Header list of 1rxl.pdb file
Complete list - b 5 2 Bytes
HEADER STRUCTURAL PROTEIN 18-DEC-03 1RXL
TITLE SOLUTION STRUCTURE OF THE ENGINEERED PROTEIN AFAE-DSC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AFIMBRIAL ADHESIN AFA-III;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AFAE-DSC; AFA-III; AFAE-3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AFAE3;
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: PRSETA
KEYWDS AFAE, DAF, AFIMBRIAL SHEATH, DAEC, UPEC, IG-LIKE DOMAIN, DONOR STRAND
KEYWDS 2 COMPLEMENTED, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.L.ANDERSON,J.BILLINGTON,D.PETTIGREW,E.COTA,P.ROVERSI,P.SIMPSON,
AUTHOR 2 H.A.CHEN,P.URVIL,L.DU MERLE,P.N.BARLOW,M.E.MEDOF,R.A.SMITH,
AUTHOR 3 B.NOWICKI,C.LE BOUGUENEC,S.M.LEA,S.MATTHEWS
REVDAT 4 05-FEB-20 1RXL 1 REMARK
REVDAT 3 08-FEB-17 1RXL 1 AUTHOR JRNL VERSN
REVDAT 2 24-FEB-09 1RXL 1 VERSN
REVDAT 1 11-JAN-05 1RXL 0
JRNL AUTH K.L.ANDERSON,J.BILLINGTON,D.PETTIGREW,E.COTA,P.SIMPSON,
JRNL AUTH 2 P.ROVERSI,H.A.CHEN,P.URVIL,L.DU MERLE,P.N.BARLOW,M.E.MEDOF,
JRNL AUTH 3 R.A.SMITH,B.NOWICKI,C.LE BOUGUENEC,S.M.LEA,S.MATTHEWS
JRNL TITL AN ATOMIC RESOLUTION MODEL FOR ASSEMBLY, ARCHITECTURE, AND
JRNL TITL 2 FUNCTION OF THE DR ADHESINS.
JRNL REF MOL.CELL V. 15 647 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15327779
JRNL DOI 10.1016/J.MOLCEL.2004.08.003
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, ARIA 1.2
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), LINGE, O'DONOGHUE,
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE BASED ON 4099 NOE-BASED
REMARK 3 RESTRAINTS (2557 UNAMBIGUOUS, 1542 AMBIGUOUS) AND 116 TORSION
REMARK 3 ANGLES (TALOS)
REMARK 4
REMARK 4 1RXL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 0.3M
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM AFAE-DSC U-15N,13C; 50MM
REMARK 210 ACETATE BUFFER PH5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 4.0, ARIA
REMARK 210 1.2
REMARK 210 METHOD USED : ARIA-IMPLEMENTED DISTANCE
REMARK 210 GEOMETRY/SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 1-15
REMARK 465 RES C SSSEQI
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 HB2 LEU A 65 HG3 GLN A 104 1.24
REMARK 500 HZ2 LYS A 86 HB2 TRP A 92 1.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 2 PHE A 54 CE1 PHE A 54 CZ 0.116
REMARK 500 11 PHE A 54 CE1 PHE A 54 CZ 0.127
REMARK 500 13 PHE A 54 CE1 PHE A 54 CZ 0.134
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 19 96.34 -65.99
REMARK 500 1 THR A 20 66.22 -102.95
REMARK 500 1 ASP A 21 -81.87 65.48
REMARK 500 1 GLN A 51 -49.33 73.13
REMARK 500 1 ASP A 73 103.45 -172.97
REMARK 500 1 ASN A 74 -32.01 -177.65
REMARK 500 1 ASP A 101 98.91 -69.23
REMARK 500 1 GLN A 103 99.52 51.98
REMARK 500 1 THR A 105 -56.23 -178.86
REMARK 500 1 ASN A 106 79.24 72.21
REMARK 500 1 PRO A 108 88.41 -21.95
REMARK 500 1 PRO A 109 -157.76 -85.16
REMARK 500 1 LYS A 123 -123.03 169.88
REMARK 500 1 ASP A 124 117.26 -166.31
