Header list of 2aas.pdb file
Complete list - v 29 2 Bytes
HEADER HYDROLASE(ENDORIBONUCLEASE) 20-NOV-92 2AAS
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN
TITLE 2 SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.27.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE(ENDORIBONUCLEASE)
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR J.SANTORO,C.GONZALEZ,M.BRUIX,J.L.NEIRA,J.L.NIETO,J.HERRANZ,M.RICO
REVDAT 4 29-NOV-17 2AAS 1 REMARK HELIX
REVDAT 3 24-FEB-09 2AAS 1 VERSN
REVDAT 2 31-JUL-94 2AAS 3 ATOM
REVDAT 1 31-JAN-94 2AAS 0
JRNL AUTH J.SANTORO,C.GONZALEZ,M.BRUIX,J.L.NEIRA,J.L.NIETO,J.HERRANZ,
JRNL AUTH 2 M.RICO
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE
JRNL TITL 2 A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF J.MOL.BIOL. V. 229 722 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8381876
JRNL DOI 10.1006/JMBI.1993.1075
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.RICO,J.SANTORO,C.GONZALEZ,M.BRUIX,J.L.NEIRA,J.L.NIETO
REMARK 1 TITL REFINED STRUCTURE OF BOVINE PANCREATIC RIBONUCLEASE A BY 1H
REMARK 1 TITL 2 NMR METHODS. SIDE CHAIN DYNAMICS
REMARK 1 REF APPL.MAGN.RESON. V. 4 385 1993
REMARK 1 REFN ISSN 0937-9347
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.RICO,J.SANTORO,C.GONZALEZ,M.BRUIX,J.L.NEIRA,J.L.NIETO,
REMARK 1 AUTH 2 J.HERRANZ
REMARK 1 TITL 3D STRUCTURE OF BOVINE PANCREATIC RIBONUCLEASE A IN AQUEOUS
REMARK 1 TITL 2 SOLUTION
REMARK 1 REF J.BIOMOL.NMR V. 1 283 1991
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.RICO,J.SANTORO,C.GONZALEZ,M.BRUIX,J.L.NEIRA
REMARK 1 TITL SOLUTION STRUCTURE OF BOVINE PANCREATIC RIBONUCLEASE A AND
REMARK 1 TITL 2 RIBONUCLEASE-PYRIMIDINE NUCLEOTIDE COMPLEXES AS DETERMINED
REMARK 1 TITL 3 BY 1H NMR
REMARK 1 EDIT C.M.CUCHILLO, R.DE LLORENS, M.V.NOGUES, S.PARES
REMARK 1 REF STRUCTURE, MECHANISM AND 9 1991
REMARK 1 REF 2 FUNCTION OF RIBONUCLEASES
REMARK 1 PUBL UNIVERSITAT AUTONOMA DE BARCELONA,BARCELONA
REMARK 1 REFN
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.RICO,M.BRUIX,J.SANTORO,C.GONZALEZ,J.L.NEIRA,J.L.NIETO,
REMARK 1 AUTH 2 J.HERRANZ
REMARK 1 TITL SEQUENTIAL 1H-NMR ASSIGNMENT AND SOLUTION STRUCTURE OF
REMARK 1 TITL 2 BOVINE PANCREATIC RIBONUCLEASE A
REMARK 1 REF EUR.J.BIOCHEM. V. 183 623 1989
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AAS 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_1000177725.
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 : 32
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 HH TYR A 73 OH TYR A 115 1.53
REMARK 500 O GLY A 88 HG SER A 89 1.58
REMARK 500
REMARK 500 REMARK: NULL
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 2 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -16.1 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 4 LYS A 1 CD - CE - NZ ANGL. DEV. = -13.9 DEGREES
REMARK 500 4 VAL A 63 CG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 4 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 ARG A 85 NH1 - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 ARG A 85 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 10 NH1 - CZ - NH2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 5 TYR A 115 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 6 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 TYR A 115 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 TYR A 97 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 LYS A 7 CD - CE - NZ ANGL. DEV. = -17.6 DEGREES
REMARK 500 9 TYR A 25 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 VAL A 63 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 9 LYS A 66 CD - CE - NZ ANGL. DEV. = -17.2 DEGREES
REMARK 500 9 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 TYR A 76 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 9 TYR A 97 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 10 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 TYR A 76 CB - CG - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 11 VAL A 63 CG1 - CB - CG2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 11 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 11 TYR A 76 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 12 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 12 ARG A 39 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 12 LYS A 61 CD - CE - NZ ANGL. DEV. = -17.5 DEGREES
REMARK 500 12 LYS A 66 CA - CB - CG ANGL. DEV. = -16.1 DEGREES
REMARK 500 12 LYS A 66 CD - CE - NZ ANGL. DEV. = -19.1 DEGREES
REMARK 500 12 TYR A 73 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 TYR A 76 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 12 TYR A 97 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 13 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 VAL A 63 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 13 TYR A 73 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 13 TYR A 76 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 14 TYR A 76 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 14 TYR A 92 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 15 TYR A 25 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 15 LYS A 37 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES
REMARK 500 15 VAL A 63 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 15 TYR A 97 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 16 LYS A 1 CD - CE - NZ ANGL. DEV. = -14.9 DEGREES
REMARK 500 16 TYR A 97 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 103 ANGLE DEVIATIONS.
