LOCUS MMP0076; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCOCCUS MARIPALUDIS; SOURCE 3 ORGANISM_TAXID: 39152; SOURCE 4 GENE: LOCUS MMP0076; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21MGK; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MRR5-21.2 KEYWDS MRR5, AUTOSTRUCTURE, AUTOASSIGN, NORTHEAST STRUCTURAL GENOMICS, KEYWDS 2 AUTOQF, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL KEYWDS 3 GENOMICS CONSORTIUM, NESG, STRUCTURAL GENOMICS, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG),P.ROSSI,J.M.ARAMINI, AUTHOR 2 R.XIAO,C.K.HO,L.C.MA,T.B.ACTON,G.T.MONTELIONE REVDAT 3 02-MAR-22 1YVC 1 REMARK REVDAT 2 24-FEB-09 1YVC 1 VERSN REVDAT 1 05-APR-05 1YVC 0 JRNL AUTH P.ROSSI,J.M.ARAMINI,R.XIAO,C.K.HO,L.C.MA,T.B.ACTON, JRNL AUTH 2 G.T.MONTELIONE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AUTOSTRUCTURE 2.1.0 REMARK 3 AUTHORS : HUANG (RUTGERS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YVC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000031961. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293; 293 REMARK 210 PH : 4.5; 4.5 REMARK 210 IONIC STRENGTH : 100 MM NACL; 100 MM NACL REMARK 210 PRESSURE : ATMOSPHERIC ATM; ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 1.1MM MRR5 U-15N, 5%13C, 10MM REMARK 210 DTT, 5MM CACL2, 100MM NACL, 20MM REMARK 210 NH4OAC, 0.02% NAN3, PH 4.5; REMARK 210 1.2MM MRR5 U-13C,15N, 10MM DTT, REMARK 210 5MM CACL2, 100MM NACL, 20MM REMARK 210 NH4OAC, 0.02% NAN3, PH 4.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HCCH-COSY,; HI- REMARK 210 RES CH-HSQC(ST. ME ASSIGN), HNHA, REMARK 210 HETNOE; TR BACKBONE, H,C_TOCSYS, REMARK 210 NH-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1, XWINNMR 3.5, NMRPIPE REMARK 210 2.1, SPARKY 3.91, AUTOASSIGN REMARK 210 1.15.1, AUTOSTRUCTURE 2.1.0 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 56 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: CS ASSIGN: AUTOASSIGN (BB), HCCH-COSY + TOCSYS (SC), REMARK 210 AUTOSTRUCTURE (NOE), HYPER (DIHE), DYANA,XPLOR,CNS(IMP. H2O) REMARK 210 (SIM. ANNEALING) AUTOQF QUALITY FACTOR CALC. 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 OD2 ASP A 25 HH21 ARG A 35 1.56 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 ALA A 7 -165.14 63.55 REMARK 500 1 MET A 8 39.80 -99.26 REMARK 500 1 ASN A 10 99.10 60.52 REMARK 500 1 ILE A 23 61.60 -110.67 REMARK 500 1 ASP A 37 16.46 58.20 REMARK 500 1 ASN A 45 20.35 -142.54 REMARK 500 1 LYS A 60 -164.17 -106.01 REMARK 500 2 ALA A 2 -80.86 -106.68 REMARK 500 2 LYS A 28 -79.27 -164.76 REMARK 500 2 ASP A 37 -4.14 67.06 REMARK 500 2 ASN A 45 21.43 -152.04 REMARK 500 3 ALA A 7 -144.10 -98.26 REMARK 500 3 LYS A 9 85.23 54.50 REMARK 500 3 ASN A 10 40.84 -81.55 REMARK 500 3 VAL A 11 106.25 -160.58 REMARK 500 3 LYS A 28 78.57 -170.20 REMARK 500 3 LYS A 60 -164.74 -112.82 REMARK 500 4 PHE A 3 -37.63 -155.64 REMARK 500 4 ALA A 7 -177.09 65.69 REMARK 500 4 VAL A 11 111.84 -160.87 REMARK 500 4 ALA A 15 96.74 -67.09 REMARK 500 4 ILE A 23 59.59 -104.39 REMARK 500 4 LYS A 28 14.57 57.20 REMARK 500 5 LYS A 5 90.96 -166.13 REMARK 500 5 PRO A 6 29.08 -78.58 REMARK 500 5 ALA A 7 -153.37 -157.59 REMARK 500 5 MET A 8 21.13 81.48 REMARK 500 5 ILE A 23 64.66 -118.62 REMARK 500 5 ARG A 68 108.06 -54.03 REMARK 500 6 PHE A 3 39.95 -85.34 REMARK 500 6 ALA A 7 -147.68 61.97 REMARK 500 6 LYS A 9 71.42 -115.09 REMARK 500 6 ASN A 10 110.32 72.98 REMARK 500 6 ILE A 23 65.33 -119.10 REMARK 500 6 PRO A 44 5.27 -68.12 REMARK 500 6 ASN A 45 14.61 -143.43 REMARK 500 6 LYS A 60 -150.21 -109.47 REMARK 500 6 GLU A 61 -76.89 -70.78 REMARK 500 7 LYS A 5 95.34 61.51 REMARK 500 7 PRO A 6 -162.84 -79.88 REMARK 500 7 LYS A 9 -90.80 63.90 REMARK 500 7 ILE A 23 59.53 -111.77 REMARK 500 7 LYS A 28 79.88 -163.71 REMARK 500 7 PHE A 63 142.25 78.89 REMARK 500 8 LYS A 5 74.66 57.92 REMARK 500 8 ALA A 7 127.61 70.70 REMARK 500 8 ILE A 23 65.91 -114.45 REMARK 500 8 LYS A 60 -165.26 -109.15 REMARK 500 9 ALA A 7 77.57 59.90 REMARK 500 9 ASN A 10 36.56 -82.42 REMARK 500 REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MRR5 RELATED DB: TARGETDB DBREF 1YVC A 1 69 UNP Q6M142 Q6M142_METMP 1 69 SEQRES 1 A 70 MET ALA PHE GLY LYS PRO ALA MET LYS ASN VAL PRO VAL SEQRES 2 A 70 GLU ALA GLY LYS GLU TYR GLU VAL THR ILE GLU ASP MET SEQRES 3 A 70 GLY LYS GLY GLY ASP GLY ILE ALA ARG ILE ASP GLY PHE SEQRES 4 A 70 VAL VAL PHE VAL PRO ASN ALA GLU LYS GLY SER VAL ILE SEQRES 5 A 70 ASN VAL LYS VAL THR ALA VAL LYS GLU LYS PHE ALA PHE SEQRES 6 A 70 ALA GLU ARG VAL LEU SHEET 1 A 6 GLU A 18 THR A 22 0 SHEET 2 A 6 VAL A 51 VAL A 59 -1 O ILE A 52 N VAL A 21 SHEET 3 A 6 ALA A 64 ARG A 68 -1 O GLU A 67 N LYS A 55 SHEET 4 A 6 PHE A 39 VAL A 43 1 N PHE A 42 O ALA A 66 SHEET 5 A 6 GLY A 32 ILE A 36 -1 N GLY A 32 O VAL A 43 SHEET 6 A 6 ASP A 25 MET A 26 -1 N ASP A 25 O ILE 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 - 2 20 Bytes