REMARK 500 1 ASN A 125 -30.86 61.43
REMARK 500 1 GLN A 127 45.85 72.79
REMARK 500 2 THR A 20 70.35 -107.42
REMARK 500 2 ASP A 21 -80.07 67.61
REMARK 500 2 ALA A 22 63.69 -101.34
REMARK 500 2 CYS A 35 -70.38 -87.08
REMARK 500 2 ASN A 36 -61.83 69.25
REMARK 500 2 GLN A 51 -57.62 68.46
REMARK 500 2 ASN A 61 25.77 177.28
REMARK 500 2 SER A 75 179.71 61.18
REMARK 500 2 TRP A 92 -53.86 -126.74
REMARK 500 2 GLN A 103 97.98 57.93
REMARK 500 2 THR A 105 -3.79 74.01
REMARK 500 2 ASN A 106 86.18 63.41
REMARK 500 2 PRO A 108 89.36 -30.50
REMARK 500 2 LYS A 123 -136.01 72.17
REMARK 500 2 ASN A 125 -38.76 67.76
REMARK 500 2 GLN A 127 72.56 65.21
REMARK 500 3 THR A 20 55.42 34.25
REMARK 500 3 ASP A 21 -62.84 70.27
REMARK 500 3 ALA A 37 83.66 -167.76
REMARK 500 3 GLN A 51 -58.56 70.79
REMARK 500 3 ASP A 73 -46.84 74.21
REMARK 500 3 SER A 75 159.48 74.40
REMARK 500 3 TRP A 92 -57.13 -157.68
REMARK 500 3 ASP A 101 97.04 -66.50
REMARK 500 3 GLN A 103 118.35 67.27
REMARK 500 3 ASN A 106 91.51 41.86
REMARK 500 3 PRO A 108 83.14 -12.04
REMARK 500 3 PRO A 109 -157.46 -74.13
REMARK 500 3 LYS A 123 -143.31 74.55
REMARK 500 3 ASN A 125 -22.81 65.53
REMARK 500 3 GLN A 127 79.24 70.37
REMARK 500 4 THR A 20 60.29 -153.80
REMARK 500 4 ASP A 21 -84.76 61.28
REMARK 500 4 PRO A 27 97.89 -60.63
REMARK 500
REMARK 500 THIS ENTRY HAS 233 RAMACHANDRAN OUTLIERS.
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 3 PHE A 49 0.07 SIDE CHAIN
REMARK 500 4 PHE A 49 0.06 SIDE CHAIN
REMARK 500 4 TYR A 85 0.05 SIDE CHAIN
REMARK 500 5 TYR A 85 0.06 SIDE CHAIN
REMARK 500 6 TYR A 66 0.07 SIDE CHAIN
REMARK 500 11 TYR A 99 0.05 SIDE CHAIN
REMARK 500 11 TYR A 112 0.08 SIDE CHAIN
REMARK 500 12 PHE A 49 0.07 SIDE CHAIN
REMARK 500 13 TYR A 120 0.05 SIDE CHAIN
REMARK 500 15 PHE A 49 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5947 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS OF AFAE-DSC
REMARK 900 RELATED ID: 1SDD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF AFAE-DSC
REMARK 900 RELATED ID: 1UT2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AFAE-3 TRIMER
REMARK 900 RELATED ID: 1UT1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DRAE TRIMER
REMARK 900 RELATED ID: 1USQ RELATED DB: PDB
REMARK 900 COMPLEX OF DRAE WITH CHLORAMPHENICOL
REMARK 900 RELATED ID: 1USZ RELATED DB: PDB
REMARK 900 SEMET AFAE-3 ADHESIN
DBREF 1RXL A 1 123 UNP Q57254 FMA3_ECOLI 38 160
SEQADV 1RXL HIS A -12 UNP Q57254 SEE REMARK 999
SEQADV 1RXL HIS A -11 UNP Q57254 SEE REMARK 999
SEQADV 1RXL HIS A -10 UNP Q57254 SEE REMARK 999
SEQADV 1RXL HIS A -9 UNP Q57254 SEE REMARK 999
SEQADV 1RXL HIS A -8 UNP Q57254 SEE REMARK 999
SEQADV 1RXL HIS A -7 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLY A -6 UNP Q57254 SEE REMARK 999
SEQADV 1RXL LEU A -5 UNP Q57254 SEE REMARK 999
SEQADV 1RXL VAL A -4 UNP Q57254 SEE REMARK 999
SEQADV 1RXL PRO A -3 UNP Q57254 SEE REMARK 999
SEQADV 1RXL ARG A -2 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLY A -1 UNP Q57254 SEE REMARK 999
