HEADER TRANSFERASE 11-JAN-02 1IT8
TITLE CRYSTAL STRUCTURE OF ARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE FROM
TITLE 2 PYROCOCCUS HORIKOSHII COMPLEXED WITH ARCHAEOSINE PRECURSOR, PREQ0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARCHAEOSINE TRNA-GUANINE TRANSGLYCOSYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.29;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS (ALPHA/BETA)8 BARREL, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ISHITANI,O.NUREKI,S.FUKAI,T.KIJIMOTO,N.NAMEKI,M.WATANABE,H.KONDO,
AUTHOR 2 M.SEKINE,N.OKADA,S.NISHIMURA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 1IT8 1 REMARK LINK
REVDAT 4 07-FEB-18 1IT8 1 REMARK
REVDAT 3 24-FEB-09 1IT8 1 VERSN
REVDAT 2 07-JAN-03 1IT8 1 REMARK
REVDAT 1 22-MAY-02 1IT8 0
JRNL AUTH R.ISHITANI,O.NUREKI,S.FUKAI,T.KIJIMOTO,N.NAMEKI,M.WATANABE,
JRNL AUTH 2 H.KONDO,M.SEKINE,N.OKADA,S.NISHIMURA,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF ARCHAEOSINE TRNA-GUANINE
JRNL TITL 2 TRANSGLYCOSYLASE.
JRNL REF J.MOL.BIOL. V. 318 665 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054814
JRNL DOI 10.1016/S0022-2836(02)00090-6
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 63193
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 SET) : 0.232
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6391
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8692
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 990
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 142
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.12000
REMARK 3 B22 (A**2) : 6.12000
REMARK 3 B33 (A**2) : -12.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.60
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.160 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.850 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 24.23
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : PQ0.PAR
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000005257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45PX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.02
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 282730
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.20200
REMARK 200 R SYM FOR SHELL (I) : 0.20200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.140
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1IQ8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA PHOSPHATE, K PHOSPHATE, NA ACETATE,
