Header list of 1gio.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE ANGIOGENESIS 12-APR-96 1GIO
TITLE NMR SOLUTION STRUCTURE OF BOVINE ANGIOGENIN, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOGENIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.27.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 SECRETION: MILK
KEYWDS ENDORIBONUCLEASE, HYDROLASE ANGIOGENESIS
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.LEQUIN,C.ALBARET,F.BONTEMS,G.SPIK,J.Y.LALLEMAND
REVDAT 3 23-FEB-22 1GIO 1 REMARK
REVDAT 2 24-FEB-09 1GIO 1 VERSN
REVDAT 1 07-DEC-96 1GIO 0
JRNL AUTH O.LEQUIN,C.ALBARET,F.BONTEMS,G.SPIK,J.Y.LALLEMAND
JRNL TITL SOLUTION STRUCTURE OF BOVINE ANGIOGENIN BY 1H NUCLEAR
JRNL TITL 2 MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 35 8870 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8688423
JRNL DOI 10.1021/BI960022R
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.REISDORF,D.ABERGEL,F.BONTEMS,J.Y.LALLEMAND,
REMARK 1 AUTH 2 J.P.DECOTTIGNIES,G.SPIK
REMARK 1 TITL PROTON RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE OF
REMARK 1 TITL 2 BOVINE ANGIOGENIN
REMARK 1 REF EUR.J.BIOCHEM. V. 224 811 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GIO 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_1000173589.
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 : DIANA
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 1 ALA A 17 N - CA - CB ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 PHE A 46 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 TYR A 66 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 PHE A 46 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 2 PHE A 46 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 TYR A 66 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 PHE A 46 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 3 TYR A 95 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 TYR A 95 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 5 TYR A 7 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 PHE A 28 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 PHE A 28 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 PHE A 46 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 6 PHE A 46 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 6 PHE A 46 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 7 PHE A 46 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 8 TYR A 5 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 8 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 8 PHE A 46 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 PHE A 46 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 9 PHE A 46 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 9 PHE A 46 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 10 TYR A 7 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 10 PHE A 46 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 10 PHE A 46 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
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 GLN A 2 74.22 62.91
REMARK 500 1 ASP A 3 75.71 -113.48
REMARK 500 1 HIS A 14 -70.93 -87.81
REMARK 500 1 ASP A 16 -84.62 -129.95
REMARK 500 1 ALA A 17 122.92 95.11
REMARK 500 1 LYS A 18 82.00 69.52
REMARK 500 1 LYS A 20 73.87 -100.57
REMARK 500 1 ASN A 23 -93.40 -98.51
REMARK 500 1 ASP A 24 -42.12 -166.24
REMARK 500 1 CYS A 40 78.21 60.81
REMARK 500 1 ASP A 42 -78.07 -80.31
REMARK 500 1 ALA A 56 32.24 -90.07
REMARK 500 1 CYS A 58 38.15 -95.41
REMARK 500 1 GLU A 59 -85.49 -75.87
REMARK 500 1 ASP A 60 -24.94 152.40
REMARK 500 1 ARG A 67 48.34 32.60
REMARK 500 1 ASP A 69 -41.13 -171.87
REMARK 500 1 SER A 89 -84.29 -145.12
REMARK 500 1 ARG A 94 174.11 68.99
REMARK 500 1 ASN A 110 -27.45 82.20
REMARK 500 2 PRO A 19 -88.71 -80.93
REMARK 500 2 LYS A 20 103.78 78.71
REMARK 500 2 ASN A 23 -152.37 -104.54
REMARK 500 2 THR A 37 -88.10 -81.65
REMARK 500 2 ARG A 38 87.58 38.84
REMARK 500 2 CYS A 40 91.74 -164.42
REMARK 500 2 ASP A 42 -89.20 -79.53
REMARK 500 2 CYS A 58 38.59 -92.07
REMARK 500 2 ASP A 60 -41.00 124.40
REMARK 500 2 GLN A 64 144.68 168.88
REMARK 500 2 ARG A 67 -157.83 46.84
REMARK 500 2 SER A 89 -51.24 80.45
REMARK 500 2 ASN A 110 -68.58 81.46
REMARK 500 2 ARG A 124 88.37 60.24
REMARK 500 3 ASP A 3 -45.01 -150.75
REMARK 500 3 TYR A 5 -67.00 -137.32
REMARK 500 3 ASP A 16 95.03 -163.05
REMARK 500 3 ASN A 23 -162.15 -118.25
REMARK 500 3 ARG A 35 66.14 73.13
REMARK 500 3 THR A 37 62.02 -115.48
REMARK 500 3 LYS A 41 168.85 85.16
REMARK 500 3 ASP A 42 -94.93 -97.61
REMARK 500 3 CYS A 58 43.61 -93.90
REMARK 500 3 ASP A 60 -37.34 114.38
REMARK 500 3 ARG A 94 -121.27 75.99
REMARK 500 3 TYR A 95 144.80 128.00
REMARK 500 3 ASN A 110 -34.28 82.05
REMARK 500 3 VAL A 114 -30.27 -133.09
REMARK 500 4 GLN A 2 60.62 63.89
REMARK 500 4 ASP A 3 15.53 -145.52
REMARK 500
REMARK 500 THIS ENTRY HAS 184 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 62 GLY A 63 2 140.06
REMARK 500 ASN A 62 GLY A 63 5 144.63
REMARK 500 ASN A 62 GLY A 63 6 144.57
REMARK 500 ASN A 62 GLY A 63 7 145.50
REMARK 500 ARG A 35 LEU A 36 8 143.68
REMARK 500 ASN A 62 GLY A 63 8 143.54
REMARK 500 ASN A 62 GLY A 63 10 143.66
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 1 TYR A 95 0.08 SIDE CHAIN
REMARK 500 2 TYR A 26 0.07 SIDE CHAIN
REMARK 500 4 TYR A 95 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RIB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RIBONUCLEOLYTIC ACTIVE SITE.
