Header list of 1hpw.pdb file
Complete list - b 23 2 Bytes
HEADER CONTRACTILE PROTEIN 13-DEC-00 1HPW
TITLE STRUCTURE OF A PILIN MONOMER FROM PSEUDOMONAS AERUGINOSA: IMPLICATIONS
TITLE 2 FOR THE ASSEMBLY OF PILI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIMBRIAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PILIN (RESIDUES 29-150);
COMPND 5 SYNONYM: PILIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: K122-4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRLD
KEYWDS FIMBRIA, METHYLATION, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.W.KEIZER,C.M.SLUPSKY,A.P.CAMPBELL,R.T.IRVIN,B.D.SYKES
REVDAT 5 23-FEB-22 1HPW 1 REMARK
REVDAT 4 24-FEB-09 1HPW 1 VERSN
REVDAT 3 01-APR-03 1HPW 1 JRNL
REVDAT 2 04-JUL-01 1HPW 1 JRNL
REVDAT 1 02-MAY-01 1HPW 0
JRNL AUTH D.W.KEIZER,C.M.SLUPSKY,M.KALISIAK,A.P.CAMPBELL,M.P.CRUMP,
JRNL AUTH 2 P.A.SASTRY,B.HAZES,R.T.IRVIN,B.D.SYKES
JRNL TITL STRUCTURE OF A PILIN MONOMER FROM PSEUDOMONAS AERUGINOSA:
JRNL TITL 2 IMPLICATIONS FOR THE ASSEMBLY OF PILI.
JRNL REF J.BIOL.CHEM. V. 276 24186 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11294863
JRNL DOI 10.1074/JBC.M100659200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.2B, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1213 RESTRAINTS, 1032 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 181
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 30 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1HPW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012501.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.5 MM K122-4 PILIN DISSOLVED IN
REMARK 210 EITHER 90% H2O/10% D2O OR 99%
REMARK 210 D2O CONTAINING 20 MM DEUTERATED
REMARK 210 SODIUM ACETATE, 1 MM NAN3 AND 1
REMARK 210 MM DSS, PH 5.0.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
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 GLU A 27 -53.29 -131.58
REMARK 500 1 PHE A 28 -71.81 -62.26
REMARK 500 1 ALA A 29 -59.58 77.57
REMARK 500 1 GLN A 53 -82.39 -55.74
REMARK 500 1 ASN A 60 29.01 47.01
REMARK 500 1 ALA A 65 -47.60 -131.64
REMARK 500 1 LYS A 69 -47.20 -148.73
REMARK 500 1 THR A 71 77.47 -103.62
REMARK 500 1 ASP A 72 -96.27 -76.22
REMARK 500 1 ALA A 79 103.34 -161.87
REMARK 500 1 ALA A 88 45.25 166.86
REMARK 500 1 ALA A 89 -30.89 171.74
REMARK 500 1 SER A 90 -75.25 -116.13
REMARK 500 1 SER A 102 -142.06 -82.86
REMARK 500 1 ASP A 103 32.55 -162.51
REMARK 500 1 ALA A 105 152.78 62.42
REMARK 500 1 THR A 106 155.16 58.58
REMARK 500 1 LEU A 108 -75.11 -95.77
REMARK 500 1 LYS A 111 -164.32 82.27
REMARK 500 1 ALA A 120 -1.36 75.31
REMARK 500 1 LYS A 122 40.01 178.77