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 183.08400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.23350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.23350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 274.62600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.23350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.23350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 91.54200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.23350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.23350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 274.62600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.23350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.23350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 91.54200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 183.08400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 4
REMARK 465 ASP A 5
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 ASP B 5
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 ASP A 16 131.95 -172.18
REMARK 500 ASN A 27 56.97 34.49
REMARK 500 LYS A 43 -79.55 -82.82
REMARK 500 LEU A 129 46.67 -68.87
REMARK 500 ASP A 136 2.60 54.10
REMARK 500 GLN A 169 -161.33 -113.06
REMARK 500 SER A 171 -137.94 46.10
REMARK 500 ALA A 231 92.46 -64.37
REMARK 500 PRO A 234 -35.78 -39.26
REMARK 500 PRO A 361 155.13 -45.22
REMARK 500 SER A 372 175.91 176.47
REMARK 500 SER A 408 136.32 -33.74
REMARK 500 GLN A 419 46.71 -95.91
REMARK 500 ALA A 422 -157.82 -132.98
REMARK 500 ALA A 436 -81.03 -1.26
REMARK 500 ASP A 457 -70.20 -29.10
REMARK 500 ASP A 458 28.41 -73.67
REMARK 500 ARG A 470 -105.92 -128.21
REMARK 500 ASN A 475 69.72 5.14
REMARK 500 ASP A 486 4.23 -151.58
REMARK 500 ARG A 507 121.84 -37.96
REMARK 500 LYS B 43 -89.45 -79.24
REMARK 500 ILE B 82 -26.89 -33.93
REMARK 500 SER B 106 115.13 174.70
REMARK 500 GLU B 108 56.59 -114.55
REMARK 500 PRO B 135 -74.35 -44.79
REMARK 500 ASP B 136 57.33 -96.34
REMARK 500 GLU B 158 -73.13 -69.20
REMARK 500 GLN B 169 54.83 -147.99
REMARK 500 SER B 171 -141.67 66.91
REMARK 500 VAL B 283 -61.97 -90.21
REMARK 500 ARG B 394 -66.88 -102.49
REMARK 500 ARG B 409 -18.26 -48.73
REMARK 500 ALA B 422 -157.59 -125.05
REMARK 500 THR B 432 -117.10 -80.58
REMARK 500 LYS B 433 -13.68 -140.45
REMARK 500 ALA B 436 -62.78 -16.25
REMARK 500 GLU B 450 138.32 -23.69
REMARK 500 ASP B 458 42.95 -69.61
REMARK 500 SER B 464 -165.22 -74.86
REMARK 500 LYS B 465 -70.83 -46.04
REMARK 500 ASN B 475 5.25 56.13
REMARK 500 LEU B 479 -72.28 -88.01
REMARK 500 ASP B 486 -6.05 -162.92
REMARK 500 ILE B 493 -43.15 -20.95
REMARK 500 MET B 508 -3.06 73.85
REMARK 500 LYS B 522 -73.48 -74.94
REMARK 500 ALA B 528 -37.02 -35.35
REMARK 500 ASP B 551 42.35 73.45
REMARK 500 ALA B 555 164.10 177.79
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 600 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 279 SG
REMARK 620 2 CYS A 281 SG 102.7
REMARK 620 3 CYS A 284 SG 116.0 108.6