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 4 -85.56 18.98
REMARK 500 1 ALA A 20 91.59 -62.55
REMARK 500 1 ASN A 34 -10.30 66.76
REMARK 500 1 HIS A 48 45.18 -82.88
REMARK 500 1 GLN A 60 -76.94 -104.14
REMARK 500 1 SER A 89 96.06 67.96
REMARK 500 1 ASP A 121 -76.04 -118.89
REMARK 500 2 ASN A 34 -2.69 62.19
REMARK 500 2 ASP A 38 -54.83 -120.47
REMARK 500 2 GLN A 60 -79.99 -94.44
REMARK 500 2 ASP A 121 -74.22 -117.88
REMARK 500 3 ASP A 38 -37.72 94.20
REMARK 500 3 GLN A 60 -78.32 -101.09
REMARK 500 3 ASN A 71 40.47 -99.37
REMARK 500 3 SER A 89 46.91 -102.05
REMARK 500 3 PRO A 93 34.56 -99.76
REMARK 500 3 ASN A 94 66.18 -111.87
REMARK 500 3 ASP A 121 -78.04 -116.25
REMARK 500 4 ASN A 34 -18.18 71.41
REMARK 500 4 ASP A 38 -56.12 -124.10
REMARK 500 4 GLN A 60 -122.60 -104.55
REMARK 500 4 SER A 89 36.96 -86.48
REMARK 500 4 ASN A 94 64.51 -102.05
REMARK 500 4 ASP A 121 -74.48 -119.05
REMARK 500 5 ASN A 34 18.37 -47.08
REMARK 500 5 ASP A 38 -58.35 -127.87
REMARK 500 5 HIS A 48 58.75 -95.97
REMARK 500 5 GLN A 60 -77.75 -99.28
REMARK 500 5 SER A 89 38.33 -92.05
REMARK 500 5 ASP A 121 -79.23 -118.53
REMARK 500 6 ASN A 34 -4.56 64.96
REMARK 500 6 GLN A 60 -82.29 -99.66
REMARK 500 6 SER A 89 41.38 -89.83
REMARK 500 6 TYR A 92 126.66 -37.64
REMARK 500 7 ALA A 20 97.49 -63.86
REMARK 500 7 ARG A 33 33.30 -80.68
REMARK 500 7 ASN A 34 -14.14 64.97
REMARK 500 7 ASP A 38 -57.48 -121.66
REMARK 500 7 GLN A 60 -117.44 -107.97
REMARK 500 7 ASN A 71 40.74 -107.98
REMARK 500 7 ASP A 121 -80.62 -122.89
REMARK 500 8 ASN A 34 67.00 -43.05
REMARK 500 8 LYS A 37 21.35 -78.40
REMARK 500 8 ASP A 38 -49.45 -158.73
REMARK 500 8 HIS A 48 53.30 -91.02
REMARK 500 8 GLN A 60 -73.82 -93.57
REMARK 500 8 SER A 89 35.51 -81.60
REMARK 500 8 ASP A 121 -78.06 -117.46
REMARK 500 9 SER A 22 -162.69 177.27
REMARK 500 9 GLN A 60 -159.63 -112.84
REMARK 500
REMARK 500 THIS ENTRY HAS 192 RAMACHANDRAN OUTLIERS.