REMARK 500 1 SER A 124 33.96 -170.35
REMARK 500 1 TYR A 125 136.71 62.67
REMARK 500 1 THR A 130 84.30 -160.40
REMARK 500 1 ASP A 134 89.15 41.36
REMARK 500 1 LYS A 140 125.01 -177.65
REMARK 500 1 THR A 141 -68.35 68.83
REMARK 500 1 THR A 148 166.66 62.27
REMARK 500 2 LEU A 23 -56.92 -137.18
REMARK 500 2 GLU A 24 -79.63 63.69
REMARK 500 2 GLN A 53 -82.68 -54.51
REMARK 500 2 SER A 56 -159.03 -156.37
REMARK 500 2 PRO A 58 -165.12 -79.47
REMARK 500 2 ALA A 62 32.90 -144.22
REMARK 500 2 LYS A 69 -46.54 -155.36
REMARK 500 2 ASP A 70 87.73 -61.04
REMARK 500 2 THR A 71 88.42 -156.54
REMARK 500 2 TYR A 77 42.68 -144.82
REMARK 500 2 VAL A 78 21.01 -151.05
REMARK 500 2 LYS A 80 77.73 -159.88
REMARK 500 2 ALA A 87 -154.71 -129.63
REMARK 500 2 ALA A 88 37.03 80.84
REMARK 500 2 ALA A 89 -43.86 -176.40
REMARK 500 2 SER A 90 21.31 -141.58
REMARK 500 2 SER A 102 -142.80 -79.68
REMARK 500 2 ASP A 103 34.57 -169.85
REMARK 500 2 THR A 106 160.43 58.82
REMARK 500 2 ARG A 109 -177.32 61.12
REMARK 500 2 LYS A 111 -159.15 84.61
REMARK 500 2 LEU A 113 110.64 -160.33
REMARK 500
REMARK 500 THIS ENTRY HAS 291 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HPW A 29 150 UNP P17838 FMP1_PSEAE 36 157
SEQADV 1HPW ALA A 22 UNP P17838 SEE REMARK 999
SEQADV 1HPW LEU A 23 UNP P17838 SEE REMARK 999
SEQADV 1HPW GLU A 24 UNP P17838 SEE REMARK 999
SEQADV 1HPW GLY A 25 UNP P17838 SEE REMARK 999
SEQADV 1HPW THR A 26 UNP P17838 SEE REMARK 999
SEQADV 1HPW GLU A 27 UNP P17838 SEE REMARK 999
SEQADV 1HPW PHE A 28 UNP P17838 SEE REMARK 999
SEQADV 1HPW ALA A 36 UNP P17838 ARG 43 SEE REMARK 999
SEQRES 1 A 129 ALA LEU GLU GLY THR GLU PHE ALA ARG ALA GLN LEU SER
SEQRES 2 A 129 GLU ALA MET THR LEU ALA SER GLY LEU LYS THR LYS VAL
SEQRES 3 A 129 SER ASP ILE PHE SER GLN ASP GLY SER CYS PRO ALA ASN
SEQRES 4 A 129 THR ALA ALA THR ALA GLY ILE GLU LYS ASP THR ASP ILE
SEQRES 5 A 129 ASN GLY LYS TYR VAL ALA LYS VAL THR THR GLY GLY THR
SEQRES 6 A 129 ALA ALA ALA SER GLY GLY CYS THR ILE VAL ALA THR MET
SEQRES 7 A 129 LYS ALA SER ASP VAL ALA THR PRO LEU ARG GLY LYS THR
SEQRES 8 A 129 LEU THR LEU THR LEU GLY ASN ALA ASP LYS GLY SER TYR
SEQRES 9 A 129 THR TRP ALA CYS THR SER ASN ALA ASP ASN LYS TYR LEU
SEQRES 10 A 129 PRO LYS THR CYS GLN THR ALA THR THR THR THR PRO
HELIX 1 1 ALA A 31 GLY A 55 1 25
SHEET 1 A 4 CYS A 93 MET A 99 0
SHEET 2 A 4 LYS A 111 LEU A 117 -1 N LYS A 111 O MET A 99
SHEET 3 A 4 TRP A 127 ASN A 132 -1 N ALA A 128 O THR A 116
SHEET 4 A 4 GLN A 143 THR A 144 1 N GLN A 143 O CYS A 129
SSBOND 1 CYS A 57 CYS A 93 1555 1555 2.03
SSBOND 2 CYS A 129 CYS A 142 1555 1555 2.02
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