HEADER LIGASE 03-JAN-05 1YFR
TITLE CRYSTAL STRUCTURE OF ALANYL-TRNA SYNTHETASE IN COMPLEX WITH ATP AND
TITLE 2 MAGNESIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALANINE-TRNA LIGASE, ALARS;
COMPND 5 EC: 6.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: ALAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS ALPHA-BETA FOLD, BENT ATP CONFORMATION, MAGNESIUM BRIDGE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SWAIRJO,P.R.SCHIMMEL
REVDAT 5 23-AUG-23 1YFR 1 REMARK LINK
REVDAT 4 26-FEB-20 1YFR 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1YFR 1 VERSN
REVDAT 2 08-FEB-05 1YFR 1 JRNL
REVDAT 1 25-JAN-05 1YFR 0
JRNL AUTH M.A.SWAIRJO,P.R.SCHIMMEL
JRNL TITL BREAKING SIEVE FOR STERIC EXCLUSION OF A NONCOGNATE AMINO
JRNL TITL 2 ACID FROM ACTIVE SITE OF A TRNA SYNTHETASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 988 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15657145
JRNL DOI 10.1073/PNAS.0409024102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.SWAIRJO,F.J.OTERO,X.-L.YANG,M.A.LOVATO,R.J.SKENE,
REMARK 1 AUTH 2 D.E.MCREE,L.RIBAS DE POUPLANA,P.SCHIMMEL
REMARK 1 TITL ALANYL-TRNA SYNTHETASE CRYSTAL STRUCTURE AND DESIGN FOR
REMARK 1 TITL 2 ACCEPTOR-STEM RECOGNITION.
REMARK 1 REF MOL.CELL V. 13 829 2004
REMARK 1 REFN ISSN 1097-2765
REMARK 1 PMID 15053876
REMARK 1 DOI 10.1016/S1097-2765(04)00126-1
REMARK 2
REMARK 2 RESOLUTION. 2.15 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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 50235
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) : 0.194
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4965
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 : 7282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.70
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.056
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1YFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97976
REMARK 200 MONOCHROMATOR : CURVED CRYSTAL
REMARK 200 OPTICS : CURVED CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RIQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MONOMETHYL ETHER, NACL, TRIS
REMARK 280 -CL, TRIS-BASE, ATP, MGCL2, PH 6.2, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 298K
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 86.80100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.98800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.96300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.98800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 86.80100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.96300
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 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 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 0
REMARK 465 PHE A 428
REMARK 465 LYS A 429
REMARK 465 VAL A 430
REMARK 465 GLU A 431
REMARK 465 ALA A 432
REMARK 465 LYS A 433
REMARK 465 LYS A 434
REMARK 465 VAL A 435
REMARK 465 LYS A 436
REMARK 465 GLU A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 HIS A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
REMARK 465 MET B 0
REMARK 465 PHE B 428
REMARK 465 LYS B 429
REMARK 465 VAL B 430
REMARK 465 GLU B 431
REMARK 465 ALA B 432
REMARK 465 LYS B 433
REMARK 465 LYS B 434
REMARK 465 VAL B 435
REMARK 465 LYS B 436
REMARK 465 GLU B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
REMARK 465 HIS B 461
REMARK 465 HIS B 462
REMARK 465 HIS B 463
REMARK 465 HIS B 464