DBREF 1GIO A 1 125 UNP P10152 ANG1_BOVIN 1 125
SEQRES 1 A 125 ALA GLN ASP ASP TYR ARG TYR ILE HIS PHE LEU THR GLN
SEQRES 2 A 125 HIS TYR ASP ALA LYS PRO LYS GLY ARG ASN ASP GLU TYR
SEQRES 3 A 125 CYS PHE ASN MET MET LYS ASN ARG ARG LEU THR ARG PRO
SEQRES 4 A 125 CYS LYS ASP ARG ASN THR PHE ILE HIS GLY ASN LYS ASN
SEQRES 5 A 125 ASP ILE LYS ALA ILE CYS GLU ASP ARG ASN GLY GLN PRO
SEQRES 6 A 125 TYR ARG GLY ASP LEU ARG ILE SER LYS SER GLU PHE GLN
SEQRES 7 A 125 ILE THR ILE CYS LYS HIS LYS GLY GLY SER SER ARG PRO
SEQRES 8 A 125 PRO CYS ARG TYR GLY ALA THR GLU ASP SER ARG VAL ILE
SEQRES 9 A 125 VAL VAL GLY CYS GLU ASN GLY LEU PRO VAL HIS PHE ASP
SEQRES 10 A 125 GLU SER PHE ILE THR PRO ARG HIS
HELIX 1 1 ILE A 8 GLN A 13 1 6
HELIX 2 2 GLU A 25 ARG A 34 1 10
HELIX 3 3 LYS A 51 ILE A 57 1 7
SHEET 1 A 3 ARG A 43 HIS A 48 0
SHEET 2 A 3 PHE A 77 LYS A 83 -1 N CYS A 82 O ASN A 44
SHEET 3 A 3 GLY A 96 ARG A 102 -1 N ARG A 102 O PHE A 77
SHEET 1 B 4 GLY A 63 TYR A 66 0
SHEET 2 B 4 LEU A 70 SER A 73 -1 N ILE A 72 O GLN A 64
SHEET 3 B 4 VAL A 105 GLU A 109 -1 N VAL A 106 O ARG A 71
SHEET 4 B 4 LEU A 112 ASP A 117 -1 N ASP A 117 O VAL A 105
SSBOND 1 CYS A 27 CYS A 82 1555 1555 2.03
SSBOND 2 CYS A 40 CYS A 93 1555 1555 2.03
SSBOND 3 CYS A 58 CYS A 108 1555 1555 2.02
CISPEP 1 ARG A 38 PRO A 39 1 -17.18
CISPEP 2 PRO A 91 PRO A 92 1 10.11
CISPEP 3 ARG A 38 PRO A 39 2 -13.85
CISPEP 4 PRO A 91 PRO A 92 2 9.46
CISPEP 5 ARG A 38 PRO A 39 3 -21.21
CISPEP 6 PRO A 91 PRO A 92 3 12.19
CISPEP 7 ARG A 38 PRO A 39 4 -3.48
CISPEP 8 PRO A 91 PRO A 92 4 -17.08
CISPEP 9 ARG A 38 PRO A 39 5 -19.34
CISPEP 10 PRO A 91 PRO A 92 5 16.93
CISPEP 11 ARG A 38 PRO A 39 6 -16.39
CISPEP 12 PRO A 91 PRO A 92 6 17.58
CISPEP 13 ARG A 38 PRO A 39 7 -4.55
CISPEP 14 PRO A 91 PRO A 92 7 16.41
CISPEP 15 ARG A 38 PRO A 39 8 -27.49
CISPEP 16 PRO A 91 PRO A 92 8 13.55
CISPEP 17 ARG A 38 PRO A 39 9 -20.42
CISPEP 18 PRO A 91 PRO A 92 9 -3.74
CISPEP 19 ARG A 38 PRO A 39 10 -15.46
CISPEP 20 PRO A 91 PRO A 92 10 4.34
SITE 1 RIB 8 GLN A 13 HIS A 14 LYS A 41 THR A 45
SITE 2 RIB 8 HIS A 115 PHE A 116 ASP A 117 GLU A 118
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