Header list of 1ygw.pdb file
Complete list - v 29 2 Bytes
HEADER HYDROLASE 28-SEP-96 1YGW
TITLE NMR STRUCTURE OF RIBONUCLEASE T1, 34 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE T1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GUANYLORIBONUCLEASE, RNASE T1;
COMPND 5 EC: 3.1.27.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_TAXID: 5062;
SOURCE 4 GENE: RIBONUCLEASE T1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PA2T1-1;
SOURCE 9 EXPRESSION_SYSTEM_GENE: RIBONUCLEASE T1
KEYWDS HYDROLASE, RIBONUCLEASE, ENDONUCLEASE, RIBONUCLEASE T1 PRECURSOR,
KEYWDS 2 ENDORIBONUCLEASE
EXPDTA SOLUTION NMR
NUMMDL 34
AUTHOR S.PFEIFFER,Y.KARIMI-NEJAD,H.RUTERJANS
REVDAT 3 29-NOV-17 1YGW 1 REMARK HELIX
REVDAT 2 24-FEB-09 1YGW 1 VERSN
REVDAT 1 08-OCT-97 1YGW 0
JRNL AUTH S.PFEIFFER,Y.KARIMI-NEJAD,H.RUTERJANS
JRNL TITL LIMITS OF NMR STRUCTURE DETERMINATION USING VARIABLE TARGET
JRNL TITL 2 FUNCTION CALCULATIONS: RIBONUCLEASE T1, A CASE STUDY.
JRNL REF J.MOL.BIOL. V. 266 400 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9047372
JRNL DOI 10.1006/JMBI.1996.0784
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.PFEIFFER,J.ENGELKE,H.RUTERJANS
REMARK 1 TITL COMPLETE 1H, 15N AND 13C RESONANCE ASSIGNMENT OF
REMARK 1 TITL 2 RIBONUCLEASE T1: SECONDARY STRUCTURE AND BACKBONE DYNAMICS
REMARK 1 TITL 3 AS DERIVED FROM THE CHEMICAL SHIFTS
REMARK 1 REF Q.MAGN.RESON.BIOL.MED. V. 3 69 1996
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.KARIMI-NEJAD,J.M.SCHMIDT,H.RUTERJANS,H.SCHWALBE,
REMARK 1 AUTH 2 C.GRIESINGER
REMARK 1 TITL CONFORMATION OF VALINE SIDE CHAINS IN RIBONUCLEASE T1
REMARK 1 TITL 2 DETERMINED BY NMR STUDIES OF HOMONUCLEAR AND HETERONUCLEAR
REMARK 1 TITL 3 3J COUPLING CONSTANTS
REMARK 1 REF BIOCHEMISTRY V. 33 5481 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YGW 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_1000177397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.5
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : VARIABLE TARGET FUNCTION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 34
REMARK 210 CONFORMERS, SELECTION CRITERIA : SEE JRNL REFERENCE
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 H TYR A 57 O PHE A 80 1.09
REMARK 500 O VAL A 79 H ALA A 87 1.10
REMARK 500 O VAL A 89 H CYS A 103 1.15
REMARK 500 O TRP A 59 H VAL A 78 1.43
REMARK 500 O TYR A 24 H GLU A 28 1.45
REMARK 500 H TRP A 59 O VAL A 78 1.47
REMARK 500 O TYR A 57 H PHE A 80 1.48
REMARK 500 O CYS A 6 H SER A 8 1.59
REMARK 500 N TYR A 57 O PHE A 80 2.04
REMARK 500 O VAL A 79 N ALA A 87 2.06
REMARK 500 O VAL A 89 N CYS A 103 2.11
REMARK 500 O SER A 53 OD1 ASN A 81 2.12
REMARK 500 OH TYR A 24 O GLU A 82 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 CYS A 2 125.51 -36.70
REMARK 500 1 CYS A 10 61.87 -177.61
REMARK 500 1 ALA A 21 -34.09 -35.69
