HEADER LYASE 15-OCT-15 5E9G
TITLE STRUCTURAL INSIGHTS OF ISOCITRATE LYASES FROM MAGNAPORTHE ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ICL,ISOCITRASE,ISOCITRATASE,METHYLISOCITRATE LYASE,MICA,
COMPND 5 THREO-D(S)-ISOCITRATE GLYOXYLATE-LYASE;
COMPND 6 EC: 4.1.3.1,4.1.3.30;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MAGNAPORTHE ORYZAE 70-15;
SOURCE 3 ORGANISM_COMMON: RICE BLAST FUNGUS;
SOURCE 4 ORGANISM_TAXID: 242507;
SOURCE 5 STRAIN: 70-15;
SOURCE 6 GENE: ICL1, MGG_04895;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TIM BETA/ALPHA-BARREL, LYASE ACTIVITY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PARK,Y.CHO,Y.-H.LEE,Y.-W.LEE,S.RHEE
REVDAT 3 08-NOV-23 5E9G 1 JRNL REMARK HETSYN LINK
REVDAT 2 18-MAY-16 5E9G 1 JRNL
REVDAT 1 27-APR-16 5E9G 0
JRNL AUTH Y.PARK,Y.CHO,Y.-H.LEE,Y.-W.LEE,S.RHEE
JRNL TITL CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ISOCITRATE
JRNL TITL 2 LYASES FROM MAGNAPORTHE ORYZAE AND FUSARIUM GRAMINEARUM
JRNL REF J.STRUCT.BIOL. V. 194 395 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 27016285
JRNL DOI 10.1016/J.JSB.2016.03.019
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
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) (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 137814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13732
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 : 16063
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.56200
REMARK 3 B22 (A**2) : -1.40700
REMARK 3 B33 (A**2) : 13.96800
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) : 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 1.183 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.757 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.566 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 38.49
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : GLV.PAR
REMARK 3 PARAMETER FILE 7 : GOL.PAR
REMARK 3 PARAMETER FILE 8 : 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 TOPOLOGY FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 8 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E9G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 142312
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 93.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
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: NULL
REMARK 200 STARTING MODEL: 1DQU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE, 20%
REMARK 280 PEG-3350, 10% (V/V) GLYCEROL, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295.0K, VAPOR DIFFUSION, SITTING DROP
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 60.56100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.35200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.53900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.35200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.56100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.53900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ALA A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 GLY A 529
REMARK 465 GLY A 530
REMARK 465 VAL A 531
REMARK 465 SER A 532
REMARK 465 SER A 533
REMARK 465 THR A 534
REMARK 465 ALA A 535
REMARK 465 ALA A 536
REMARK 465 MET A 537
REMARK 465 GLY A 538
REMARK 465 LYS A 539
REMARK 465 GLY A 540
REMARK 465 VAL A 541
REMARK 465 THR A 542
REMARK 465 GLU A 543
REMARK 465 ASP A 544
REMARK 465 GLN A 545
REMARK 465 PHE A 546
REMARK 465 HIS A 547
REMARK 465 ALA A 548
REMARK 465 ALA A 549
REMARK 465 ALA A 550
REMARK 465 LEU A 551
REMARK 465 GLU A 552
REMARK 465 HIS A 553
REMARK 465 HIS A 554
REMARK 465 HIS A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 GLY B 530
REMARK 465 VAL B 531
REMARK 465 SER B 532
REMARK 465 SER B 533
REMARK 465 THR B 534
REMARK 465 ALA B 535
REMARK 465 ALA B 536
REMARK 465 MET B 537
REMARK 465 GLY B 538
REMARK 465 LYS B 539
REMARK 465 GLY B 540
REMARK 465 VAL B 541
REMARK 465 THR B 542
REMARK 465 GLU B 543
REMARK 465 ASP B 544
REMARK 465 GLN B 545
REMARK 465 PHE B 546
REMARK 465 HIS B 547
REMARK 465 ALA B 548
REMARK 465 ALA B 549
REMARK 465 ALA B 550
REMARK 465 LEU B 551
REMARK 465 GLU B 552
REMARK 465 HIS B 553
REMARK 465 HIS B 554
REMARK 465 HIS B 555
REMARK 465 HIS B 556
REMARK 465 HIS B 557
REMARK 465 HIS B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 LYS C 4
REMARK 465 GLU C 292
REMARK 465 GLN C 293
REMARK 465 SER C 294
REMARK 465 GLY C 295