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 OE1 GLU A 191 O3' ATP A 1500 1.69
REMARK 500 ND1 HIS A 87 N1 ATP A 1500 1.69
REMARK 500 CD GLU A 191 O3' ATP A 1500 1.84
REMARK 500 OE2 GLU B 191 O3G ATP B 2500 1.90
REMARK 500 CE1 HIS A 87 N1 ATP A 1500 1.97
REMARK 500 CE1 HIS A 87 C2 ATP A 1500 2.11
REMARK 500 NH1 ARG A 224 O3G ATP A 1500 2.12
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 LEU A 2 128.17 57.63
REMARK 500 GLU A 31 -73.12 -65.89
REMARK 500 ASN A 32 73.07 -112.41
REMARK 500 ASP A 33 92.19 -168.19
REMARK 500 VAL A 70 13.96 -141.66
REMARK 500 HIS A 74 67.70 -111.40
REMARK 500 LEU A 77 -35.50 -37.70
REMARK 500 ASP A 100 -120.95 -97.71
REMARK 500 PHE A 102 -133.20 -130.09
REMARK 500 VAL A 117 -32.53 -131.11
REMARK 500 ASP A 133 71.85 -114.25
REMARK 500 HIS A 143 -74.41 -63.10
REMARK 500 LEU A 154 -169.05 -100.29
REMARK 500 MET A 163 50.63 -100.24
REMARK 500 TYR A 189 64.07 -110.78
REMARK 500 PRO A 214 170.58 -58.83
REMARK 500 ASP A 239 -19.08 -49.34
REMARK 500 GLU A 258 -69.83 -157.80
REMARK 500 GLU A 261 8.40 -69.46
REMARK 500 PRO A 286 108.76 -54.84
REMARK 500 SER A 287 -150.34 -122.23
REMARK 500 PHE A 315 -34.46 -131.33
REMARK 500 ASP A 388 -74.23 -92.75
REMARK 500 THR A 389 -16.16 -49.23
REMARK 500 ASP A 409 102.73 -51.66
REMARK 500 ARG A 425 30.71 -92.73
REMARK 500 LYS A 426 -41.22 -152.75
REMARK 500 HIS A 441 -177.76 -68.72
REMARK 500 LYS A 443 -14.70 73.61
REMARK 500 LEU B 2 149.60 67.08
REMARK 500 LEU B 12 -9.65 -54.25
REMARK 500 SER B 25 107.01 -55.17
REMARK 500 GLU B 31 -79.52 -49.80
REMARK 500 ASP B 33 82.93 -162.23
REMARK 500 PRO B 34 2.07 -69.50
REMARK 500 LEU B 37 -77.16 -39.62
REMARK 500 PRO B 45 4.51 -66.94
REMARK 500 LEU B 53 -73.28 -55.73
REMARK 500 PRO B 57 -70.22 -60.35
REMARK 500 THR B 62 142.67 177.94
REMARK 500 LEU B 77 -75.06 -47.65
REMARK 500 ARG B 85 -28.40 -142.31
REMARK 500 ASP B 100 -84.99 -116.65
REMARK 500 PHE B 102 -150.29 -128.56
REMARK 500 SER B 128 114.43 -164.75
REMARK 500 ASP B 132 32.03 -80.66
REMARK 500 GLU B 142 -46.89 -131.99
REMARK 500 HIS B 143 -82.08 -55.84
REMARK 500 SER B 148 22.43 -79.60
REMARK 500 ARG B 153 90.50 -68.46
REMARK 500
REMARK 500 THIS ENTRY HAS 68 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 MG A1502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 174 OE2
REMARK 620 2 ASN A 194 OD1 57.8
REMARK 620 3 ATP A1500 O1A 98.9 80.5
REMARK 620 4 ATP A1500 O1B 133.3 160.4 81.5
REMARK 620 5 HOH A1510 O 114.8 69.4 107.7 109.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A1500 O2B
REMARK 620 2 ATP A1500 O2G 71.0
REMARK 620 3 ATP A1500 O1G 96.1 58.6
REMARK 620 4 HOH A1505 O 81.9 59.4 114.6
REMARK 620 5 HOH A1506 O 126.8 131.7 137.0 77.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1509 O
REMARK 620 2 HOH A1531 O 76.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 174 OE2
REMARK 620 2 GLU B 191 OE1 54.8
REMARK 620 3 ASN B 194 OD1 64.3 93.9
REMARK 620 4 ATP B2500 O1B 123.4 88.8 171.5
REMARK 620 5 ATP B2500 O1A 118.7 71.8 94.8 78.4
REMARK 620 6 MG B2504 MG 60.4 74.9 118.7 69.8 133.8
REMARK 620 7 HOH B2506 O 117.5 171.6 84.6 93.8 116.6 98.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B2500 O2B
REMARK 620 2 ATP B2500 O2G 74.8
REMARK 620 3 ATP B2500 O1G 93.9 55.1
REMARK 620 4 HOH B2505 O 143.0 124.5 123.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 2500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RIQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC FRAGMENT OF AQUIFEX AEOLICUS
REMARK 900 ALANYL TRNA SYNTHETASE.
