HEADER TRANSFERASE 22-MAR-13 4JSP
TITLE STRUCTURE OF MTORDELTAN-MLST8-ATPGAMMAS-MG COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 1376-2549;
COMPND 5 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED
COMPND 6 PROTEIN 1, FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN, MAMMALIAN
COMPND 7 TARGET OF RAPAMYCIN, MTOR, MECHANISTIC TARGET OF RAPAMYCIN, RAPAMYCIN
COMPND 8 AND FKBP12 TARGET 1, RAPAMYCIN TARGET PROTEIN 1;
COMPND 9 EC: 2.7.11.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: TARGET OF RAPAMYCIN COMPLEX SUBUNIT LST8;
COMPND 13 CHAIN: D, C;
COMPND 14 SYNONYM: TORC SUBUNIT LST8, G PROTEIN BETA SUBUNIT-LIKE, GABLE,
COMPND 15 PROTEIN GBETAL, MAMMALIAN LETHAL WITH SEC13 PROTEIN 8, MLST8;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+)HYGROMYCIN;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: GBL, LST8, MLST8;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+)BLASTICIDIN
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.P.PAVLETICH,H.YANG
REVDAT 3 29-MAY-13 4JSP 1 JRNL
REVDAT 2 08-MAY-13 4JSP 1 TITLE
REVDAT 1 01-MAY-13 4JSP 0
JRNL AUTH H.YANG,D.G.RUDGE,J.D.KOOS,B.VAIDIALINGAM,H.J.YANG,
JRNL AUTH 2 N.P.PAVLETICH
JRNL TITL MTOR KINASE STRUCTURE, MECHANISM AND REGULATION.
JRNL REF NATURE V. 497 217 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23636326
JRNL DOI 10.1038/NATURE12122
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 64758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1611
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3639
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97000
REMARK 3 B22 (A**2) : -2.25000
REMARK 3 B33 (A**2) : 3.22000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.547
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.429
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.171
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22716 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30796 ; 1.260 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2742 ; 6.563 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1088 ;37.545 ;23.952
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3982 ;20.642 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 158 ;18.506 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3374 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17152 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 17
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 284 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 80 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 376 ; 0.010 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 300 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 88 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 116 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1012 ; 0.020 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1268 ; 0.020 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 B (A): 223 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 232 ; 2.250 ;99.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 223 ; 2.860 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 271 ; 0.010 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 248 ; 4.760 ;99.000
REMARK 3 MEDIUM THERMAL 2 B (A**2): 271 ; 5.050 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 B (A): 121 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 3 B (A**2): 132 ; 7.350 ;99.000
REMARK 3 MEDIUM THERMAL 3 B (A**2): 121 ; 7.840 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 B (A): 161 ; 0.010 ; 0.500
REMARK 3 TIGHT THERMAL 4 B (A**2): 172 ;11.300 ;99.000
REMARK 3 MEDIUM THERMAL 4 B (A**2): 161 ;10.980 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 B (A): 211 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 5 B (A**2): 188 ;19.370 ;99.000
REMARK 3 MEDIUM THERMAL 5 B (A**2): 211 ;18.760 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 6 B (A): 204 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 6 B (A**2): 204 ;10.850 ;99.000
REMARK 3 MEDIUM THERMAL 6 B (A**2): 204 ;10.890 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 7 B (A): 238 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 7 B (A**2): 224 ; 3.900 ;99.000
REMARK 3 MEDIUM THERMAL 7 B (A**2): 238 ; 3.900 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 8 B (A): 363 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 8 B (A**2): 320 ; 2.600 ;99.000