REMARK 465 LYS C 296
REMARK 465 THR C 297
REMARK 465 GLY C 298
REMARK 465 ASP C 299
REMARK 465 GLN C 300
REMARK 465 LEU C 301
REMARK 465 GLN C 302
REMARK 465 ALA C 303
REMARK 465 SER C 327
REMARK 465 SER C 328
REMARK 465 SER C 329
REMARK 465 SER C 330
REMARK 465 ILE C 331
REMARK 465 ARG C 332
REMARK 465 ASN C 333
REMARK 465 PRO C 334
REMARK 465 LYS C 335
REMARK 465 ASP C 336
REMARK 465 VAL C 337
REMARK 465 ALA C 338
REMARK 465 THR C 528
REMARK 465 GLY C 529
REMARK 465 GLY C 530
REMARK 465 VAL C 531
REMARK 465 SER C 532
REMARK 465 SER C 533
REMARK 465 THR C 534
REMARK 465 ALA C 535
REMARK 465 ALA C 536
REMARK 465 MET C 537
REMARK 465 GLY C 538
REMARK 465 LYS C 539
REMARK 465 GLY C 540
REMARK 465 VAL C 541
REMARK 465 THR C 542
REMARK 465 GLU C 543
REMARK 465 ASP C 544
REMARK 465 GLN C 545
REMARK 465 PHE C 546
REMARK 465 HIS C 547
REMARK 465 ALA C 548
REMARK 465 ALA C 549
REMARK 465 ALA C 550
REMARK 465 LEU C 551
REMARK 465 GLU C 552
REMARK 465 HIS C 553
REMARK 465 HIS C 554
REMARK 465 HIS C 555
REMARK 465 HIS C 556
REMARK 465 HIS C 557
REMARK 465 HIS C 558
REMARK 465 HIS C 559
REMARK 465 HIS C 560
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 LYS D 4
REMARK 465 THR D 290
REMARK 465 ALA D 291
REMARK 465 GLU D 292
REMARK 465 GLN D 293
REMARK 465 SER D 294
REMARK 465 GLY D 295
REMARK 465 LYS D 296
REMARK 465 THR D 297
REMARK 465 GLY D 298
REMARK 465 ASP D 299
REMARK 465 GLN D 300
REMARK 465 LEU D 301
REMARK 465 GLN D 302
REMARK 465 ALA D 303
REMARK 465 ILE D 304
REMARK 465 GLU D 305
REMARK 465 ASP D 306
REMARK 465 VAL D 324
REMARK 465 ILE D 325
REMARK 465 ASN D 326
REMARK 465 SER D 327
REMARK 465 SER D 328
REMARK 465 SER D 329
REMARK 465 SER D 330
REMARK 465 ILE D 331
REMARK 465 ARG D 332
REMARK 465 ASN D 333
REMARK 465 PRO D 334
REMARK 465 LYS D 335
REMARK 465 ASP D 336
REMARK 465 VAL D 337
REMARK 465 ALA D 338
REMARK 465 LEU D 360
REMARK 465 GLY D 361
REMARK 465 VAL D 362
REMARK 465 PRO D 363
REMARK 465 GLU D 364
REMARK 465 ILE D 365
REMARK 465 THR D 442
REMARK 465 GLY D 530
REMARK 465 VAL D 531
REMARK 465 SER D 532
REMARK 465 SER D 533
REMARK 465 THR D 534
REMARK 465 ALA D 535
REMARK 465 ALA D 536
REMARK 465 MET D 537
REMARK 465 GLY D 538
REMARK 465 LYS D 539
REMARK 465 GLY D 540
REMARK 465 VAL D 541
REMARK 465 THR D 542
REMARK 465 GLU D 543
REMARK 465 ASP D 544
REMARK 465 GLN D 545
REMARK 465 PHE D 546
REMARK 465 HIS D 547
REMARK 465 ALA D 548
REMARK 465 ALA D 549
REMARK 465 ALA D 550
REMARK 465 LEU D 551
REMARK 465 GLU D 552
REMARK 465 HIS D 553
REMARK 465 HIS D 554
REMARK 465 HIS D 555
REMARK 465 HIS D 556
REMARK 465 HIS D 557
REMARK 465 HIS D 558
REMARK 465 HIS D 559
REMARK 465 HIS D 560
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 PRO A 42 38.81 -81.83
REMARK 500 THR A 113 -3.55 -141.51
REMARK 500 ALA A 114 18.98 -144.79
REMARK 500 ASP A 123 85.04 -60.45
REMARK 500 ASP A 179 -122.99 53.88
REMARK 500 ASP A 207 35.52 -79.97
REMARK 500 GLN A 293 29.40 -71.71
REMARK 500 SER A 294 57.67 -169.13
REMARK 500 LYS A 296 -34.63 72.29
REMARK 500 THR A 297 115.63 -28.73
REMARK 500 VAL A 497 -72.71 -121.26
REMARK 500 LYS A 510 68.01 -102.73
REMARK 500 PRO B 42 31.79 -81.29
REMARK 500 THR B 84 -159.96 -153.39
REMARK 500 THR B 113 -2.10 -140.07
REMARK 500 ALA B 114 23.08 -146.96
REMARK 500 ASP B 118 -0.03 67.61
REMARK 500 TYR B 129 0.64 -59.77
REMARK 500 ASP B 179 -118.88 53.17
REMARK 500 ASP B 207 35.52 -76.03
REMARK 500 LEU B 247 127.94 -37.56
REMARK 500 ASN B 333 72.89 54.99
REMARK 500 VAL B 497 -72.46 -117.69
REMARK 500 PRO C 42 34.23 -76.43
REMARK 500 THR C 84 -156.82 -147.81
REMARK 500 ALA C 114 19.96 -146.40
REMARK 500 ASP C 123 88.19 -65.30
REMARK 500 TYR C 129 0.43 -68.69
REMARK 500 SER C 160 -9.47 -57.62
REMARK 500 ASN C 167 55.69 -147.70
REMARK 500 ASP C 179 -122.94 48.58
REMARK 500 ASP C 207 31.46 -84.27
REMARK 500 HIS C 217 31.66 -83.01
REMARK 500 LEU C 247 126.93 -37.17
REMARK 500 THR C 290 48.41 -79.72
REMARK 500 LYS C 407 -60.10 -98.12
REMARK 500 VAL C 497 -72.65 -123.30
REMARK 500 MET D 6 -5.86 73.12
REMARK 500 PRO D 42 38.48 -84.65
REMARK 500 SER D 50 3.86 -68.76
REMARK 500 ALA D 114 35.67 -155.26
REMARK 500 ASP D 123 85.86 -67.37
REMARK 500 TYR D 129 -6.53 -54.81
REMARK 500 ASN D 167 47.96 -146.49
REMARK 500 ASP D 179 -125.45 47.96
REMARK 500 ASP D 207 32.00 -82.98
REMARK 500 HIS D 217 41.30 -101.17
REMARK 500 LEU D 247 126.54 -33.28
REMARK 500 MET D 309 -70.66 -55.16
