HEADER HYDROLASE 23-MAR-05 1Z6S
TITLE RIBONUCLEASE A- AMP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RIBONUCLEASE A, RNASE A, RNASE 1;
COMPND 5 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE, RIBONUCLEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.N.HATZOPOULOS,D.D.LEONIDAS,R.KARDAKARIS,J.KOBE,N.G.OIKONOMAKOS
REVDAT 3 13-JUL-11 1Z6S 1 VERSN
REVDAT 2 24-FEB-09 1Z6S 1 VERSN
REVDAT 1 16-AUG-05 1Z6S 0
JRNL AUTH G.N.HATZOPOULOS,D.D.LEONIDAS,R.KARDAKARIS,J.KOBE,
JRNL AUTH 2 N.G.OIKONOMAKOS
JRNL TITL THE BINDING OF IMP TO RIBONUCLEASE A
JRNL REF FEBS J. V. 272 3988 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 16045769
JRNL DOI 10.1111/J.1742-4658.2005.04822.X
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 35273
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1852
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2587
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 18.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.064
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2006 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2727 ; 1.456 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 6.101 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;33.712 ;25.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 336 ;13.188 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.369 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 302 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1499 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 928 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1385 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 241 ; 0.145 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.214 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.163 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1265 ; 0.718 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2008 ; 1.162 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 835 ; 2.054 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 719 ; 3.211 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2958 0.3843 9.9726
REMARK 3 T TENSOR
REMARK 3 T11: -0.1547 T22: -0.1368
REMARK 3 T33: -0.1351 T12: -0.0074
REMARK 3 T13: 0.0159 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.7534 L22: 1.4734
REMARK 3 L33: 4.3377 L12: -0.0189
REMARK 3 L13: -0.6496 L23: -0.0720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0315 S12: 0.2976 S13: -0.0479
REMARK 3 S21: -0.1624 S22: 0.0710 S23: -0.1574
REMARK 3 S31: -0.1306 S32: -0.0592 S33: -0.1025
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2056 -0.0441 31.1226
REMARK 3 T TENSOR
REMARK 3 T11: -0.1129 T22: -0.1283
REMARK 3 T33: -0.1037 T12: -0.0279
REMARK 3 T13: -0.0263 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 2.3566 L22: 1.6208
REMARK 3 L33: 2.6418 L12: 0.0845
REMARK 3 L13: 0.9787 L23: 0.8446
REMARK 3 S TENSOR
REMARK 3 S11: -0.0951 S12: 0.3154 S13: 0.0413
REMARK 3 S21: -0.3158 S22: 0.0274 S23: 0.1493
REMARK 3 S31: -0.0683 S32: -0.0247 S33: 0.0677
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1Z6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8115
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PEG 4000, PH 5.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.16500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.30450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.16500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.30450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B1170 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1148 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 NE2 GLN A 101 O HOH A 1177 2.04
REMARK 500 O3P AMP A 1101 O HOH A 1172 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1157 O HOH B 1259 4546 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 92 CG TYR A 92 CD1 0.125
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 62.98 112.85
REMARK 500 SER A 21 109.30 -22.58
REMARK 500 HIS A 48 65.66 -102.21
REMARK 500 GLN A 60 -139.37 -99.43
REMARK 500 ASN A 71 31.46 -98.02
REMARK 500 SER B 21 37.47 25.60
REMARK 500 HIS B 48 59.85 -102.10
REMARK 500 GLN B 60 -130.45 -106.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1102 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH A1209 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH B1243 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH B1247 DISTANCE = 5.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z6D RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - IMP COMPLEX
REMARK 900 RELATED ID: 1O0F RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - 3'5'ADP COMPLEX
REMARK 900 RELATED ID: 1O0O RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - 2'5'ADP COMPLEX
REMARK 900 RELATED ID: 1O0H RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - 5'ADP COMPLEX
REMARK 900 RELATED ID: 1O0M RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - U-2'P COMPLEX
REMARK 900 RELATED ID: 1O0N RELATED DB: PDB
REMARK 900 RIBONUCLEASE A - U-3'P COMPLEX
DBREF 1Z6S A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1Z6S B 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
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET AMP A1101 36
HET AMP B1102 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 5 HOH *330(H2 O)
HELIX 1 1 THR A 3 MET A 13 1 11
HELIX 2 2 ASN A 24 ARG A 33 1 10
HELIX 3 3 SER A 50 VAL A 57 1 8
HELIX 4 4 CYS A 58 GLN A 60 5 3
HELIX 5 5 THR B 3 MET B 13 1 11
HELIX 6 6 ASN B 24 ARG B 33 1 10
HELIX 7 7 SER B 50 ALA B 56 1 7
HELIX 8 8 VAL B 57 GLN B 60 5 4
SHEET 1 A 5 VAL A 43 VAL A 47 0
SHEET 2 A 5 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 A 5 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 A 5 CYS A 72 GLN A 74 -1 N TYR A 73 O VAL A 108
SHEET 5 A 5 LYS A 61 VAL A 63 -1 N LYS A 61 O GLN A 74
SHEET 1 B 4 VAL A 43 VAL A 47 0
SHEET 2 B 4 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 B 4 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 B 4 VAL A 116 VAL A 124 -1 O VAL A 118 N ALA A 109
SHEET 1 C 5 VAL B 43 VAL B 47 0
SHEET 2 C 5 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 C 5 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 C 5 CYS B 72 GLN B 74 -1 N TYR B 73 O VAL B 108
SHEET 5 C 5 LYS B 61 VAL B 63 -1 N LYS B 61 O GLN B 74
SHEET 1 D 4 VAL B 43 VAL B 47 0
SHEET 2 D 4 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 D 4 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 D 4 VAL B 116 VAL B 124 -1 O VAL B 118 N ALA B 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.02
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.02
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.04
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.04
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.03
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.04
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.06
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.01
CISPEP 1 TYR A 92 PRO A 93 0 5.93
CISPEP 2 ASN A 113 PRO A 114 0 8.84
CISPEP 3 TYR B 92 PRO B 93 0 5.13
CISPEP 4 ASN B 113 PRO B 114 0 5.95
SITE 1 AC1 19 GLN A 11 HIS A 12 LYS A 41 CYS A 65
SITE 2 AC1 19 ASN A 67 GLN A 69 ASN A 71 ALA A 109
SITE 3 AC1 19 GLU A 111 HIS A 119 PHE A 120 HOH A1103
SITE 4 AC1 19 HOH A1109 HOH A1121 HOH A1172 HOH A1236
SITE 5 AC1 19 HOH A1237 HOH A1261 LYS B 91
SITE 1 AC2 15 GLN B 11 HIS B 12 LYS B 41 CYS B 65
SITE 2 AC2 15 ASN B 67 GLN B 69 ASN B 71 ALA B 109
SITE 3 AC2 15 GLU B 111 VAL B 118 HIS B 119 PHE B 120
SITE 4 AC2 15 HOH B1115 HOH B1123 HOH B1227
CRYST1 100.330 32.609 72.419 90.00 90.83 90.00 C 1 2 1 8
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 0.009967 0.000000 0.000144 0.00000
SCALE2 0.000000 0.030666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