REMARK 900 RELATED ID: 1YFS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AEOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH L-ALANINE
REMARK 900 RELATED ID: 1YFT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC FRAGMENT OF A. AEOLICUS ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH GLYCINE
REMARK 900 RELATED ID: 1YGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC FRAGMENT OF ALANYL-TRNA
REMARK 900 SYNTHETASE IN COMPLEX WITH L-SERINE
DBREF 1YFR A 0 453 UNP O67323 SYA_AQUAE 1 454
DBREF 1YFR B 0 453 UNP O67323 SYA_AQUAE 1 454
SEQADV 1YFR ALA A 454 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR ALA A 455 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR ALA A 456 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR LEU A 457 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR GLU A 458 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR HIS A 459 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS A 460 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS A 461 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS A 462 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS A 463 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS A 464 UNP O67323 EXPRESSION TAG
SEQADV 1YFR ALA B 454 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR ALA B 455 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR ALA B 456 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR LEU B 457 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR GLU B 458 UNP O67323 CLONING ARTIFACT
SEQADV 1YFR HIS B 459 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS B 460 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS B 461 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS B 462 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS B 463 UNP O67323 EXPRESSION TAG
SEQADV 1YFR HIS B 464 UNP O67323 EXPRESSION TAG
SEQRES 1 A 465 MET SER LEU SER ALA HIS GLU ILE ARG GLU LEU PHE LEU
SEQRES 2 A 465 SER PHE PHE GLU LYS LYS GLY HIS THR ARG VAL LYS SER
SEQRES 3 A 465 ALA PRO LEU VAL PRO GLU ASN ASP PRO THR LEU LEU PHE
SEQRES 4 A 465 VAL ASN ALA GLY MET VAL PRO PHE LYS ASN VAL PHE LEU
SEQRES 5 A 465 GLY LEU GLU LYS ARG PRO TYR LYS ARG ALA THR SER CYS
SEQRES 6 A 465 GLN LYS CYS LEU ARG VAL SER GLY LYS HIS ASN ASP LEU
SEQRES 7 A 465 GLU GLN VAL GLY TYR THR SER ARG HIS HIS THR PHE PHE
SEQRES 8 A 465 GLU MET LEU GLY ASN PHE SER PHE GLY ASP TYR PHE LYS
