HEADER COMPLEX (AMINOACYL-TRNA SYNTHASE/TRNA) 19-JAN-95 1ASZ
TITLE THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND
TITLE 2 FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-RNA (75-MER);
COMPND 3 CHAIN: R, S;
COMPND 4 EC: 6.1.1.12;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ASPARTYL-TRNA SYNTHETASE;
COMPND 8 CHAIN: A, B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE
KEYWDS COMPLEX (AMINOACYL-TRNA SYNTHASE-TRNA), COMPLEX (AMINOACYL-TRNA
KEYWDS 2 SYNTHASE-TRNA) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CAVARELLI,B.REES,J.C.THIERRY,D.MORAS
REVDAT 3 07-FEB-24 1ASZ 1 REMARK LINK
REVDAT 2 24-FEB-09 1ASZ 1 VERSN
REVDAT 1 08-MAY-95 1ASZ 0
JRNL AUTH J.CAVARELLI,G.ERIANI,B.REES,M.RUFF,M.BOEGLIN,A.MITSCHLER,
JRNL AUTH 2 F.MARTIN,J.GANGLOFF,J.C.THIERRY,D.MORAS
JRNL TITL THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE:
JRNL TITL 2 STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION
JRNL TITL 3 REACTION.
JRNL REF EMBO J. V. 13 327 1994
JRNL REFN ISSN 0261-4189
JRNL PMID 8313877
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.CAVARELLI,B.REES,J.C.THIERRY,D.MORAS
REMARK 1 TITL YEAST ASPARTYL-TRNA SYNTHETASE: A STRUCTURAL VIEW OF THE
REMARK 1 TITL 2 AMINOACYLATION REACTION AMINOACYL-TRNA SYNTHETASE
REMARK 1 REF BIOCHIMIE V. 75 1117 1993
REMARK 1 REFN ISSN 0300-9084
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.CAVARELLI,B.REES,M.RUFF,J.C.THIERRY,D.MORAS
REMARK 1 TITL YEAST TRNA ASP RECOGNITION BY ITS COGNATE CLASS II
REMARK 1 TITL 2 AMINOACYL-TRNA SYNTHETASE
REMARK 1 REF NATURE V. 362 181 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.RUFF,S.KRISHNASWAMY,M.BOEGLIN,A.POTERSZMAN,A.MITSCHLER,
REMARK 1 AUTH 2 A.PODJARNY,B.REES,J.C.THIERRY,D.MORAS
REMARK 1 TITL CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL
REMARK 1 TITL 2 STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH
REMARK 1 TITL 3 TRNA ASP
REMARK 1 REF SCIENCE V. 252 1682 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.0
REMARK 3 NUMBER OF REFLECTIONS : 42994
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) : 0.203
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 : 7892
REMARK 3 NUCLEIC ACID ATOMS : 3204
REMARK 3 HETEROGEN ATOMS : 62
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) : 30.00
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) : 0.34
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.300
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:
REMARK 3 TRNA RIBOSES 607, 609, 617, 618, 619, 637, 648, 658, 660,
REMARK 3 676, FROM EACH CHAIN, HAVE BEEN CONSTRAINED TO 2' ENDO
REMARK 3 PUCKER. ALL OTHER TRNA RIBOSES ARE 3' ENDO PUCKER.
