Header list of 1rch.pdb file
Complete list - r 2 2 Bytes
HEADER ENDONUCLEASE 23-JUN-95 1RCH
TITLE SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI, 8
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE HI;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE H;
COMPND 5 EC: 3.1.26.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS HYDROLASE, NUCLEASE, ENDONUCLEASE, MAGNESIUM
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR T.YAMAZAKI,M.FUJIWARA,T.KATO,K.YAMASAKI,K.NAGAYAMA
REVDAT 4 02-MAR-22 1RCH 1 REMARK
REVDAT 3 24-FEB-09 1RCH 1 VERSN
REVDAT 2 22-FEB-05 1RCH 1 JRNL
REVDAT 1 12-FEB-97 1RCH 0
JRNL AUTH M.FUJIWARA,T.KATO,T.YAMAZAKI,K.YAMASAKI,K.NAGAYAMA
JRNL TITL SOLUTION STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI
JRNL REF BIOL.PHARM.BULL. V. 23 1147 2000
JRNL REFN ISSN 0918-6158
JRNL PMID 11041241
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.YAMAZAKI,M.YOSHIDA,K.NAGAYAMA
REMARK 1 TITL COMPLETE ASSIGNMENTS OF MAGNETIC RESONANCES OF RIBONUCLEASE
REMARK 1 TITL 2 H FROM ESCHERICHIA COLI BY DOUBLE-AND TRIPLE-RESONANCE 2D
REMARK 1 TITL 3 AND 3D NMR SPECTROSCOPIES
REMARK 1 REF BIOCHEMISTRY V. 32 5656 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.ENDO,H.WAKO,K.NAGAYAMA,N.GO
REMARK 1 TITL A NEW VERSION OF DADAS (DISTANCE ANALYSIS IN DIHEDRAL ANGLE
REMARK 1 TITL 2 SPACE) AND ITS PERFORMANCE
REMARK 1 EDIT J.C.HOCH, F.M.POULSEN, C.REDFIELD
REMARK 1 REF COMPUTATIONAL ASPECTS OF THE 233 1991
REMARK 1 REF 2 STUDY OF BIOLOGICAL
REMARK 1 REF 3 MACROMOLECULES BY NUCLEAR
REMARK 1 REF 4 MAGNETIC RESONANCE
REMARK 1 REF 5 SPECTROSCOPY (IN: NATO ASI
REMARK 1 REF 6 SER.,SER.A, V.225)
REMARK 1 PUBL NEW YORK : PLENUM PRESS
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DADAS90
REMARK 3 AUTHORS : JEOL.LTD
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RCH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176016.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 10 108.08 -160.37
REMARK 500 1 ASN A 16 76.71 -176.60
REMARK 500 1 TYR A 28 -165.01 -111.67
REMARK 500 1 ARG A 29 97.03 -54.81
REMARK 500 1 GLU A 61 105.25 179.18
REMARK 500 1 HIS A 62 97.18 -55.68
REMARK 500 1 ASP A 70 31.99 -156.15
REMARK 500 1 THR A 79 39.29 -94.71
REMARK 500 1 GLN A 80 -51.70 -158.85
REMARK 500 1 ASP A 94 32.88 -99.54
REMARK 500 1 LYS A 95 90.38 50.91
REMARK 500 1 GLN A 113 -52.25 -147.56
REMARK 500 1 HIS A 124 -52.58 -151.46
REMARK 500 1 ALA A 125 35.58 -93.91
REMARK 500 1 MET A 142 33.09 -95.75
REMARK 500 1 ASN A 143 72.68 -160.39
REMARK 500 1 THR A 145 38.68 -148.74
REMARK 500 2 ASP A 10 92.92 -160.69
REMARK 500 2 ASN A 16 77.66 -168.24
REMARK 500 2 ARG A 29 94.89 -58.98
REMARK 500 2 LEU A 59 97.59 -61.83