REMARK 500 ASP D 319 0.13 -63.80
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 MG A 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 177 OD2
REMARK 620 2 GLV A 601 O1 90.4
REMARK 620 3 GLV A 601 O3 81.8 71.6
REMARK 620 4 HOH A 701 O 86.3 89.2 157.2
REMARK 620 5 HOH A 716 O 177.9 87.5 97.8 93.4
REMARK 620 6 HOH A 717 O 87.2 172.4 100.9 97.8 95.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 177 OD2
REMARK 620 2 GLV B 601 O1 79.0
REMARK 620 3 GLV B 601 O2 77.6 71.7
REMARK 620 4 HOH B 702 O 79.6 95.3 155.5
REMARK 620 5 HOH B 704 O 166.9 93.8 89.7 112.2
REMARK 620 6 HOH B 705 O 80.3 155.2 90.7 94.3 103.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 177 OD2
REMARK 620 2 GLV C 601 O3 77.4
REMARK 620 3 HOH C 706 O 156.7 89.9
REMARK 620 4 HOH C 707 O 86.0 163.4 105.7
REMARK 620 5 HOH C 726 O 65.4 90.2 95.7 82.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 177 OD2
REMARK 620 2 GLV D 601 O1 82.3
REMARK 620 3 GLV D 601 O3 85.3 76.4
REMARK 620 4 HOH D 703 O 164.0 112.1 104.5
REMARK 620 5 HOH D 709 O 69.3 103.3 154.2 99.5
REMARK 620 6 HOH D 710 O 80.7 159.1 90.2 86.5 81.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLV A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLV B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLV C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLV D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E9F RELATED DB: PDB
REMARK 900 RELATED ID: 5E9H RELATED DB: PDB
DBREF 5E9G A 1 547 UNP P0CT06 ACEA_MAGO7 1 547
DBREF 5E9G B 1 547 UNP P0CT06 ACEA_MAGO7 1 547
DBREF 5E9G C 1 547 UNP P0CT06 ACEA_MAGO7 1 547
DBREF 5E9G D 1 547 UNP P0CT06 ACEA_MAGO7 1 547
SEQADV 5E9G GLY A 219 UNP P0CT06 ALA 219 ENGINEERED MUTATION
SEQADV 5E9G ALA A 548 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA A 549 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA A 550 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G LEU A 551 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLU A 552 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 553 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 554 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 555 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 556 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 557 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 558 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 559 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS A 560 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLY B 219 UNP P0CT06 ALA 219 ENGINEERED MUTATION
SEQADV 5E9G ALA B 548 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA B 549 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA B 550 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G LEU B 551 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLU B 552 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 553 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 554 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 555 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 556 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 557 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 558 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 559 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS B 560 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLY C 219 UNP P0CT06 ALA 219 ENGINEERED MUTATION
SEQADV 5E9G ALA C 548 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA C 549 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA C 550 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G LEU C 551 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLU C 552 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 553 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 554 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 555 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 556 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 557 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 558 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 559 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS C 560 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLY D 219 UNP P0CT06 ALA 219 ENGINEERED MUTATION