REMARK 4
REMARK 4 1ASZ 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_1000171220.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-92
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, MARXDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46698
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.08800
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 (%): 70.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 105.63500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.63500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.67500
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 300 REMARK: MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 A 68 .. R 676 B 68 .. S 676 0.91
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S, A, 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 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 N3 PSU R 655 OP2 A R 658 2.15
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 G R 606 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 U R 608 O3' - P - OP1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 U R 612 O3' - P - OP2 ANGL. DEV. = 13.5 DEGREES
REMARK 500 U R 612 OP1 - P - OP2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 U R 612 N1 - C1' - C2' ANGL. DEV. = -7.3 DEGREES
REMARK 500 A R 614 C5' - C4' - C3' ANGL. DEV. = -9.5 DEGREES
REMARK 500 A R 615 O3' - P - OP1 ANGL. DEV. = 16.0 DEGREES
REMARK 500 H2U R 616 O3' - P - OP1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 G R 617 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 A R 621 O3' - P - OP2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 A R 623 O3' - P - OP1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 A R 624 O3' - P - OP1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 U R 625 O3' - P - OP1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 G R 626 O3' - P - OP1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 G R 628 O3' - P - O5' ANGL. DEV. = -12.5 DEGREES
REMARK 500 G R 628 O3' - P - OP1 ANGL. DEV. = 13.7 DEGREES
REMARK 500 C R 629 O3' - P - OP2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 G R 630 O3' - P - OP1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 U R 633 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G R 634 O4' - C1' - N9 ANGL. DEV. = 5.4 DEGREES
REMARK 500 G R 634 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 C R 638 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 C R 643 O3' - P - OP1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 A R 646 O3' - P - OP1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 G R 653 O4' - C1' - N9 ANGL. DEV. = 5.1 DEGREES
REMARK 500 C R 664 O4' - C1' - N1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 C R 667 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 G R 668 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 A R 676 O4' - C1' - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 G S 604 N9 - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 G S 610 O3' - P - OP1 ANGL. DEV. = 22.1 DEGREES
REMARK 500 G S 610 OP1 - P - OP2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 U S 612 O3' - P - OP1 ANGL. DEV. = 18.8 DEGREES
