HEADER HYDROLASE(NUCLEIC ACID,RNA) 28-AUG-92 1RTB
TITLE CRYSTAL STRUCTURE DISPOSITION OF THYMIDYLIC ACID TETRAMER IN COMPLEX
TITLE 2 WITH RIBONUCLEASE A
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;
SOURCE 5 ORGAN: PANCREAS
KEYWDS HYDROLASE(NUCLEIC ACID, RNA)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.BIRDSALL,A.MCPHERSON
REVDAT 4 14-AUG-19 1RTB 1 REMARK
REVDAT 3 17-JUL-19 1RTB 1 REMARK
REVDAT 2 24-FEB-09 1RTB 1 VERSN
REVDAT 1 31-OCT-93 1RTB 0
JRNL AUTH D.L.BIRDSALL,A.MCPHERSON
JRNL TITL CRYSTAL STRUCTURE DISPOSITION OF THYMIDYLIC ACID TETRAMER IN
JRNL TITL 2 COMPLEX WITH RIBONUCLEASE A.
JRNL REF J.BIOL.CHEM. V. 267 22230 1992
JRNL REFN ISSN 0021-9258
JRNL PMID 1429575
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.WLODAWER,N.BORKAKOTI,D.S.MOSS,B.HOWLIN
REMARK 1 TITL COMPARISON OF TWO INDEPENDENTLY REFINED MODELS OF
REMARK 1 TITL 2 RIBONUCLEASE-A
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 42 379 1986
REMARK 1 REFN ISSN 0108-7681
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.BORAH,C.-W.CHEN,W.EGAN,M.MILLER,A.WLODAWER,J.S.COHEN
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE AND NEUTRON DIFFRACTION STUDIES
REMARK 1 TITL 2 OF THE COMPLEX OF RIBONUCLEASE A WITH URIDINE VANADATE, A
REMARK 1 TITL 3 TRANSITION-STATE ANALOGUE
REMARK 1 REF BIOCHEMISTRY V. 24 2058 1985
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.WLODAWER,M.MILLER,L.SJOLIN
REMARK 1 TITL ACTIVE SITE OF RNASE: NEUTRON DIFFRACTION STUDY OF A COMPLEX
REMARK 1 TITL 2 WITH URIDINE VANADATE, A TRANSITION-STATE ANALOG
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 80 3628 1983
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 4
REMARK 1 AUTH A.WLODAWER,L.SJOLIN
REMARK 1 TITL STRUCTURE OF RIBONUCLEASE A: RESULTS OF JOINT NEUTRON AND
REMARK 1 TITL 2 X-RAY REFINEMENT AT 2.0 ANGSTROMS RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 22 2720 1983
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH A.WLODAWER,R.BOTT,L.SJOLIN
REMARK 1 TITL THE REFINED CRYSTAL STRUCTURE OF RIBONUCLEASE A AT 2.0
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 257 1325 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 6
REMARK 1 AUTH A.WLODAWER,L.SJOLIN
REMARK 1 TITL HYDROGEN EXCHANGE IN RNASE A: NEUTRON DIFFRACTION STUDY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 79 1418 1982
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 7
REMARK 1 AUTH A.WLODAWER,R.BOTT,L.SJOLIN
REMARK 1 TITL STRUCTURE OF RIBONUCLEASE A: X-RAY AND NEUTRON REFINEMENT
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 37 13 1981
REMARK 1 REF 2 (SUPPLEMENT)
REMARK 1 REFN ISSN 0567-7394
REMARK 1 REFERENCE 8
REMARK 1 AUTH A.WLODAWER,W.A.HENDRICKSON
REMARK 1 TITL JOINT REFINEMENT OF MACROMOLECULAR STRUCTURES WITH X-RAY AND
REMARK 1 TITL 2 NEUTRON SINGLE-CRYSTAL DIFFRACTION DATA
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 37 8 1981
REMARK 1 REF 2 (SUPPLEMENT)
REMARK 1 REFN ISSN 0567-7394
REMARK 1 REFERENCE 9
REMARK 1 AUTH A.WLODAWER,L.SJOLIN
REMARK 1 TITL ORIENTATION OF HISTIDINE RESIDUES IN RNASE A: NEUTRON
REMARK 1 TITL 2 DIFFRACTION STUDY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 78 2853 1981
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 10
REMARK 1 AUTH A.WLODAWER
REMARK 1 TITL STUDIES OF RIBONUCLEASE-A BY X-RAY AND NEUTRON DIFFRACTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 36 1826 1980
REMARK 1 REFN ISSN 0108-7681
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 951
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.022