REMARK 3 MEDIUM THERMAL 8 B (A**2): 363 ; 3.110 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 9 B (A): 258 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 9 B (A**2): 256 ; 4.630 ;99.000
REMARK 3 MEDIUM THERMAL 9 B (A**2): 258 ; 4.860 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 10 B (A): 283 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 10 B (A**2): 284 ; 6.090 ;99.000
REMARK 3 MEDIUM THERMAL 10 B (A**2): 283 ; 6.250 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 11 B (A): 73 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 11 B (A**2): 80 ; 7.670 ;99.000
REMARK 3 MEDIUM THERMAL 11 B (A**2): 73 ; 7.820 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 12 B (A): 425 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 12 B (A**2): 376 ;19.370 ;99.000
REMARK 3 MEDIUM THERMAL 12 B (A**2): 425 ;19.050 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 13 B (A): 293 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 13 B (A**2): 300 ; 7.340 ;99.000
REMARK 3 MEDIUM THERMAL 13 B (A**2): 293 ; 7.640 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 14 B (A): 90 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 14 B (A**2): 88 ; 3.970 ;99.000
REMARK 3 MEDIUM THERMAL 14 B (A**2): 90 ; 4.210 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 15 B (A): 108 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 15 B (A**2): 116 ; 4.380 ;99.000
REMARK 3 MEDIUM THERMAL 15 B (A**2): 108 ; 4.660 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 16 B (A): 1055 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 16 B (A**2): 1012 ; 3.290 ;99.000
REMARK 3 MEDIUM THERMAL 16 B (A**2): 1055 ; 3.430 ;99.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 17
REMARK 3 CHAIN NAMES : D C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 17 D (A): 1186 ; 0.020 ; 0.500
REMARK 3 TIGHT THERMAL 17 D (A**2): 1268 ;10.650 ;99.000
REMARK 3 MEDIUM THERMAL 17 D (A**2): 1186 ;10.940 ;99.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.30
REMARK 3 ION PROBE RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4JSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70381
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.61200
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: MIR
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NACL , PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.90000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.60000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.90000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 ASP B 1376
REMARK 465 ASP B 1377
REMARK 465 ASN B 1378
REMARK 465 GLY B 1379
REMARK 465 ILE B 1380
REMARK 465 VAL B 1381
REMARK 465 LEU B 1382
REMARK 465 LEU B 1383
REMARK 465 GLY B 1384
REMARK 465 LYS B 1815
REMARK 465 LYS B 1816
REMARK 465 LEU B 1817
REMARK 465 ARG B 1818
REMARK 465 HIS B 1819
REMARK 465 ALA B 1820
REMARK 465 SER B 1821
REMARK 465 GLY B 1822
REMARK 465 ALA B 1823
REMARK 465 ASN B 1824
REMARK 465 ILE B 1825
REMARK 465 THR B 1826
REMARK 465 ASN B 1827
REMARK 465 ALA B 1828
REMARK 465 THR B 1829
REMARK 465 THR B 1830
REMARK 465 ALA B 1831
REMARK 465 ALA B 1832
REMARK 465 THR B 1833
REMARK 465 THR B 1834
REMARK 465 ALA B 1835
REMARK 465 ALA B 1836
REMARK 465 THR B 1837
REMARK 465 ALA B 1838
REMARK 465 THR B 1839
REMARK 465 THR B 1840
REMARK 465 THR B 1841
REMARK 465 ALA B 1842
REMARK 465 SER B 1843
REMARK 465 THR B 1844
REMARK 465 GLU B 1845
REMARK 465 GLY B 1846
REMARK 465 SER B 1847
REMARK 465 ASN B 1848
REMARK 465 SER B 1849
REMARK 465 GLU B 1850
REMARK 465 SER B 1851
REMARK 465 GLU B 1852
REMARK 465 ALA B 1853
REMARK 465 GLU B 1854
REMARK 465 SER B 1855
REMARK 465 THR B 1856
REMARK 465 GLU B 1857
REMARK 465 ASN B 1858
REMARK 465 SER B 1859
REMARK 465 PRO B 1860
REMARK 465 THR B 1861
REMARK 465 PRO B 1862
REMARK 465 SER B 1863
REMARK 465 PRO B 1864
REMARK 465 LEU B 1865
REMARK 465 GLN B 1866
REMARK 465 LYS B 2437
REMARK 465 GLY B 2438
REMARK 465 ASN B 2439
REMARK 465 LYS B 2440
REMARK 465 ARG B 2441
REMARK 465 SER B 2442
REMARK 465 ARG B 2443
REMARK 465 THR B 2444
REMARK 465 ARG B 2445
REMARK 465 THR B 2446
REMARK 465 ASP B 2447
REMARK 465 SER B 2448
REMARK 465 TYR B 2449
REMARK 465 SER B 2450
REMARK 465 ALA B 2451
REMARK 465 GLY B 2452
REMARK 465 GLN B 2453
REMARK 465 SER B 2454
REMARK 465 VAL B 2455
