Header list of 1z8r.pdb file
Complete list - t 20 2 Bytes
HEADER HYDROLASE 31-MAR-05 1Z8R
TITLE 2A CYSTEINE PROTEINASE FROM HUMAN COXSACKIEVIRUS B4 (STRAIN JVB /
TITLE 2 BENSCHOTEN / NEW YORK / 51)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COXSACKIEVIRUS B4 POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PICORNAIN 2A;
COMPND 5 EC: 3.4.22.29;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN COXSACKIEVIRUS B4;
SOURCE 3 ORGANISM_TAXID: 12073;
SOURCE 4 GENE: PICORNAIN 2A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS BETA BARREL COORDINATED ZINC ION, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR N.J.BAXTER,A.ROETZER,H.D.LIEBIG,S.E.SEDELNIKOVA,A.M.HOUNSLOW,T.SKERN,
AUTHOR 2 J.P.WALTHO
REVDAT 3 20-OCT-21 1Z8R 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Z8R 1 VERSN
REVDAT 1 14-FEB-06 1Z8R 0
JRNL AUTH N.J.BAXTER,A.ROETZER,H.D.LIEBIG,S.E.SEDELNIKOVA,
JRNL AUTH 2 A.M.HOUNSLOW,T.SKERN,J.P.WALTHO
JRNL TITL STRUCTURE AND DYNAMICS OF COXSACKIEVIRUS B4 2A PROTEINASE,
JRNL TITL 2 AN ENYZME INVOLVED IN THE ETIOLOGY OF HEART DISEASE.
JRNL REF J.VIROL. V. 80 1451 2006
JRNL REFN ISSN 0022-538X
JRNL PMID 16415022
JRNL DOI 10.1128/JVI.80.3.1451-1462.2006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 TOTAL OF 1905 EXPERIMENTALLY DETERMINED RESTRAINTS,
REMARK 3 1577 NOE-DERIVED DISTANCE RESTRAINTS,
REMARK 3 168 DIHEDRAL ANGLE RESTRAINTS,
REMARK 3 112 HYDROGEN BOND DISTANCE RESTRAINTS,
REMARK 3 4 ZINC-PROTEIN BOND RESTRAINTS,
REMARK 3 16 ZINC-PROTEIN ANGLE RESTRAINTS
REMARK 4
REMARK 4 1Z8R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032440.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303; 303
REMARK 210 PH : 7.6; 7.6; 7.6; 7.6; 7.6
REMARK 210 IONIC STRENGTH : 50 MM POTASSIUM PHOSPHATE; 50 MM
REMARK 210 POTASSIUM PHOSPHATE; 50 MM
REMARK 210 POTASSIUM PHOSPHATE; 50 MM
REMARK 210 POTASSIUM PHOSPHATE; 50 MM
REMARK 210 POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.25 MM U-15N 2A PROTEINASE 10
REMARK 210 MM DTT 90% H2O, 10% D2O; 0.25 MM
REMARK 210 U-15N U-13C 2A PROTEINASE 10 MM
REMARK 210 DTT 90% H2O, 10% D2O; 0.50 MM U-
REMARK 210 15N U-13C 2A PROTEINASE 10 MM
REMARK 210 DTT 90% H2O, 10% D2O; 0.25 MM U-
REMARK 210 15N U-13C 2A PROTEINASE 10 MM
REMARK 210 DTT 100% D2O; 0.55 MM
REMARK 210 BIOSYNTHETICALLY DIRECTED
REMARK 210 FRACTIONAL 10%-13C 2A PROTEINASE
REMARK 210 10 MM DTT 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SIMULTANEOUSLY ACQUIRED 15N- AND
REMARK 210 13C-EDITED 3D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY CARTESIAN SLOW-COOL ANNEALING
REMARK 210 ENERGY MINIMISATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
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: 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 1-17
REMARK 465 RES C SSSEQI
REMARK 465 MET A -15
REMARK 465 ALA A -14
REMARK 465 HIS A -13
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 GLU A -7
REMARK 465 ARG A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 LEU A -3
REMARK 465 ILE A -2
REMARK 465 THR A -1
REMARK 465 THR 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
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 TYR A 3 -46.71 -161.62
REMARK 500 1 GLU A 34 118.15 -160.34
REMARK 500 1 GLU A 88 -81.36 56.95
REMARK 500 1 TYR A 89 22.93 -155.64
REMARK 500 1 LYS A 92 89.52 -49.20
REMARK 500 1 PRO A 107 174.42 -59.40
REMARK 500 1 ILE A 121 -64.60 -98.94
REMARK 500 1 THR A 125 -88.60 -91.34
REMARK 500 1 LEU A 140 64.71 -156.10
REMARK 500 1 TRP A 142 80.19 -53.70
REMARK 500 1 LEU A 143 -48.19 -153.36
REMARK 500 2 GLN A 6 111.12 62.07
REMARK 500 2 SER A 7 131.37 63.87
REMARK 500 2 ARG A 55 42.50 -93.31
REMARK 500 2 GLU A 88 -79.14 57.41
REMARK 500 2 TYR A 89 25.38 -159.59
REMARK 500 2 LYS A 92 92.26 -53.14
REMARK 500 2 HIS A 97 55.53 75.76
REMARK 500 2 PHE A 104 -46.02 -156.32
REMARK 500 2 SER A 105 80.79 -171.63