REMARK 620 4 HIS A 307 ND1 111.1 114.2 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 528 O
REMARK 620 2 MET A 566 O 79.3
REMARK 620 3 ILE A 567 O 161.6 83.0
REMARK 620 4 PHE A 569 O 84.8 92.8 91.0
REMARK 620 5 GLN A 570 NE2 113.3 143.0 78.5 56.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 600 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 279 SG
REMARK 620 2 CYS B 281 SG 110.3
REMARK 620 3 CYS B 284 SG 111.0 104.6
REMARK 620 4 HIS B 307 ND1 117.0 119.4 91.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 528 O
REMARK 620 2 VAL B 531 O 85.5
REMARK 620 3 MET B 566 O 67.3 89.8
REMARK 620 4 ILE B 567 O 137.7 99.9 70.7
REMARK 620 5 PHE B 569 O 70.3 155.5 77.9 95.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ0 A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IQ8 RELATED DB: PDB
REMARK 900 1IQ8 CONTAINS THE SAME PROTEIN.
REMARK 900 RELATED ID: 1IT7 RELATED DB: PDB
REMARK 900 1IT7 CONTAINS THE SAME PROTEIN COMPLEXED WITH GUANINE.
REMARK 900 RELATED ID: TRT001000258.3 RELATED DB: TARGETDB
DBREF 1IT8 A 1 582 UNP O58843 O58843_PYRHO 1 582
DBREF 1IT8 B 1 582 UNP O58843 O58843_PYRHO 1 582
SEQRES 1 A 582 MET SER ARG GLY ASP LYS MET LEU LYS PHE GLU ILE LYS
SEQRES 2 A 582 ALA ARG ASP GLY ALA GLY ARG ILE GLY LYS LEU GLU VAL
SEQRES 3 A 582 ASN GLY LYS LYS ILE GLU THR PRO ALA ILE MET PRO VAL
SEQRES 4 A 582 VAL ASN PRO LYS GLN MET VAL VAL GLU PRO LYS GLU LEU
SEQRES 5 A 582 GLU LYS MET GLY PHE GLU ILE ILE ILE THR ASN SER TYR
SEQRES 6 A 582 ILE ILE TYR LYS ASP GLU GLU LEU ARG ARG LYS ALA LEU
SEQRES 7 A 582 GLU LEU GLY ILE HIS ARG MET LEU ASP TYR ASN GLY ILE
SEQRES 8 A 582 ILE GLU VAL ASP SER GLY SER PHE GLN LEU MET LYS TYR
SEQRES 9 A 582 GLY SER ILE GLU VAL SER ASN ARG GLU ILE ILE GLU PHE
SEQRES 10 A 582 GLN HIS ARG ILE GLY VAL ASP ILE GLY THR PHE LEU ASP
SEQRES 11 A 582 ILE PRO THR PRO PRO ASP ALA PRO ARG GLU GLN ALA VAL
SEQRES 12 A 582 LYS GLU LEU GLU ILE THR LEU SER ARG ALA ARG GLU ALA
SEQRES 13 A 582 GLU GLU ILE LYS GLU ILE PRO MET ASN ALA THR ILE GLN
SEQRES 14 A 582 GLY SER THR TYR THR ASP LEU ARG ARG TYR ALA ALA ARG
SEQRES 15 A 582 ARG LEU SER SER MET ASN PHE GLU ILE HIS PRO ILE GLY
SEQRES 16 A 582 GLY VAL VAL PRO LEU LEU GLU SER TYR ARG PHE ARG ASP
SEQRES 17 A 582 VAL VAL ASP ILE VAL ILE SER SER LYS MET ALA LEU ARG
SEQRES 18 A 582 PRO ASP ARG PRO VAL HIS LEU PHE GLY ALA GLY HIS PRO
SEQRES 19 A 582 ILE VAL PHE ALA LEU ALA VAL ALA MET GLY VAL ASP LEU
SEQRES 20 A 582 PHE ASP SER ALA SER TYR ALA LEU TYR ALA LYS ASP ASP
SEQRES 21 A 582 ARG TYR MET THR PRO GLU GLY THR LYS ARG LEU ASP GLU
SEQRES 22 A 582 LEU ASP TYR PHE PRO CYS SER CYS PRO VAL CYS SER LYS
SEQRES 23 A 582 TYR THR PRO GLN GLU LEU ARG GLU MET PRO LYS GLU GLU
SEQRES 24 A 582 ARG THR ARG LEU LEU ALA LEU HIS ASN LEU TRP VAL ILE