REMARK 465 GLU B 2456
REMARK 465 ILE B 2457
REMARK 465 LEU B 2458
REMARK 465 ASP B 2459
REMARK 465 GLY B 2460
REMARK 465 VAL B 2461
REMARK 465 GLU B 2462
REMARK 465 LEU B 2463
REMARK 465 GLY B 2464
REMARK 465 GLU B 2465
REMARK 465 PRO B 2466
REMARK 465 ALA B 2467
REMARK 465 HIS B 2468
REMARK 465 LYS B 2469
REMARK 465 LYS B 2470
REMARK 465 THR B 2471
REMARK 465 GLY B 2472
REMARK 465 THR B 2473
REMARK 465 THR B 2474
REMARK 465 VAL B 2475
REMARK 465 PRO B 2476
REMARK 465 GLU B 2477
REMARK 465 SER B 2478
REMARK 465 ILE B 2479
REMARK 465 HIS B 2480
REMARK 465 SER B 2481
REMARK 465 PHE B 2482
REMARK 465 ILE B 2483
REMARK 465 GLY B 2484
REMARK 465 ASP B 2485
REMARK 465 GLY B 2486
REMARK 465 LEU B 2487
REMARK 465 VAL B 2488
REMARK 465 LYS B 2489
REMARK 465 PRO B 2490
REMARK 465 GLU B 2491
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 SER D 4
REMARK 465 PRO D 5
REMARK 465 GLY D 6
REMARK 465 THR D 7
REMARK 465 LEU D 325
REMARK 465 GLY D 326
REMARK 465 ASP A 1376
REMARK 465 ASP A 1377
REMARK 465 ASN A 1378
REMARK 465 GLY A 1379
REMARK 465 ILE A 1380
REMARK 465 VAL A 1381
REMARK 465 LEU A 1382
REMARK 465 LEU A 1383
REMARK 465 GLY A 1384
REMARK 465 LYS A 1815
REMARK 465 LYS A 1816
REMARK 465 LEU A 1817
REMARK 465 ARG A 1818
REMARK 465 HIS A 1819
REMARK 465 ALA A 1820
REMARK 465 SER A 1821
REMARK 465 GLY A 1822
REMARK 465 ALA A 1823
REMARK 465 ASN A 1824
REMARK 465 ILE A 1825
REMARK 465 THR A 1826
REMARK 465 ASN A 1827
REMARK 465 ALA A 1828
REMARK 465 THR A 1829
REMARK 465 THR A 1830
REMARK 465 ALA A 1831
REMARK 465 ALA A 1832
REMARK 465 THR A 1833
REMARK 465 THR A 1834
REMARK 465 ALA A 1835
REMARK 465 ALA A 1836
REMARK 465 THR A 1837
REMARK 465 ALA A 1838
REMARK 465 THR A 1839
REMARK 465 THR A 1840
REMARK 465 THR A 1841
REMARK 465 ALA A 1842
REMARK 465 SER A 1843
REMARK 465 THR A 1844
REMARK 465 GLU A 1845
REMARK 465 GLY A 1846
REMARK 465 SER A 1847
REMARK 465 ASN A 1848
REMARK 465 SER A 1849
REMARK 465 GLU A 1850
REMARK 465 SER A 1851
REMARK 465 GLU A 1852
REMARK 465 ALA A 1853
REMARK 465 GLU A 1854
REMARK 465 SER A 1855
REMARK 465 THR A 1856
REMARK 465 GLU A 1857
REMARK 465 ASN A 1858
REMARK 465 SER A 1859
REMARK 465 PRO A 1860
REMARK 465 THR A 1861
REMARK 465 PRO A 1862
REMARK 465 SER A 1863
REMARK 465 PRO A 1864
REMARK 465 LEU A 1865
REMARK 465 GLN A 1866
REMARK 465 LYS A 2437
REMARK 465 GLY A 2438
REMARK 465 ASN A 2439
REMARK 465 LYS A 2440
REMARK 465 ARG A 2441
REMARK 465 SER A 2442
REMARK 465 ARG A 2443
REMARK 465 THR A 2444
REMARK 465 ARG A 2445
REMARK 465 THR A 2446
REMARK 465 ASP A 2447
REMARK 465 SER A 2448
REMARK 465 TYR A 2449
REMARK 465 SER A 2450
REMARK 465 ALA A 2451
REMARK 465 GLY A 2452
REMARK 465 GLN A 2453
REMARK 465 SER A 2454
REMARK 465 VAL A 2455
REMARK 465 GLU A 2456
REMARK 465 ILE A 2457
REMARK 465 LEU A 2458
REMARK 465 ASP A 2459
REMARK 465 GLY A 2460
REMARK 465 VAL A 2461
REMARK 465 GLU A 2462
REMARK 465 LEU A 2463
REMARK 465 GLY A 2464
REMARK 465 GLU A 2465
REMARK 465 PRO A 2466
REMARK 465 ALA A 2467
REMARK 465 HIS A 2468
REMARK 465 LYS A 2469
REMARK 465 LYS A 2470
REMARK 465 THR A 2471
REMARK 465 GLY A 2472
REMARK 465 THR A 2473
REMARK 465 THR A 2474
REMARK 465 VAL A 2475
REMARK 465 PRO A 2476
REMARK 465 GLU A 2477
REMARK 465 SER A 2478
REMARK 465 ILE A 2479
REMARK 465 HIS A 2480
REMARK 465 SER A 2481
REMARK 465 PHE A 2482
REMARK 465 ILE A 2483
REMARK 465 GLY A 2484
REMARK 465 ASP A 2485
REMARK 465 GLY A 2486
REMARK 465 LEU A 2487
REMARK 465 VAL A 2488
REMARK 465 LYS A 2489
REMARK 465 PRO A 2490
REMARK 465 GLU A 2491
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 PRO C 5
REMARK 465 GLY C 6
REMARK 465 THR C 7
REMARK 465 LEU C 325
REMARK 465 GLY C 326
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 NH2 ARG A 2397 OE1 GLU A 2526 2.13
REMARK 500 O ILE A 1964 O TYR A 1967 2.13
REMARK 500 O ILE B 1964 O TYR B 1967 2.13
REMARK 500 NH2 ARG B 2397 OE1 GLU B 2526 2.15
REMARK 500 OD1 ASP D 106 OG1 THR D 108 2.18
REMARK 500 OD1 ASP C 106 OG1 THR C 108 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N LEU A 1607 O PRO A 1609 2554 1.39
REMARK 500 CA LEU A 1607 O PRO A 1609 2554 1.77
REMARK 500 O VAL A 1608 O VAL A 1608 2554 1.84
REMARK 500 C LYS A 1606 O PRO A 1609 2554 1.92
REMARK 500 N LEU A 1607 C PRO A 1609 2554 2.13
REMARK 500 C LEU A 1607 O PRO A 1609 2554 2.14
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 GLU B1444 -173.20 44.61