SEQRES 9 A 465 LYS GLU ALA ILE GLU TYR ALA TRP GLU PHE VAL THR GLU
SEQRES 10 A 465 VAL LEU LYS LEU PRO LYS GLU LYS LEU TYR VAL SER VAL
SEQRES 11 A 465 TYR LYS ASP ASP GLU GLU ALA TYR ARG ILE TRP ASN GLU
SEQRES 12 A 465 HIS ILE GLY ILE PRO SER GLU ARG ILE TRP ARG LEU GLY
SEQRES 13 A 465 GLU GLU ASP ASN PHE TRP GLN MET GLY ASP VAL GLY PRO
SEQRES 14 A 465 CYS GLY PRO SER SER GLU ILE TYR VAL ASP ARG GLY GLU
SEQRES 15 A 465 GLU TYR GLU GLY ASP GLU ARG TYR LEU GLU ILE TRP ASN
SEQRES 16 A 465 LEU VAL PHE MET GLN TYR ASN ARG ASP GLU ASN GLY VAL
SEQRES 17 A 465 LEU THR PRO LEU PRO HIS PRO ASN ILE ASP THR GLY MET
SEQRES 18 A 465 GLY LEU GLU ARG ILE ALA SER VAL LEU GLN GLY LYS ASN
SEQRES 19 A 465 SER ASN PHE GLU ILE ASP ILE ILE PHE PRO LEU ILE GLN
SEQRES 20 A 465 PHE GLY GLU GLU VAL SER GLY LYS LYS TYR GLY GLU LYS
SEQRES 21 A 465 PHE GLU THR ASP VAL ALA LEU ARG VAL ILE ALA ASP HIS
SEQRES 22 A 465 LEU ARG ALA ILE THR PHE ALA ILE SER ASP GLY VAL ILE
SEQRES 23 A 465 PRO SER ASN GLU GLY ARG GLY TYR VAL ILE ARG ARG ILE
SEQRES 24 A 465 LEU ARG ARG ALA MET ARG PHE GLY TYR LYS LEU GLY ILE
SEQRES 25 A 465 GLU ASN PRO PHE LEU TYR LYS GLY VAL ASP LEU VAL VAL
SEQRES 26 A 465 ASP ILE MET LYS GLU PRO TYR PRO GLU LEU GLU LEU SER
SEQRES 27 A 465 ARG GLU PHE VAL LYS GLY ILE VAL LYS GLY GLU GLU LYS
SEQRES 28 A 465 ARG PHE ILE LYS THR LEU LYS ALA GLY MET GLU TYR ILE
SEQRES 29 A 465 GLN GLU VAL ILE GLN LYS ALA LEU GLU GLU GLY ARG LYS
SEQRES 30 A 465 THR LEU SER GLY LYS GLU VAL PHE THR ALA TYR ASP THR
SEQRES 31 A 465 TYR GLY PHE PRO VAL ASP LEU ILE ASP GLU ILE ALA ARG
SEQRES 32 A 465 GLU LYS GLY LEU GLY ILE ASP LEU GLU GLY PHE GLN CYS
SEQRES 33 A 465 GLU LEU GLU GLU GLN ARG GLU ARG ALA ARG LYS HIS PHE
SEQRES 34 A 465 LYS VAL GLU ALA LYS LYS VAL LYS PRO VAL TYR SER HIS
SEQRES 35 A 465 LEU LYS GLU LEU GLY LYS THR SER ALA PHE VAL GLY ALA
SEQRES 36 A 465 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 465 MET SER LEU SER ALA HIS GLU ILE ARG GLU LEU PHE LEU
SEQRES 2 B 465 SER PHE PHE GLU LYS LYS GLY HIS THR ARG VAL LYS SER
SEQRES 3 B 465 ALA PRO LEU VAL PRO GLU ASN ASP PRO THR LEU LEU PHE
SEQRES 4 B 465 VAL ASN ALA GLY MET VAL PRO PHE LYS ASN VAL PHE LEU
SEQRES 5 B 465 GLY LEU GLU LYS ARG PRO TYR LYS ARG ALA THR SER CYS
SEQRES 6 B 465 GLN LYS CYS LEU ARG VAL SER GLY LYS HIS ASN ASP LEU
SEQRES 7 B 465 GLU GLN VAL GLY TYR THR SER ARG HIS HIS THR PHE PHE
SEQRES 8 B 465 GLU MET LEU GLY ASN PHE SER PHE GLY ASP TYR PHE LYS
SEQRES 9 B 465 LYS GLU ALA ILE GLU TYR ALA TRP GLU PHE VAL THR GLU