SEQADV 1RXL SER A 0 UNP Q57254 SEE REMARK 999
SEQADV 1RXL ASP A 124 UNP Q57254 SEE REMARK 999
SEQADV 1RXL ASN A 125 UNP Q57254 SEE REMARK 999
SEQADV 1RXL LYS A 126 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLN A 127 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLY A 128 UNP Q57254 SEE REMARK 999
SEQADV 1RXL PHE A 129 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 130 UNP Q57254 SEE REMARK 999
SEQADV 1RXL PRO A 131 UNP Q57254 SEE REMARK 999
SEQADV 1RXL SER A 132 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLY A 133 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 134 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 135 UNP Q57254 SEE REMARK 999
SEQADV 1RXL GLY A 136 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 137 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 138 UNP Q57254 SEE REMARK 999
SEQADV 1RXL LYS A 139 UNP Q57254 SEE REMARK 999
SEQADV 1RXL LEU A 140 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 141 UNP Q57254 SEE REMARK 999
SEQADV 1RXL VAL A 142 UNP Q57254 SEE REMARK 999
SEQADV 1RXL THR A 143 UNP Q57254 SEE REMARK 999
SEQRES 1 A 156 HIS HIS HIS HIS HIS HIS GLY LEU VAL PRO ARG GLY SER
SEQRES 2 A 156 GLU GLU CYS GLN VAL ARG VAL GLY ASP LEU THR VAL ALA
SEQRES 3 A 156 LYS THR ARG GLY GLN LEU THR ASP ALA ALA PRO ILE GLY
SEQRES 4 A 156 PRO VAL THR VAL GLN ALA LEU GLY CYS ASN ALA ARG GLN
SEQRES 5 A 156 VAL ALA LEU LYS ALA ASP THR ASP ASN PHE GLU GLN GLY
SEQRES 6 A 156 LYS PHE PHE LEU ILE SER ASP ASN ASN ARG ASP LYS LEU
SEQRES 7 A 156 TYR VAL ASN ILE ARG PRO MET ASP ASN SER ALA TRP THR
SEQRES 8 A 156 THR ASP ASN GLY VAL PHE TYR LYS ASN ASP VAL GLY SER
SEQRES 9 A 156 TRP GLY GLY THR ILE GLY ILE TYR VAL ASP GLY GLN GLN
SEQRES 10 A 156 THR ASN THR PRO PRO GLY ASN TYR THR LEU THR LEU THR
SEQRES 11 A 156 GLY GLY TYR TRP ALA LYS ASP ASN LYS GLN GLY PHE THR
SEQRES 12 A 156 PRO SER GLY THR THR GLY THR THR LYS LEU THR VAL THR
SHEET 1 A 8 GLN A 4 ARG A 6 0
SHEET 2 A 8 VAL A 28 LEU A 33 -1 O GLN A 31 N ARG A 6
SHEET 3 A 8 GLY A 94 VAL A 100 -1 O ILE A 96 N VAL A 28
SHEET 4 A 8 LYS A 64 PRO A 71 -1 N ASN A 68 O TYR A 99
SHEET 5 A 8 PHE A 55 SER A 58 -1 N LEU A 56 O LEU A 65
SHEET 6 A 8 ASN A 111 TRP A 121 -1 O THR A 113 N ILE A 57
SHEET 7 A 8 PHE A 129 THR A 141 -1 O GLY A 136 N LEU A 116
SHEET 8 A 8 THR A 11 ALA A 13 1 N VAL A 12 O LYS A 139
SHEET 1 B 9 GLN A 4 ARG A 6 0
SHEET 2 B 9 VAL A 28 LEU A 33 -1 O GLN A 31 N ARG A 6
SHEET 3 B 9 GLY A 94 VAL A 100 -1 O ILE A 96 N VAL A 28
SHEET 4 B 9 LYS A 64 PRO A 71 -1 N ASN A 68 O TYR A 99
SHEET 5 B 9 PHE A 55 SER A 58 -1 N LEU A 56 O LEU A 65
SHEET 6 B 9 ASN A 111 TRP A 121 -1 O THR A 113 N ILE A 57
SHEET 7 B 9 GLN A 39 ALA A 44 -1 N LYS A 43 O THR A 117
SHEET 8 B 9 VAL A 83 LYS A 86 -1 O PHE A 84 N LEU A 42
SHEET 9 B 9 TRP A 77 THR A 79 -1 N THR A 78 O TYR A 85
SSBOND 1 CYS A 3 CYS A 35 1555 1555 2.03
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 5 2 Bytes