REMARK 500 ILE B1445 102.54 52.70
REMARK 500 HIS B1454 12.61 49.05
REMARK 500 ASN B1470 -141.85 -77.46
REMARK 500 LYS B1471 -132.15 -121.99
REMARK 500 ASP B1473 91.58 44.75
REMARK 500 LEU B1503 50.81 34.20
REMARK 500 GLN B1525 99.80 -38.45
REMARK 500 TYR B1583 -161.56 -75.22
REMARK 500 SER B1584 35.42 -73.31
REMARK 500 LYS B1606 -37.42 -131.21
REMARK 500 PRO B1609 18.18 -61.90
REMARK 500 GLU B1610 70.61 -118.58
REMARK 500 ARG B1611 11.18 -159.90
REMARK 500 ARG B1622 41.08 -73.25
REMARK 500 LEU B1623 -61.98 -140.84
REMARK 500 VAL B1630 -67.57 -11.83
REMARK 500 MET B1650 -71.20 5.47
REMARK 500 ARG B1665 65.04 -106.41
REMARK 500 ASP B1680 144.44 -25.04
REMARK 500 PRO B1681 44.42 -56.23
REMARK 500 SER B1682 74.34 19.69
REMARK 500 SER B1707 -148.26 -73.21
REMARK 500 ALA B1728 -75.10 -82.37
REMARK 500 GLU B1735 39.62 -59.27
REMARK 500 ASP B1736 87.76 -158.68
REMARK 500 ARG B1784 -63.20 59.79
REMARK 500 TRP B1786 102.40 100.54
REMARK 500 SER B1895 -74.46 -98.44
REMARK 500 ARG B1896 86.03 59.75
REMARK 500 ASN B1899 18.39 -141.11
REMARK 500 TYR B1913 52.35 -100.14
REMARK 500 ASP B1933 -59.76 -25.98
REMARK 500 GLN B1937 -23.47 -33.17
REMARK 500 ASP B1947 38.25 -84.59
REMARK 500 GLN B1970 -64.00 115.66
REMARK 500 LYS B1981 76.69 -116.91
REMARK 500 GLU B2000 -2.75 -54.29
REMARK 500 HIS B2001 -27.94 -153.86
REMARK 500 GLU B2041 -7.15 -150.02
REMARK 500 GLN B2072 -70.22 -65.15
REMARK 500 ASN B2093 -109.55 -76.49
REMARK 500 VAL B2094 -17.07 152.82
REMARK 500 LEU B2118 96.11 -65.80
REMARK 500 ASP B2135 72.14 24.36
REMARK 500 PRO B2141 116.11 -38.04
REMARK 500 ASN B2147 -38.86 87.42
REMARK 500 ILE B2153 99.29 -68.46
REMARK 500 ARG B2168 67.87 33.28
REMARK 500 LYS B2171 78.47 -105.75
REMARK 500
REMARK 500 THIS ENTRY HAS 191 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 1914 HIS B 1915 -128.10
REMARK 500 PRO D 169 GLU D 170 122.71
REMARK 500 GLY A 1914 HIS A 1915 -128.89
REMARK 500 PRO C 169 GLU C 170 122.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B1610 24.7 L L OUTSIDE RANGE
REMARK 500 LYS B1710 24.2 L L OUTSIDE RANGE
REMARK 500 TYR B1913 22.8 L L OUTSIDE RANGE
REMARK 500 HIS B1915 14.7 L L OUTSIDE RANGE
REMARK 500 GLU A1610 20.5 L L OUTSIDE RANGE
REMARK 500 LYS A1710 24.9 L L OUTSIDE RANGE
REMARK 500 TYR A1913 22.4 L L OUTSIDE RANGE
REMARK 500 HIS A1915 14.2 L L OUTSIDE RANGE
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 A3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AGS A3000 O2G
REMARK 620 2 AGS A3000 O1A 100.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AGS B3000 O2G
REMARK 620 2 AGS B3000 O1A 106.4
REMARK 620 3 ASN B2343 OD1 119.6 126.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AGS A3000 O3G
REMARK 620 2 AGS A3000 O1B 63.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JSN RELATED DB: PDB
REMARK 900 RELATED ID: 4JSV RELATED DB: PDB
REMARK 900 RELATED ID: 4JSX RELATED DB: PDB
REMARK 900 RELATED ID: 4JT5 RELATED DB: PDB
REMARK 900 RELATED ID: 4JT6 RELATED DB: PDB
DBREF 4JSP B 1376 2549 UNP P42345 MTOR_HUMAN 1376 2549
DBREF 4JSP D 1 326 UNP Q9BVC4 LST8_HUMAN 1 326
DBREF 4JSP A 1376 2549 UNP P42345 MTOR_HUMAN 1376 2549
DBREF 4JSP C 1 326 UNP Q9BVC4 LST8_HUMAN 1 326
SEQRES 1 B 1174 ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU ARG ALA ALA
SEQRES 2 B 1174 LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS TYR LYS GLU
SEQRES 3 B 1174 LEU GLU PHE GLN LYS GLY PRO THR PRO ALA ILE LEU GLU
SEQRES 4 B 1174 SER LEU ILE SER ILE ASN ASN LYS LEU GLN GLN PRO GLU
SEQRES 5 B 1174 ALA ALA ALA GLY VAL LEU GLU TYR ALA MET LYS HIS PHE
SEQRES 6 B 1174 GLY GLU LEU GLU ILE GLN ALA THR TRP TYR GLU LYS LEU
SEQRES 7 B 1174 HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR ASP LYS LYS
SEQRES 8 B 1174 MET ASP THR ASN LYS ASP ASP PRO GLU LEU MET LEU GLY
SEQRES 9 B 1174 ARG MET ARG CYS LEU GLU ALA LEU GLY GLU TRP GLY GLN
SEQRES 10 B 1174 LEU HIS GLN GLN CYS CYS GLU LYS TRP THR LEU VAL ASN
SEQRES 11 B 1174 ASP GLU THR GLN ALA LYS MET ALA ARG MET ALA ALA ALA
SEQRES 12 B 1174 ALA ALA TRP GLY LEU GLY GLN TRP ASP SER MET GLU GLU
SEQRES 13 B 1174 TYR THR CYS MET ILE PRO ARG ASP THR HIS ASP GLY ALA
SEQRES 14 B 1174 PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN ASP LEU PHE
SEQRES 15 B 1174 SER LEU ALA GLN GLN CYS ILE ASP LYS ALA ARG ASP LEU
SEQRES 16 B 1174 LEU ASP ALA GLU LEU THR ALA MET ALA GLY GLU SER TYR
SEQRES 17 B 1174 SER ARG ALA TYR GLY ALA MET VAL SER CYS HIS MET LEU