REMARK 500 A S 614 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES
REMARK 500 H2U S 616 O3' - P - OP2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 G S 617 O4' - C1' - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 C S 629 O3' - P - OP2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 G S 630 O3' - P - OP2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 C S 631 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 C S 631 N3 - C4 - C5 ANGL. DEV. = -2.6 DEGREES
REMARK 500 U S 633 C3' - O3' - P ANGL. DEV. = 12.8 DEGREES
REMARK 500 G S 634 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 G S 634 C3' - O3' - P ANGL. DEV. = 9.4 DEGREES
REMARK 500 U S 635 OP1 - P - OP2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 C S 636 O3' - P - OP2 ANGL. DEV. = 11.8 DEGREES
REMARK 500 1MG S 637 O3' - P - OP2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 G S 641 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 G S 645 O4' - C1' - N9 ANGL. DEV. = 6.7 DEGREES
REMARK 500 U S 648 O3' - P - OP1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 A S 657 O4' - C1' - N9 ANGL. DEV. = 6.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 ALA A 71 22.97 -168.20
REMARK 500 LYS A 72 26.88 -73.44
REMARK 500 LEU A 80 107.39 -38.06
REMARK 500 ILE A 81 106.14 -56.09
REMARK 500 SER A 83 10.63 83.80
REMARK 500 ASP A 85 -15.72 -46.87
REMARK 500 ARG A 88 84.83 -50.13
REMARK 500 VAL A 97 4.91 -58.65
REMARK 500 ALA A 102 -50.63 78.06
REMARK 500 LYS A 103 -74.30 -83.39
REMARK 500 ALA A 123 94.01 -43.19
REMARK 500 THR A 124 -53.37 160.73
REMARK 500 GLN A 133 -80.67 72.31
REMARK 500 ALA A 134 26.18 -151.92
REMARK 500 GLU A 146 -34.81 -163.24
REMARK 500 THR A 148 -75.63 -66.26
REMARK 500 VAL A 154 -70.89 -65.74
REMARK 500 GLU A 163 2.06 85.69
REMARK 500 ASP A 176 -71.44 -81.83
REMARK 500 ALA A 182 166.69 169.95
REMARK 500 GLN A 185 61.16 -106.09
REMARK 500 ASN A 186 -10.91 -171.05
REMARK 500 SER A 198 137.99 166.16
REMARK 500 PRO A 201 -137.14 -73.60
REMARK 500 PRO A 205 -165.12 -53.88
REMARK 500 ILE A 206 -67.20 52.20
REMARK 500 LEU A 207 120.96 72.30
REMARK 500 GLU A 215 -1.32 -59.10
REMARK 500 ALA A 216 -62.89 -90.33
REMARK 500 LEU A 223 151.51 -26.25
REMARK 500 ARG A 235 -31.11 -37.81
REMARK 500 LEU A 239 -2.03 -55.94
REMARK 500 SER A 280 42.98 -83.90
REMARK 500 GLU A 281 -76.16 69.80
REMARK 500 PHE A 292 79.66 13.66
REMARK 500 LYS A 295 -169.47 -101.46
REMARK 500 ALA A 296 154.90 167.41
REMARK 500 SER A 301 143.67 167.13
REMARK 500 PRO A 302 26.89 -71.64
REMARK 500 GLN A 303 -81.74 -52.70
REMARK 500 GLU A 315 -60.43 80.80
REMARK 500 PRO A 322 148.42 -37.87
REMARK 500 ALA A 326 45.67 -86.32
REMARK 500 THR A 331 -145.91 -135.96
REMARK 500 GLU A 349 -46.97 -134.34
REMARK 500 PHE A 373 40.37 -108.64
REMARK 500 LEU A 379 -38.33 -37.75
REMARK 500 GLU A 407 -70.29 -55.00
REMARK 500 GLU A 415 77.68 -111.25
REMARK 500 ASP A 436 -73.52 -61.21
REMARK 500
REMARK 500 THIS ENTRY HAS 111 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 TYR B 291 0.08 SIDE CHAIN
REMARK 500 TYR B 297 0.10 SIDE CHAIN