SEQRES 10 B 465 VAL LEU LYS LEU PRO LYS GLU LYS LEU TYR VAL SER VAL
SEQRES 11 B 465 TYR LYS ASP ASP GLU GLU ALA TYR ARG ILE TRP ASN GLU
SEQRES 12 B 465 HIS ILE GLY ILE PRO SER GLU ARG ILE TRP ARG LEU GLY
SEQRES 13 B 465 GLU GLU ASP ASN PHE TRP GLN MET GLY ASP VAL GLY PRO
SEQRES 14 B 465 CYS GLY PRO SER SER GLU ILE TYR VAL ASP ARG GLY GLU
SEQRES 15 B 465 GLU TYR GLU GLY ASP GLU ARG TYR LEU GLU ILE TRP ASN
SEQRES 16 B 465 LEU VAL PHE MET GLN TYR ASN ARG ASP GLU ASN GLY VAL
SEQRES 17 B 465 LEU THR PRO LEU PRO HIS PRO ASN ILE ASP THR GLY MET
SEQRES 18 B 465 GLY LEU GLU ARG ILE ALA SER VAL LEU GLN GLY LYS ASN
SEQRES 19 B 465 SER ASN PHE GLU ILE ASP ILE ILE PHE PRO LEU ILE GLN
SEQRES 20 B 465 PHE GLY GLU GLU VAL SER GLY LYS LYS TYR GLY GLU LYS
SEQRES 21 B 465 PHE GLU THR ASP VAL ALA LEU ARG VAL ILE ALA ASP HIS
SEQRES 22 B 465 LEU ARG ALA ILE THR PHE ALA ILE SER ASP GLY VAL ILE
SEQRES 23 B 465 PRO SER ASN GLU GLY ARG GLY TYR VAL ILE ARG ARG ILE
SEQRES 24 B 465 LEU ARG ARG ALA MET ARG PHE GLY TYR LYS LEU GLY ILE
SEQRES 25 B 465 GLU ASN PRO PHE LEU TYR LYS GLY VAL ASP LEU VAL VAL
SEQRES 26 B 465 ASP ILE MET LYS GLU PRO TYR PRO GLU LEU GLU LEU SER
SEQRES 27 B 465 ARG GLU PHE VAL LYS GLY ILE VAL LYS GLY GLU GLU LYS
SEQRES 28 B 465 ARG PHE ILE LYS THR LEU LYS ALA GLY MET GLU TYR ILE
SEQRES 29 B 465 GLN GLU VAL ILE GLN LYS ALA LEU GLU GLU GLY ARG LYS
SEQRES 30 B 465 THR LEU SER GLY LYS GLU VAL PHE THR ALA TYR ASP THR
SEQRES 31 B 465 TYR GLY PHE PRO VAL ASP LEU ILE ASP GLU ILE ALA ARG
SEQRES 32 B 465 GLU LYS GLY LEU GLY ILE ASP LEU GLU GLY PHE GLN CYS
SEQRES 33 B 465 GLU LEU GLU GLU GLN ARG GLU ARG ALA ARG LYS HIS PHE
SEQRES 34 B 465 LYS VAL GLU ALA LYS LYS VAL LYS PRO VAL TYR SER HIS
SEQRES 35 B 465 LEU LYS GLU LEU GLY LYS THR SER ALA PHE VAL GLY ALA
SEQRES 36 B 465 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET MG A1502 1
HET MG A1503 1
HET MG A1504 1
HET ATP A1500 31
HET MG B2502 1
HET MG B2503 1
HET MG B2504 1
HET ATP B2500 31
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 MG 6(MG 2+)
FORMUL 6 ATP 2(C10 H16 N5 O13 P3)
FORMUL 11 HOH *190(H2 O)
HELIX 1 1 SER A 3 LYS A 18 1 16
HELIX 2 2 PHE A 46 LEU A 51 1 6
HELIX 3 3 PHE A 102 VAL A 117 1 16
HELIX 4 4 ASP A 133 GLU A 142 1 10
HELIX 5 5 PRO A 147 GLU A 149 5 3
HELIX 6 6 GLY A 155 ASN A 159 1 5
HELIX 7 7 LEU A 222 GLN A 230 1 9
HELIX 8 8 SER A 234 ILE A 238 5 5
HELIX 9 9 ILE A 241 GLY A 253 1 13
HELIX 10 10 LYS A 259 ASP A 282 1 24