SEQADV 5E9G ALA D 548 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA D 549 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G ALA D 550 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G LEU D 551 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G GLU D 552 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 553 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 554 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 555 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 556 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 557 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 558 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 559 UNP P0CT06 EXPRESSION TAG
SEQADV 5E9G HIS D 560 UNP P0CT06 EXPRESSION TAG
SEQRES 1 A 560 MET ALA SER LYS ASN MET VAL ASN PRO ALA VAL GLU PRO
SEQRES 2 A 560 SER MET GLU ASP ASP LEU PHE ALA ARG GLU VAL ALA GLU
SEQRES 3 A 560 VAL LYS GLN TRP TRP SER ASP PRO ARG TRP ARG TYR THR
SEQRES 4 A 560 LYS ARG PRO PHE THR ALA GLU GLN ILE VAL SER LYS ARG
SEQRES 5 A 560 GLY ASN LEU LYS ILE GLU TYR PRO SER ASN ALA GLN SER
SEQRES 6 A 560 LYS LYS LEU TRP LYS ILE LEU GLU GLY ARG PHE GLN LYS
SEQRES 7 A 560 ARG ASP ALA SER TYR THR TYR GLY CYS LEU GLU PRO THR
SEQRES 8 A 560 MET VAL THR GLN MET ALA LYS TYR LEU ASP THR VAL TYR
SEQRES 9 A 560 VAL SER GLY TRP GLN SER SER SER THR ALA SER SER SER
SEQRES 10 A 560 ASP GLU PRO GLY PRO ASP LEU ALA ASP TYR PRO TYR THR
SEQRES 11 A 560 THR VAL PRO ASN LYS VAL SER HIS LEU PHE MET ALA GLN
SEQRES 12 A 560 LEU PHE HIS ASP ARG LYS GLN ARG HIS GLU ARG LEU SER
SEQRES 13 A 560 ALA PRO LYS SER GLU ARG SER LYS LEU GLN ASN ILE ASP
SEQRES 14 A 560 TYR LEU ARG PRO ILE ILE ALA ASP ALA ASP THR GLY HIS
SEQRES 15 A 560 GLY GLY LEU THR ALA VAL MET LYS LEU THR LYS LEU PHE
SEQRES 16 A 560 ILE GLU LYS GLY ALA ALA GLY ILE HIS ILE GLU ASP GLN
SEQRES 17 A 560 ALA PRO GLY THR LYS LYS CYS GLY HIS MET GLY GLY LYS
SEQRES 18 A 560 VAL LEU VAL PRO ILE SER GLU HIS ILE ASN ARG LEU VAL
SEQRES 19 A 560 ALA ILE ARG ALA GLN ALA ASP ILE MET GLY VAL ASP LEU
SEQRES 20 A 560 LEU ALA ILE ALA ARG THR ASP ALA GLU ALA ALA THR LEU
SEQRES 21 A 560 ILE THR THR SER ILE ASP PRO ARG ASP HIS ALA PHE ILE
SEQRES 22 A 560 LEU GLY CYS THR ASN PRO SER LEU GLN PRO LEU ALA ASP
SEQRES 23 A 560 LEU MET ASN THR ALA GLU GLN SER GLY LYS THR GLY ASP
SEQRES 24 A 560 GLN LEU GLN ALA ILE GLU ASP GLU TRP MET ALA LYS ALA
SEQRES 25 A 560 ASN LEU LYS ARG PHE ASP ASP ALA VAL VAL ASP VAL ILE
SEQRES 26 A 560 ASN SER SER SER SER ILE ARG ASN PRO LYS ASP VAL ALA
SEQRES 27 A 560 ALA LYS TYR LEU GLN ALA ALA LYS GLY LYS SER ASN ARG
SEQRES 28 A 560 GLU ALA ARG ALA ILE ALA SER SER LEU GLY VAL PRO GLU
SEQRES 29 A 560 ILE PHE PHE ASP TRP ASP SER PRO ARG THR ARG GLU GLY
SEQRES 30 A 560 TYR PHE ARG ILE LYS GLY GLY CYS ASP CYS ALA ILE ASN
SEQRES 31 A 560 ARG ALA ILE ALA TYR ALA PRO TYR ALA ASP ALA ILE TRP
SEQRES 32 A 560 MET GLU SER LYS LEU PRO ASP TYR GLU GLN ALA LYS GLU
SEQRES 33 A 560 PHE ALA GLU GLY VAL HIS ALA VAL TYR PRO GLU GLN LYS
SEQRES 34 A 560 LEU ALA TYR ASN LEU SER PRO SER PHE ASN TRP LYS THR
SEQRES 35 A 560 ALA MET PRO ARG ASP GLU GLN GLU THR TYR ILE ARG ARG
SEQRES 36 A 560 LEU ALA GLY LEU GLY TYR CYS TRP GLN PHE ILE THR LEU
SEQRES 37 A 560 ALA GLY LEU HIS THR THR ALA LEU ILE SER ASP ARG PHE
SEQRES 38 A 560 ALA ARG ALA TYR SER GLU VAL GLY MET ARG ALA TYR GLY
SEQRES 39 A 560 GLU LEU VAL GLN GLU PRO GLU MET GLU LEU GLY VAL ASP
SEQRES 40 A 560 VAL VAL LYS HIS GLN LYS TRP SER GLY ALA THR TYR VAL
SEQRES 41 A 560 ASP GLU LEU GLN LYS MET VAL THR GLY GLY VAL SER SER
SEQRES 42 A 560 THR ALA ALA MET GLY LYS GLY VAL THR GLU ASP GLN PHE
SEQRES 43 A 560 HIS ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS HIS
SEQRES 44 A 560 HIS
SEQRES 1 B 560 MET ALA SER LYS ASN MET VAL ASN PRO ALA VAL GLU PRO
SEQRES 2 B 560 SER MET GLU ASP ASP LEU PHE ALA ARG GLU VAL ALA GLU
SEQRES 3 B 560 VAL LYS GLN TRP TRP SER ASP PRO ARG TRP ARG TYR THR
SEQRES 4 B 560 LYS ARG PRO PHE THR ALA GLU GLN ILE VAL SER LYS ARG
SEQRES 5 B 560 GLY ASN LEU LYS ILE GLU TYR PRO SER ASN ALA GLN SER
SEQRES 6 B 560 LYS LYS LEU TRP LYS ILE LEU GLU GLY ARG PHE GLN LYS
SEQRES 7 B 560 ARG ASP ALA SER TYR THR TYR GLY CYS LEU GLU PRO THR
SEQRES 8 B 560 MET VAL THR GLN MET ALA LYS TYR LEU ASP THR VAL TYR
SEQRES 9 B 560 VAL SER GLY TRP GLN SER SER SER THR ALA SER SER SER
SEQRES 10 B 560 ASP GLU PRO GLY PRO ASP LEU ALA ASP TYR PRO TYR THR
SEQRES 11 B 560 THR VAL PRO ASN LYS VAL SER HIS LEU PHE MET ALA GLN
SEQRES 12 B 560 LEU PHE HIS ASP ARG LYS GLN ARG HIS GLU ARG LEU SER