REMARK 500 TYR B 402 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 701
DBREF 1ASZ A 68 557 UNP P04802 SYDC_YEAST 67 556
DBREF 1ASZ B 68 557 UNP P04802 SYDC_YEAST 67 556
DBREF 1ASZ R 601 676 PDB 1ASZ 1ASZ 601 676
DBREF 1ASZ S 601 676 PDB 1ASZ 1ASZ 601 676
SEQRES 1 R 75 U C C G U G A U A G U U PSU
SEQRES 2 R 75 A A H2U G G H2U C A G A A U G
SEQRES 3 R 75 G G C G C PSU U G U C 1MG C G
SEQRES 4 R 75 U G C C A G A U 5MC G G G G
SEQRES 5 R 75 5MU PSU C A A U U C C C C G U
SEQRES 6 R 75 C G C G G A G C C A
SEQRES 1 S 75 U C C G U G A U A G U U PSU
SEQRES 2 S 75 A A H2U G G H2U C A G A A U G
SEQRES 3 S 75 G G C G C PSU U G U C 1MG C G
SEQRES 4 S 75 U G C C A G A U 5MC G G G G
SEQRES 5 S 75 5MU PSU C A A U U C C C C G U
SEQRES 6 S 75 C G C G G A G C C A
SEQRES 1 A 490 GLU ASP THR ALA LYS ASP ASN TYR GLY LYS LEU PRO LEU
SEQRES 2 A 490 ILE GLN SER ARG ASP SER ASP ARG THR GLY GLN LYS ARG
SEQRES 3 A 490 VAL LYS PHE VAL ASP LEU ASP GLU ALA LYS ASP SER ASP
SEQRES 4 A 490 LYS GLU VAL LEU PHE ARG ALA ARG VAL HIS ASN THR ARG
SEQRES 5 A 490 GLN GLN GLY ALA THR LEU ALA PHE LEU THR LEU ARG GLN
SEQRES 6 A 490 GLN ALA SER LEU ILE GLN GLY LEU VAL LYS ALA ASN LYS
SEQRES 7 A 490 GLU GLY THR ILE SER LYS ASN MET VAL LYS TRP ALA GLY
SEQRES 8 A 490 SER LEU ASN LEU GLU SER ILE VAL LEU VAL ARG GLY ILE
SEQRES 9 A 490 VAL LYS LYS VAL ASP GLU PRO ILE LYS SER ALA THR VAL
SEQRES 10 A 490 GLN ASN LEU GLU ILE HIS ILE THR LYS ILE TYR THR ILE
SEQRES 11 A 490 SER GLU THR PRO GLU ALA LEU PRO ILE LEU LEU GLU ASP
SEQRES 12 A 490 ALA SER ARG SER GLU ALA GLU ALA GLU ALA ALA GLY LEU
SEQRES 13 A 490 PRO VAL VAL ASN LEU ASP THR ARG LEU ASP TYR ARG VAL
SEQRES 14 A 490 ILE ASP LEU ARG THR VAL THR ASN GLN ALA ILE PHE ARG
SEQRES 15 A 490 ILE GLN ALA GLY VAL CYS GLU LEU PHE ARG GLU TYR LEU
SEQRES 16 A 490 ALA THR LYS LYS PHE THR GLU VAL HIS THR PRO LYS LEU
SEQRES 17 A 490 LEU GLY ALA PRO SER GLU GLY GLY SER SER VAL PHE GLU
SEQRES 18 A 490 VAL THR TYR PHE LYS GLY LYS ALA TYR LEU ALA GLN SER
SEQRES 19 A 490 PRO GLN PHE ASN LYS GLN GLN LEU ILE VAL ALA ASP PHE
SEQRES 20 A 490 GLU ARG VAL TYR GLU ILE GLY PRO VAL PHE ARG ALA GLU
SEQRES 21 A 490 ASN SER ASN THR HIS ARG HIS MET THR GLU PHE THR GLY
SEQRES 22 A 490 LEU ASP MET GLU MET ALA PHE GLU GLU HIS TYR HIS GLU
SEQRES 23 A 490 VAL LEU ASP THR LEU SER GLU LEU PHE VAL PHE ILE PHE
SEQRES 24 A 490 SER GLU LEU PRO LYS ARG PHE ALA HIS GLU ILE GLU LEU
SEQRES 25 A 490 VAL ARG LYS GLN TYR PRO VAL GLU GLU PHE LYS LEU PRO
SEQRES 26 A 490 LYS ASP GLY LYS MET VAL ARG LEU THR TYR LYS GLU GLY
SEQRES 27 A 490 ILE GLU MET LEU ARG ALA ALA GLY LYS GLU ILE GLY ASP
SEQRES 28 A 490 PHE GLU ASP LEU SER THR GLU ASN GLU LYS PHE LEU GLY
SEQRES 29 A 490 LYS LEU VAL ARG ASP LYS TYR ASP THR ASP PHE TYR ILE
SEQRES 30 A 490 LEU ASP LYS PHE PRO LEU GLU ILE ARG PRO PHE TYR THR
SEQRES 31 A 490 MET PRO ASP PRO ALA ASN PRO LYS TYR SER ASN SER TYR
SEQRES 32 A 490 ASP PHE PHE MET ARG GLY GLU GLU ILE LEU SER GLY ALA
SEQRES 33 A 490 GLN ARG ILE HIS ASP HIS ALA LEU LEU GLN GLU ARG MET
SEQRES 34 A 490 LYS ALA HIS GLY LEU SER PRO GLU ASP PRO GLY LEU LYS
SEQRES 35 A 490 ASP TYR CYS ASP GLY PHE SER TYR GLY CYS PRO PRO HIS
