Header list of 2b0f.pdb file
Complete list - r 22 2 Bytes
HEADER HYDROLASE/HYDROLASE INHIBITOR 13-SEP-05 2B0F
TITLE NMR STRUCTURE OF THE HUMAN RHINOVIRUS 3C PROTEASE (SEROTYPE 14) WITH
TITLE 2 COVALENTLY BOUND ACE-LEALFQ-ETHYLPROPIONATE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE 3C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HUMAN RHINOVIRUS SEROTYPE 14 3C PROTEASE;
COMPND 5 SYNONYM: PICORNAIN 3C,P3C;
COMPND 6 EC: 3.4.22.28;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACE-LEALFQ-ETHYLPROPIONATE;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHINOVIRUS B14;
SOURCE 3 ORGANISM_TAXID: 12131;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLYSS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630;
SOURCE 13 OTHER_DETAILS: PEPTIDYL INHIBITOR SYNTHESIZED VIA SOLID AND SOLUTION
SOURCE 14 PHASE PEDTIDE SYNTHESIS
KEYWDS BETA BARREL, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.C.BJORNDAHL,L.C.ANDREW,D.S.WISHART
REVDAT 4 01-MAR-23 2B0F 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQRES HET HETNAM FORMUL
REVDAT 4 3 1 LINK ATOM
REVDAT 3 13-JUL-11 2B0F 1 VERSN
REVDAT 2 20-MAY-08 2B0F 1 JRNL VERSN
REVDAT 1 05-SEP-06 2B0F 0
JRNL AUTH T.C.BJORNDAHL,L.C.ANDREW,V.SEMENCHENKO,D.S.WISHART
JRNL TITL NMR SOLUTION STRUCTURES OF THE APO AND PEPTIDE-INHIBITED
JRNL TITL 2 HUMAN RHINOVIRUS 3C PROTEASE (SEROTYPE 14): STRUCTURAL AND
JRNL TITL 3 DYNAMIC COMPARISON
JRNL REF BIOCHEMISTRY V. 46 12945 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17944485
JRNL DOI 10.1021/BI7010866
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR XPLOR-NIH V.2.10, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B0F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034519.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25; 25
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 20MM KH2PO4; 20MM KH2PO4
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75MM HRV14-3C WITH COVALENT
REMARK 210 INHIBITOR 20MM KH2PO4 15MM DTT
REMARK 210 0.5MM EDTA 0.1MM DSS PH 6.5; 90%
REMARK 210 H2O, 10% D2O; 0.75MM HRV14-3C
REMARK 210 WITH COVALENT INHIBITOR 20MM
REMARK 210 KH2PO4 15MM DTT 0.5MM EDTA 0.1MM
REMARK 210 DSS PD 6.5; 99.96% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA;
REMARK 210 15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210 RECOORD WATER REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: H-BOND DONORS DETERMINED FROM 15N HSQC EXCHANGED INTO D2O.
