Header list of 1zdv.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 15-APR-05 1ZDV
TITLE SOLUTION STRUCTURE OF THE TYPE 1 PILUS ASSEMBLY PLATFORM FIMD(25-139)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE USHER PROTEIN FIMD;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 70-184;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FIMD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA SHEET, ALPHA HELIX, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.NISHIYAMA,R.HORST,T.HERRMANN,M.VETSCH,P.BETTENDORFF,O.IGNATOV,
AUTHOR 2 M.GRUTTER,K.WUTHRICH,R.GLOCKSHUBER,G.CAPITANI
REVDAT 4 02-MAR-22 1ZDV 1 REMARK
REVDAT 3 24-FEB-09 1ZDV 1 VERSN
REVDAT 2 28-JUN-05 1ZDV 1 JRNL
REVDAT 1 14-JUN-05 1ZDV 0
JRNL AUTH M.NISHIYAMA,R.HORST,O.EIDAM,T.HERRMANN,O.IGNATOV,M.VETSCH,
JRNL AUTH 2 P.BETTENDORFF,I.JELESAROV,R.GLOCKSHUBER,G.CAPITANI
JRNL TITL STRUCTURAL BASIS OF CHAPERONE-SUBUNIT COMPLEX RECOGNITION BY
JRNL TITL 2 THE TYPE 1 PILUS ASSEMBLY PLATFORM FIMD.
JRNL REF EMBO J. V. 24 2075 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 15920478
JRNL DOI 10.1038/SJ.EMBOJ.7600693
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, ATHNOS/CANDID
REMARK 3 AUTHORS : BRUKER (XWINNMR), HERRMANN (ATHNOS/CANDID)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZDV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032608.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : UNIFORM LABELING WITH 13C, 15N;
REMARK 210 90 % H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ATHNOS/CANDID
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
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 HD2 ASP A 87 H TYR A 127 0.94
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 1 LEU A 74 CB - CG - CD2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 9 LEU A 74 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 10 ASP A 48 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 11 PRO A 116 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 12 LEU A 74 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 13 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 14 TYR A 33 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 14 LEU A 74 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 15 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 16 ARG A 110 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 17 LEU A 74 CB - CG - CD2 ANGL. DEV. = 11.2 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 LEU A 28 59.16 -157.05
REMARK 500 1 THR A 32 147.94 64.75
REMARK 500 1 MET A 44 -73.62 -126.16
REMARK 500 1 ASP A 55 93.56 -171.81
REMARK 500 1 THR A 95 -61.10 -143.30
REMARK 500 1 GLN A 109 71.70 50.28
REMARK 500 1 TYR A 127 129.13 76.32
REMARK 500 1 ASP A 134 106.63 -51.77
REMARK 500 1 ILE A 137 92.04 -67.03
REMARK 500 2 LEU A 28 56.31 -156.42
REMARK 500 2 MET A 44 -84.87 -117.01
REMARK 500 2 THR A 95 -38.95 -135.37
REMARK 500 2 ASP A 99 -7.36 65.36
REMARK 500 2 GLN A 109 71.41 46.68
REMARK 500 2 ARG A 123 104.37 -50.94
REMARK 500 2 ASP A 134 97.78 -31.56
REMARK 500 3 GLU A 27 118.03 -174.76
REMARK 500 3 LEU A 28 57.56 -147.56
REMARK 500 3 THR A 32 146.27 70.51
REMARK 500 3 MET A 44 -67.12 -121.28
REMARK 500 3 ASP A 99 1.72 57.38
REMARK 500 3 ALA A 102 84.48 -151.65
REMARK 500 3 ASP A 134 98.56 -41.60
REMARK 500 3 ILE A 137 89.86 -68.96