SEQRES 36 A 490 ALA GLY GLY GLY ILE GLY LEU GLU ARG VAL VAL MET PHE
SEQRES 37 A 490 TYR LEU ASP LEU LYS ASN ILE ARG ARG ALA SER LEU PHE
SEQRES 38 A 490 PRO ARG ASP PRO LYS ARG LEU ARG PRO
SEQRES 1 B 490 GLU ASP THR ALA LYS ASP ASN TYR GLY LYS LEU PRO LEU
SEQRES 2 B 490 ILE GLN SER ARG ASP SER ASP ARG THR GLY GLN LYS ARG
SEQRES 3 B 490 VAL LYS PHE VAL ASP LEU ASP GLU ALA LYS ASP SER ASP
SEQRES 4 B 490 LYS GLU VAL LEU PHE ARG ALA ARG VAL HIS ASN THR ARG
SEQRES 5 B 490 GLN GLN GLY ALA THR LEU ALA PHE LEU THR LEU ARG GLN
SEQRES 6 B 490 GLN ALA SER LEU ILE GLN GLY LEU VAL LYS ALA ASN LYS
SEQRES 7 B 490 GLU GLY THR ILE SER LYS ASN MET VAL LYS TRP ALA GLY
SEQRES 8 B 490 SER LEU ASN LEU GLU SER ILE VAL LEU VAL ARG GLY ILE
SEQRES 9 B 490 VAL LYS LYS VAL ASP GLU PRO ILE LYS SER ALA THR VAL
SEQRES 10 B 490 GLN ASN LEU GLU ILE HIS ILE THR LYS ILE TYR THR ILE
SEQRES 11 B 490 SER GLU THR PRO GLU ALA LEU PRO ILE LEU LEU GLU ASP
SEQRES 12 B 490 ALA SER ARG SER GLU ALA GLU ALA GLU ALA ALA GLY LEU
SEQRES 13 B 490 PRO VAL VAL ASN LEU ASP THR ARG LEU ASP TYR ARG VAL
SEQRES 14 B 490 ILE ASP LEU ARG THR VAL THR ASN GLN ALA ILE PHE ARG
SEQRES 15 B 490 ILE GLN ALA GLY VAL CYS GLU LEU PHE ARG GLU TYR LEU
SEQRES 16 B 490 ALA THR LYS LYS PHE THR GLU VAL HIS THR PRO LYS LEU
SEQRES 17 B 490 LEU GLY ALA PRO SER GLU GLY GLY SER SER VAL PHE GLU
SEQRES 18 B 490 VAL THR TYR PHE LYS GLY LYS ALA TYR LEU ALA GLN SER
SEQRES 19 B 490 PRO GLN PHE ASN LYS GLN GLN LEU ILE VAL ALA ASP PHE
SEQRES 20 B 490 GLU ARG VAL TYR GLU ILE GLY PRO VAL PHE ARG ALA GLU
SEQRES 21 B 490 ASN SER ASN THR HIS ARG HIS MET THR GLU PHE THR GLY
SEQRES 22 B 490 LEU ASP MET GLU MET ALA PHE GLU GLU HIS TYR HIS GLU
SEQRES 23 B 490 VAL LEU ASP THR LEU SER GLU LEU PHE VAL PHE ILE PHE
SEQRES 24 B 490 SER GLU LEU PRO LYS ARG PHE ALA HIS GLU ILE GLU LEU
SEQRES 25 B 490 VAL ARG LYS GLN TYR PRO VAL GLU GLU PHE LYS LEU PRO
SEQRES 26 B 490 LYS ASP GLY LYS MET VAL ARG LEU THR TYR LYS GLU GLY
SEQRES 27 B 490 ILE GLU MET LEU ARG ALA ALA GLY LYS GLU ILE GLY ASP
SEQRES 28 B 490 PHE GLU ASP LEU SER THR GLU ASN GLU LYS PHE LEU GLY
SEQRES 29 B 490 LYS LEU VAL ARG ASP LYS TYR ASP THR ASP PHE TYR ILE
SEQRES 30 B 490 LEU ASP LYS PHE PRO LEU GLU ILE ARG PRO PHE TYR THR
SEQRES 31 B 490 MET PRO ASP PRO ALA ASN PRO LYS TYR SER ASN SER TYR
SEQRES 32 B 490 ASP PHE PHE MET ARG GLY GLU GLU ILE LEU SER GLY ALA
SEQRES 33 B 490 GLN ARG ILE HIS ASP HIS ALA LEU LEU GLN GLU ARG MET
SEQRES 34 B 490 LYS ALA HIS GLY LEU SER PRO GLU ASP PRO GLY LEU LYS
SEQRES 35 B 490 ASP TYR CYS ASP GLY PHE SER TYR GLY CYS PRO PRO HIS
SEQRES 36 B 490 ALA GLY GLY GLY ILE GLY LEU GLU ARG VAL VAL MET PHE
SEQRES 37 B 490 TYR LEU ASP LEU LYS ASN ILE ARG ARG ALA SER LEU PHE
SEQRES 38 B 490 PRO ARG ASP PRO LYS ARG LEU ARG PRO