SEQRES 25 A 582 LYS GLU GLU ILE LYS ARG VAL LYS GLN ALA ILE LYS GLU
SEQRES 26 A 582 GLY GLU LEU TRP ARG LEU VAL ASP GLU ARG ALA ARG SER
SEQRES 27 A 582 HIS PRO LYS LEU TYR SER ALA TYR LYS ARG LEU LEU GLU
SEQRES 28 A 582 HIS TYR THR PHE LEU GLU GLU PHE GLU PRO ILE THR LYS
SEQRES 29 A 582 LYS SER ALA LEU PHE LYS ILE SER ASN GLU SER LEU ARG
SEQRES 30 A 582 TRP PRO VAL VAL ARG ARG ALA LYS GLU ARG ALA LYS SER
SEQRES 31 A 582 ILE ASN GLU ARG PHE GLY GLU LEU VAL GLU HIS PRO ILE
SEQRES 32 A 582 PHE GLY ARG VAL SER ARG TYR LEU SER LEU THR TYR PRO
SEQRES 33 A 582 PHE ALA GLN SER GLU ALA GLU ASP ASP PHE LYS ILE GLU
SEQRES 34 A 582 LYS PRO THR LYS GLU ASP ALA ILE LYS TYR VAL MET ALA
SEQRES 35 A 582 ILE ALA GLU TYR GLN PHE GLY GLU GLY ALA SER ARG ALA
SEQRES 36 A 582 PHE ASP ASP ALA LYS VAL GLU LEU SER LYS THR GLY MET
SEQRES 37 A 582 PRO ARG GLN VAL LYS VAL ASN GLY LYS ARG LEU ALA THR
SEQRES 38 A 582 VAL ARG ALA ASP ASP GLY LEU LEU THR LEU GLY ILE GLU
SEQRES 39 A 582 GLY ALA LYS ARG LEU HIS ARG VAL LEU PRO TYR PRO ARG
SEQRES 40 A 582 MET ARG VAL VAL VAL ASN LYS GLU ALA GLU PRO PHE ALA
SEQRES 41 A 582 ARG LYS GLY LYS ASP VAL PHE ALA LYS PHE VAL ILE PHE
SEQRES 42 A 582 ALA ASP PRO GLY ILE ARG PRO TYR ASP GLU VAL LEU VAL
SEQRES 43 A 582 VAL ASN GLU ASN ASP GLU LEU LEU ALA THR GLY GLN ALA
SEQRES 44 A 582 LEU LEU SER GLY ARG GLU MET ILE VAL PHE GLN TYR GLY
SEQRES 45 A 582 ARG ALA VAL LYS VAL ARG LYS GLY VAL GLU
SEQRES 1 B 582 MET SER ARG GLY ASP LYS MET LEU LYS PHE GLU ILE LYS
SEQRES 2 B 582 ALA ARG ASP GLY ALA GLY ARG ILE GLY LYS LEU GLU VAL
SEQRES 3 B 582 ASN GLY LYS LYS ILE GLU THR PRO ALA ILE MET PRO VAL
SEQRES 4 B 582 VAL ASN PRO LYS GLN MET VAL VAL GLU PRO LYS GLU LEU
SEQRES 5 B 582 GLU LYS MET GLY PHE GLU ILE ILE ILE THR ASN SER TYR
SEQRES 6 B 582 ILE ILE TYR LYS ASP GLU GLU LEU ARG ARG LYS ALA LEU
SEQRES 7 B 582 GLU LEU GLY ILE HIS ARG MET LEU ASP TYR ASN GLY ILE
SEQRES 8 B 582 ILE GLU VAL ASP SER GLY SER PHE GLN LEU MET LYS TYR
SEQRES 9 B 582 GLY SER ILE GLU VAL SER ASN ARG GLU ILE ILE GLU PHE
SEQRES 10 B 582 GLN HIS ARG ILE GLY VAL ASP ILE GLY THR PHE LEU ASP
SEQRES 11 B 582 ILE PRO THR PRO PRO ASP ALA PRO ARG GLU GLN ALA VAL
SEQRES 12 B 582 LYS GLU LEU GLU ILE THR LEU SER ARG ALA ARG GLU ALA
SEQRES 13 B 582 GLU GLU ILE LYS GLU ILE PRO MET ASN ALA THR ILE GLN
SEQRES 14 B 582 GLY SER THR TYR THR ASP LEU ARG ARG TYR ALA ALA ARG
SEQRES 15 B 582 ARG LEU SER SER MET ASN PHE GLU ILE HIS PRO ILE GLY
SEQRES 16 B 582 GLY VAL VAL PRO LEU LEU GLU SER TYR ARG PHE ARG ASP
SEQRES 17 B 582 VAL VAL ASP ILE VAL ILE SER SER LYS MET ALA LEU ARG
SEQRES 18 B 582 PRO ASP ARG PRO VAL HIS LEU PHE GLY ALA GLY HIS PRO
SEQRES 19 B 582 ILE VAL PHE ALA LEU ALA VAL ALA MET GLY VAL ASP LEU
