Header list of 1q9f.pdb file
Complete list - t 27 2 Bytes
HEADER MEMBRANE PROTEIN 25-AUG-03 1Q9F
TITLE NMR STRUCTURE 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,C.HILTY,G.WIDER,P.GUNTERT,K.WUTHRICH
REVDAT 3 27-OCT-21 1Q9F 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q9F 1 VERSN
REVDAT 1 23-MAR-04 1Q9F 0
JRNL AUTH C.FERNANDEZ,C.HILTY,G.WIDER,P.GUNTERT,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE INTEGRAL MEMBRANE PROTEIN OMPX.
JRNL REF J.MOL.BIOL. V. 336 1211 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15037080
JRNL DOI 10.1016/J.JMB.2003.09.014
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HILTY,C.FERNANDEZ,G.WIDER,K.WUTHRICH
REMARK 1 TITL SIDE CHAIN NMR ASSIGNMENTS IN THE MEMBRANE PROTEIN OMPX
REMARK 1 TITL 2 RECONSTITUTED IN DHPC MICELLES
REMARK 1 REF J.BIOMOL.NMR V. 23 289 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1020218419190
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.HILTY,G.WIDER,C.FERNANDEZ,K.WUTHRICH
REMARK 1 TITL STEREOSPECIFIC ASSIGNMENTS OF THE ISOPROPYL METHYL GROUPS OF
REMARK 1 TITL 2 THE MEMBRANE PROTEIN OMPX IN DHPC MICELLES
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP 2.6
REMARK 3 AUTHORS : KORADI, R., LUGINBUHL, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AUTOMATIC IDENTIFICATION OF HYDROGEN
REMARK 3 BOND CONSTRAINTS
REMARK 4
REMARK 4 1Q9F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020082.
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; 2MM OMPX
REMARK 210 U-15N,13C,2H/L,V,ID1- 13CH3; 2MM
REMARK 210 OMPX U-15N,10%-13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_H(C)(CC)-TOCSY-(CO)-[15N,1H]-TROSY; 2D_[13C,
REMARK 210 1H]-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 1.0, TALOS
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (CANDID)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 ARG A 147 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 10 TYR A 28 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
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 17 96.97 -45.38
REMARK 500 1 MET A 18 -2.44 -148.82
REMARK 500 1 LYS A 20 96.12 -66.68
REMARK 500 1 ASN A 34 -75.42 -167.59
REMARK 500 1 GLU A 47 29.41 -147.59
REMARK 500 1 ALA A 52 -86.37 -171.44
REMARK 500 1 SER A 53 78.85 -170.14
REMARK 500 1 SER A 54 -43.24 -162.99
REMARK 500 1 TYR A 57 76.38 -110.89
REMARK 500 1 ASN A 58 93.11 -51.94
REMARK 500 1 ASN A 60 176.90 61.58
REMARK 500 1 ASN A 74 -75.90 -132.43
REMARK 500 1 ASP A 75 74.98 -165.55
REMARK 500 1 TRP A 76 -60.28 -130.89
REMARK 500 1 GLU A 94 -70.16 -148.59
REMARK 500 1 THR A 97 -28.27 -156.24
REMARK 500 1 TYR A 98 -150.77 50.57
REMARK 500 1 ASN A 100 -91.80 -80.18
REMARK 500 1 ASP A 101 24.06 -141.73
REMARK 500 1 SER A 103 104.40 132.67
REMARK 500 1 ASN A 120 12.18 -156.72
REMARK 500 1 ARG A 133 -74.88 75.27
REMARK 500 1 SER A 134 27.05 -148.75
REMARK 500 2 LYS A 20 106.12 -58.74
REMARK 500 2 ASN A 34 -37.97 -164.96
REMARK 500 2 ALA A 52 -87.31 -90.26
REMARK 500 2 SER A 53 79.46 -160.55
REMARK 500 2 SER A 54 84.85 57.41
REMARK 500 2 ASN A 58 -60.19 -171.49
REMARK 500 2 ASN A 60 19.25 -146.46
REMARK 500 2 ASN A 74 -79.31 -135.72
REMARK 500 2 ASP A 75 80.52 -158.69
REMARK 500 2 GLU A 94 -47.52 -150.60
REMARK 500 2 THR A 97 5.48 -67.53
REMARK 500 2 TYR A 98 -39.31 -24.59
REMARK 500 2 ASN A 120 -7.92 -174.68
REMARK 500 2 ARG A 133 18.89 58.45
REMARK 500 3 GLN A 15 -60.09 61.60
REMARK 500 3 MET A 18 -69.02 -152.91
REMARK 500 3 ASN A 34 -47.37 -159.21
REMARK 500 3 GLU A 47 -11.49 -141.78
REMARK 500 3 THR A 51 89.40 177.09
REMARK 500 3 SER A 53 -56.50 -148.27
REMARK 500 3 SER A 54 102.14 -161.99
REMARK 500 3 ASN A 60 -177.69 84.92
REMARK 500 3 ASN A 74 37.48 -88.73