MODRES 1ASZ PSU R 613 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ H2U R 616 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ H2U R 619 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ PSU R 632 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ 1MG R 637 G 1N-METHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 1ASZ 5MC R 649 C 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ 5MU R 654 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 1ASZ PSU R 655 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ PSU S 613 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ H2U S 616 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ H2U S 619 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ PSU S 632 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ 1MG S 637 G 1N-METHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 1ASZ 5MC S 649 C 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
MODRES 1ASZ 5MU S 654 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 1ASZ PSU S 655 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET PSU R 613 20
HET H2U R 616 20
HET H2U R 619 20
HET PSU R 632 20
HET 1MG R 637 24
HET 5MC R 649 21
HET 5MU R 654 21
HET PSU R 655 20
HET PSU S 613 20
HET H2U S 616 20
HET H2U S 619 20
HET PSU S 632 20
HET 1MG S 637 24
HET 5MC S 649 21
HET 5MU S 654 21
HET PSU S 655 20
HET ATP A 701 31
HET ATP B 701 31
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM 1MG 1N-METHYLGUANOSINE-5'-MONOPHOSPHATE
HETNAM 5MC 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 1 PSU 6(C9 H13 N2 O9 P)
FORMUL 1 H2U 4(C9 H15 N2 O9 P)
FORMUL 1 1MG 2(C11 H16 N5 O8 P)
FORMUL 1 5MC 2(C10 H16 N3 O8 P)
FORMUL 1 5MU 2(C10 H15 N2 O9 P)
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
HELIX 1 1 PHE A 96 ASP A 98 5 3
HELIX 2 2 LYS A 151 SER A 159 1 9
HELIX 3 3 LEU A 208 SER A 212 1 5
HELIX 4 4 GLU A 215 GLU A 219 1 5
HELIX 5 5 LEU A 228 ARG A 240 1 13
HELIX 6 6 VAL A 242 THR A 264 1 23
HELIX 7 7 GLN A 303 VAL A 311 1 9
HELIX 8 8 TYR A 351 PHE A 366 1 16
HELIX 9 9 LEU A 369 ARG A 372 1 4
HELIX 10 10 ALA A 374 ARG A 381 1 8
HELIX 11 11 TYR A 402 ALA A 412 1 11
HELIX 12 12 THR A 424 TYR A 438 1 15
HELIX 13 13 HIS A 489 ALA A 498 1 10
HELIX 14 14 PRO A 506 PHE A 515 1 10
HELIX 15 15 LEU A 529 LEU A 537 1 9
HELIX 16 16 ARG A 543 ALA A 545 5 3
HELIX 17 17 THR B 70 ASP B 73 5 4
HELIX 18 18 PHE B 96 ASP B 98 5 3
HELIX 19 19 GLU B 101 ASP B 104 1 4
HELIX 20 20 LYS B 151 SER B 159 1 9
HELIX 21 21 LEU B 208 SER B 212 1 5
HELIX 22 22 GLU B 215 ALA B 220 1 6
HELIX 23 23 LEU B 228 ARG B 240 1 13
HELIX 24 24 VAL B 242 LYS B 265 1 24
HELIX 25 25 GLN B 303 VAL B 311 1 9
HELIX 26 26 HIS B 352 ARG B 372 1 21
HELIX 27 27 ALA B 374 ARG B 381 1 8
HELIX 28 28 TYR B 402 ALA B 412 1 11
HELIX 29 29 THR B 424 LYS B 437 1 14
HELIX 30 30 HIS B 489 ALA B 498 1 10
HELIX 31 31 PRO B 506 TYR B 517 1 12
HELIX 32 32 LEU B 529 LEU B 537 1 9
SHEET 1 A 6 TYR A 75 LYS A 77 0
SHEET 2 A 6 LYS A 193 SER A 198 1 N ILE A 194 O GLY A 76
SHEET 3 A 6 ILE A 165 ILE A 171 -1 N ARG A 169 O LYS A 193
SHEET 4 A 6 GLU A 108 GLN A 120 -1 N ALA A 113 O VAL A 166
SHEET 5 A 6 LEU A 125 GLN A 132 -1 N ARG A 131 O ARG A 114
SHEET 6 A 6 SER A 135 LYS A 142 -1 N VAL A 141 O ALA A 126
SHEET 1 B 2 GLY A 170 LYS A 174 0
SHEET 2 B 2 LEU A 187 ILE A 191 -1 N HIS A 190 O ILE A 171
SHEET 1 C 7 ARG A 316 PHE A 324 0
SHEET 2 C 7 GLU A 337 ALA A 346 -1 N GLU A 344 O VAL A 317
SHEET 3 C 7 HIS A 522 GLY A 528 -1 N ILE A 527 O LEU A 341