REMARK 210 3J HNHA COUPLINGS DETERMINED FROM HNHA. 13C-SEPERATED NOESY
REMARK 210 COLLECTED IN 99.96% D2O WITHOUT WET WATER SUPPRESSION TO ACHIEVE
REMARK 210 CROSS STRAND BETA-SHEET HA-HA NOES.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLN A 182 O
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 ASP A 32 -89.21 52.06
REMARK 500 1 GLN A 42 69.07 61.12
REMARK 500 1 ASN A 67 61.98 39.99
REMARK 500 1 GLU A 71 7.89 80.61
REMARK 500 1 GLU A 95 13.48 55.75
REMARK 500 1 ASN A 110 70.40 69.39
REMARK 500 1 TYR A 139 114.70 -163.06
REMARK 500 1 THR A 143 155.68 -45.03
REMARK 500 2 ASP A 32 -90.89 55.12
REMARK 500 2 HIS A 40 4.02 -68.42
REMARK 500 2 GLN A 42 70.97 57.99
REMARK 500 2 PRO A 65 -5.16 -55.88
REMARK 500 2 LEU A 94 -80.78 -74.82
REMARK 500 2 GLU A 95 71.38 45.26
REMARK 500 2 SER A 105 -163.91 -121.63
REMARK 500 2 ASN A 110 71.87 74.44
REMARK 500 2 SER A 128 0.58 81.41
REMARK 500 2 ALA A 140 90.66 -69.85
REMARK 500 2 THR A 143 158.92 -44.30
REMARK 500 3 THR A 20 -162.95 -118.05
REMARK 500 3 ASP A 32 -101.37 44.99
REMARK 500 3 GLN A 42 71.38 62.51
REMARK 500 3 ASP A 58 132.23 -171.96
REMARK 500 3 PRO A 65 -10.21 -48.00
REMARK 500 3 LEU A 94 -68.09 -100.07
REMARK 500 3 GLU A 95 73.87 41.70
REMARK 500 3 SER A 105 -160.67 -109.77
REMARK 500 3 SER A 128 -3.68 85.65
REMARK 500 3 TYR A 139 133.75 -178.42
REMARK 500 3 THR A 143 161.46 -43.30
REMARK 500 4 THR A 20 -157.55 -146.40
REMARK 500 4 ASP A 32 -88.07 58.36
REMARK 500 4 GLN A 42 71.96 56.31
REMARK 500 4 LEU A 94 -72.23 -60.75
REMARK 500 4 ASN A 110 73.36 66.73
REMARK 500 4 ALA A 121 -66.24 -90.07
REMARK 500 4 THR A 143 150.25 -43.10
REMARK 500 4 GLU B 3 71.85 -114.59
REMARK 500 5 ASP A 32 -88.74 57.18
REMARK 500 5 GLN A 42 72.83 60.58
REMARK 500 5 ASN A 67 72.52 71.76
REMARK 500 5 GLU A 71 31.14 71.62
REMARK 500 5 ASN A 110 72.45 77.24
REMARK 500 5 TYR A 139 133.19 -176.12
REMARK 500 5 THR A 143 158.72 -42.24
REMARK 500 6 ASP A 32 -90.49 51.65
REMARK 500 6 ARG A 33 16.36 -140.15
REMARK 500 6 GLN A 42 73.23 62.44
REMARK 500 6 GLU A 71 22.00 84.07
REMARK 500 6 ASP A 85 90.26 -60.64
REMARK 500
REMARK 500 THIS ENTRY HAS 226 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 9 ARG A 133 0.08 SIDE CHAIN
REMARK 500 10 ARG A 33 0.09 SIDE CHAIN
REMARK 500 15 ARG A 166 0.07 SIDE CHAIN
REMARK 500 16 ARG A 55 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF ACE-LEALFQ
REMARK 800 -ETHYLPROPIONATE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CQQ RELATED DB: PDB
REMARK 900 SAME PROTEIN OF A DIFFERENT SEROTYPE (2) SHARES 51% SEQUENCE
REMARK 900 IDENTITY
REMARK 900 RELATED ID: 1L1N RELATED DB: PDB
REMARK 900 POLIO 3C PROTEASE, ANOTHER HOMOLOGUE SHARING 46% SEQENCE IDENTITY.