SEQRES 13 B 560 ALA PRO LYS SER GLU ARG SER LYS LEU GLN ASN ILE ASP
SEQRES 14 B 560 TYR LEU ARG PRO ILE ILE ALA ASP ALA ASP THR GLY HIS
SEQRES 15 B 560 GLY GLY LEU THR ALA VAL MET LYS LEU THR LYS LEU PHE
SEQRES 16 B 560 ILE GLU LYS GLY ALA ALA GLY ILE HIS ILE GLU ASP GLN
SEQRES 17 B 560 ALA PRO GLY THR LYS LYS CYS GLY HIS MET GLY GLY LYS
SEQRES 18 B 560 VAL LEU VAL PRO ILE SER GLU HIS ILE ASN ARG LEU VAL
SEQRES 19 B 560 ALA ILE ARG ALA GLN ALA ASP ILE MET GLY VAL ASP LEU
SEQRES 20 B 560 LEU ALA ILE ALA ARG THR ASP ALA GLU ALA ALA THR LEU
SEQRES 21 B 560 ILE THR THR SER ILE ASP PRO ARG ASP HIS ALA PHE ILE
SEQRES 22 B 560 LEU GLY CYS THR ASN PRO SER LEU GLN PRO LEU ALA ASP
SEQRES 23 B 560 LEU MET ASN THR ALA GLU GLN SER GLY LYS THR GLY ASP
SEQRES 24 B 560 GLN LEU GLN ALA ILE GLU ASP GLU TRP MET ALA LYS ALA
SEQRES 25 B 560 ASN LEU LYS ARG PHE ASP ASP ALA VAL VAL ASP VAL ILE
SEQRES 26 B 560 ASN SER SER SER SER ILE ARG ASN PRO LYS ASP VAL ALA
SEQRES 27 B 560 ALA LYS TYR LEU GLN ALA ALA LYS GLY LYS SER ASN ARG
SEQRES 28 B 560 GLU ALA ARG ALA ILE ALA SER SER LEU GLY VAL PRO GLU
SEQRES 29 B 560 ILE PHE PHE ASP TRP ASP SER PRO ARG THR ARG GLU GLY
SEQRES 30 B 560 TYR PHE ARG ILE LYS GLY GLY CYS ASP CYS ALA ILE ASN
SEQRES 31 B 560 ARG ALA ILE ALA TYR ALA PRO TYR ALA ASP ALA ILE TRP
SEQRES 32 B 560 MET GLU SER LYS LEU PRO ASP TYR GLU GLN ALA LYS GLU
SEQRES 33 B 560 PHE ALA GLU GLY VAL HIS ALA VAL TYR PRO GLU GLN LYS
SEQRES 34 B 560 LEU ALA TYR ASN LEU SER PRO SER PHE ASN TRP LYS THR
SEQRES 35 B 560 ALA MET PRO ARG ASP GLU GLN GLU THR TYR ILE ARG ARG
SEQRES 36 B 560 LEU ALA GLY LEU GLY TYR CYS TRP GLN PHE ILE THR LEU
SEQRES 37 B 560 ALA GLY LEU HIS THR THR ALA LEU ILE SER ASP ARG PHE
SEQRES 38 B 560 ALA ARG ALA TYR SER GLU VAL GLY MET ARG ALA TYR GLY
SEQRES 39 B 560 GLU LEU VAL GLN GLU PRO GLU MET GLU LEU GLY VAL ASP
SEQRES 40 B 560 VAL VAL LYS HIS GLN LYS TRP SER GLY ALA THR TYR VAL
SEQRES 41 B 560 ASP GLU LEU GLN LYS MET VAL THR GLY GLY VAL SER SER
SEQRES 42 B 560 THR ALA ALA MET GLY LYS GLY VAL THR GLU ASP GLN PHE
SEQRES 43 B 560 HIS ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS HIS
SEQRES 44 B 560 HIS
SEQRES 1 C 560 MET ALA SER LYS ASN MET VAL ASN PRO ALA VAL GLU PRO
SEQRES 2 C 560 SER MET GLU ASP ASP LEU PHE ALA ARG GLU VAL ALA GLU
SEQRES 3 C 560 VAL LYS GLN TRP TRP SER ASP PRO ARG TRP ARG TYR THR
SEQRES 4 C 560 LYS ARG PRO PHE THR ALA GLU GLN ILE VAL SER LYS ARG
SEQRES 5 C 560 GLY ASN LEU LYS ILE GLU TYR PRO SER ASN ALA GLN SER
SEQRES 6 C 560 LYS LYS LEU TRP LYS ILE LEU GLU GLY ARG PHE GLN LYS
SEQRES 7 C 560 ARG ASP ALA SER TYR THR TYR GLY CYS LEU GLU PRO THR
SEQRES 8 C 560 MET VAL THR GLN MET ALA LYS TYR LEU ASP THR VAL TYR
SEQRES 9 C 560 VAL SER GLY TRP GLN SER SER SER THR ALA SER SER SER
SEQRES 10 C 560 ASP GLU PRO GLY PRO ASP LEU ALA ASP TYR PRO TYR THR
SEQRES 11 C 560 THR VAL PRO ASN LYS VAL SER HIS LEU PHE MET ALA GLN
SEQRES 12 C 560 LEU PHE HIS ASP ARG LYS GLN ARG HIS GLU ARG LEU SER
SEQRES 13 C 560 ALA PRO LYS SER GLU ARG SER LYS LEU GLN ASN ILE ASP
SEQRES 14 C 560 TYR LEU ARG PRO ILE ILE ALA ASP ALA ASP THR GLY HIS
SEQRES 15 C 560 GLY GLY LEU THR ALA VAL MET LYS LEU THR LYS LEU PHE
SEQRES 16 C 560 ILE GLU LYS GLY ALA ALA GLY ILE HIS ILE GLU ASP GLN
SEQRES 17 C 560 ALA PRO GLY THR LYS LYS CYS GLY HIS MET GLY GLY LYS
SEQRES 18 C 560 VAL LEU VAL PRO ILE SER GLU HIS ILE ASN ARG LEU VAL
SEQRES 19 C 560 ALA ILE ARG ALA GLN ALA ASP ILE MET GLY VAL ASP LEU
SEQRES 20 C 560 LEU ALA ILE ALA ARG THR ASP ALA GLU ALA ALA THR LEU
SEQRES 21 C 560 ILE THR THR SER ILE ASP PRO ARG ASP HIS ALA PHE ILE
SEQRES 22 C 560 LEU GLY CYS THR ASN PRO SER LEU GLN PRO LEU ALA ASP
SEQRES 23 C 560 LEU MET ASN THR ALA GLU GLN SER GLY LYS THR GLY ASP
SEQRES 24 C 560 GLN LEU GLN ALA ILE GLU ASP GLU TRP MET ALA LYS ALA
SEQRES 25 C 560 ASN LEU LYS ARG PHE ASP ASP ALA VAL VAL ASP VAL ILE
SEQRES 26 C 560 ASN SER SER SER SER ILE ARG ASN PRO LYS ASP VAL ALA
SEQRES 27 C 560 ALA LYS TYR LEU GLN ALA ALA LYS GLY LYS SER ASN ARG
SEQRES 28 C 560 GLU ALA ARG ALA ILE ALA SER SER LEU GLY VAL PRO GLU
SEQRES 29 C 560 ILE PHE PHE ASP TRP ASP SER PRO ARG THR ARG GLU GLY
SEQRES 30 C 560 TYR PHE ARG ILE LYS GLY GLY CYS ASP CYS ALA ILE ASN
SEQRES 31 C 560 ARG ALA ILE ALA TYR ALA PRO TYR ALA ASP ALA ILE TRP
SEQRES 32 C 560 MET GLU SER LYS LEU PRO ASP TYR GLU GLN ALA LYS GLU
SEQRES 33 C 560 PHE ALA GLU GLY VAL HIS ALA VAL TYR PRO GLU GLN LYS