REMARK 3 BOND ANGLES (DEGREES) : 4.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 22.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 22.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 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 HIS A 48 NE2 HIS A 48 CD2 -0.098
REMARK 500 SER A 89 CA SER A 89 CB 0.114
REMARK 500 HIS A 105 NE2 HIS A 105 CD2 -0.075
REMARK 500 HIS A 119 CG HIS A 119 CD2 0.062
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 ALA A 5 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 MET A 13 CA - CB - CG ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 14 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 39 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 HIS A 48 CE1 - NE2 - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 LYS A 66 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 THR A 70 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 SER A 77 N - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 MET A 79 CG - SD - CE ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 85 CA - CB - CG ANGL. DEV. = -15.3 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASN A 94 CA - C - N ANGL. DEV. = -16.0 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 ALA A 19 -177.40 -172.14
REMARK 500 SER A 22 -127.41 176.73
REMARK 500 SER A 23 -16.07 -151.51
REMARK 500 LYS A 37 -84.21 -70.99
REMARK 500 PRO A 42 -38.50 -29.30
REMARK 500 VAL A 43 146.66 -176.75
REMARK 500 HIS A 48 71.76 -119.11
REMARK 500 CYS A 58 -3.59 -54.81
REMARK 500 ASN A 67 12.75 -57.88
REMARK 500 ASN A 71 41.94 -91.45
REMARK 500 THR A 87 -168.38 -121.53
REMARK 500 SER A 89 -13.07 127.24
REMARK 500 TYR A 92 106.52 -58.77
REMARK 500 ASP A 121 -68.68 -107.91
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 TYR A 92 PRO A 93 41.50
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 ARG A 33 0.07 SIDE CHAIN
REMARK 500 TYR A 73 0.09 SIDE CHAIN
REMARK 500 TYR A 76 0.07 SIDE CHAIN
REMARK 500 TYR A 92 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE OF THE ENZYME
DBREF 1RTB 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 THR A 3 MET A 13 1 11
HELIX 2 H2 ASN A 24 ASN A 34 1RESIDUE 34 IN 3/10 CONFIG 11
HELIX 3 H3 SER A 50 GLN A 60 1RESIDUES 56-60 IN 3/10 CONFIG 11
SHEET 1 S1A 3 LYS A 41 HIS A 48 0
SHEET 2 S1A 3 MET A 79 THR A 87 -1 N GLU A 86 O PRO A 42
SHEET 3 S1A 3 ASN A 94 LYS A 104 -1 O LYS A 104 N MET A 79
SHEET 1 S1B 3 LYS A 41 HIS A 48 0
SHEET 2 S1B 3 SER A 90 LYS A 91 -1
SHEET 3 S1B 3 ASN A 94 LYS A 104 -1 O ASN A 94 N LYS A 91
SHEET 1 S2A 4 LYS A 61 ALA A 64 0
SHEET 2 S2A 4 ASN A 71 SER A 75 -1 O CYS A 72 N VAL A 63
SHEET 3 S2A 4 HIS A 105 ASN A 113 -1 O VAL A 108 N TYR A 73
SHEET 4 S2A 4 PRO A 114 HIS A 119 -1 O VAL A 116 N GLU A 111
SHEET 1 S2B 4 LYS A 61 ALA A 64 0
SHEET 2 S2B 4 ASN A 71 SER A 75 -1 O CYS A 72 N VAL A 63
SHEET 3 S2B 4 HIS A 105 ASN A 113 -1 O VAL A 108 N TYR A 73
SHEET 4 S2B 4 ASP A 121 VAL A 124 -1 N VAL A 124 O HIS A 105
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.05
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.52
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.45
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.41
CISPEP 1 ASN A 113 PRO A 114 0 -24.03
SITE 1 ACT 9 HIS A 12 LYS A 41 VAL A 43 ASN A 44
SITE 2 ACT 9 THR A 45 HIS A 119 PHE A 120 ASP A 121
SITE 3 ACT 9 SER A 123
CRYST1 44.900 74.900 44.000 90.00 90.00 90.00 P 21 21 21 4
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 0.022272 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022727 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