HELIX 11 11 GLY A 290 GLY A 310 1 21
HELIX 12 12 PHE A 315 LYS A 328 1 14
HELIX 13 13 PRO A 332 GLU A 373 1 42
HELIX 14 14 SER A 379 ASP A 388 1 10
HELIX 15 15 PRO A 393 GLU A 403 1 11
HELIX 16 16 ASP A 409 GLU A 422 1 14
HELIX 17 17 GLU A 444 THR A 448 5 5
HELIX 18 18 SER B 3 SER B 13 1 11
HELIX 19 19 MET B 43 PRO B 45 5 3
HELIX 20 20 PHE B 46 GLY B 52 1 7
HELIX 21 21 SER B 71 ASN B 75 5 5
HELIX 22 22 ASP B 76 VAL B 80 5 5
HELIX 23 23 PHE B 102 GLU B 116 1 15
HELIX 24 24 PRO B 121 GLU B 123 5 3
HELIX 25 25 ASP B 133 GLU B 142 1 10
HELIX 26 26 GLY B 155 ASN B 159 1 5
HELIX 27 27 GLU B 184 GLU B 187 5 4
HELIX 28 28 LEU B 222 GLN B 230 1 9
HELIX 29 29 ILE B 241 GLU B 250 1 10
HELIX 30 30 PHE B 260 SER B 281 1 22
HELIX 31 31 ARG B 291 LEU B 309 1 19
HELIX 32 32 PHE B 315 MET B 327 1 13
HELIX 33 33 TYR B 331 GLU B 335 5 5
HELIX 34 34 SER B 337 LEU B 371 1 35
HELIX 35 35 SER B 379 THR B 389 1 11
HELIX 36 36 PRO B 393 ARG B 402 1 10
HELIX 37 37 PHE B 413 GLU B 419 1 7
HELIX 38 38 GLN B 420 GLU B 422 5 3
HELIX 39 39 GLU B 444 SER B 449 1 6
HELIX 40 40 ALA B 450 VAL B 452 5 3
SHEET 1 A 7 THR A 21 VAL A 23 0
SHEET 2 A 7 ARG A 60 LEU A 68 1 O THR A 62 N VAL A 23
SHEET 3 A 7 PHE A 89 PHE A 98 -1 O PHE A 90 N CYS A 67
SHEET 4 A 7 LEU A 208 THR A 218 -1 O ILE A 216 N SER A 97
SHEET 5 A 7 TYR A 189 ARG A 202 -1 N VAL A 196 O ASP A 217
SHEET 6 A 7 GLY A 167 ASP A 178 -1 N CYS A 169 O TYR A 200
SHEET 7 A 7 PHE A 160 GLN A 162 -1 N TRP A 161 O GLY A 170
SHEET 1 B 7 ILE A 151 LEU A 154 0
SHEET 2 B 7 LEU A 125 TYR A 130 1 N VAL A 127 O TRP A 152
SHEET 3 B 7 GLY A 167 ASP A 178 -1 O TYR A 176 N TYR A 126
SHEET 4 B 7 TYR A 189 ARG A 202 -1 O TYR A 200 N CYS A 169
SHEET 5 B 7 LEU A 208 THR A 218 -1 O ASP A 217 N VAL A 196
SHEET 6 B 7 PHE A 89 PHE A 98 -1 N SER A 97 O ILE A 216
SHEET 7 B 7 MET A 220 GLY A 221 -1 O MET A 220 N LEU A 93
SHEET 1 C 2 VAL A 70 SER A 71 0
SHEET 2 C 2 HIS A 74 ASN A 75 -1 O HIS A 74 N SER A 71
SHEET 1 D 2 THR A 377 LEU A 378 0
SHEET 2 D 2 GLY A 407 ILE A 408 1 O GLY A 407 N LEU A 378
SHEET 1 E 6 ARG B 60 LEU B 68 0
SHEET 2 E 6 PHE B 89 SER B 97 -1 O PHE B 90 N CYS B 67
SHEET 3 E 6 LEU B 208 GLY B 221 -1 O MET B 220 N LEU B 93
SHEET 4 E 6 TYR B 189 ARG B 202 -1 N VAL B 196 O ASP B 217
SHEET 5 E 6 GLY B 167 ASP B 178 -1 N SER B 173 O LEU B 195
SHEET 6 E 6 LEU B 125 TYR B 126 -1 N TYR B 126 O TYR B 176
SHEET 1 F 6 ARG B 60 LEU B 68 0
SHEET 2 F 6 PHE B 89 SER B 97 -1 O PHE B 90 N CYS B 67
SHEET 3 F 6 LEU B 208 GLY B 221 -1 O MET B 220 N LEU B 93