DBREF 2B0F A 1 182 UNP P03303 POLG_HRV14 1538 1719
DBREF 2B0F B 1 7 PDB 2B0F 2B0F 1 7
SEQRES 1 A 182 GLY PRO ASN THR GLU PHE ALA LEU SER LEU LEU ARG LYS
SEQRES 2 A 182 ASN ILE MET THR ILE THR THR SER LYS GLY GLU PHE THR
SEQRES 3 A 182 GLY LEU GLY ILE HIS ASP ARG VAL CYS VAL ILE PRO THR
SEQRES 4 A 182 HIS ALA GLN PRO GLY ASP ASP VAL LEU VAL ASN GLY GLN
SEQRES 5 A 182 LYS ILE ARG VAL LYS ASP LYS TYR LYS LEU VAL ASP PRO
SEQRES 6 A 182 GLU ASN ILE ASN LEU GLU LEU THR VAL LEU THR LEU ASP
SEQRES 7 A 182 ARG ASN GLU LYS PHE ARG ASP ILE ARG GLY PHE ILE SER
SEQRES 8 A 182 GLU ASP LEU GLU GLY VAL ASP ALA THR LEU VAL VAL HIS
SEQRES 9 A 182 SER ASN ASN PHE THR ASN THR ILE LEU GLU VAL GLY PRO
SEQRES 10 A 182 VAL THR MET ALA GLY LEU ILE ASN LEU SER SER THR PRO
SEQRES 11 A 182 THR ASN ARG MET ILE ARG TYR ASP TYR ALA THR LYS THR
SEQRES 12 A 182 GLY GLN CYS GLY GLY VAL LEU CYS ALA THR GLY LYS ILE
SEQRES 13 A 182 PHE GLY ILE HIS VAL GLY GLY ASN GLY ARG GLN GLY PHE
SEQRES 14 A 182 SER ALA GLN LEU LYS LYS GLN TYR PHE VAL GLU LYS GLN
SEQRES 1 B 7 ACE LEU GLU ALA LEU PHE YTF
HET ACE B 1 6
HET YTF B 7 30
HETNAM ACE ACETYL GROUP
HETNAM YTF ETHYL (4~{S})-4,7-BIS(AZANYL)-7-OXIDANYLIDENE-
HETNAM 2 YTF HEPTANOATE
FORMUL 2 ACE C2 H4 O
FORMUL 2 YTF C9 H18 N2 O3
HELIX 1 1 GLY A 1 ASN A 14 1 14
HELIX 2 2 ASP A 85 ILE A 90 5 6
HELIX 3 3 LYS A 174 VAL A 179 1 6
SHEET 1 A 7 ILE A 15 THR A 19 0
SHEET 2 A 7 GLU A 24 HIS A 31 -1 O GLY A 27 N MET A 16
SHEET 3 A 7 VAL A 34 ILE A 37 -1 O VAL A 36 N LEU A 28
SHEET 4 A 7 ILE A 68 ASP A 78 -1 O LEU A 75 N CYS A 35
SHEET 5 A 7 GLN A 52 ASP A 64 -1 N LEU A 62 O LEU A 72
SHEET 6 A 7 ASP A 46 VAL A 49 -1 N VAL A 47 O ILE A 54
SHEET 7 A 7 ILE A 15 THR A 19 -1 N THR A 19 O LEU A 48
SHEET 1 B10 THR A 111 LEU A 126 0
SHEET 2 B10 PRO A 130 ASP A 138 -1 O ARG A 136 N THR A 119
SHEET 3 B10 GLN A 167 GLN A 172 -1 O SER A 170 N ILE A 135
SHEET 4 B10 LYS A 155 ASN A 164 -1 N ASN A 164 O GLN A 167
SHEET 5 B10 THR A 111 LEU A 126 0
SHEET 6 B10 ASP A 98 VAL A 103 -1 N LEU A 101 O LEU A 113
SHEET 7 B10 VAL A 149 ALA A 152 -1 O VAL A 149 N VAL A 102
SHEET 8 B10 LYS A 155 ASN A 164 -1 O LYS A 155 N ALA A 152
SHEET 9 B10 GLU B 3 PHE B 6 -1 O LEU B 5 N GLY A 163
SHEET 10 B10 LYS A 155 ASN A 164 -1 N GLY A 163 O LEU B 5
LINK SG CYS A 146 CX5 YTF B 7 1555 1555 1.82
LINK C ACE B 1 N LEU B 2 1555 1555 1.32
LINK C PHE B 6 N YTF B 7 1555 1555 1.33
SITE 1 AC1 19 LYS A 22 HIS A 40 GLU A 71 ILE A 124
SITE 2 AC1 19 ASN A 125 LEU A 126 SER A 127 SER A 128
SITE 3 AC1 19 THR A 141 LYS A 142 THR A 143 GLY A 144
SITE 4 AC1 19 CYS A 146 HIS A 160 VAL A 161 GLY A 162
SITE 5 AC1 19 GLY A 163 ASN A 164 PHE A 169
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 22 2 Bytes