Header list of 1nwb.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 05-FEB-03 1NWB TITLE SOLUTION NMR STRUCTURE OF PROTEIN AQ_1857 FROM AQUIFEX AEOLICUS: TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET QR6. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN AQ_1857; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS; SOURCE 3 ORGANISM_TAXID: 63363; SOURCE 4 GENE: AQ_1857; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS QR6, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NESG, REDUCED KEYWDS 2 DIMENSIONALITY NMR, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, KEYWDS 3 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.XU,G.LIU,R.XIAO,T.ACTON,G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 5 23-FEB-22 1NWB 1 REMARK SEQADV REVDAT 4 24-FEB-09 1NWB 1 VERSN REVDAT 3 25-JAN-05 1NWB 1 AUTHOR KEYWDS REMARK REVDAT 2 07-SEP-04 1NWB 1 JRNL REVDAT 1 03-JUN-03 1NWB 0 JRNL AUTH D.XU,G.LIU,R.XIAO,T.ACTON,S.GOLDSMITH-FISCHMAN,B.HONIG, JRNL AUTH 2 G.T.MONTELIONE,T.SZYPERSKI JRNL TITL NMR STRUCTURE OF THE HYPOTHETICAL PROTEIN AQ-1857 ENCODED BY JRNL TITL 2 THE Y157 GENE FROM AQUIFEX AEOLICUS REVEALS A NOVEL PROTEIN JRNL TITL 3 FOLD. JRNL REF PROTEINS V. 54 794 2004 JRNL REFN ISSN 0887-3585 JRNL PMID 14997575 JRNL DOI 10.1002/PROT.10424 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, CYANA 1.0.3 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NWB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-03. REMARK 100 THE DEPOSITION ID IS D_1000018278. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293; 293 REMARK 210 PH : 6.5; 6.5 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.08MM QR6 U-15N,13C; 1.01MM QR6 REMARK 210 100% 15N, 5%13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; CT-13C- REMARK 210 HSQC; 3D-HNNCACB; 3D-RD- REMARK 210 HABCABCONHN; 3D-RD-HCCH-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.0, XEASY 1.3.1, PROSA REMARK 210 5.0, CYANA 1.0.3 REMARK 210 METHOD USED : DISTANCE GEOMETRY TORSION ANGLE REMARK 210 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 REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED WITH THE HELP OF REDUCED REMARK 210 DIMENSIONALITY NMR SPECTROSCOPY 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 ASN A 102 REMARK 465 ALA A 103 REMARK 465 THR A 104 REMARK 465 GLY A 105 REMARK 465 SER A 106 REMARK 465 CYS A 107 REMARK 465 GLY A 108 REMARK 465 CYS A 109 REMARK 465 GLY A 110 REMARK 465 SER A 111 REMARK 465 SER A 112 REMARK 465 PHE A 113 REMARK 465 SER A 114 REMARK 465 CYS A 115 REMARK 465 GLY A 116 REMARK 465 LEU A 117 REMARK 465 GLU A 118 REMARK 465 HIS A 119 REMARK 465 HIS A 120 REMARK 465 HIS A 121 REMARK 465 HIS A 122 REMARK 465 HIS A 123 REMARK 465 HIS A 124 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 MET A 1 N 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 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 GLN A 2 171.49 171.56 REMARK 500 1 GLN A 6 126.84 -173.38 REMARK 500 1 ASN A 31 66.82 -150.71 REMARK 500 1 GLU A 58 47.32 -81.08 REMARK 500 1 HIS A 61 88.63 -64.97 REMARK 500 1 TYR A 65 -167.25 -112.43 REMARK 500 1 ASP A 66 70.73 -66.53 REMARK 500 1 VAL A 80 33.37 -151.85 REMARK 500 1 PHE A 91 -140.27 35.06 REMARK 500 2 ASN