SEQRES 34 C 560 LEU ALA TYR ASN LEU SER PRO SER PHE ASN TRP LYS THR
SEQRES 35 C 560 ALA MET PRO ARG ASP GLU GLN GLU THR TYR ILE ARG ARG
SEQRES 36 C 560 LEU ALA GLY LEU GLY TYR CYS TRP GLN PHE ILE THR LEU
SEQRES 37 C 560 ALA GLY LEU HIS THR THR ALA LEU ILE SER ASP ARG PHE
SEQRES 38 C 560 ALA ARG ALA TYR SER GLU VAL GLY MET ARG ALA TYR GLY
SEQRES 39 C 560 GLU LEU VAL GLN GLU PRO GLU MET GLU LEU GLY VAL ASP
SEQRES 40 C 560 VAL VAL LYS HIS GLN LYS TRP SER GLY ALA THR TYR VAL
SEQRES 41 C 560 ASP GLU LEU GLN LYS MET VAL THR GLY GLY VAL SER SER
SEQRES 42 C 560 THR ALA ALA MET GLY LYS GLY VAL THR GLU ASP GLN PHE
SEQRES 43 C 560 HIS ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS HIS
SEQRES 44 C 560 HIS
SEQRES 1 D 560 MET ALA SER LYS ASN MET VAL ASN PRO ALA VAL GLU PRO
SEQRES 2 D 560 SER MET GLU ASP ASP LEU PHE ALA ARG GLU VAL ALA GLU
SEQRES 3 D 560 VAL LYS GLN TRP TRP SER ASP PRO ARG TRP ARG TYR THR
SEQRES 4 D 560 LYS ARG PRO PHE THR ALA GLU GLN ILE VAL SER LYS ARG
SEQRES 5 D 560 GLY ASN LEU LYS ILE GLU TYR PRO SER ASN ALA GLN SER
SEQRES 6 D 560 LYS LYS LEU TRP LYS ILE LEU GLU GLY ARG PHE GLN LYS
SEQRES 7 D 560 ARG ASP ALA SER TYR THR TYR GLY CYS LEU GLU PRO THR
SEQRES 8 D 560 MET VAL THR GLN MET ALA LYS TYR LEU ASP THR VAL TYR
SEQRES 9 D 560 VAL SER GLY TRP GLN SER SER SER THR ALA SER SER SER
SEQRES 10 D 560 ASP GLU PRO GLY PRO ASP LEU ALA ASP TYR PRO TYR THR
SEQRES 11 D 560 THR VAL PRO ASN LYS VAL SER HIS LEU PHE MET ALA GLN
SEQRES 12 D 560 LEU PHE HIS ASP ARG LYS GLN ARG HIS GLU ARG LEU SER
SEQRES 13 D 560 ALA PRO LYS SER GLU ARG SER LYS LEU GLN ASN ILE ASP
SEQRES 14 D 560 TYR LEU ARG PRO ILE ILE ALA ASP ALA ASP THR GLY HIS
SEQRES 15 D 560 GLY GLY LEU THR ALA VAL MET LYS LEU THR LYS LEU PHE
SEQRES 16 D 560 ILE GLU LYS GLY ALA ALA GLY ILE HIS ILE GLU ASP GLN
SEQRES 17 D 560 ALA PRO GLY THR LYS LYS CYS GLY HIS MET GLY GLY LYS
SEQRES 18 D 560 VAL LEU VAL PRO ILE SER GLU HIS ILE ASN ARG LEU VAL
SEQRES 19 D 560 ALA ILE ARG ALA GLN ALA ASP ILE MET GLY VAL ASP LEU
SEQRES 20 D 560 LEU ALA ILE ALA ARG THR ASP ALA GLU ALA ALA THR LEU
SEQRES 21 D 560 ILE THR THR SER ILE ASP PRO ARG ASP HIS ALA PHE ILE
SEQRES 22 D 560 LEU GLY CYS THR ASN PRO SER LEU GLN PRO LEU ALA ASP
SEQRES 23 D 560 LEU MET ASN THR ALA GLU GLN SER GLY LYS THR GLY ASP
SEQRES 24 D 560 GLN LEU GLN ALA ILE GLU ASP GLU TRP MET ALA LYS ALA
SEQRES 25 D 560 ASN LEU LYS ARG PHE ASP ASP ALA VAL VAL ASP VAL ILE
SEQRES 26 D 560 ASN SER SER SER SER ILE ARG ASN PRO LYS ASP VAL ALA
SEQRES 27 D 560 ALA LYS TYR LEU GLN ALA ALA LYS GLY LYS SER ASN ARG
SEQRES 28 D 560 GLU ALA ARG ALA ILE ALA SER SER LEU GLY VAL PRO GLU
SEQRES 29 D 560 ILE PHE PHE ASP TRP ASP SER PRO ARG THR ARG GLU GLY
SEQRES 30 D 560 TYR PHE ARG ILE LYS GLY GLY CYS ASP CYS ALA ILE ASN
SEQRES 31 D 560 ARG ALA ILE ALA TYR ALA PRO TYR ALA ASP ALA ILE TRP
SEQRES 32 D 560 MET GLU SER LYS LEU PRO ASP TYR GLU GLN ALA LYS GLU
SEQRES 33 D 560 PHE ALA GLU GLY VAL HIS ALA VAL TYR PRO GLU GLN LYS
SEQRES 34 D 560 LEU ALA TYR ASN LEU SER PRO SER PHE ASN TRP LYS THR
SEQRES 35 D 560 ALA MET PRO ARG ASP GLU GLN GLU THR TYR ILE ARG ARG
SEQRES 36 D 560 LEU ALA GLY LEU GLY TYR CYS TRP GLN PHE ILE THR LEU
SEQRES 37 D 560 ALA GLY LEU HIS THR THR ALA LEU ILE SER ASP ARG PHE
SEQRES 38 D 560 ALA ARG ALA TYR SER GLU VAL GLY MET ARG ALA TYR GLY
SEQRES 39 D 560 GLU LEU VAL GLN GLU PRO GLU MET GLU LEU GLY VAL ASP
SEQRES 40 D 560 VAL VAL LYS HIS GLN LYS TRP SER GLY ALA THR TYR VAL
SEQRES 41 D 560 ASP GLU LEU GLN LYS MET VAL THR GLY GLY VAL SER SER
SEQRES 42 D 560 THR ALA ALA MET GLY LYS GLY VAL THR GLU ASP GLN PHE
SEQRES 43 D 560 HIS ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS HIS
SEQRES 44 D 560 HIS
HET GLV A 601 5
HET GOL A 602 6
HET MG A 603 1
HET GLV B 601 5
HET GOL B 602 6
HET MG B 603 1
HET GLV C 601 5
HET MG C 602 1
HET GLV D 601 5
HET GOL D 602 6
HET MG D 603 1
HETNAM GLV GLYOXYLIC ACID
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GLV GLYOXALATE; GLYOXYLATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GLV 4(C2 H2 O3)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 7 MG 4(MG 2+)
FORMUL 16 HOH *304(H2 O)
HELIX 1 AA1 MET A 15 SER A 32 1 18
HELIX 2 AA2 ASP A 33 ARG A 37 5 5
HELIX 3 AA3 THR A 44 SER A 50 1 7
HELIX 4 AA4 TYR A 59 ARG A 79 1 21
HELIX 5 AA5 GLU A 89 ALA A 97 1 9
HELIX 6 AA6 SER A 106 ALA A 114 1 9
HELIX 7 AA7 THR A 130 ALA A 157 1 28
HELIX 8 AA8 PRO A 158 LEU A 165 5 8