SEQRES 20 B 582 PHE ASP SER ALA SER TYR ALA LEU TYR ALA LYS ASP ASP
SEQRES 21 B 582 ARG TYR MET THR PRO GLU GLY THR LYS ARG LEU ASP GLU
SEQRES 22 B 582 LEU ASP TYR PHE PRO CYS SER CYS PRO VAL CYS SER LYS
SEQRES 23 B 582 TYR THR PRO GLN GLU LEU ARG GLU MET PRO LYS GLU GLU
SEQRES 24 B 582 ARG THR ARG LEU LEU ALA LEU HIS ASN LEU TRP VAL ILE
SEQRES 25 B 582 LYS GLU GLU ILE LYS ARG VAL LYS GLN ALA ILE LYS GLU
SEQRES 26 B 582 GLY GLU LEU TRP ARG LEU VAL ASP GLU ARG ALA ARG SER
SEQRES 27 B 582 HIS PRO LYS LEU TYR SER ALA TYR LYS ARG LEU LEU GLU
SEQRES 28 B 582 HIS TYR THR PHE LEU GLU GLU PHE GLU PRO ILE THR LYS
SEQRES 29 B 582 LYS SER ALA LEU PHE LYS ILE SER ASN GLU SER LEU ARG
SEQRES 30 B 582 TRP PRO VAL VAL ARG ARG ALA LYS GLU ARG ALA LYS SER
SEQRES 31 B 582 ILE ASN GLU ARG PHE GLY GLU LEU VAL GLU HIS PRO ILE
SEQRES 32 B 582 PHE GLY ARG VAL SER ARG TYR LEU SER LEU THR TYR PRO
SEQRES 33 B 582 PHE ALA GLN SER GLU ALA GLU ASP ASP PHE LYS ILE GLU
SEQRES 34 B 582 LYS PRO THR LYS GLU ASP ALA ILE LYS TYR VAL MET ALA
SEQRES 35 B 582 ILE ALA GLU TYR GLN PHE GLY GLU GLY ALA SER ARG ALA
SEQRES 36 B 582 PHE ASP ASP ALA LYS VAL GLU LEU SER LYS THR GLY MET
SEQRES 37 B 582 PRO ARG GLN VAL LYS VAL ASN GLY LYS ARG LEU ALA THR
SEQRES 38 B 582 VAL ARG ALA ASP ASP GLY LEU LEU THR LEU GLY ILE GLU
SEQRES 39 B 582 GLY ALA LYS ARG LEU HIS ARG VAL LEU PRO TYR PRO ARG
SEQRES 40 B 582 MET ARG VAL VAL VAL ASN LYS GLU ALA GLU PRO PHE ALA
SEQRES 41 B 582 ARG LYS GLY LYS ASP VAL PHE ALA LYS PHE VAL ILE PHE
SEQRES 42 B 582 ALA ASP PRO GLY ILE ARG PRO TYR ASP GLU VAL LEU VAL
SEQRES 43 B 582 VAL ASN GLU ASN ASP GLU LEU LEU ALA THR GLY GLN ALA
SEQRES 44 B 582 LEU LEU SER GLY ARG GLU MET ILE VAL PHE GLN TYR GLY
SEQRES 45 B 582 ARG ALA VAL LYS VAL ARG LYS GLY VAL GLU
HET ZN A 600 1
HET MG A 601 1
HET PQ0 A 602 13
HET ZN B 600 1
HET MG B 601 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM PQ0 2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDINE-
HETNAM 2 PQ0 5-CARBONITRILE
HETSYN PQ0 7-DEAZA-7-CYANO-GUANINE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 PQ0 C7 H5 N5 O
FORMUL 8 HOH *142(H2 O)
HELIX 1 1 GLU A 48 GLY A 56 1 9
HELIX 2 2 SER A 64 LYS A 69 1 6
HELIX 3 3 ASP A 70 ASP A 87 1 18
HELIX 4 4 GLY A 97 GLY A 105 1 9
HELIX 5 5 SER A 110 ILE A 121 1 12
HELIX 6 6 PRO A 138 LYS A 160 1 23
HELIX 7 7 TYR A 173 MET A 187 1 15
HELIX 8 8 VAL A 197 SER A 203 1 7
HELIX 9 9 ARG A 205 LEU A 220 1 16
HELIX 10 10 HIS A 233 GLY A 244 1 12
HELIX 11 11 ALA A 251 ASP A 259 1 9
HELIX 12 12 ASP A 272 LEU A 274 5 3
HELIX 13 13 THR A 288 ARG A 293 1 6
HELIX 14 14 PRO A 296 GLU A 325 1 30
HELIX 15 15 GLU A 327 ARG A 337 1 11
HELIX 16 16 HIS A 339 LEU A 350 1 12
HELIX 17 17 HIS A 352 GLU A 360 1 9
HELIX 18 18 ASN A 373 ARG A 377 5 5