A 31 66.04 -151.35 REMARK 500 2 PHE A 46 106.33 57.26 REMARK 500 2 TYR A 65 -165.52 -113.75 REMARK 500 2 ASP A 66 71.48 -66.15 REMARK 500 2 ASP A 73 158.72 -47.27 REMARK 500 2 ALA A 83 -178.85 -54.20 REMARK 500 2 PHE A 91 -140.51 35.25 REMARK 500 3 GLN A 2 90.30 -61.67 REMARK 500 3 THR A 13 170.60 -58.55 REMARK 500 3 PHE A 46 99.72 -169.30 REMARK 500 3 GLU A 58 40.42 -83.30 REMARK 500 3 HIS A 61 81.63 -65.01 REMARK 500 3 TYR A 65 -167.22 -113.76 REMARK 500 3 ASP A 66 70.29 -68.62 REMARK 500 3 ASP A 73 161.94 -44.96 REMARK 500 3 ALA A 83 176.52 -55.46 REMARK 500 3 ASP A 90 -149.05 -166.57 REMARK 500 4 GLN A 6 130.58 -177.69 REMARK 500 4 ASN A 31 75.08 -151.18 REMARK 500 4 TYR A 65 -162.88 -120.29 REMARK 500 4 ASP A 66 70.83 -66.96 REMARK 500 4 PHE A 91 -139.89 35.35 REMARK 500 5 GLN A 4 79.47 -69.46 REMARK 500 5 GLN A 6 118.59 -173.15 REMARK 500 5 ASN A 31 66.16 -151.30 REMARK 500 5 THR A 55 160.35 -42.61 REMARK 500 5 TYR A 65 -166.62 -122.57 REMARK 500 5 ASP A 66 70.89 -67.15 REMARK 500 5 PHE A 91 -140.54 35.24 REMARK 500 6 GLN A 2 -174.84 175.97 REMARK 500 6 ASN A 31 72.40 -151.47 REMARK 500 6 HIS A 61 97.60 -65.13 REMARK 500 6 TYR A 65 -168.42 -101.21 REMARK 500 6 ASP A 66 70.87 -67.38 REMARK 500 6 ASP A 90 -149.74 -165.66 REMARK 500 7 GLN A 2 65.48 76.57 REMARK 500 7 ALA A 5 100.57 -55.30 REMARK 500 7 THR A 13 170.56 -57.94 REMARK 500 7 ASN A 31 66.18 -151.24 REMARK 500 7 PHE A 46 100.33 60.85 REMARK 500 7 HIS A 61 93.14 -64.29 REMARK 500 REMARK 500 THIS ENTRY HAS 161 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5683 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT REMARK 900 RELATED ID: QR6 RELATED DB: TARGETDB DBREF 1NWB A 1 116 UNP O67709 Y1857_AQUAE 1 116 SEQADV 1NWB LEU A 117 UNP O67709 EXPRESSION TAG SEQADV 1NWB GLU A 118 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 119 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 120 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 121 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 122 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 123 UNP O67709 EXPRESSION TAG SEQADV 1NWB HIS A 124 UNP O67709 EXPRESSION TAG SEQRES 1 A 124 MET GLN GLU GLN ALA GLN GLN PHE ILE PHE LYS VAL THR SEQRES 2 A 124 ASP LYS ALA VAL GLU GLU ILE LYS LYS VAL ALA GLN GLU SEQRES 3 A 124 ASN ASN ILE GLU ASN PRO ILE LEU ARG ILE ARG VAL VAL SEQRES 4 A 124 PRO GLY GLY CYS SER GLY PHE GLN TYR ALA MET GLY PHE SEQRES 5 A 124 ASP ASP THR VAL GLU GLU GLY ASP HIS VAL PHE GLU TYR SEQRES 6 A 124 ASP GLY VAL LYS VAL VAL ILE ASP PRO PHE SER MET PRO SEQRES 7 A 124 TYR VAL ASN GLY ALA GLU LEU ASP TYR VAL VAL ASP PHE SEQRES 8 A 124 MET GLY GLY GLY PHE THR ILE ARG ASN PRO ASN ALA THR SEQRES 9 A 124 GLY SER CYS GLY CYS GLY SER SER PHE SER CYS GLY LEU SEQRES 10 A 124 GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 THR A 13 GLU A 26 1 14 HELIX 2 2 SER A 76 VAL A 80 5 5 SHEET 1 A 3 LYS A 11 VAL A 12 0 SHEET 2 A 3 GLU A 84 ASP A 90 1 O LEU A 85 N LYS A 11 SHEET 3 A 3 GLY A 93 ARG A 99 -1 O GLY A 93 N ASP A 90 SHEET 1 B 3 PHE A 52 ASP A 53 0 SHEET 2 B 3 ILE A 33 ILE A 36 -1 N ILE A 33 O ASP A 53 SHEET 3 B 3 LYS A 69 ILE A 72 1 O VAL A 71 N LEU A 34 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 - b 23 2 Bytes