REMARK 500 2 THR A 125 -88.95 -105.27
REMARK 500 2 LEU A 140 51.80 -162.11
REMARK 500 2 TRP A 142 81.92 -53.86
REMARK 500 2 LEU A 143 -44.84 -150.95
REMARK 500 2 GLU A 144 -159.23 -146.59
REMARK 500 2 MET A 148 -175.81 -64.49
REMARK 500 3 PRO A 2 91.10 -52.23
REMARK 500 3 TYR A 3 174.82 60.82
REMARK 500 3 THR A 46 45.97 -95.14
REMARK 500 3 CYS A 50 -46.15 -154.10
REMARK 500 3 LYS A 68 -169.06 -125.08
REMARK 500 3 SER A 69 33.49 -97.63
REMARK 500 3 GLU A 88 -80.21 59.25
REMARK 500 3 TYR A 89 22.18 -152.11
REMARK 500 3 LYS A 92 71.51 -67.77
REMARK 500 3 PHE A 104 95.58 -58.21
REMARK 500 3 SER A 105 -46.48 -154.45
REMARK 500 3 ASP A 109 -57.63 -170.65
REMARK 500 3 THR A 125 -90.35 -120.56
REMARK 500 3 LEU A 140 48.67 -173.14
REMARK 500 3 TRP A 142 82.06 -56.65
REMARK 500 3 LEU A 143 -47.29 -149.06
REMARK 500 3 MET A 148 -57.75 -155.88
REMARK 500 4 TYR A 3 -63.95 -127.12
REMARK 500 4 CYS A 50 -46.70 -142.23
REMARK 500 4 ARG A 55 34.76 -92.33
REMARK 500 4 GLU A 88 -83.87 51.41
REMARK 500 4 TYR A 89 19.75 -145.67
REMARK 500 4 LYS A 92 70.44 -65.36
REMARK 500 4 SER A 105 62.69 -101.10
REMARK 500
REMARK 500 THIS ENTRY HAS 262 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 151 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 56 SG
REMARK 620 2 CYS A 58 SG 108.1
REMARK 620 3 CYS A 116 SG 111.3 109.2
REMARK 620 4 HIS A 118 ND1 108.8 109.8 109.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 151
DBREF 1Z8R A -7 150 UNP P08292 POLG_CXB4J 842 999
SEQADV 1Z8R MET A -15 UNP P08292 CLONING ARTIFACT
SEQADV 1Z8R ALA A -14 UNP P08292 CLONING ARTIFACT
SEQADV 1Z8R HIS A -13 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R HIS A -12 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R HIS A -11 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R HIS A -10 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R HIS A -9 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R HIS A -8 UNP P08292 EXPRESSION TAG
SEQADV 1Z8R ALA A 110 UNP P08292 CYS 959 ENGINEERED MUTATION
SEQRES 1 A 166 MET ALA HIS HIS HIS HIS HIS HIS GLU ARG ALA SER LEU
SEQRES 2 A 166 ILE THR THR GLY PRO TYR GLY HIS GLN SER GLY ALA VAL
SEQRES 3 A 166 TYR VAL GLY ASN TYR LYS VAL VAL ASN ARG HIS LEU ALA
SEQRES 4 A 166 THR HIS VAL ASP TRP GLN ASN CYS VAL TRP GLU ASP TYR
SEQRES 5 A 166 ASN ARG ASP LEU LEU VAL SER THR THR THR ALA HIS GLY
SEQRES 6 A 166 CYS ASP THR ILE ALA ARG CYS GLN CYS THR THR GLY VAL
SEQRES 7 A 166 TYR PHE CYS ALA SER LYS SER LYS HIS TYR PRO VAL SER
SEQRES 8 A 166 PHE GLU GLY PRO GLY LEU VAL GLU VAL GLN GLU SER GLU
SEQRES 9 A 166 TYR TYR PRO LYS ARG TYR GLN SER HIS VAL LEU LEU ALA
SEQRES 10 A 166 THR GLY PHE SER GLU PRO GLY ASP ALA GLY GLY ILE LEU
SEQRES 11 A 166 ARG CYS GLU HIS GLY VAL ILE GLY LEU VAL THR MET GLY
SEQRES 12 A 166 GLY GLU GLY VAL VAL GLY PHE ALA ASP VAL ARG ASP LEU
SEQRES 13 A 166 LEU TRP LEU GLU ASP ASP ALA MET GLU GLN
HET ZN A 151 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 HIS A 21 ALA A 23 5 3
HELIX 2 2 THR A 24 ASN A 30 1 7
SHEET 1 A 4 VAL A 10 VAL A 12 0
SHEET 2 A 4 TYR A 15 ASN A 19 -1 O TYR A 15 N VAL A 12
SHEET 3 A 4 LEU A 40 THR A 44 -1 O SER A 43 N LYS A 16
SHEET 4 A 4 CYS A 31 ASP A 35 -1 N VAL A 32 O VAL A 42
SHEET 1 B 2 THR A 60 PHE A 64 0
SHEET 2 B 2 HIS A 71 SER A 75 -1 O TYR A 72 N TYR A 63
SHEET 1 C 2 LEU A 81 VAL A 84 0
SHEET 2 C 2 ARG A 93 SER A 96 -1 O GLN A 95 N VAL A 82
SHEET 1 D 4 VAL A 98 THR A 102 0
SHEET 2 D 4 VAL A 131 ASP A 136 -1 O PHE A 134 N LEU A 99
SHEET 3 D 4 VAL A 120 GLY A 127 -1 N LEU A 123 O ALA A 135
SHEET 4 D 4 ILE A 113 ARG A 115 -1 N LEU A 114 O ILE A 121
LINK SG CYS A 56 ZN ZN A 151 1555 1555 2.30
LINK SG CYS A 58 ZN ZN A 151 1555 1555 2.30
LINK SG CYS A 116 ZN ZN A 151 1555 1555 2.31
LINK ND1 HIS A 118 ZN ZN A 151 1555 1555 2.10
SITE 1 AC1 4 CYS A 56 CYS A 58 CYS A 116 HIS A 118
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 20 2 Bytes