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 97 0.09 SIDE CHAIN
REMARK 500 2 TYR A 97 0.07 SIDE CHAIN
REMARK 500 3 ARG A 10 0.15 SIDE CHAIN
REMARK 500 3 TYR A 92 0.07 SIDE CHAIN
REMARK 500 3 TYR A 97 0.07 SIDE CHAIN
REMARK 500 3 TYR A 115 0.08 SIDE CHAIN
REMARK 500 4 TYR A 97 0.08 SIDE CHAIN
REMARK 500 4 TYR A 115 0.08 SIDE CHAIN
REMARK 500 5 ARG A 10 0.11 SIDE CHAIN
REMARK 500 5 HIS A 12 0.08 SIDE CHAIN
REMARK 500 5 TYR A 115 0.09 SIDE CHAIN
REMARK 500 6 TYR A 92 0.07 SIDE CHAIN
REMARK 500 6 TYR A 97 0.12 SIDE CHAIN
REMARK 500 6 TYR A 115 0.08 SIDE CHAIN
REMARK 500 7 TYR A 73 0.07 SIDE CHAIN
REMARK 500 7 TYR A 97 0.10 SIDE CHAIN
REMARK 500 7 TYR A 115 0.09 SIDE CHAIN
REMARK 500 8 TYR A 73 0.08 SIDE CHAIN
REMARK 500 8 TYR A 92 0.10 SIDE CHAIN
REMARK 500 8 TYR A 97 0.09 SIDE CHAIN
REMARK 500 8 TYR A 115 0.09 SIDE CHAIN
REMARK 500 9 TYR A 76 0.34 SIDE CHAIN
REMARK 500 9 TYR A 97 0.09 SIDE CHAIN
REMARK 500 10 PHE A 8 0.08 SIDE CHAIN
REMARK 500 10 TYR A 76 0.34 SIDE CHAIN
REMARK 500 10 TYR A 115 0.08 SIDE CHAIN
REMARK 500 11 TYR A 73 0.07 SIDE CHAIN
REMARK 500 11 TYR A 76 0.33 SIDE CHAIN
REMARK 500 11 TYR A 97 0.10 SIDE CHAIN
REMARK 500 11 TYR A 115 0.09 SIDE CHAIN
REMARK 500 12 TYR A 73 0.11 SIDE CHAIN
REMARK 500 12 TYR A 76 0.43 SIDE CHAIN
REMARK 500 12 TYR A 97 0.12 SIDE CHAIN
REMARK 500 12 TYR A 115 0.11 SIDE CHAIN
REMARK 500 13 TYR A 76 0.31 SIDE CHAIN
REMARK 500 13 TYR A 97 0.10 SIDE CHAIN
REMARK 500 14 TYR A 76 0.33 SIDE CHAIN
REMARK 500 14 TYR A 97 0.14 SIDE CHAIN
REMARK 500 15 TYR A 97 0.09 SIDE CHAIN
REMARK 500 16 TYR A 97 0.08 SIDE CHAIN
REMARK 500 16 TYR A 115 0.09 SIDE CHAIN
REMARK 500 17 TYR A 92 0.08 SIDE CHAIN
REMARK 500 17 TYR A 115 0.07 SIDE CHAIN
REMARK 500 18 HIS A 48 0.10 SIDE CHAIN
REMARK 500 19 TYR A 92 0.10 SIDE CHAIN
REMARK 500 19 TYR A 97 0.07 SIDE CHAIN
REMARK 500 20 TYR A 97 0.08 SIDE CHAIN
REMARK 500 21 TYR A 115 0.07 SIDE CHAIN
REMARK 500 22 TYR A 92 0.07 SIDE CHAIN
REMARK 500 22 TYR A 97 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 ASP A 14 -10.34
REMARK 500 3 ARG A 10 12.84
REMARK 500 3 LYS A 37 14.86
REMARK 500 5 ARG A 10 12.23
REMARK 500 7 MET A 13 -10.66
REMARK 500 8 ARG A 33 11.91
REMARK 500 10 ASN A 34 -10.18
REMARK 500 11 MET A 13 -13.76
REMARK 500 12 GLU A 9 -10.69
REMARK 500 12 ARG A 33 11.31
REMARK 500 12 ASN A 44 10.77
REMARK 500 12 GLN A 69 -11.11
REMARK 500 16 GLN A 69 -10.51
REMARK 500 18 LYS A 1 -14.35
REMARK 500 18 GLU A 2 11.82
REMARK 500 19 LYS A 1 -11.42
REMARK 500 19 LYS A 37 14.38
REMARK 500 21 LYS A 1 -14.91
REMARK 500 22 GLU A 2 11.29
REMARK 500 23 LYS A 1 -10.37
REMARK 500 23 GLU A 2 12.50
REMARK 500 24 LYS A 1 -12.89
REMARK 500 24 ILE A 81 10.09
REMARK 500 28 THR A 78 -10.02
REMARK 500 31 LYS A 1 -10.43
REMARK 500 32 GLN A 69 -10.51
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AAS A 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
HELIX 1 H1 ALA A 4 MET A 13 1 10
HELIX 2 H2 ASN A 24 ARG A 33 1 10
HELIX 3 H3 LEU A 51 SER A 59 1RESIDUES 54-59 IN 3/10 CONFIG 9