REMARK 500 4 LEU A 28 59.16 -152.71
REMARK 500 4 MET A 44 -69.01 -124.37
REMARK 500 4 SER A 56 -173.89 -174.34
REMARK 500 4 CYS A 63 95.78 -61.33
REMARK 500 4 ALA A 67 -70.76 -33.02
REMARK 500 4 ALA A 80 -119.13 30.34
REMARK 500 4 ASP A 88 39.78 -93.14
REMARK 500 4 CYS A 90 74.65 45.08
REMARK 500 4 ASP A 99 -4.88 62.40
REMARK 500 4 ARG A 123 89.81 -24.49
REMARK 500 4 PRO A 130 0.71 -66.26
REMARK 500 4 ASP A 134 94.05 -40.68
REMARK 500 4 PRO A 135 -71.59 -80.35
REMARK 500 5 GLN A 26 34.87 -149.17
REMARK 500 5 GLU A 27 96.51 62.01
REMARK 500 5 LEU A 28 55.28 -141.13
REMARK 500 5 THR A 32 143.92 65.79
REMARK 500 5 ASN A 40 48.94 38.41
REMARK 500 5 ASP A 55 109.88 -160.21
REMARK 500 5 SER A 56 -177.34 -177.20
REMARK 500 5 ASN A 83 9.47 -64.02
REMARK 500 5 ASP A 88 78.95 -106.57
REMARK 500 5 CYS A 90 88.80 -58.75
REMARK 500 5 ASP A 99 -7.42 55.96
REMARK 500 5 ALA A 102 89.69 -153.39
REMARK 500 5 TYR A 127 118.38 66.83
REMARK 500
REMARK 500 THIS ENTRY HAS 230 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 ASN A 138 ALA A 139 5 142.83
REMARK 500 ARG A 125 GLY A 126 10 -147.37
REMARK 500 ALA A 124 ARG A 125 11 148.57
REMARK 500 ALA A 124 ARG A 125 13 145.57
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 110 0.09 SIDE CHAIN
REMARK 500 1 ARG A 123 0.09 SIDE CHAIN
REMARK 500 2 PHE A 51 0.08 SIDE CHAIN
REMARK 500 4 ARG A 34 0.14 SIDE CHAIN
REMARK 500 5 TYR A 43 0.08 SIDE CHAIN
REMARK 500 5 ARG A 123 0.11 SIDE CHAIN
REMARK 500 7 ARG A 66 0.32 SIDE CHAIN
REMARK 500 7 ARG A 123 0.07 SIDE CHAIN
REMARK 500 8 ARG A 110 0.29 SIDE CHAIN
REMARK 500 11 TYR A 127 0.07 SIDE CHAIN
REMARK 500 12 ARG A 34 0.12 SIDE CHAIN
REMARK 500 12 ARG A 66 0.22 SIDE CHAIN
REMARK 500 12 ARG A 125 0.12 SIDE CHAIN
REMARK 500 14 ARG A 34 0.19 SIDE CHAIN
REMARK 500 15 TYR A 43 0.08 SIDE CHAIN
REMARK 500 15 ARG A 47 0.09 SIDE CHAIN
REMARK 500 15 ARG A 66 0.09 SIDE CHAIN
REMARK 500 16 ARG A 34 0.08 SIDE CHAIN
REMARK 500 16 PHE A 51 0.08 SIDE CHAIN
REMARK 500 17 TYR A 33 0.07 SIDE CHAIN
REMARK 500 17 ARG A 47 0.08 SIDE CHAIN
REMARK 500 17 ARG A 66 0.13 SIDE CHAIN
REMARK 500 18 TYR A 127 0.07 SIDE CHAIN
REMARK 500 20 ARG A 34 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZDX RELATED DB: PDB
DBREF 1ZDV A 25 139 UNP P30130 FIMD_ECOLI 70 184
SEQRES 1 A 115 GLY GLN GLU LEU PRO PRO GLY THR TYR ARG VAL ASP ILE
SEQRES 2 A 115 TYR LEU ASN ASN GLY TYR MET ALA THR ARG ASP VAL THR
SEQRES 3 A 115 PHE ASN THR GLY ASP SER GLU GLN GLY ILE VAL PRO CYS
SEQRES 4 A 115 LEU THR ARG ALA GLN LEU ALA SER MET GLY LEU ASN THR
SEQRES 5 A 115 ALA SER VAL ALA GLY MET ASN LEU LEU ALA ASP ASP ALA
SEQRES 6 A 115 CYS VAL PRO LEU THR THR MET VAL GLN ASP ALA THR ALA
SEQRES 7 A 115 HIS LEU ASP VAL GLY GLN GLN ARG LEU ASN LEU THR ILE
SEQRES 8 A 115 PRO GLN ALA PHE MET SER ASN ARG ALA ARG GLY TYR ILE
SEQRES 9 A 115 PRO PRO GLU LEU TRP ASP PRO GLY ILE ASN ALA
HELIX 1 1 THR A 65 GLY A 73 1 9
HELIX 2 2 GLY A 81 LEU A 85 5 5
HELIX 3 3 PRO A 116 MET A 120 5 5
SHEET 1 A 4 GLY A 42 VAL A 49 0
SHEET 2 A 4 TYR A 33 LEU A 39 -1 N ILE A 37 O ALA A 45
SHEET 3 A 4 ARG A 110 THR A 114 1 O LEU A 111 N TYR A 38
SHEET 4 A 4 THR A 101 ASP A 105 -1 N ASP A 105 O ARG A 110
SHEET 1 B 2 PHE A 51 THR A 53 0
SHEET 2 B 2 ILE A 60 PRO A 62 -1 O VAL A 61 N ASN A 52
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 2 2 Bytes