HELIX 9 AA9 GLY A 184 GLY A 199 1 16
HELIX 10 AB1 PRO A 225 GLY A 244 1 20
HELIX 11 AB2 ASP A 266 HIS A 270 5 5
HELIX 12 AB3 PRO A 283 GLN A 293 1 11
HELIX 13 AB4 GLY A 298 ASN A 313 1 16
HELIX 14 AB5 ARG A 316 ASN A 326 1 11
HELIX 15 AB6 ASN A 333 LYS A 346 1 14
HELIX 16 AB7 SER A 349 LEU A 360 1 12
HELIX 17 AB8 GLY A 384 ALA A 396 1 13
HELIX 18 AB9 PRO A 397 ALA A 399 5 3
HELIX 19 AC1 ASP A 410 ALA A 423 1 14
HELIX 20 AC2 ASN A 439 MET A 444 1 6
HELIX 21 AC3 PRO A 445 LEU A 459 1 15
HELIX 22 AC4 LEU A 468 GLY A 489 1 22
HELIX 23 AC5 GLY A 489 VAL A 497 1 9
HELIX 24 AC6 VAL A 497 GLY A 505 1 9
HELIX 25 AC7 VAL A 506 VAL A 509 5 4
HELIX 26 AC8 LYS A 510 SER A 515 1 6
HELIX 27 AC9 GLY A 516 VAL A 527 1 12
HELIX 28 AD1 GLU B 12 SER B 14 5 3
HELIX 29 AD2 MET B 15 TRP B 31 1 17
HELIX 30 AD3 SER B 32 ARG B 37 5 6
HELIX 31 AD4 THR B 44 SER B 50 1 7
HELIX 32 AD5 TYR B 59 ARG B 79 1 21
HELIX 33 AD6 GLU B 89 ALA B 97 1 9
HELIX 34 AD7 SER B 106 ALA B 114 1 9
HELIX 35 AD8 THR B 130 ALA B 157 1 28
HELIX 36 AD9 PRO B 158 LEU B 165 5 8
HELIX 37 AE1 GLY B 184 GLY B 199 1 16
HELIX 38 AE2 PRO B 225 MET B 243 1 19
HELIX 39 AE3 ASP B 266 ILE B 273 5 8
HELIX 40 AE4 PRO B 283 GLN B 293 1 11
HELIX 41 AE5 GLY B 298 ASN B 313 1 16
HELIX 42 AE6 ARG B 316 SER B 328 1 13
HELIX 43 AE7 ASN B 333 LYS B 346 1 14
HELIX 44 AE8 SER B 349 LEU B 360 1 12
HELIX 45 AE9 GLY B 384 ALA B 396 1 13
HELIX 46 AF1 PRO B 397 ALA B 399 5 3
HELIX 47 AF2 ASP B 410 ALA B 423 1 14
HELIX 48 AF3 ASN B 439 MET B 444 1 6
HELIX 49 AF4 PRO B 445 GLY B 458 1 14
HELIX 50 AF5 LEU B 468 GLY B 489 1 22
HELIX 51 AF6 GLY B 489 VAL B 497 1 9
HELIX 52 AF7 VAL B 497 GLY B 505 1 9
HELIX 53 AF8 VAL B 506 VAL B 509 5 4
HELIX 54 AF9 LYS B 510 SER B 515 1 6
HELIX 55 AG1 GLY B 516 GLY B 529 1 14
HELIX 56 AG2 GLU C 12 SER C 32 1 21
HELIX 57 AG3 ASP C 33 ARG C 37 5 5
HELIX 58 AG4 THR C 44 SER C 50 1 7
HELIX 59 AG5 TYR C 59 LYS C 78 1 20
HELIX 60 AG6 GLU C 89 ALA C 97 1 9
HELIX 61 AG7 SER C 106 ALA C 114 1 9
HELIX 62 AG8 THR C 130 ALA C 157 1 28
HELIX 63 AG9 PRO C 158 SER C 163 1 6
HELIX 64 AH1 GLY C 184 GLY C 199 1 16
HELIX 65 AH2 ALA C 209 LYS C 213 5 5
HELIX 66 AH3 PRO C 225 GLY C 244 1 20
HELIX 67 AH4 ASP C 266 HIS C 270 5 5
HELIX 68 AH5 PRO C 283 THR C 290 1 8
HELIX 69 AH6 GLU C 305 ASN C 313 1 9
HELIX 70 AH7 ARG C 316 ASN C 326 1 11
HELIX 71 AH8 LYS C 340 ALA C 345 1 6
HELIX 72 AH9 SER C 349 LEU C 360 1 12
HELIX 73 AI1 GLY C 384 ALA C 396 1 13
HELIX 74 AI2 PRO C 397 ALA C 399 5 3
HELIX 75 AI3 ASP C 410 ALA C 423 1 14
HELIX 76 AI4 ASN C 439 MET C 444 1 6
HELIX 77 AI5 PRO C 445 GLY C 458 1 14
HELIX 78 AI6 LEU C 468 GLY C 489 1 22
HELIX 79 AI7 GLY C 489 VAL C 497 1 9
HELIX 80 AI8 VAL C 497 GLY C 505 1 9
HELIX 81 AI9 VAL C 506 VAL C 509 5 4
HELIX 82 AJ1 LYS C 510 GLY C 516 1 7
HELIX 83 AJ2 GLY C 516 VAL C 527 1 12
HELIX 84 AJ3 MET D 15 SER D 32 1 18
HELIX 85 AJ4 ASP D 33 ARG D 37 5 5
HELIX 86 AJ5 THR D 44 SER D 50 1 7
HELIX 87 AJ6 TYR D 59 LYS D 78 1 20
HELIX 88 AJ7 GLU D 89 ALA D 97 1 9
HELIX 89 AJ8 SER D 106 ALA D 114 1 9
HELIX 90 AJ9 THR D 130 ALA D 157 1 28
HELIX 91 AK1 PRO D 158 LEU D 165 5 8
HELIX 92 AK2 GLY D 184 GLY D 199 1 16
HELIX 93 AK3 PRO D 225 GLY D 244 1 20
HELIX 94 AK4 ASP D 266 ALA D 271 1 6
HELIX 95 AK5 PRO D 283 MET D 288 1 6
HELIX 96 AK6 TRP D 308 ASN D 313 1 6
HELIX 97 AK7 PHE D 317 VAL D 322 1 6
HELIX 98 AK8 TYR D 341 LYS D 346 1 6
HELIX 99 AK9 SER D 349 SER D 359 1 11
HELIX 100 AL1 GLY D 384 ALA D 396 1 13
HELIX 101 AL2 PRO D 397 ALA D 399 5 3
HELIX 102 AL3 ASP D 410 ALA D 423 1 14
HELIX 103 AL4 PRO D 445 LEU D 459 1 15
HELIX 104 AL5 LEU D 468 GLY D 489 1 22
HELIX 105 AL6 GLY D 489 VAL D 497 1 9
HELIX 106 AL7 VAL D 497 GLY D 505 1 9
HELIX 107 AL8 VAL D 506 VAL D 509 5 4
HELIX 108 AL9 LYS D 510 SER D 515 1 6
HELIX 109 AM1 GLY D 516 GLY D 529 1 14
SHEET 1 AA1 8 SER A 82 TYR A 85 0
SHEET 2 AA1 8 TYR A 461 ILE A 466 1 O CYS A 462 N SER A 82
SHEET 3 AA1 8 LEU A 430 ASN A 433 1 N TYR A 432 O PHE A 465
SHEET 4 AA1 8 ALA A 401 MET A 404 1 N ILE A 402 O ALA A 431
SHEET 5 AA1 8 LEU A 248 THR A 253 1 N THR A 253 O TRP A 403
SHEET 6 AA1 8 GLY A 202 GLU A 206 1 N ILE A 203 O ILE A 250
SHEET 7 AA1 8 ILE A 174 ASP A 177 1 N ALA A 176 O GLY A 202
SHEET 8 AA1 8 VAL A 103 VAL A 105 1 N VAL A 103 O ILE A 175
SHEET 1 AA2 3 VAL A 222 LEU A 223 0
SHEET 2 AA2 3 LEU A 260 ILE A 261 1 O LEU A 260 N LEU A 223
SHEET 3 AA2 3 PHE A 379 ARG A 380 -1 O PHE A 379 N ILE A 261
