Header list of 1nso.pdb file
Complete list - v 10 2 Bytes
HEADER HYDROLASE 28-JAN-03 1NSO
TITLE FOLDED MONOMER OF PROTEASE FROM MASON-PFIZER MONKEY VIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE 13 KDA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.23.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SIMIAN RETROVIRUS SRV-1;
SOURCE 3 ORGANISM_TAXID: 11942;
SOURCE 4 GENE: POL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS M-PMV, PROTEASE, VIRUS MATURATION, FOLDED MONOMER, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR V.VEVERKA,H.BAUEROVA,A.ZABRANSKY,J.LANG,T.RUML,I.PICHOVA,R.HRABAL
REVDAT 5 10-NOV-21 1NSO 1 COMPND SOURCE DBREF SEQADV
REVDAT 4 27-OCT-21 1NSO 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1NSO 1 VERSN
REVDAT 2 18-NOV-03 1NSO 1 JRNL
REVDAT 1 18-FEB-03 1NSO 0
JRNL AUTH V.VEVERKA,H.BAUEROVA,A.ZABRANSKY,J.LANG,T.RUML,I.PICHOVA,
JRNL AUTH 2 R.HRABAL
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF A MONOMERIC FORM OF A
JRNL TITL 2 RETROVIRAL PROTEASE
JRNL REF J.MOL.BIOL. V. 333 771 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14568536
JRNL DOI 10.1016/J.JMB.2003.08.049
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, ARIA 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE, J., O'DONOGHUE, S.,
REMARK 3 NILGES, M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018165.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEASE U-15N,13C; 50MM
REMARK 210 ACETATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.106, ARIA
REMARK 210 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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 O ASP A 47 HA LYS A 62 1.37
REMARK 500 O ASP A 47 CA LYS A 62 2.02
REMARK 500 O ASP A 47 CB LYS A 62 2.18
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 ALA A 7 153.76 61.38
REMARK 500 1 GLN A 8 90.31 -66.90
REMARK 500 1 ASP A 17 -66.78 67.06
REMARK 500 1 ASP A 18 34.96 -173.52
REMARK 500 1 GLN A 57 93.12 -43.32
REMARK 500 1 SER A 64 163.23 -34.50
REMARK 500 1 LYS A 66 111.77 -33.97
REMARK 500 1 LYS A 73 -27.30 -39.78
REMARK 500 1 ASN A 75 45.04 75.39
REMARK 500 1 ASN A 76 140.68 174.64
REMARK 500 1 SER A 77 -47.11 -168.73
REMARK 500 1 LEU A 88 84.61 68.36
REMARK 500 1 PRO A 89 29.61 -77.25
REMARK 500 1 ASN A 91 90.33 40.61
REMARK 500 1 LYS A 102 49.75 179.04
REMARK 500 1 MET A 105 72.97 -65.40
REMARK 500 2 ALA A 7 -171.19 60.68
REMARK 500 2 ASP A 17 34.30 24.07
REMARK 500 2 ASP A 18 -47.80 167.97
REMARK 500 2 ASP A 30 -36.70 -147.45
REMARK 500 2 LYS A 35 162.94 -46.61
REMARK 500 2 PRO A 40 107.85 -53.50
REMARK 500 2 THR A 46 -179.78 -65.99
REMARK 500 2 ASP A 47 -58.73 148.56
REMARK 500 2 GLN A 57 93.44 -42.81
REMARK 500 2 LYS A 66 119.77 -18.79
REMARK 500 2 LYS A 73 -30.20 -36.69
REMARK 500 2 ASN A 76 144.32 177.88
REMARK 500 2 SER A 77 -45.64 177.53
REMARK 500 2 PRO A 86 48.29 -86.09
REMARK 500 2 ASN A 87 13.67 -144.99
REMARK 500 2 LEU A 88 78.53 66.17
REMARK 500 2 PRO A 89 9.18 -69.20
REMARK 500 2 VAL A 90 -8.01 95.09
REMARK 500 2 ASN A 91 86.53 54.71
REMARK 500 2 LYS A 102 -29.79 -147.10
REMARK 500 2 ILE A 103 -87.41 -76.36
REMARK 500 2 MET A 105 81.61 -62.29
REMARK 500 3 ALA A 7 -178.53 61.74
REMARK 500 3 GLN A 57 94.20 -41.41
REMARK 500 3 SER A 64 154.77 -27.67
REMARK 500 3 LYS A 66 146.22 -31.59
REMARK 500 3 LYS A 73 -33.31 -35.50
REMARK 500 3 SER A 77 -68.06 -174.21
REMARK 500 3 PRO A 86 43.41 -83.75
REMARK 500 3 LEU A 88 86.03 65.69
REMARK 500 3 PRO A 89 27.13 -77.87
REMARK 500 3 MET A 104 -174.82 -63.81
REMARK 500 3 MET A 105 72.73 -67.80
REMARK 500 4 ALA A 7 -162.08 60.51
REMARK 500
REMARK 500 THIS ENTRY HAS 170 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NSO A 1 107 UNP P04025 POL_SRV1 761 867
SEQADV 1NSO ALA A 7 UNP P04025 CYS 767 ENGINEERED MUTATION
SEQADV 1NSO ASN A 26 UNP P04025 ASP 786 ENGINEERED MUTATION
SEQADV 1NSO ALA A 106 UNP P04025 CYS 866 ENGINEERED MUTATION
SEQRES 1 A 107 TRP VAL GLN PRO ILE THR ALA GLN LYS PRO SER LEU THR
SEQRES 2 A 107 LEU TRP LEU ASP ASP LYS MET PHE THR GLY LEU ILE ASN
SEQRES 3 A 107 THR GLY ALA ASP VAL THR ILE ILE LYS LEU GLU ASP TRP
SEQRES 4 A 107 PRO PRO ASN TRP PRO ILE THR ASP THR LEU THR ASN LEU
SEQRES 5 A 107 ARG GLY ILE GLY GLN SER ASN ASN PRO LYS GLN SER SER
SEQRES 6 A 107 LYS TYR LEU THR TRP ARG ASP LYS GLU ASN ASN SER GLY
SEQRES 7 A 107 LEU ILE LYS PRO PHE VAL ILE PRO ASN LEU PRO VAL ASN
SEQRES 8 A 107 LEU TRP GLY ARG ASP LEU LEU SER GLN MET LYS ILE MET
SEQRES 9 A 107 MET ALA SER
HELIX 1 1 LYS A 35 TRP A 39 5 5
HELIX 2 2 GLY A 94 ILE A 103 1 10
SHEET 1 A 4 LYS A 19 GLY A 23 0
SHEET 2 A 4 LEU A 12 LEU A 16 -1 N LEU A 16 O LYS A 19
SHEET 3 A 4 LEU A 68 ASP A 72 -1 O ARG A 71 N TRP A 15
SHEET 4 A 4 ASN A 76 ILE A 80 -1 O GLY A 78 N TRP A 70
SHEET 1 B 2 LEU A 49 LEU A 52 0
SHEET 2 B 2 GLN A 57 ASN A 60 -1 O ASN A 60 N LEU A 49
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 - v 10 2 Bytes