SHEET 4 F 6 TYR B 189 ARG B 202 -1 N VAL B 196 O ASP B 217
SHEET 5 F 6 GLY B 167 ASP B 178 -1 N SER B 173 O LEU B 195
SHEET 6 F 6 PHE B 160 TRP B 161 -1 N TRP B 161 O GLY B 170
SHEET 1 G 2 THR B 377 LEU B 378 0
SHEET 2 G 2 GLY B 407 ILE B 408 1 O GLY B 407 N LEU B 378
LINK OE2 GLU A 174 MG MG A1502 1555 1555 2.58
LINK OD1 ASN A 194 MG MG A1502 1555 1555 2.84
LINK O1A ATP A1500 MG MG A1502 1555 1555 2.44
LINK O1B ATP A1500 MG MG A1502 1555 1555 2.30
LINK O2B ATP A1500 MG MG A1503 1555 1555 2.29
LINK O2G ATP A1500 MG MG A1503 1555 1555 2.73
LINK O1G ATP A1500 MG MG A1503 1555 1555 2.45
LINK MG MG A1502 O HOH A1510 1555 1555 3.04
LINK MG MG A1503 O HOH A1505 1555 1555 2.92
LINK MG MG A1503 O HOH A1506 1555 1555 2.71
LINK MG MG A1504 O HOH A1509 1555 1555 2.46
LINK MG MG A1504 O HOH A1531 1555 1555 2.70
LINK OE2 GLU B 174 MG MG B2502 1555 1555 2.70
LINK OE2 GLU B 174 MG MG B2504 1555 1555 2.90
LINK OE1 GLU B 191 MG MG B2502 1555 1555 3.03
LINK OD1 ASN B 194 MG MG B2502 1555 1555 2.99
LINK O1B ATP B2500 MG MG B2502 1555 1555 2.50
LINK O1A ATP B2500 MG MG B2502 1555 1555 2.39
LINK O2B ATP B2500 MG MG B2503 1555 1555 2.01
LINK O2G ATP B2500 MG MG B2503 1555 1555 2.73
LINK O1G ATP B2500 MG MG B2503 1555 1555 2.77
LINK MG MG B2502 MG MG B2504 1555 1555 3.04
LINK MG MG B2502 O HOH B2506 1555 1555 2.88
LINK MG MG B2503 O HOH B2505 1555 1555 3.00
SITE 1 AC1 6 GLU A 174 GLU A 191 ASN A 194 ATP A1500
SITE 2 AC1 6 MG A1504 HOH A1510
SITE 1 AC2 3 ATP A1500 HOH A1505 HOH A1506
SITE 1 AC3 5 GLU A 174 ATP A1500 MG A1502 HOH A1509
SITE 2 AC3 5 HOH A1531
SITE 1 AC4 6 GLU B 174 GLU B 191 ASN B 194 ATP B2500
SITE 2 AC4 6 MG B2504 HOH B2506
SITE 1 AC5 3 ARG B 69 ATP B2500 HOH B2505
SITE 1 AC6 5 GLU B 174 GLU B 191 LYS B 354 ATP B2500
SITE 2 AC6 5 MG B2502
SITE 1 AC7 17 ARG A 85 HIS A 86 HIS A 87 GLU A 191
SITE 2 AC7 17 ASN A 194 GLY A 219 GLY A 221 ARG A 224
SITE 3 AC7 17 ASN A 235 MG A1502 MG A1503 MG A1504
SITE 4 AC7 17 HOH A1505 HOH A1507 HOH A1531 HOH A1569
SITE 5 AC7 17 HOH A1590
SITE 1 AC8 16 ARG B 69 ARG B 85 HIS B 86 HIS B 87
SITE 2 AC8 16 MET B 92 GLU B 191 ILE B 192 ASN B 194
SITE 3 AC8 16 GLY B 219 GLY B 221 ARG B 224 MG B2502
SITE 4 AC8 16 MG B2503 MG B2504 HOH B2572 HOH B2600
CRYST1 173.602 73.926 73.976 90.00 90.00 90.00 P 21 21 21 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 0.005760 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013518 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