SHEET 4 C 7 GLU A 477 GLN A 484 -1 N ALA A 483 O GLY A 524
SHEET 5 C 7 TYR A 470 MET A 474 -1 N MET A 474 O GLU A 477
SHEET 6 C 7 PHE A 442 ASP A 446 -1 N LEU A 445 O ASP A 471
SHEET 7 C 7 VAL A 398 THR A 401 1 N VAL A 398 O ILE A 444
SHEET 1 D 4 TYR B 75 LYS B 77 0
SHEET 2 D 4 LYS B 193 SER B 198 1 N ILE B 194 O GLY B 76
SHEET 3 D 4 ILE B 165 ILE B 171 -1 N ARG B 169 O LYS B 193
SHEET 4 D 4 GLU B 108 ARG B 114 -1 N ALA B 113 O VAL B 166
SHEET 1 E 2 PHE B 127 ARG B 131 0
SHEET 2 E 2 LEU B 136 LEU B 140 -1 N GLY B 139 O LEU B 128
SHEET 1 F 2 GLY B 170 LYS B 174 0
SHEET 2 F 2 LEU B 187 ILE B 191 -1 N HIS B 190 O ILE B 171
SHEET 1 G 2 GLU B 288 TYR B 291 0
SHEET 2 G 2 GLY B 294 TYR B 297 -1 N ALA B 296 O VAL B 289
SHEET 1 H 2 VAL B 317 PHE B 324 0
SHEET 2 H 2 GLU B 337 GLU B 344 -1 N GLU B 344 O VAL B 317
SHEET 1 I 4 VAL B 398 THR B 401 0
SHEET 2 I 4 PHE B 442 ASP B 446 1 N ILE B 444 O VAL B 398
SHEET 3 I 4 SER B 469 MET B 474 -1 N PHE B 473 O TYR B 443
SHEET 4 I 4 GLU B 477 ALA B 483 -1 N GLY B 482 O TYR B 470
LINK O3' U R 612 P PSU R 613 1555 1555 1.60
LINK O3' PSU R 613 P A R 614 1555 1555 1.59
LINK O3' A R 615 P H2U R 616 1555 1555 1.61
LINK O3' H2U R 616 P G R 617 1555 1555 1.62
LINK O3' G R 618 P H2U R 619 1555 1555 1.63
LINK O3' H2U R 619 P C R 620 1555 1555 1.61
LINK O3' C R 631 P PSU R 632 1555 1555 1.61
LINK O3' PSU R 632 P U R 633 1555 1555 1.61
LINK O3' C R 636 P 1MG R 637 1555 1555 1.61
LINK O3' 1MG R 637 P C R 638 1555 1555 1.61
LINK O3' U R 648 P 5MC R 649 1555 1555 1.60
LINK O3' 5MC R 649 P G R 650 1555 1555 1.62
LINK O3' G R 653 P 5MU R 654 1555 1555 1.61
LINK O3' 5MU R 654 P PSU R 655 1555 1555 1.61
LINK O3' PSU R 655 P C R 656 1555 1555 1.61
LINK O3' U S 612 P PSU S 613 1555 1555 1.61
LINK O3' PSU S 613 P A S 614 1555 1555 1.62
LINK O3' A S 615 P H2U S 616 1555 1555 1.61
LINK O3' H2U S 616 P G S 617 1555 1555 1.62
LINK O3' G S 618 P H2U S 619 1555 1555 1.62
LINK O3' H2U S 619 P C S 620 1555 1555 1.61
LINK O3' C S 631 P PSU S 632 1555 1555 1.62
LINK O3' PSU S 632 P U S 633 1555 1555 1.63
LINK O3' C S 636 P 1MG S 637 1555 1555 1.62
LINK O3' 1MG S 637 P C S 638 1555 1555 1.61
LINK O3' U S 648 P 5MC S 649 1555 1555 1.61
LINK O3' 5MC S 649 P G S 650 1555 1555 1.61
LINK O3' G S 653 P 5MU S 654 1555 1555 1.60
LINK O3' 5MU S 654 P PSU S 655 1555 1555 1.61
LINK O3' PSU S 655 P C S 656 1555 1555 1.61
CISPEP 1 ARG A 556 PRO A 557 0 -0.19
CISPEP 2 ARG B 556 PRO B 557 0 1.13
SITE 1 AC1 11 ARG A 325 HIS A 334 MET A 335 PHE A 338
SITE 2 AC1 11 GLU A 478 ILE A 479 LEU A 480 GLY A 526
SITE 3 AC1 11 ARG A 531 C R 675 A R 676
SITE 1 AC2 11 ARG B 325 MET B 335 PHE B 338 GLU B 478
SITE 2 AC2 11 ILE B 479 LEU B 480 SER B 481 ILE B 527
SITE 3 AC2 11 ARG B 531 C S 675 A S 676
CRYST1 211.270 145.350 86.190 90.00 90.00 90.00 P 21 21 2 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 0.004733 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006880 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011602 0.00000
MTRIX1 1 -0.989850 -0.061210 -0.128240 142.50000 1
MTRIX2 1 -0.076360 -0.531990 0.843300 98.60000 1
MTRIX3 1 -0.119840 0.844540 0.521910 -43.15000 1
(ATOM LINES ARE NOT SHOWN.)
END