REMARK 500 2 LYS A 60 46.20 -96.18
REMARK 500 2 ASP A 70 34.70 -160.15
REMARK 500 2 THR A 79 40.82 -93.98
REMARK 500 2 GLN A 80 -51.12 -152.50
REMARK 500 2 ASP A 94 34.66 -99.01
REMARK 500 2 ALA A 125 51.15 -91.38
REMARK 500 2 THR A 145 -49.93 -156.78
REMARK 500 2 GLN A 152 -81.05 -146.92
REMARK 500 2 VAL A 153 60.67 60.39
REMARK 500 3 GLN A 4 128.92 -174.10
REMARK 500 3 ASP A 10 97.69 -160.25
REMARK 500 3 ASN A 16 76.98 -175.49
REMARK 500 3 TYR A 28 -165.07 -114.88
REMARK 500 3 ARG A 29 97.21 -55.79
REMARK 500 3 ARG A 41 114.40 -164.51
REMARK 500 3 LYS A 60 52.67 -141.40
REMARK 500 3 HIS A 62 76.74 -68.18
REMARK 500 3 ILE A 78 -70.09 -68.28
REMARK 500 3 THR A 79 40.29 -94.99
REMARK 500 3 GLN A 80 -52.17 -159.48
REMARK 500 3 TRP A 90 78.62 56.51
REMARK 500 3 THR A 92 -61.66 -132.79
REMARK 500 3 ALA A 93 -72.94 -157.25
REMARK 500 3 ASP A 94 45.53 -96.16
REMARK 500 3 LYS A 95 90.29 59.02
REMARK 500 3 GLN A 113 -50.02 -137.64
REMARK 500 3 HIS A 124 -55.32 -150.84
REMARK 500 3 MET A 142 36.53 -94.28
REMARK 500 3 ASN A 143 67.96 -155.69
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RCH A 1 155 UNP P0A7Y4 RNH_ECOLI 1 155
SEQRES 1 A 155 MET LEU LYS GLN VAL GLU ILE PHE THR ASP GLY SER CYS
SEQRES 2 A 155 LEU GLY ASN PRO GLY PRO GLY GLY TYR GLY ALA ILE LEU
SEQRES 3 A 155 ARG TYR ARG GLY ARG GLU LYS THR PHE SER ALA GLY TYR
SEQRES 4 A 155 THR ARG THR THR ASN ASN ARG MET GLU LEU MET ALA ALA
SEQRES 5 A 155 ILE VAL ALA LEU GLU ALA LEU LYS GLU HIS CYS GLU VAL
SEQRES 6 A 155 ILE LEU SER THR ASP SER GLN TYR VAL ARG GLN GLY ILE
SEQRES 7 A 155 THR GLN TRP ILE HIS ASN TRP LYS LYS ARG GLY TRP LYS
SEQRES 8 A 155 THR ALA ASP LYS LYS PRO VAL LYS ASN VAL ASP LEU TRP
SEQRES 9 A 155 GLN ARG LEU ASP ALA ALA LEU GLY GLN HIS GLN ILE LYS
SEQRES 10 A 155 TRP GLU TRP VAL LYS GLY HIS ALA GLY HIS PRO GLU ASN
SEQRES 11 A 155 GLU ARG CYS ASP GLU LEU ALA ARG ALA ALA ALA MET ASN
SEQRES 12 A 155 PRO THR LEU GLU ASP THR GLY TYR GLN VAL GLU VAL
HELIX 1 1 ASN A 44 ALA A 58 1 15
HELIX 2 2 GLN A 72 ILE A 78 1 7
HELIX 3 3 TRP A 81 ARG A 88 1 8
HELIX 4 4 VAL A 101 LEU A 111 1 11
HELIX 5 5 PRO A 128 ALA A 141 1 14
SHEET 1 A 5 ARG A 31 SER A 36 0
SHEET 2 A 5 GLY A 21 TYR A 28 -1 N TYR A 28 O ARG A 31
SHEET 3 A 5 GLN A 4 CYS A 13 -1 N SER A 12 O GLY A 21
SHEET 4 A 5 GLU A 64 SER A 68 1 N ILE A 66 O VAL A 5
SHEET 5 A 5 HIS A 114 LYS A 122 1 N LYS A 117 O VAL A 65
CISPEP 1 ASN A 16 PRO A 17 1 -4.09
CISPEP 2 ASN A 16 PRO A 17 2 -2.11
CISPEP 3 ASN A 16 PRO A 17 3 -6.30
CISPEP 4 ASN A 16 PRO A 17 4 5.43
CISPEP 5 ASN A 16 PRO A 17 5 -2.26
CISPEP 6 ASN A 16 PRO A 17 6 -5.90
CISPEP 7 ASN A 16 PRO A 17 7 -0.43
CISPEP 8 ASN A 16 PRO A 17 8 -0.94
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