HELIX 19 19 TRP A 378 GLY A 396 1 19
HELIX 20 20 ASP A 435 GLY A 449 1 15
HELIX 21 21 GLY A 451 PHE A 456 5 6
HELIX 22 22 GLY A 492 LEU A 503 1 12
HELIX 23 23 ALA A 516 GLY A 523 1 8
HELIX 24 24 SER A 562 PHE A 569 1 8
HELIX 25 25 GLU B 48 GLY B 56 1 9
HELIX 26 26 SER B 64 LYS B 69 1 6
HELIX 27 27 ASP B 70 LEU B 86 1 17
HELIX 28 28 GLY B 97 GLY B 105 1 9
HELIX 29 29 SER B 110 ILE B 121 1 12
HELIX 30 30 PRO B 138 LYS B 160 1 23
HELIX 31 31 TYR B 173 SER B 186 1 14
HELIX 32 32 VAL B 197 SER B 203 1 7
HELIX 33 33 ARG B 205 LEU B 220 1 16
HELIX 34 34 VAL B 236 MET B 243 1 8
HELIX 35 35 ALA B 251 LYS B 258 1 8
HELIX 36 36 ASP B 272 LEU B 274 5 3
HELIX 37 37 THR B 288 MET B 295 1 8
HELIX 38 38 PRO B 296 GLU B 325 1 30
HELIX 39 39 GLU B 327 ALA B 336 1 10
HELIX 40 40 HIS B 339 HIS B 352 1 14
HELIX 41 41 HIS B 352 GLU B 358 1 7
HELIX 42 42 ASN B 373 ARG B 377 5 5
HELIX 43 43 TRP B 378 GLY B 396 1 19
HELIX 44 44 GLU B 434 PHE B 448 1 15
HELIX 45 45 GLY B 451 ASP B 457 5 7
HELIX 46 46 GLY B 492 LEU B 503 1 12
HELIX 47 47 ALA B 516 GLY B 523 1 8
HELIX 48 48 SER B 562 PHE B 569 1 8
SHEET 1 A 3 LEU A 8 ASP A 16 0
SHEET 2 A 3 GLY A 19 VAL A 26 -1 O ILE A 21 N ALA A 14
SHEET 3 A 3 LYS A 29 THR A 33 -1 O ILE A 31 N LEU A 24
SHEET 1 B 4 ALA A 35 PRO A 38 0
SHEET 2 B 4 LEU A 247 SER A 250 1 O PHE A 248 N MET A 37
SHEET 3 B 4 VAL A 226 LEU A 228 1 N LEU A 228 O LEU A 247
SHEET 4 B 4 HIS A 192 PRO A 193 1 N HIS A 192 O HIS A 227
SHEET 1 C 2 ILE A 59 ASN A 63 0
SHEET 2 C 2 ILE A 91 ASP A 95 1 O ASP A 95 N THR A 62
SHEET 1 D 2 GLY A 126 THR A 127 0
SHEET 2 D 2 MET A 164 ASN A 165 1 O ASN A 165 N GLY A 126
SHEET 1 E 2 ARG A 261 THR A 264 0
SHEET 2 E 2 GLY A 267 ARG A 270 -1 O LYS A 269 N TYR A 262
SHEET 1 F 2 LEU A 368 PHE A 369 0
SHEET 2 F 2 SER A 420 GLU A 421 1 O GLU A 421 N LEU A 368
SHEET 1 G 2 LEU A 398 HIS A 401 0
SHEET 2 G 2 GLY A 405 SER A 408 -1 O GLY A 405 N HIS A 401
SHEET 1 H 4 LYS A 460 LEU A 463 0
SHEET 2 H 4 PRO A 469 LYS A 473 -1 O LYS A 473 N LYS A 460
SHEET 3 H 4 ARG A 478 VAL A 482 -1 O LEU A 479 N VAL A 472
SHEET 4 H 4 LEU A 489 LEU A 491 -1 O THR A 490 N THR A 481
SHEET 1 I 6 VAL A 526 PHE A 527 0
SHEET 2 I 6 ARG A 573 GLY A 580 -1 O VAL A 575 N VAL A 526
SHEET 3 I 6 LEU A 553 ALA A 559 -1 N GLN A 558 O LYS A 576
SHEET 4 I 6 GLU A 543 VAL A 547 -1 N VAL A 544 O GLY A 557
SHEET 5 I 6 ARG A 509 VAL A 512 1 N VAL A 510 O VAL A 547
SHEET 6 I 6 VAL A 531 ALA A 534 -1 O PHE A 533 N VAL A 511
SHEET 1 J 3 LEU B 8 ASP B 16 0
SHEET 2 J 3 GLY B 19 VAL B 26 -1 O LYS B 23 N GLU B 11
SHEET 3 J 3 LYS B 29 THR B 33 -1 O LYS B 29 N VAL B 26
SHEET 1 K 4 ILE B 91 ASP B 95 0
SHEET 2 K 4 ILE B 59 ASN B 63 1 N THR B 62 O ASP B 95
SHEET 3 K 4 ALA B 35 VAL B 40 1 N VAL B 40 O ILE B 61
SHEET 4 K 4 LEU B 247 SER B 250 1 O PHE B 248 N MET B 37