SEQRES 18 B 1174 SER GLU LEU GLU GLU VAL ILE GLN TYR LYS LEU VAL PRO
SEQRES 19 B 1174 GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP TRP GLU ARG
SEQRES 20 B 1174 LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP TRP GLN LYS
SEQRES 21 B 1174 ILE LEU MET VAL ARG SER LEU VAL VAL SER PRO HIS GLU
SEQRES 22 B 1174 ASP MET ARG THR TRP LEU LYS TYR ALA SER LEU CYS GLY
SEQRES 23 B 1174 LYS SER GLY ARG LEU ALA LEU ALA HIS LYS THR LEU VAL
SEQRES 24 B 1174 LEU LEU LEU GLY VAL ASP PRO SER ARG GLN LEU ASP HIS
SEQRES 25 B 1174 PRO LEU PRO THR VAL HIS PRO GLN VAL THR TYR ALA TYR
SEQRES 26 B 1174 MET LYS ASN MET TRP LYS SER ALA ARG LYS ILE ASP ALA
SEQRES 27 B 1174 PHE GLN HIS MET GLN HIS PHE VAL GLN THR MET GLN GLN
SEQRES 28 B 1174 GLN ALA GLN HIS ALA ILE ALA THR GLU ASP GLN GLN HIS
SEQRES 29 B 1174 LYS GLN GLU LEU HIS LYS LEU MET ALA ARG CYS PHE LEU
SEQRES 30 B 1174 LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN GLY ILE ASN
SEQRES 31 B 1174 GLU SER THR ILE PRO LYS VAL LEU GLN TYR TYR SER ALA
SEQRES 32 B 1174 ALA THR GLU HIS ASP ARG SER TRP TYR LYS ALA TRP HIS
SEQRES 33 B 1174 ALA TRP ALA VAL MET ASN PHE GLU ALA VAL LEU HIS TYR
SEQRES 34 B 1174 LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS LYS LYS LEU
SEQRES 35 B 1174 ARG HIS ALA SER GLY ALA ASN ILE THR ASN ALA THR THR
SEQRES 36 B 1174 ALA ALA THR THR ALA ALA THR ALA THR THR THR ALA SER
SEQRES 37 B 1174 THR GLU GLY SER ASN SER GLU SER GLU ALA GLU SER THR
SEQRES 38 B 1174 GLU ASN SER PRO THR PRO SER PRO LEU GLN LYS LYS VAL
SEQRES 39 B 1174 THR GLU ASP LEU SER LYS THR LEU LEU MET TYR THR VAL
SEQRES 40 B 1174 PRO ALA VAL GLN GLY PHE PHE ARG SER ILE SER LEU SER
SEQRES 41 B 1174 ARG GLY ASN ASN LEU GLN ASP THR LEU ARG VAL LEU THR
SEQRES 42 B 1174 LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP VAL ASN GLU
SEQRES 43 B 1174 ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN ILE ASP THR
SEQRES 44 B 1174 TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA ARG ILE ASP
SEQRES 45 B 1174 THR PRO ARG PRO LEU VAL GLY ARG LEU ILE HIS GLN LEU
SEQRES 46 B 1174 LEU THR ASP ILE GLY ARG TYR HIS PRO GLN ALA LEU ILE
SEQRES 47 B 1174 TYR PRO LEU THR VAL ALA SER LYS SER THR THR THR ALA
SEQRES 48 B 1174 ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS ASN MET CYS
SEQRES 49 B 1174 GLU HIS SER ASN THR LEU VAL GLN GLN ALA MET MET VAL
SEQRES 50 B 1174 SER GLU GLU LEU ILE ARG VAL ALA ILE LEU TRP HIS GLU
SEQRES 51 B 1174 MET TRP HIS GLU GLY LEU GLU GLU ALA SER ARG LEU TYR
SEQRES 52 B 1174 PHE GLY GLU ARG ASN VAL LYS GLY MET PHE GLU VAL LEU
SEQRES 53 B 1174 GLU PRO LEU HIS ALA MET MET GLU ARG GLY PRO GLN THR
SEQRES 54 B 1174 LEU LYS GLU THR SER PHE ASN GLN ALA TYR GLY ARG ASP
SEQRES 55 B 1174 LEU MET GLU ALA GLN GLU TRP CYS ARG LYS TYR MET LYS
SEQRES 56 B 1174 SER GLY ASN VAL LYS ASP LEU THR GLN ALA TRP ASP LEU
SEQRES 57 B 1174 TYR TYR HIS VAL PHE ARG ARG ILE SER LYS GLN LEU PRO
SEQRES 58 B 1174 GLN LEU THR SER LEU GLU LEU GLN TYR VAL SER PRO LYS
SEQRES 59 B 1174 LEU LEU MET CYS ARG ASP LEU GLU LEU ALA VAL PRO GLY
SEQRES 60 B 1174 THR TYR ASP PRO ASN GLN PRO ILE ILE ARG ILE GLN SER
SEQRES 61 B 1174 ILE ALA PRO SER LEU GLN VAL ILE THR SER LYS GLN ARG
SEQRES 62 B 1174 PRO ARG LYS LEU THR LEU MET GLY SER ASN GLY HIS GLU
SEQRES 63 B 1174 PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP LEU ARG GLN
SEQRES 64 B 1174 ASP GLU ARG VAL MET GLN LEU PHE GLY LEU VAL ASN THR
SEQRES 65 B 1174 LEU LEU ALA ASN ASP PRO THR SER LEU ARG LYS ASN LEU
SEQRES 66 B 1174 SER ILE GLN ARG TYR ALA VAL ILE PRO LEU SER THR ASN
SEQRES 67 B 1174 SER GLY LEU ILE GLY TRP VAL PRO HIS CYS ASP THR LEU
SEQRES 68 B 1174 HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS LYS LYS ILE
SEQRES 69 B 1174 LEU LEU ASN ILE GLU HIS ARG ILE MET LEU ARG MET ALA
SEQRES 70 B 1174 PRO ASP TYR ASP HIS LEU THR LEU MET GLN LYS VAL GLU
SEQRES 71 B 1174 VAL PHE GLU HIS ALA VAL ASN ASN THR ALA GLY ASP ASP
SEQRES 72 B 1174 LEU ALA LYS LEU LEU TRP LEU LYS SER PRO SER SER GLU
SEQRES 73 B 1174 VAL TRP PHE ASP ARG ARG THR ASN TYR THR ARG SER LEU
SEQRES 74 B 1174 ALA VAL MET SER MET VAL GLY TYR ILE LEU GLY LEU GLY
SEQRES 75 B 1174 ASP ARG HIS PRO SER ASN LEU MET LEU ASP ARG LEU SER
SEQRES 76 B 1174 GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP CYS PHE GLU
SEQRES 77 B 1174 VAL ALA MET THR ARG GLU LYS PHE PRO GLU LYS ILE PRO