SHEET 1 AA3 3 SER B 82 TYR B 85 0
SHEET 2 AA3 3 TYR B 461 ILE B 466 1 O CYS B 462 N SER B 82
SHEET 3 AA3 3 LEU B 430 ASN B 433 1 N TYR B 432 O PHE B 465
SHEET 1 AA4 5 VAL B 103 VAL B 105 0
SHEET 2 AA4 5 ILE B 174 ASP B 177 1 O ILE B 175 N VAL B 103
SHEET 3 AA4 5 GLY B 202 GLU B 206 1 O GLY B 202 N ALA B 176
SHEET 4 AA4 5 LEU B 248 THR B 253 1 O ILE B 250 N ILE B 203
SHEET 5 AA4 5 ALA B 401 MET B 404 1 O TRP B 403 N ALA B 251
SHEET 1 AA5 3 VAL B 222 LEU B 223 0
SHEET 2 AA5 3 LEU B 260 ILE B 261 1 O LEU B 260 N LEU B 223
SHEET 3 AA5 3 PHE B 379 ARG B 380 -1 O PHE B 379 N ILE B 261
SHEET 1 AA6 8 SER C 82 TYR C 85 0
SHEET 2 AA6 8 TYR C 461 ILE C 466 1 O CYS C 462 N SER C 82
SHEET 3 AA6 8 LEU C 430 ASN C 433 1 N TYR C 432 O PHE C 465
SHEET 4 AA6 8 ALA C 401 MET C 404 1 N ILE C 402 O ALA C 431
SHEET 5 AA6 8 LEU C 248 THR C 253 1 N THR C 253 O TRP C 403
SHEET 6 AA6 8 GLY C 202 GLU C 206 1 N ILE C 205 O ARG C 252
SHEET 7 AA6 8 ILE C 174 ASP C 177 1 N ALA C 176 O GLY C 202
SHEET 8 AA6 8 VAL C 103 VAL C 105 1 N VAL C 103 O ILE C 175
SHEET 1 AA7 3 VAL C 222 LEU C 223 0
SHEET 2 AA7 3 LEU C 260 ILE C 261 1 O LEU C 260 N LEU C 223
SHEET 3 AA7 3 PHE C 379 ARG C 380 -1 O PHE C 379 N ILE C 261
SHEET 1 AA8 8 SER D 82 TYR D 85 0
SHEET 2 AA8 8 TYR D 461 ILE D 466 1 O GLN D 464 N SER D 82
SHEET 3 AA8 8 LEU D 430 ASN D 433 1 N TYR D 432 O PHE D 465
SHEET 4 AA8 8 ALA D 401 MET D 404 1 N ILE D 402 O ALA D 431
SHEET 5 AA8 8 LEU D 248 THR D 253 1 N ALA D 251 O TRP D 403
SHEET 6 AA8 8 GLY D 202 GLU D 206 1 N ILE D 203 O ILE D 250
SHEET 7 AA8 8 ILE D 174 ASP D 177 1 N ALA D 176 O GLY D 202
SHEET 8 AA8 8 VAL D 103 VAL D 105 1 N VAL D 103 O ILE D 175
SHEET 1 AA9 3 VAL D 222 LEU D 223 0
SHEET 2 AA9 3 LEU D 260 ILE D 261 1 O LEU D 260 N LEU D 223
SHEET 3 AA9 3 PHE D 379 ARG D 380 -1 O PHE D 379 N ILE D 261
LINK OD2 ASP A 177 MG MG A 603 1555 1555 2.21
LINK O1 GLV A 601 MG MG A 603 1555 1555 2.40
LINK O3 GLV A 601 MG MG A 603 1555 1555 2.35
LINK MG MG A 603 O HOH A 701 1555 1555 2.40
LINK MG MG A 603 O HOH A 716 1555 1555 2.20
LINK MG MG A 603 O HOH A 717 1555 1555 2.24
LINK OD2 ASP B 177 MG MG B 603 1555 1555 2.34
LINK O1 GLV B 601 MG MG B 603 1555 1555 2.50
LINK O2 GLV B 601 MG MG B 603 1555 1555 2.40
LINK MG MG B 603 O HOH B 702 1555 1555 2.29
LINK MG MG B 603 O HOH B 704 1555 1555 2.37
LINK MG MG B 603 O HOH B 705 1555 1555 2.36
LINK OD2 ASP C 177 MG MG C 602 1555 1555 2.29
LINK O3 GLV C 601 MG MG C 602 1555 1555 2.78
LINK MG MG C 602 O HOH C 706 1555 1555 2.41
LINK MG MG C 602 O HOH C 707 1555 1555 2.45
LINK MG MG C 602 O HOH C 726 1555 1555 2.61
LINK OD2 ASP D 177 MG MG D 603 1555 1555 2.26
LINK O1 GLV D 601 MG MG D 603 1555 1555 2.44
LINK O3 GLV D 601 MG MG D 603 1555 1555 2.39
LINK MG MG D 603 O HOH D 703 1555 1555 2.32
LINK MG MG D 603 O HOH D 709 1555 1555 2.36
LINK MG MG D 603 O HOH D 710 1555 1555 2.49
SITE 1 AC1 10 TYR A 104 SER A 106 GLY A 107 TRP A 108
SITE 2 AC1 10 ASP A 177 HIS A 204 ARG A 252 TRP A 403
SITE 3 AC1 10 THR A 467 MG A 603
SITE 1 AC2 10 TRP A 108 CYS A 215 GLY A 216 HIS A 217
SITE 2 AC2 10 ARG A 252 GLU A 405 ASN A 433 SER A 435
SITE 3 AC2 10 THR A 467 HOH A 716
SITE 1 AC3 5 ASP A 177 GLV A 601 HOH A 701 HOH A 716
SITE 2 AC3 5 HOH A 717
SITE 1 AC4 11 TYR B 104 SER B 106 GLY B 107 TRP B 108
SITE 2 AC4 11 ASP B 177 HIS B 204 ARG B 252 TRP B 403
SITE 3 AC4 11 THR B 467 GOL B 602 MG B 603
SITE 1 AC5 11 CYS B 215 GLY B 216 HIS B 217 ARG B 252
SITE 2 AC5 11 GLU B 405 ASN B 433 SER B 435 SER B 437
SITE 3 AC5 11 THR B 467 GLV B 601 HOH B 704
SITE 1 AC6 6 ASP B 177 LYS B 213 GLV B 601 HOH B 702
SITE 2 AC6 6 HOH B 704 HOH B 705
SITE 1 AC7 11 TYR C 104 SER C 106 GLY C 107 TRP C 108
SITE 2 AC7 11 ASP C 177 ARG C 252 TRP C 403 MG C 602
SITE 3 AC7 11 HOH C 706 HOH C 723 HOH C 728
SITE 1 AC8 5 ASP C 177 GLV C 601 HOH C 706 HOH C 707
SITE 2 AC8 5 HOH C 726
SITE 1 AC9 11 TYR D 104 SER D 106 GLY D 107 TRP D 108
SITE 2 AC9 11 ASP D 177 HIS D 204 ARG D 252 TRP D 403
SITE 3 AC9 11 THR D 467 GOL D 602 MG D 603
SITE 1 AD1 10 CYS D 215 GLY D 216 HIS D 217 ARG D 252
SITE 2 AD1 10 GLU D 405 ASN D 433 SER D 435 SER D 437
SITE 3 AD1 10 GLV D 601 HOH D 703
SITE 1 AD2 5 ASP D 177 GLV D 601 HOH D 703 HOH D 709
SITE 2 AD2 5 HOH D 710
CRYST1 121.122 135.078 158.704 90.00 90.00 90.00 P 21 21 21 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 0.008256 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
