Header list of 1poq.pdb file
Complete list - r 2 2 Bytes
HEADER IMMUNE SYSTEM 16-JUN-03 1POQ
TITLE SOLUTION STRUCTURE OF A SUPERANTIGEN FROM YERSINIA PSEUDOTUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YPM;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: YPM(RESIDUES 33-151);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 633;
SOURCE 4 GENE: YPMA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NOVABLUE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-P2X
KEYWDS JELLY ROLL FOLD, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.DONADINI,C.W.LIEW,A.H.KWAN,J.P.MACKAY,B.A.FIELDS
REVDAT 3 02-MAR-22 1POQ 1 REMARK
REVDAT 2 24-FEB-09 1POQ 1 VERSN
REVDAT 1 27-JAN-04 1POQ 0
JRNL AUTH R.DONADINI,C.W.LIEW,A.H.KWAN,J.P.MACKAY,B.A.FIELDS
JRNL TITL CRYSTAL AND SOLUTION STRUCTURES OF A SUPERANTIGEN FROM
JRNL TITL 2 YERSINIA PSEUDOTUBERCULOSIS REVEAL A JELLY-ROLL FOLD.
JRNL REF STRUCTURE V. 12 145 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 14725774
JRNL DOI 10.1016/J.STR.2003.12.002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT ET AL (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FINAL STRUCTURES WERE BASED ON 1934
REMARK 3 UNAMBIGUOUS NOE-DERIVED DISTANCE CONSTRAINTS, 139 AMBIGUOUS
REMARK 3 CONSTRAINTS, 135 DIHEDRAL ANGLE RESTRAINTS AND 26 HYDROGEN BOND
REMARK 3 DISTANCE RESTRAINTS.
REMARK 4
REMARK 4 1POQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019466.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM YPM PROTEIN (33-151), 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 HNHA; HN(CO)CA; HNCA; CBCA(CO)NH;
REMARK 210 HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, ARIA 1.1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND TRIPLE-RESONANCE NMR SPECTROSCOPY.
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 HA LEU A 64 HB2 GLU A 74 1.23
REMARK 500 HG2 ARG A 65 HG3 GLU A 74 1.26
REMARK 500 HG LEU A 64 H GLU A 74 1.29
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 PRO A 16 -94.45 -48.35
REMARK 500 1 ILE A 34 22.21 -144.67
REMARK 500 1 LYS A 37 34.88 -162.78
REMARK 500 1 GLU A 38 -159.21 -129.51
REMARK 500 1 GLU A 45 99.54 -57.78
REMARK 500 1 ASN A 54 -150.91 -167.30
REMARK 500 1 VAL A 55 -86.72 -72.10
REMARK 500 1 THR A 91 60.40 65.23
REMARK 500 1 SER A 92 34.85 -78.34
REMARK 500 1 ASP A 119 14.17 -158.21
REMARK 500 1 LEU A 126 -77.88 -152.03
REMARK 500 1 THR A 127 77.46 -157.03
REMARK 500 2 PRO A 16 42.12 -73.55
REMARK 500 2 ASN A 17 -65.04 -156.70
REMARK 500 2 LYS A 40 -162.13 -171.94
REMARK 500 2 THR A 41 -74.42 -57.56
REMARK 500 2 GLU A 45 121.15 -171.04
REMARK 500 2 LEU A 46 135.55 72.11
REMARK 500 2 VAL A 55 -74.26 -53.39
REMARK 500 2 ASP A 58 57.98 -107.36
REMARK 500 2 VAL A 67 10.68 -168.93
REMARK 500 2 TRP A 72 -166.68 -77.83
REMARK 500 2 ILE A 75 -62.05 -129.60
REMARK 500 2 GLU A 87 -74.07 -78.90
REMARK 500 2 TYR A 90 -91.87 -163.06
REMARK 500 2 THR A 91 -54.14 -151.84
REMARK 500 2 LYS A 120 68.28 -178.06
REMARK 500 2 LEU A 126 -44.91 -176.42
REMARK 500 2 LYS A 128 -53.51 -130.07
REMARK 500 3 ALA A 19 79.71 -160.39
REMARK 500 3 ILE A 34 101.30 47.44
REMARK 500 3 LYS A 40 33.10 -147.91
REMARK 500 3 THR A 41 -60.04 -109.24
REMARK 500 3 ASN A 54 -151.81 -176.21
REMARK 500 3 ASP A 58 48.08 -109.46
REMARK 500 3 ILE A 75 -86.37 -124.59
REMARK 500 3 GLU A 87 -82.50 -73.96
REMARK 500 3 TYR A 90 -64.70 68.13
REMARK 500 3 LEU A 94 -74.46 -79.68
REMARK 500 3 THR A 107 106.95 -57.61
REMARK 500 3 ASP A 118 -122.84 -122.18
REMARK 500 3 ASP A 119 126.48 -172.73
REMARK 500 3 LYS A 120 -176.21 134.73
REMARK 500 3 ASP A 124 -80.47 -91.26
REMARK 500 3 LEU A 126 -144.45 -134.16
REMARK 500 4 LYS A 40 96.69 59.75
REMARK 500 4 GLU A 45 -164.51 57.77
REMARK 500 4 VAL A 55 -74.40 -47.52
REMARK 500 4 ASP A 58 56.39 -119.53
REMARK 500 4 ASN A 70 20.65 -141.15
REMARK 500
REMARK 500 THIS ENTRY HAS 305 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 GLU A 30 VAL A 31 16 -145.76
REMARK 500 GLU A 106 THR A 107 20 148.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1POQ A 14 131 UNP Q57221 Q57221_YERPS 34 151
SEQRES 1 A 118 ARG ILE PRO ASN ILE ALA THR TYR THR GLY THR ILE GLN
SEQRES 2 A 118 GLY LYS GLY GLU VAL CYS ILE ILE GLY ASN LYS GLU GLY
SEQRES 3 A 118 LYS THR ARG GLY GLY GLU LEU TYR ALA VAL LEU HIS SER
SEQRES 4 A 118 THR ASN VAL ASN ALA ASP MET THR LEU ILE LEU LEU ARG
SEQRES 5 A 118 ASN VAL GLY GLY ASN GLY TRP GLY GLU ILE LYS ARG ASN
SEQRES 6 A 118 ASP ILE ASP LYS PRO LEU LYS TYR GLU ASP TYR TYR THR
SEQRES 7 A 118 SER GLY LEU SER TRP ILE TRP LYS ILE LYS ASN ASN SER
SEQRES 8 A 118 SER GLU THR SER ASN TYR SER LEU ASP ALA THR VAL HIS
SEQRES 9 A 118 ASP ASP LYS GLU ASP SER ASP VAL LEU THR LYS CYS PRO
SEQRES 10 A 118 VAL
SHEET 1 A 4 ALA A 19 ILE A 25 0
SHEET 2 A 4 SER A 108 ALA A 114 -1 O LEU A 112 N TYR A 21
SHEET 3 A 4 TYR A 47 HIS A 51 -1 N HIS A 51 O SER A 111
SHEET 4 A 4 LYS A 82 LYS A 85 -1 O LEU A 84 N ALA A 48
SHEET 1 B 4 GLU A 30 ILE A 33 0
SHEET 2 B 4 TRP A 96 ASN A 102 -1 O TRP A 98 N ILE A 33
SHEET 3 B 4 MET A 59 ARG A 65 -1 N LEU A 64 O ILE A 97
SHEET 4 B 4 LYS A 76 ASN A 78 -1 O LYS A 76 N LEU A 63
SSBOND 1 CYS A 32 CYS A 129 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 - r 2 2 Bytes