SEQRES 78 B 1174 PHE ARG LEU THR ARG MET LEU THR ASN ALA MET GLU VAL
SEQRES 79 B 1174 THR GLY LEU ASP GLY ASN TYR ARG ILE THR CYS HIS THR
SEQRES 80 B 1174 VAL MET GLU VAL LEU ARG GLU HIS LYS ASP SER VAL MET
SEQRES 81 B 1174 ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO LEU LEU ASN
SEQRES 82 B 1174 TRP ARG LEU MET ASP THR ASN THR LYS GLY ASN LYS ARG
SEQRES 83 B 1174 SER ARG THR ARG THR ASP SER TYR SER ALA GLY GLN SER
SEQRES 84 B 1174 VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY GLU PRO ALA
SEQRES 85 B 1174 HIS LYS LYS THR GLY THR THR VAL PRO GLU SER ILE HIS
SEQRES 86 B 1174 SER PHE ILE GLY ASP GLY LEU VAL LYS PRO GLU ALA LEU
SEQRES 87 B 1174 ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG VAL ARG ASP
SEQRES 88 B 1174 LYS LEU THR GLY ARG ASP PHE SER HIS ASP ASP THR LEU
SEQRES 89 B 1174 ASP VAL PRO THR GLN VAL GLU LEU LEU ILE LYS GLN ALA
SEQRES 90 B 1174 THR SER HIS GLU ASN LEU CYS GLN CYS TYR ILE GLY TRP
SEQRES 91 B 1174 CYS PRO PHE TRP
SEQRES 1 D 326 MET ASN THR SER PRO GLY THR VAL GLY SER ASP PRO VAL
SEQRES 2 D 326 ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL ARG PHE
SEQRES 3 D 326 TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR VAL GLN
SEQRES 4 D 326 HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL THR PRO
SEQRES 5 D 326 ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN HIS ILE
SEQRES 6 D 326 ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN PRO ILE
SEQRES 7 D 326 ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA SER VAL
SEQRES 8 D 326 GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR GLY GLY
SEQRES 9 D 326 GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG SER ARG
SEQRES 10 D 326 ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN ALA PRO
SEQRES 11 D 326 ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA GLU LEU
SEQRES 12 D 326 ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE TRP ASP
SEQRES 13 D 326 LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO GLU PRO
SEQRES 14 D 326 GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO ASP ALA
SEQRES 15 D 326 SER TYR MET ALA ALA VAL ASN SER THR GLY ASN CYS TYR
SEQRES 16 D 326 VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU VAL THR
SEQRES 17 D 326 GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS THR ARG
SEQRES 18 D 326 TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER THR LEU
SEQRES 19 D 326 LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS ILE TRP
SEQRES 20 D 326 ARG THR SER ASN PHE SER LEU MET THR GLU LEU SER ILE
SEQRES 21 D 326 LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY TRP MET
SEQRES 22 D 326 TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR ILE VAL
SEQRES 23 D 326 THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP CYS VAL
SEQRES 24 D 326 GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY HIS GLN
SEQRES 25 D 326 LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER VAL LEU
SEQRES 26 D 326 GLY
SEQRES 1 A 1174 ASP ASP ASN GLY ILE VAL LEU LEU GLY GLU ARG ALA ALA
SEQRES 2 A 1174 LYS CYS ARG ALA TYR ALA LYS ALA LEU HIS TYR LYS GLU
SEQRES 3 A 1174 LEU GLU PHE GLN LYS GLY PRO THR PRO ALA ILE LEU GLU
SEQRES 4 A 1174 SER LEU ILE SER ILE ASN ASN LYS LEU GLN GLN PRO GLU
SEQRES 5 A 1174 ALA ALA ALA GLY VAL LEU GLU TYR ALA MET LYS HIS PHE
SEQRES 6 A 1174 GLY GLU LEU GLU ILE GLN ALA THR TRP TYR GLU LYS LEU
SEQRES 7 A 1174 HIS GLU TRP GLU ASP ALA LEU VAL ALA TYR ASP LYS LYS
SEQRES 8 A 1174 MET ASP THR ASN LYS ASP ASP PRO GLU LEU MET LEU GLY
SEQRES 9 A 1174 ARG MET ARG CYS LEU GLU ALA LEU GLY GLU TRP GLY GLN
SEQRES 10 A 1174 LEU HIS GLN GLN CYS CYS GLU LYS TRP THR LEU VAL ASN
SEQRES 11 A 1174 ASP GLU THR GLN ALA LYS MET ALA ARG MET ALA ALA ALA
SEQRES 12 A 1174 ALA ALA TRP GLY LEU GLY GLN TRP ASP SER MET GLU GLU
SEQRES 13 A 1174 TYR THR CYS MET ILE PRO ARG ASP THR HIS ASP GLY ALA
SEQRES 14 A 1174 PHE TYR ARG ALA VAL LEU ALA LEU HIS GLN ASP LEU PHE
SEQRES 15 A 1174 SER LEU ALA GLN GLN CYS ILE ASP LYS ALA ARG ASP LEU
SEQRES 16 A 1174 LEU ASP ALA GLU LEU THR ALA MET ALA GLY GLU SER TYR
SEQRES 17 A 1174 SER ARG ALA TYR GLY ALA MET VAL SER CYS HIS MET LEU
SEQRES 18 A 1174 SER GLU LEU GLU GLU VAL ILE GLN TYR LYS LEU VAL PRO
SEQRES 19 A 1174 GLU ARG ARG GLU ILE ILE ARG GLN ILE TRP TRP GLU ARG
SEQRES 20 A 1174 LEU GLN GLY CYS GLN ARG ILE VAL GLU ASP TRP GLN LYS
SEQRES 21 A 1174 ILE LEU MET VAL ARG SER LEU VAL VAL SER PRO HIS GLU
