Header list of 1o1w.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 12-FEB-03 1O1W
TITLE SOLUTION STRUCTURE OF THE RNASE H DOMAIN OF THE HIV-1 REVERSE
TITLE 2 TRANSCRIPTASE IN THE PRESENCE OF MAGNESIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE H;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE H;
COMPND 5 EC: 3.1.26.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 VARIANT: STRAIN HXB2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLR
KEYWDS HIV-1, RNASE H DOMAIN, HIV-1 REVERSE TRANSCRIPTASE, SOLUTION
KEYWDS 2 STRUCTURE, METAL BINDING, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR K.PARI,G.A.MUELLER,E.F.DEROSE,T.W.KIRBY,R.E.LONDON
REVDAT 3 23-FEB-22 1O1W 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1O1W 1 VERSN
REVDAT 1 18-FEB-03 1O1W 0
SPRSDE 18-FEB-03 1O1W 1LKU
JRNL AUTH K.PARI,G.A.MUELLER,E.F.DEROSE,T.W.KIRBY,R.E.LONDON
JRNL TITL SOLUTION STRUCTURE OF THE RNASE H DOMAIN OF THE HIV-1
JRNL TITL 2 REVERSE TRANSCRIPTASE IN THE PRESENCE OF MAGNESIUM
JRNL REF BIOCHEMISTRY V. 42 639 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12534276
JRNL DOI 10.1021/BI0204894
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O1W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000001700.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1 MM RNASE H U-15N, 13C MM
REMARK 210 TRIS, PH6.8; 90% H20, 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_ 15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.0, NMRPIPE 2.1, NMRVIEW
REMARK 210 5.0.4
REMARK 210 METHOD USED : AUTOMATED STRUCTURE
REMARK 210 DETERMINATION WITH ARIA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
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 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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 HG SER A 67 H GLY A 68 1.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 2 TYR A 19 CE1 TYR A 19 CZ 0.092
REMARK 500 2 TYR A 19 CZ TYR A 19 CE2 -0.095
REMARK 500 4 TYR A 35 CE1 TYR A 35 CZ -0.079
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 ASN A 2 -157.96 53.94
REMARK 500 1 TYR A 5 -179.46 173.36
REMARK 500 1 GLU A 8 -89.66 -110.69
REMARK 500 1 LYS A 9 0.50 59.19
REMARK 500 1 PRO A 11 122.17 -39.74
REMARK 500 1 LYS A 29 70.36 50.06
REMARK 500 1 LEU A 30 149.99 -173.09
REMARK 500 1 ALA A 33 118.59 -165.35
REMARK 500 1 ASN A 38 -4.40 -55.93
REMARK 500 1 LEU A 69 -85.99 -103.90
REMARK 500 1 SER A 77 108.44 -165.10
REMARK 500 1 ALA A 86 47.65 -90.22
REMARK 500 1 GLN A 87 70.53 32.85
REMARK 500 1 PRO A 88 32.76 -81.08
REMARK 500 1 GLN A 90 20.68 -163.78
REMARK 500 1 GLU A 92 -132.40 49.25
REMARK 500 1 SER A 93 144.66 -38.88
REMARK 500 1 GLU A 107 -80.77 -92.93
REMARK 500 1 PRO A 115 111.50 -38.16
REMARK 500 1 ALA A 116 -133.96 169.08
REMARK 500 1 HIS A 117 -1.96 -179.24
REMARK 500 1 ASP A 127 -72.29 -97.02
REMARK 500 1 LYS A 128 34.86 -161.72
REMARK 500 1 LEU A 129 79.68 55.79
REMARK 500 1 SER A 131 61.61 -109.14
REMARK 500 1 ILE A 134 53.52 -90.81
REMARK 500 1 ARG A 135 33.40 -141.34
REMARK 500 2 ASN A 2 -158.89 -99.58
REMARK 500 2 LEU A 4 -24.30 -148.69
REMARK 500 2 GLU A 8 -85.63 -120.58
REMARK 500 2 LYS A 9 3.75 57.49
REMARK 500 2 PRO A 11 103.65 -43.30
REMARK 500 2 ASP A 21 133.36 -171.62
REMARK 500 2 ASN A 25 100.69 -50.47
REMARK 500 2 ALA A 33 119.02 -164.50
REMARK 500 2 ASN A 38 -6.35 -55.43
REMARK 500 2 LEU A 69 -95.73 -132.13
REMARK 500 2 SER A 77 111.77 -165.66
REMARK 500 2 ALA A 86 47.30 -97.74
REMARK 500 2 GLN A 87 68.26 35.53
REMARK 500 2 PRO A 88 33.27 -82.87
REMARK 500 2 GLN A 90 21.14 -165.62
REMARK 500 2 GLU A 92 -121.94 52.09
REMARK 500 2 SER A 93 142.87 -37.92
REMARK 500 2 LYS A 108 166.81 162.16
REMARK 500 2 PRO A 115 111.68 -39.87
REMARK 500 2 ALA A 116 -160.49 178.52
REMARK 500 2 HIS A 117 46.86 -177.94
REMARK 500 2 ILE A 120 -85.46 -160.95
REMARK 500 2 ASN A 123 29.23 44.19
REMARK 500
REMARK 500 THIS ENTRY HAS 186 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1O1W A 5 138 UNP P04585 POL_HV1H2 582 715
SEQADV 1O1W MET A 1 UNP P04585 CLONING ARTIFACT
SEQADV 1O1W ASN A 2 UNP P04585 CLONING ARTIFACT
SEQADV 1O1W GLU A 3 UNP P04585 CLONING ARTIFACT
SEQADV 1O1W LEU A 4 UNP P04585 CLONING ARTIFACT
SEQRES 1 A 138 MET ASN GLU LEU TYR GLN LEU GLU LYS GLU PRO ILE VAL
SEQRES 2 A 138 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA ALA ASN ARG
SEQRES 3 A 138 GLU THR LYS LEU GLY LYS ALA GLY TYR VAL THR ASN ARG
SEQRES 4 A 138 GLY ARG GLN LYS VAL VAL THR LEU THR ASP THR THR ASN
SEQRES 5 A 138 GLN LYS THR GLU LEU GLN ALA ILE TYR LEU ALA LEU GLN
SEQRES 6 A 138 ASP SER GLY LEU GLU VAL ASN ILE VAL THR ASP SER GLN
SEQRES 7 A 138 TYR ALA LEU GLY ILE ILE GLN ALA GLN PRO ASP GLN SER
SEQRES 8 A 138 GLU SER GLU LEU VAL ASN GLN ILE ILE GLU GLN LEU ILE
SEQRES 9 A 138 LYS LYS GLU LYS VAL TYR LEU ALA TRP VAL PRO ALA HIS
SEQRES 10 A 138 LYS GLY ILE GLY GLY ASN GLU GLN VAL ASP LYS LEU VAL
SEQRES 11 A 138 SER ALA GLY ILE ARG LYS VAL LEU
HELIX 1 1 THR A 51 LEU A 64 1 14
HELIX 2 2 SER A 77 GLN A 85 1 9
HELIX 3 3 SER A 93 LYS A 106 1 14
SHEET 1 A 5 ARG A 41 THR A 46 0
SHEET 2 A 5 LYS A 32 THR A 37 -1 N ALA A 33 O VAL A 45
SHEET 3 A 5 THR A 17 VAL A 20 -1 N TYR A 19 O VAL A 36
SHEET 4 A 5 GLU A 70 VAL A 74 1 O ASN A 72 N PHE A 18
SHEET 5 A 5 LYS A 108 ALA A 112 1 O LYS A 108 N VAL A 71
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