Header list of 1orm.pdb file
Complete list - t 27 2 Bytes
HEADER MEMBRANE PROTEIN 14-MAR-03 1ORM TITLE NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES COMPND MOL_ID: 1; COMPND 2 MOLECULE: OUTER MEMBRANE PROTEIN X; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: OUTER MEMBRANE PROTEIN OMPX; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: OMPX; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3B KEYWDS OMPX, MEMBRANE PROTEIN, TROSY, DHPC, DETERGENTS, LIPIDS, MICELLES EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.FERNANDEZ,K.ADEISHVILI,K.WUTHRICH REVDAT 3 27-OCT-21 1ORM 1 REMARK SEQADV REVDAT 2 24-FEB-09 1ORM 1 VERSN REVDAT 1 22-APR-03 1ORM 0 JRNL AUTH C.FERNANDEZ,K.ADEISHVILI,K.WUTHRICH JRNL TITL TRANSVERSE RELAXATION-OPTIMIZED NMR SPECTROSCOPY WITH THE JRNL TITL 2 OUTER MEMBRANE PROTEIN OMPX IN DIHEXANOYL JRNL TITL 3 PHOSPHATIDYLCHOLINE MICELLES JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 2358 2001 JRNL REFN ISSN 0027-8424 JRNL PMID 11226244 JRNL DOI 10.1073/PNAS.051629298 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.FERNANDEZ,C.HILTY,S.BONJOUR,K.ADEISHVILI,K.PERVUSHIN, REMARK 1 AUTH 2 K.WUTHRICH REMARK 1 TITL SOLUTION NMR STUDIES OF THE INTERGRAL MEMBRANE PROTEINS OMPX REMARK 1 TITL 2 AND OMPA FROM ESCHERICHIA COLI REMARK 1 REF FEBS LETT. V. 504 173 2001 REMARK 1 REFN ISSN 0014-5793 REMARK 1 DOI 10.1016/S0014-5793(01)02742-9 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ORM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-03. REMARK 100 THE DEPOSITION ID IS D_1000018598. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE, 100MM REMARK 210 NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM OMPX U-15N,13C,2H REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; TROSY REMARK 210 -TYPE TRIPLE RESONANCE REMARK 210 EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET 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 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 71.55 177.61 REMARK 500 1 GLN A 17 72.41 43.95 REMARK 500 1 MET A 18 46.12 -154.05 REMARK 500 1 MET A 21 -175.54 57.12 REMARK 500 1 TYR A 30 91.65 -167.30 REMARK 500 1 ASP A 33 81.79 52.83 REMARK 500 1 ASN A 34 -45.26 176.52 REMARK 500 1 SER A 35 129.57 -170.59 REMARK 500 1 LEU A 37 127.10 -174.60 REMARK 500 1 SER A 49 -178.29 61.30 REMARK 500 1 ARG A 50 151.35 169.52 REMARK 500 1 SER A 53 -65.39 -164.50 REMARK 500 1 SER A 54 34.09 -170.11 REMARK 500 1 TYR A 57 -63.50 -179.91 REMARK 500 1 ASN A 60 157.28 59.43 REMARK 500 1 ILE A 73 -171.19 46.34 REMARK 500 1 ASN A 74 162.61 57.98 REMARK 500 1 TRP A 76 55.98 -175.22 REMARK 500 1 LYS A 89 77.62 -103.51 REMARK 500 1 GLN A 91 -44.95 175.33 REMARK 500 1 GLU A 94 33.34 -171.27 REMARK 500 1 THR A 97 82.49 74.74 REMARK 500 1 LYS A 99 -173.87 47.91 REMARK 500 1 ASP A 101 63.52 63.59 REMARK 500 1 LEU A 113 71.61 -163.72 REMARK 500 1 ASN A 120 74.86 -171.33 REMARK 500 1 VAL A 121 141.13 -170.90 REMARK 500 1 ARG A 131 48.79 -154.80 REMARK 500 1 ARG A 133 -66.23 68.97 REMARK 500 1 SER A 134 74.85 -166.16 REMARK 500 2 THR A 4 56.13 -165.65 REMARK 500 2 THR A 6 42.28 -178.57 REMARK 500 2 GLN A 11 82.52 -159.11 REMARK 500 2 GLN A 15 -65.78 73.70 REMARK 500 2 GLN A 17 92.16 175.93 REMARK 500 2 LEU A 26 62.28 -163.92 REMARK 500 2 GLU A 32 100.04 -177.61 REMARK 500 2 ASP A 33 -65.39 178.39 REMARK 500 2 ASN A 34 38.63 179.19 REMARK 500 2 VAL A 39 44.82 -142.96 REMARK 500 2 ILE A 40 148.10 -176.90 REMARK 500 2 GLU A 47 149.80 165.32 REMARK 500 2 SER A 49 -175.47 62.90 REMARK 500 2 ARG A 50 -77.39 176.80 REMARK 500 2 THR A 51 148.48 168.99 REMARK 500 2 ALA A 52 30.23 80.16 REMARK 500 2 SER A 53 -47.51 -159.56 REMARK 500 2 ASP A 56 -170.44 174.49 REMARK 500 2 TYR A 57 -64.84 68.13 REMARK 500 2 LYS A 59 -79.76 -129.97 REMARK 500 REMARK 500 THIS ENTRY HAS 873 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QJ8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF OMPX IN THE PRESENCE OF THE DETERGENT N- REMARK 900 OCTYLTETRAOXYETHYLENE REMARK 900 RELATED ID: 1QJ9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF OMPX IN THE PRESENCE OF THE DETERGENT N- REMARK 900 OCTYLTETRAOXYETHYLENE DBREF 1ORM A 1 148 UNP P0A917 OMPX_ECOLI 24 171 SEQADV 1ORM ASN A 100 UNP P0A917 HIS 123 ENGINEERED MUTATION SEQRES 1 A 148 ALA THR SER THR VAL THR GLY GLY TYR ALA GLN SER ASP SEQRES 2 A 148 ALA GLN GLY GLN MET ASN LYS MET GLY GLY PHE ASN LEU SEQRES 3 A 148 LYS TYR ARG TYR GLU GLU ASP ASN SER PRO LEU GLY VAL SEQRES 4 A 148 ILE GLY SER PHE THR TYR THR GLU LYS SER ARG THR ALA SEQRES 5 A 148 SER SER GLY ASP TYR ASN LYS ASN GLN TYR TYR GLY ILE SEQRES 6 A 148 THR ALA GLY PRO ALA TYR ARG ILE ASN ASP TRP ALA SER SEQRES 7 A 148 ILE TYR GLY VAL VAL GLY VAL GLY TYR GLY LYS PHE GLN SEQRES 8 A 148 THR THR GLU TYR PRO THR TYR LYS ASN ASP THR SER ASP SEQRES 9 A 148 TYR GLY PHE SER TYR GLY ALA GLY LEU GLN PHE ASN PRO SEQRES 10 A 148 MET GLU ASN VAL ALA LEU ASP PHE SER TYR GLU GLN SER SEQRES 11 A 148 ARG ILE ARG SER VAL ASP VAL GLY THR TRP ILE ALA GLY SEQRES 12 A 148 VAL GLY TYR ARG PHE SHEET 1 A 2 VAL A 83 GLY A 84 0 SHEET 2 A 2 SER A 108 TYR A 109 -1 O SER A 108 N GLY A 84 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 - t 27 2 Bytes