SHEET 1 L 2 GLY B 126 THR B 127 0
SHEET 2 L 2 MET B 164 ASN B 165 1 O ASN B 165 N GLY B 126
SHEET 1 M 2 HIS B 192 PRO B 193 0
SHEET 2 M 2 VAL B 226 HIS B 227 1 O HIS B 227 N HIS B 192
SHEET 1 N 2 ARG B 261 THR B 264 0
SHEET 2 N 2 GLY B 267 ARG B 270 -1 O LYS B 269 N TYR B 262
SHEET 1 O 2 LEU B 368 PHE B 369 0
SHEET 2 O 2 SER B 420 GLU B 421 1 O GLU B 421 N LEU B 368
SHEET 1 P 2 LEU B 398 HIS B 401 0
SHEET 2 P 2 GLY B 405 SER B 408 -1 O GLY B 405 N HIS B 401
SHEET 1 Q 4 LYS B 460 LEU B 463 0
SHEET 2 Q 4 PRO B 469 VAL B 474 -1 O LYS B 473 N LYS B 460
SHEET 3 Q 4 LYS B 477 VAL B 482 -1 O LYS B 477 N VAL B 474
SHEET 4 Q 4 LEU B 489 LEU B 491 -1 O THR B 490 N THR B 481
SHEET 1 R 6 VAL B 526 PHE B 527 0
SHEET 2 R 6 ARG B 573 GLY B 580 -1 O ALA B 574 N VAL B 526
SHEET 3 R 6 LEU B 553 ALA B 559 -1 N GLN B 558 O LYS B 576
SHEET 4 R 6 GLU B 543 VAL B 547 -1 N VAL B 546 O LEU B 554
SHEET 5 R 6 ARG B 509 VAL B 512 1 N VAL B 510 O VAL B 547
SHEET 6 R 6 VAL B 531 ALA B 534 -1 O PHE B 533 N VAL B 511
LINK SG CYS A 279 ZN ZN A 600 1555 1555 2.43
LINK SG CYS A 281 ZN ZN A 600 1555 1555 2.36
LINK SG CYS A 284 ZN ZN A 600 1555 1555 2.35
LINK ND1 HIS A 307 ZN ZN A 600 1555 1555 2.08
LINK O ALA A 528 MG MG A 601 1555 1555 2.64
LINK O MET A 566 MG MG A 601 1555 1555 2.89
LINK O ILE A 567 MG MG A 601 1555 1555 2.46
LINK O PHE A 569 MG MG A 601 1555 1555 2.67
LINK NE2 GLN A 570 MG MG A 601 1555 1555 3.13
LINK SG CYS B 279 ZN ZN B 600 1555 1555 2.43
LINK SG CYS B 281 ZN ZN B 600 1555 1555 2.35
LINK SG CYS B 284 ZN ZN B 600 1555 1555 2.34
LINK ND1 HIS B 307 ZN ZN B 600 1555 1555 2.13
LINK O ALA B 528 MG MG B 601 1555 1555 2.46
LINK O VAL B 531 MG MG B 601 1555 1555 3.07
LINK O MET B 566 MG MG B 601 1555 1555 3.12
LINK O ILE B 567 MG MG B 601 1555 1555 2.27
LINK O PHE B 569 MG MG B 601 1555 1555 2.92
CISPEP 1 THR A 33 PRO A 34 0 -0.08
CISPEP 2 TYR A 415 PRO A 416 0 0.12
CISPEP 3 TYR A 505 PRO A 506 0 0.24
CISPEP 4 THR B 33 PRO B 34 0 0.35
CISPEP 5 TYR B 415 PRO B 416 0 -0.13
CISPEP 6 TYR B 505 PRO B 506 0 0.25
SITE 1 AC1 4 CYS A 279 CYS A 281 CYS A 284 HIS A 307
SITE 1 AC2 6 ALA A 528 VAL A 531 MET A 566 ILE A 567
SITE 2 AC2 6 PHE A 569 GLN A 570
SITE 1 AC3 4 CYS B 279 CYS B 281 CYS B 284 HIS B 307
SITE 1 AC4 6 ALA B 528 VAL B 531 MET B 566 ILE B 567
SITE 2 AC4 6 PHE B 569 GLN B 570
SITE 1 AC5 12 ASP A 95 SER A 98 PHE A 99 THR A 127
SITE 2 AC5 12 ASP A 130 PRO A 132 GLN A 169 GLY A 195
SITE 3 AC5 12 GLY A 196 VAL A 197 VAL A 198 PHE A 229
CRYST1 100.467 100.467 366.168 90.00 90.00 90.00 P 43 21 2 16
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 0.009954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002731 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