SHEET 1 S1 3 PRO A 42 HIS A 48 0
SHEET 2 S1 3 MET A 79 THR A 87 -1 N GLU A 86 O PRO A 42
SHEET 3 S1 3 ALA A 96 LYS A 104 -1 O ALA A 96 N THR A 87
SHEET 1 S2 4 LYS A 61 ALA A 64 0
SHEET 2 S2 4 ASN A 71 GLN A 74 -1 N CYS A 72 O VAL A 63
SHEET 3 S2 4 HIS A 105 GLU A 111 -1 N VAL A 108 O TYR A 73
SHEET 4 S2 4 VAL A 116 VAL A 124 -1 N VAL A 116 O ALA A 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.04
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.04
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.04
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.04
CISPEP 1 TYR A 92 PRO A 93 1 1.61
CISPEP 2 ASN A 113 PRO A 114 1 -1.99
CISPEP 3 TYR A 92 PRO A 93 2 5.15
CISPEP 4 ASN A 113 PRO A 114 2 -4.13
CISPEP 5 TYR A 92 PRO A 93 3 -1.38
CISPEP 6 ASN A 113 PRO A 114 3 -5.43
CISPEP 7 TYR A 92 PRO A 93 4 -4.48
CISPEP 8 ASN A 113 PRO A 114 4 -3.19
CISPEP 9 TYR A 92 PRO A 93 5 0.70
CISPEP 10 ASN A 113 PRO A 114 5 -3.10
CISPEP 11 TYR A 92 PRO A 93 6 3.40
CISPEP 12 ASN A 113 PRO A 114 6 -2.00
CISPEP 13 TYR A 92 PRO A 93 7 -0.42
CISPEP 14 ASN A 113 PRO A 114 7 -2.73
CISPEP 15 TYR A 92 PRO A 93 8 5.20
CISPEP 16 ASN A 113 PRO A 114 8 -2.16
CISPEP 17 TYR A 92 PRO A 93 9 -0.31
CISPEP 18 ASN A 113 PRO A 114 9 -3.93
CISPEP 19 TYR A 92 PRO A 93 10 -3.93
CISPEP 20 ASN A 113 PRO A 114 10 -1.85
CISPEP 21 TYR A 92 PRO A 93 11 2.09
CISPEP 22 ASN A 113 PRO A 114 11 -1.48
CISPEP 23 TYR A 92 PRO A 93 12 -3.56
CISPEP 24 ASN A 113 PRO A 114 12 -4.15
CISPEP 25 TYR A 92 PRO A 93 13 0.74
CISPEP 26 ASN A 113 PRO A 114 13 -2.49
CISPEP 27 TYR A 92 PRO A 93 14 4.89
CISPEP 28 ASN A 113 PRO A 114 14 -3.23
CISPEP 29 TYR A 92 PRO A 93 15 -3.16
CISPEP 30 ASN A 113 PRO A 114 15 -0.63
CISPEP 31 TYR A 92 PRO A 93 16 -4.98
CISPEP 32 ASN A 113 PRO A 114 16 -3.89
CISPEP 33 TYR A 92 PRO A 93 17 -3.62
CISPEP 34 ASN A 113 PRO A 114 17 -4.37
CISPEP 35 TYR A 92 PRO A 93 18 9.72
CISPEP 36 ASN A 113 PRO A 114 18 -1.35
CISPEP 37 TYR A 92 PRO A 93 19 -2.01
CISPEP 38 ASN A 113 PRO A 114 19 -2.56
CISPEP 39 TYR A 92 PRO A 93 20 -2.82
CISPEP 40 ASN A 113 PRO A 114 20 -3.12
CISPEP 41 TYR A 92 PRO A 93 21 -6.11
CISPEP 42 ASN A 113 PRO A 114 21 -4.64
CISPEP 43 TYR A 92 PRO A 93 22 4.82
CISPEP 44 ASN A 113 PRO A 114 22 -0.92
CISPEP 45 TYR A 92 PRO A 93 23 1.07
CISPEP 46 ASN A 113 PRO A 114 23 -3.09
CISPEP 47 TYR A 92 PRO A 93 24 1.42
CISPEP 48 ASN A 113 PRO A 114 24 -2.57
CISPEP 49 TYR A 92 PRO A 93 25 -4.32
CISPEP 50 ASN A 113 PRO A 114 25 -2.08
CISPEP 51 TYR A 92 PRO A 93 26 -1.59
CISPEP 52 ASN A 113 PRO A 114 26 -2.73
CISPEP 53 TYR A 92 PRO A 93 27 -1.60
CISPEP 54 ASN A 113 PRO A 114 27 -3.60
CISPEP 55 TYR A 92 PRO A 93 28 -6.19
CISPEP 56 ASN A 113 PRO A 114 28 -2.65
CISPEP 57 TYR A 92 PRO A 93 29 -0.62
CISPEP 58 ASN A 113 PRO A 114 29 -2.41
CISPEP 59 TYR A 92 PRO A 93 30 -0.71
CISPEP 60 ASN A 113 PRO A 114 30 0.36
CISPEP 61 TYR A 92 PRO A 93 31 -5.53
CISPEP 62 ASN A 113 PRO A 114 31 -0.70
CISPEP 63 TYR A 92 PRO A 93 32 -4.98
CISPEP 64 ASN A 113 PRO A 114 32 -3.89
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