REMARK 500 3 ASP A 75 -119.98 -149.51
REMARK 500 3 LYS A 99 117.27 -163.03
REMARK 500 3 GLU A 119 27.08 103.89
REMARK 500 3 ARG A 133 -64.84 56.75
REMARK 500
REMARK 500 THIS ENTRY HAS 320 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 138 THR A 139 2 146.66
REMARK 500 ILE A 40 GLY A 41 3 142.44
REMARK 500 TYR A 98 LYS A 99 5 148.84
REMARK 500 ALA A 1 THR A 2 6 149.82
REMARK 500 THR A 46 GLU A 47 8 149.97
REMARK 500 TYR A 87 GLY A 88 8 149.58
REMARK 500 GLY A 68 PRO A 69 9 145.94
REMARK 500 ILE A 40 GLY A 41 11 148.78
REMARK 500 TYR A 57 ASN A 58 11 -149.52
REMARK 500 LYS A 20 MET A 21 15 138.27
REMARK 500 ILE A 40 GLY A 41 15 144.72
REMARK 500 GLY A 41 SER A 42 15 143.72
REMARK 500 ASN A 74 ASP A 75 15 149.68
REMARK 500 SER A 134 VAL A 135 15 143.30
REMARK 500 ASN A 25 LEU A 26 16 149.72
REMARK 500 VAL A 121 ALA A 122 18 149.59
REMARK 500 GLY A 41 SER A 42 19 146.72
REMARK 500 PHE A 125 SER A 126 19 145.10
REMARK 500 GLY A 138 THR A 139 20 146.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 133 0.10 SIDE CHAIN
REMARK 500 3 ARG A 29 0.13 SIDE CHAIN
REMARK 500 3 ARG A 72 0.11 SIDE CHAIN
REMARK 500 4 TYR A 30 0.09 SIDE CHAIN
REMARK 500 4 ARG A 50 0.12 SIDE CHAIN
REMARK 500 5 ARG A 29 0.08 SIDE CHAIN
REMARK 500 5 TYR A 45 0.07 SIDE CHAIN
REMARK 500 5 TYR A 95 0.07 SIDE CHAIN
REMARK 500 6 TYR A 30 0.08 SIDE CHAIN
REMARK 500 6 ARG A 72 0.10 SIDE CHAIN
REMARK 500 6 TYR A 146 0.12 SIDE CHAIN
REMARK 500 7 TYR A 57 0.10 SIDE CHAIN
REMARK 500 7 TYR A 71 0.10 SIDE CHAIN
REMARK 500 8 ARG A 50 0.10 SIDE CHAIN
REMARK 500 8 TYR A 109 0.08 SIDE CHAIN
REMARK 500 9 ARG A 29 0.11 SIDE CHAIN
REMARK 500 9 TYR A 57 0.10 SIDE CHAIN
REMARK 500 9 ARG A 72 0.08 SIDE CHAIN
REMARK 500 9 TYR A 127 0.08 SIDE CHAIN
REMARK 500 9 ARG A 133 0.08 SIDE CHAIN
REMARK 500 10 TYR A 127 0.10 SIDE CHAIN
REMARK 500 11 TYR A 45 0.07 SIDE CHAIN
REMARK 500 12 ARG A 50 0.08 SIDE CHAIN
REMARK 500 13 TYR A 80 0.07 SIDE CHAIN
REMARK 500 13 ARG A 133 0.11 SIDE CHAIN
REMARK 500 13 TYR A 146 0.08 SIDE CHAIN
REMARK 500 14 TYR A 28 0.09 SIDE CHAIN
REMARK 500 14 ARG A 29 0.10 SIDE CHAIN
REMARK 500 14 ARG A 147 0.11 SIDE CHAIN
REMARK 500 15 ARG A 29 0.09 SIDE CHAIN
REMARK 500 15 TYR A 146 0.11 SIDE CHAIN
REMARK 500 16 TYR A 71 0.07 SIDE CHAIN
REMARK 500 16 TYR A 146 0.09 SIDE CHAIN
REMARK 500 17 TYR A 28 0.08 SIDE CHAIN
REMARK 500 17 TYR A 71 0.08 SIDE CHAIN
REMARK 500 17 TYR A 105 0.07 SIDE CHAIN
REMARK 500 18 ARG A 29 0.09 SIDE CHAIN
REMARK 500 18 TYR A 62 0.07 SIDE CHAIN
REMARK 500 18 ARG A 133 0.11 SIDE CHAIN
REMARK 500 20 TYR A 62 0.10 SIDE CHAIN
REMARK 500 20 ARG A 131 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ORM RELATED DB: PDB
REMARK 900 NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES
REMARK 900 RELATED ID: 4936 RELATED DB: BMRB
DBREF 1Q9F A 1 148 UNP P36546 OMPX_ECOLI 24 171
SEQADV 1Q9F ASN A 100 UNP P36546 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 7 ALA A 10 ALA A 14 0
SHEET 2 A 7 VAL A 135 ARG A 147 -1 O GLY A 138 N ASP A 13
SHEET 3 A 7 ALA A 122 ILE A 132 -1 N ASP A 124 O GLY A 143
SHEET 4 A 7 TYR A 109 GLN A 114 -1 N LEU A 113 O PHE A 125
SHEET 5 A 7 SER A 78 TYR A 87 -1 N TYR A 80 O GLY A 112
SHEET 6 A 7 TYR A 63 TYR A 71 -1 N TYR A 63 O TYR A 87
SHEET 7 A 7 LEU A 37 TYR A 45 -1 N GLY A 38 O ALA A 70
SHEET 1 B 7 LEU A 26 LYS A 27 0
SHEET 2 B 7 THR A 4 GLY A 7 -1 N THR A 6 O LYS A 27
SHEET 3 B 7 VAL A 135 ARG A 147 -1 O VAL A 144 N GLY A 7
SHEET 4 B 7 ALA A 122 ILE A 132 -1 N ASP A 124 O GLY A 143
SHEET 5 B 7 TYR A 109 GLN A 114 -1 N LEU A 113 O PHE A 125
SHEET 6 B 7 SER A 78 TYR A 87 -1 N TYR A 80 O GLY A 112
SHEET 7 B 7 TYR A 105 GLY A 106 -1 O GLY A 106 N GLY A 86
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