SEQRES 22 A 1174 ASP MET ARG THR TRP LEU LYS TYR ALA SER LEU CYS GLY
SEQRES 23 A 1174 LYS SER GLY ARG LEU ALA LEU ALA HIS LYS THR LEU VAL
SEQRES 24 A 1174 LEU LEU LEU GLY VAL ASP PRO SER ARG GLN LEU ASP HIS
SEQRES 25 A 1174 PRO LEU PRO THR VAL HIS PRO GLN VAL THR TYR ALA TYR
SEQRES 26 A 1174 MET LYS ASN MET TRP LYS SER ALA ARG LYS ILE ASP ALA
SEQRES 27 A 1174 PHE GLN HIS MET GLN HIS PHE VAL GLN THR MET GLN GLN
SEQRES 28 A 1174 GLN ALA GLN HIS ALA ILE ALA THR GLU ASP GLN GLN HIS
SEQRES 29 A 1174 LYS GLN GLU LEU HIS LYS LEU MET ALA ARG CYS PHE LEU
SEQRES 30 A 1174 LYS LEU GLY GLU TRP GLN LEU ASN LEU GLN GLY ILE ASN
SEQRES 31 A 1174 GLU SER THR ILE PRO LYS VAL LEU GLN TYR TYR SER ALA
SEQRES 32 A 1174 ALA THR GLU HIS ASP ARG SER TRP TYR LYS ALA TRP HIS
SEQRES 33 A 1174 ALA TRP ALA VAL MET ASN PHE GLU ALA VAL LEU HIS TYR
SEQRES 34 A 1174 LYS HIS GLN ASN GLN ALA ARG ASP GLU LYS LYS LYS LEU
SEQRES 35 A 1174 ARG HIS ALA SER GLY ALA ASN ILE THR ASN ALA THR THR
SEQRES 36 A 1174 ALA ALA THR THR ALA ALA THR ALA THR THR THR ALA SER
SEQRES 37 A 1174 THR GLU GLY SER ASN SER GLU SER GLU ALA GLU SER THR
SEQRES 38 A 1174 GLU ASN SER PRO THR PRO SER PRO LEU GLN LYS LYS VAL
SEQRES 39 A 1174 THR GLU ASP LEU SER LYS THR LEU LEU MET TYR THR VAL
SEQRES 40 A 1174 PRO ALA VAL GLN GLY PHE PHE ARG SER ILE SER LEU SER
SEQRES 41 A 1174 ARG GLY ASN ASN LEU GLN ASP THR LEU ARG VAL LEU THR
SEQRES 42 A 1174 LEU TRP PHE ASP TYR GLY HIS TRP PRO ASP VAL ASN GLU
SEQRES 43 A 1174 ALA LEU VAL GLU GLY VAL LYS ALA ILE GLN ILE ASP THR
SEQRES 44 A 1174 TRP LEU GLN VAL ILE PRO GLN LEU ILE ALA ARG ILE ASP
SEQRES 45 A 1174 THR PRO ARG PRO LEU VAL GLY ARG LEU ILE HIS GLN LEU
SEQRES 46 A 1174 LEU THR ASP ILE GLY ARG TYR HIS PRO GLN ALA LEU ILE
SEQRES 47 A 1174 TYR PRO LEU THR VAL ALA SER LYS SER THR THR THR ALA
SEQRES 48 A 1174 ARG HIS ASN ALA ALA ASN LYS ILE LEU LYS ASN MET CYS
SEQRES 49 A 1174 GLU HIS SER ASN THR LEU VAL GLN GLN ALA MET MET VAL
SEQRES 50 A 1174 SER GLU GLU LEU ILE ARG VAL ALA ILE LEU TRP HIS GLU
SEQRES 51 A 1174 MET TRP HIS GLU GLY LEU GLU GLU ALA SER ARG LEU TYR
SEQRES 52 A 1174 PHE GLY GLU ARG ASN VAL LYS GLY MET PHE GLU VAL LEU
SEQRES 53 A 1174 GLU PRO LEU HIS ALA MET MET GLU ARG GLY PRO GLN THR
SEQRES 54 A 1174 LEU LYS GLU THR SER PHE ASN GLN ALA TYR GLY ARG ASP
SEQRES 55 A 1174 LEU MET GLU ALA GLN GLU TRP CYS ARG LYS TYR MET LYS
SEQRES 56 A 1174 SER GLY ASN VAL LYS ASP LEU THR GLN ALA TRP ASP LEU
SEQRES 57 A 1174 TYR TYR HIS VAL PHE ARG ARG ILE SER LYS GLN LEU PRO
SEQRES 58 A 1174 GLN LEU THR SER LEU GLU LEU GLN TYR VAL SER PRO LYS
SEQRES 59 A 1174 LEU LEU MET CYS ARG ASP LEU GLU LEU ALA VAL PRO GLY
SEQRES 60 A 1174 THR TYR ASP PRO ASN GLN PRO ILE ILE ARG ILE GLN SER
SEQRES 61 A 1174 ILE ALA PRO SER LEU GLN VAL ILE THR SER LYS GLN ARG
SEQRES 62 A 1174 PRO ARG LYS LEU THR LEU MET GLY SER ASN GLY HIS GLU
SEQRES 63 A 1174 PHE VAL PHE LEU LEU LYS GLY HIS GLU ASP LEU ARG GLN
SEQRES 64 A 1174 ASP GLU ARG VAL MET GLN LEU PHE GLY LEU VAL ASN THR
SEQRES 65 A 1174 LEU LEU ALA ASN ASP PRO THR SER LEU ARG LYS ASN LEU
SEQRES 66 A 1174 SER ILE GLN ARG TYR ALA VAL ILE PRO LEU SER THR ASN
SEQRES 67 A 1174 SER GLY LEU ILE GLY TRP VAL PRO HIS CYS ASP THR LEU
SEQRES 68 A 1174 HIS ALA LEU ILE ARG ASP TYR ARG GLU LYS LYS LYS ILE
SEQRES 69 A 1174 LEU LEU ASN ILE GLU HIS ARG ILE MET LEU ARG MET ALA
SEQRES 70 A 1174 PRO ASP TYR ASP HIS LEU THR LEU MET GLN LYS VAL GLU
SEQRES 71 A 1174 VAL PHE GLU HIS ALA VAL ASN ASN THR ALA GLY ASP ASP
SEQRES 72 A 1174 LEU ALA LYS LEU LEU TRP LEU LYS SER PRO SER SER GLU
SEQRES 73 A 1174 VAL TRP PHE ASP ARG ARG THR ASN TYR THR ARG SER LEU
SEQRES 74 A 1174 ALA VAL MET SER MET VAL GLY TYR ILE LEU GLY LEU GLY
SEQRES 75 A 1174 ASP ARG HIS PRO SER ASN LEU MET LEU ASP ARG LEU SER
SEQRES 76 A 1174 GLY LYS ILE LEU HIS ILE ASP PHE GLY ASP CYS PHE GLU
SEQRES 77 A 1174 VAL ALA MET THR ARG GLU LYS PHE PRO GLU LYS ILE PRO
SEQRES 78 A 1174 PHE ARG LEU THR ARG MET LEU THR ASN ALA MET GLU VAL
SEQRES 79 A 1174 THR GLY LEU ASP GLY ASN TYR ARG ILE THR CYS HIS THR
SEQRES 80 A 1174 VAL MET GLU VAL LEU ARG GLU HIS LYS ASP SER VAL MET
SEQRES 81 A 1174 ALA VAL LEU GLU ALA PHE VAL TYR ASP PRO LEU LEU ASN
SEQRES 82 A 1174 TRP ARG LEU MET ASP THR ASN THR LYS GLY ASN LYS ARG
SEQRES 83 A 1174 SER ARG THR ARG THR ASP SER TYR SER ALA GLY GLN SER
SEQRES 84 A 1174 VAL GLU ILE LEU ASP GLY VAL GLU LEU GLY GLU PRO ALA