REMARK 500 1 LYS A 41 155.61 -44.12
REMARK 500 1 TYR A 42 10.80 -144.40
REMARK 500 1 ASN A 43 88.76 -7.94
REMARK 500 1 ASN A 44 174.45 -51.11
REMARK 500 1 TYR A 45 -43.99 177.46
REMARK 500 1 SER A 51 29.68 -71.42
REMARK 500 1 TYR A 68 161.27 -43.73
REMARK 500 1 SER A 69 52.53 -162.37
REMARK 500 1 ASN A 84 21.23 110.96
REMARK 500 1 THR A 93 87.28 -50.74
REMARK 500 1 SER A 96 46.39 99.59
REMARK 500 1 CYS A 103 -168.79 -56.48
REMARK 500 2 CYS A 2 124.87 -32.38
REMARK 500 2 CYS A 10 59.97 -177.11
REMARK 500 2 ALA A 21 -38.60 -35.69
REMARK 500 2 ASN A 36 -167.25 -102.76
REMARK 500 2 HIS A 40 162.62 179.46
REMARK 500 2 LYS A 41 168.15 -45.13
REMARK 500 2 TYR A 42 12.67 -151.03
REMARK 500 2 ASN A 43 85.08 -7.63
REMARK 500 2 TYR A 45 -43.15 -166.95
REMARK 500 2 SER A 51 28.89 -75.11
REMARK 500 2 PRO A 73 43.67 -75.01
REMARK 500 2 ALA A 75 -37.98 -154.01
REMARK 500 2 PHE A 80 -158.04 -148.85
REMARK 500 2 ASN A 84 24.06 103.65
REMARK 500 2 THR A 93 -125.94 -58.71
REMARK 500 2 SER A 96 36.96 80.50
REMARK 500 2 ASN A 99 -165.68 -69.98
REMARK 500 2 CYS A 103 -165.79 -55.42
REMARK 500 3 CYS A 2 60.76 -106.87
REMARK 500 3 ASP A 3 -29.62 -39.59
REMARK 500 3 SER A 8 49.72 -157.96
REMARK 500 3 ASN A 9 -166.80 -124.27
REMARK 500 3 CYS A 10 76.57 -172.46
REMARK 500 3 TYR A 11 50.78 -90.67
REMARK 500 3 SER A 12 152.25 -27.76
REMARK 500 3 SER A 13 -23.47 -39.15
REMARK 500 3 VAL A 16 -71.79 -76.46
REMARK 500 3 ALA A 21 -36.90 -33.88
REMARK 500 3 PRO A 39 -166.04 -75.02
REMARK 500 3 HIS A 40 166.54 179.63
REMARK 500 3 LYS A 41 169.32 -46.65
REMARK 500 3 TYR A 42 14.20 -154.64
REMARK 500 3 ASN A 43 87.60 -9.60
REMARK 500 3 ASN A 44 172.91 -52.93
REMARK 500 3 TYR A 45 -43.24 176.54
REMARK 500
REMARK 500 THIS ENTRY HAS 782 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: REC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: GUANINE RECOGNITION SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE.
DBREF 1YGW A 1 104 UNP P00651 RNT1_ASPOR 22 125
SEQRES 1 A 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER
SEQRES 2 A 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR LYS LEU
SEQRES 3 A 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO
SEQRES 4 A 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL
SEQRES 5 A 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY
SEQRES 6 A 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL
SEQRES 7 A 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR
SEQRES 8 A 104 HIS THR GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR
HELIX 1 A SER A 13 ASP A 29 1 17
SHEET 1 A1 2 TYR A 4 CYS A 6 0
SHEET 2 A1 2 ASN A 9 TYR A 11 -1 N TYR A 11 O TYR A 4
SHEET 1 A2 5 TYR A 38 HIS A 40 0
SHEET 2 A2 5 TYR A 57 ILE A 61 -1 O GLU A 58 N HIS A 40
SHEET 3 A2 5 ASP A 76 ASN A 81 -1 O VAL A 78 N TRP A 59
SHEET 4 A2 5 GLN A 85 THR A 91 -1 O ILE A 90 N ARG A 77
SHEET 5 A2 5 PHE A 100 CYS A 103 -1 O VAL A 101 N THR A 91
SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.10
SSBOND 2 CYS A 6 CYS A 103 1555 1555 1.15
CISPEP 1 TYR A 38 PRO A 39 1 0.10
CISPEP 2 SER A 54 PRO A 55 1 0.04
CISPEP 3 TYR A 38 PRO A 39 2 0.07
CISPEP 4 SER A 54 PRO A 55 2 -0.03
CISPEP 5 TYR A 38 PRO A 39 3 -0.01
CISPEP 6 SER A 54 PRO A 55 3 0.02
CISPEP 7 TYR A 38 PRO A 39 4 -0.06
CISPEP 8 SER A 54 PRO A 55 4 -0.04
CISPEP 9 TYR A 38 PRO A 39 5 0.01
CISPEP 10 SER A 54 PRO A 55 5 0.06
CISPEP 11 TYR A 38 PRO A 39 6 0.07
CISPEP 12 SER A 54 PRO A 55 6 0.04
CISPEP 13 TYR A 38 PRO A 39 7 -0.01
CISPEP 14 SER A 54 PRO A 55 7 0.00
CISPEP 15 TYR A 38 PRO A 39 8 -0.01
CISPEP 16 SER A 54 PRO A 55 8 0.08
CISPEP 17 TYR A 38 PRO A 39 9 -0.03
CISPEP 18 SER A 54 PRO A 55 9 0.02
CISPEP 19 TYR A 38 PRO A 39 10 0.10
CISPEP 20 SER A 54 PRO A 55 10 -0.09
CISPEP 21 TYR A 38 PRO A 39 11 -0.09
CISPEP 22 SER A 54 PRO A 55 11 -0.06
CISPEP 23 TYR A 38 PRO A 39 12 0.04
CISPEP 24 SER A 54 PRO A 55 12 0.06
CISPEP 25 TYR A 38 PRO A 39 13 -0.04
CISPEP 26 SER A 54 PRO A 55 13 0.04
CISPEP 27 TYR A 38 PRO A 39 14 -0.05
CISPEP 28 SER A 54 PRO A 55 14 0.06
CISPEP 29 TYR A 38 PRO A 39 15 -0.07
CISPEP 30 SER A 54 PRO A 55 15 0.04
CISPEP 31 TYR A 38 PRO A 39 16 -0.03
CISPEP 32 SER A 54 PRO A 55 16 0.00
CISPEP 33 TYR A 38 PRO A 39 17 0.02
CISPEP 34 SER A 54 PRO A 55 17 0.03
CISPEP 35 TYR A 38 PRO A 39 18 0.03
CISPEP 36 SER A 54 PRO A 55 18 0.09
CISPEP 37 TYR A 38 PRO A 39 19 -0.03
CISPEP 38 SER A 54 PRO A 55 19 -0.09
CISPEP 39 TYR A 38 PRO A 39 20 0.04
CISPEP 40 SER A 54 PRO A 55 20 0.01
CISPEP 41 TYR A 38 PRO A 39 21 0.00
CISPEP 42 SER A 54 PRO A 55 21 -0.03
CISPEP 43 TYR A 38 PRO A 39 22 -0.08
CISPEP 44 SER A 54 PRO A 55 22 0.10
CISPEP 45 TYR A 38 PRO A 39 23 0.00
CISPEP 46 SER A 54 PRO A 55 23 0.08
CISPEP 47 TYR A 38 PRO A 39 24 -0.11
CISPEP 48 SER A 54 PRO A 55 24 0.02
CISPEP 49 TYR A 38 PRO A 39 25 0.04
CISPEP 50 SER A 54 PRO A 55 25 0.02
CISPEP 51 TYR A 38 PRO A 39 26 -0.03
CISPEP 52 SER A 54 PRO A 55 26 -0.07
CISPEP 53 TYR A 38 PRO A 39 27 -0.01
CISPEP 54 SER A 54 PRO A 55 27 0.02
CISPEP 55 TYR A 38 PRO A 39 28 0.06
CISPEP 56 SER A 54 PRO A 55 28 0.00
CISPEP 57 TYR A 38 PRO A 39 29 0.07
CISPEP 58 SER A 54 PRO A 55 29 0.06
CISPEP 59 TYR A 38 PRO A 39 30 -0.02
CISPEP 60 SER A 54 PRO A 55 30 0.04
CISPEP 61 TYR A 38 PRO A 39 31 -0.05
CISPEP 62 SER A 54 PRO A 55 31 0.15
CISPEP 63 TYR A 38 PRO A 39 32 0.06
CISPEP 64 SER A 54 PRO A 55 32 0.08
CISPEP 65 TYR A 38 PRO A 39 33 -0.03
CISPEP 66 SER A 54 PRO A 55 33 -0.12
CISPEP 67 TYR A 38 PRO A 39 34 -0.05
CISPEP 68 SER A 54 PRO A 55 34 -0.08
SITE 1 REC 6 TYR A 42 ASN A 43 ASN A 44 TYR A 45
SITE 2 REC 6 GLU A 46 ASN A 98
SITE 1 CAT 5 TYR A 38 HIS A 40 GLU A 58 ARG A 77
SITE 2 CAT 5 HIS A 92
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 29 2 Bytes