SEQRES 85 A 1174 HIS LYS LYS THR GLY THR THR VAL PRO GLU SER ILE HIS
SEQRES 86 A 1174 SER PHE ILE GLY ASP GLY LEU VAL LYS PRO GLU ALA LEU
SEQRES 87 A 1174 ASN LYS LYS ALA ILE GLN ILE ILE ASN ARG VAL ARG ASP
SEQRES 88 A 1174 LYS LEU THR GLY ARG ASP PHE SER HIS ASP ASP THR LEU
SEQRES 89 A 1174 ASP VAL PRO THR GLN VAL GLU LEU LEU ILE LYS GLN ALA
SEQRES 90 A 1174 THR SER HIS GLU ASN LEU CYS GLN CYS TYR ILE GLY TRP
SEQRES 91 A 1174 CYS PRO PHE TRP
SEQRES 1 C 326 MET ASN THR SER PRO GLY THR VAL GLY SER ASP PRO VAL
SEQRES 2 C 326 ILE LEU ALA THR ALA GLY TYR ASP HIS THR VAL ARG PHE
SEQRES 3 C 326 TRP GLN ALA HIS SER GLY ILE CYS THR ARG THR VAL GLN
SEQRES 4 C 326 HIS GLN ASP SER GLN VAL ASN ALA LEU GLU VAL THR PRO
SEQRES 5 C 326 ASP ARG SER MET ILE ALA ALA ALA GLY TYR GLN HIS ILE
SEQRES 6 C 326 ARG MET TYR ASP LEU ASN SER ASN ASN PRO ASN PRO ILE
SEQRES 7 C 326 ILE SER TYR ASP GLY VAL ASN LYS ASN ILE ALA SER VAL
SEQRES 8 C 326 GLY PHE HIS GLU ASP GLY ARG TRP MET TYR THR GLY GLY
SEQRES 9 C 326 GLU ASP CYS THR ALA ARG ILE TRP ASP LEU ARG SER ARG
SEQRES 10 C 326 ASN LEU GLN CYS GLN ARG ILE PHE GLN VAL ASN ALA PRO
SEQRES 11 C 326 ILE ASN CYS VAL CYS LEU HIS PRO ASN GLN ALA GLU LEU
SEQRES 12 C 326 ILE VAL GLY ASP GLN SER GLY ALA ILE HIS ILE TRP ASP
SEQRES 13 C 326 LEU LYS THR ASP HIS ASN GLU GLN LEU ILE PRO GLU PRO
SEQRES 14 C 326 GLU VAL SER ILE THR SER ALA HIS ILE ASP PRO ASP ALA
SEQRES 15 C 326 SER TYR MET ALA ALA VAL ASN SER THR GLY ASN CYS TYR
SEQRES 16 C 326 VAL TRP ASN LEU THR GLY GLY ILE GLY ASP GLU VAL THR
SEQRES 17 C 326 GLN LEU ILE PRO LYS THR LYS ILE PRO ALA HIS THR ARG
SEQRES 18 C 326 TYR ALA LEU GLN CYS ARG PHE SER PRO ASP SER THR LEU
SEQRES 19 C 326 LEU ALA THR CYS SER ALA ASP GLN THR CYS LYS ILE TRP
SEQRES 20 C 326 ARG THR SER ASN PHE SER LEU MET THR GLU LEU SER ILE
SEQRES 21 C 326 LYS SER GLY ASN PRO GLY GLU SER SER ARG GLY TRP MET
SEQRES 22 C 326 TRP GLY CYS ALA PHE SER GLY ASP SER GLN TYR ILE VAL
SEQRES 23 C 326 THR ALA SER SER ASP ASN LEU ALA ARG LEU TRP CYS VAL
SEQRES 24 C 326 GLU THR GLY GLU ILE LYS ARG GLU TYR GLY GLY HIS GLN
SEQRES 25 C 326 LYS ALA VAL VAL CYS LEU ALA PHE ASN ASP SER VAL LEU
SEQRES 26 C 326 GLY
HET AGS B3000 31
HET MG B3001 1
HET MG B3002 1
HET AGS A3000 31
HET MG A3001 1
HET MG A3002 1
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
HETSYN 2 AGS ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-
HETSYN 3 AGS DIPHOSPHATE MONOTHIOPHOSPHATE
FORMUL 5 AGS 2(C10 H16 N5 O12 P3 S)
FORMUL 6 MG 4(MG 2+)
HELIX 1 1 GLU B 1385 GLY B 1407 1 23
HELIX 2 2 THR B 1409 LEU B 1423 1 15
HELIX 3 3 GLN B 1425 PHE B 1440 1 16
HELIX 4 4 ILE B 1445 LEU B 1453 1 9
HELIX 5 5 GLU B 1455 ASN B 1470 1 16
HELIX 6 6 ASP B 1473 GLY B 1488 1 16
HELIX 7 7 GLU B 1489 GLU B 1499 1 11
HELIX 8 8 ASP B 1506 LEU B 1523 1 18
HELIX 9 9 GLN B 1525 CYS B 1534 1 10
HELIX 10 10 THR B 1540 ASP B 1555 1 16
HELIX 11 11 LEU B 1556 MET B 1578 1 23
HELIX 12 12 GLY B 1588 TYR B 1605 1 18
HELIX 13 13 GLU B 1613 GLY B 1625 1 13
HELIX 14 14 ILE B 1629 LEU B 1642 1 14
HELIX 15 15 SER B 1645 MET B 1650 1 6
HELIX 16 16 MET B 1650 SER B 1663 1 14
HELIX 17 17 ARG B 1665 GLY B 1678 1 14
HELIX 18 18 HIS B 1693 SER B 1707 1 15
HELIX 19 19 ARG B 1709 HIS B 1730 1 22
HELIX 20 20 GLN B 1737 GLY B 1763 1 27
HELIX 21 21 SER B 1767 ARG B 1784 1 18
HELIX 22 22 TRP B 1786 ASP B 1812 1 27
HELIX 23 23 LYS B 1868 SER B 1893 1 26
HELIX 24 24 ASN B 1899 TYR B 1913 1 15
HELIX 25 25 TRP B 1916 ILE B 1930 1 15
HELIX 26 26 GLN B 1931 GLN B 1937 5 7
HELIX 27 27 VAL B 1938 ALA B 1944 1 7
HELIX 28 28 ARG B 1950 TYR B 1967 1 18
HELIX 29 29 LEU B 1972 LYS B 1981 1 10
HELIX 30 30 THR B 1984 ILE B 2021 1 38
HELIX 31 31 LEU B 2022 GLY B 2040 1 19
HELIX 32 32 ASN B 2043 ARG B 2060 1 18
HELIX 33 33 THR B 2064 GLY B 2092 1 29
HELIX 34 34 LYS B 2095 LEU B 2115 1 21
HELIX 35 35 PRO B 2116 LEU B 2118 5 3
HELIX 36 36 LEU B 2123 SER B 2127 1 5
HELIX 37 37 SER B 2127 CYS B 2133 1 7
HELIX 38 38 LEU B 2192 ASP B 2212 1 21
HELIX 39 39 ASP B 2212 LYS B 2218 1 7
HELIX 40 40 LEU B 2246 LYS B 2257 1 12
HELIX 41 41 ASN B 2262 ALA B 2272 1 11
HELIX 42 42 ASP B 2274 LEU B 2278 5 5
HELIX 43 43 THR B 2279 ASN B 2292 1 14
HELIX 44 44 ASP B 2297 SER B 2307 1 11
HELIX 45 45 SER B 2310 GLY B 2335 1 26
HELIX 46 46 GLU B 2363 ARG B 2368 1 6
HELIX 47 47 THR B 2380 MET B 2387 1 8
HELIX 48 48 GLY B 2394 HIS B 2410 1 17
HELIX 49 49 HIS B 2410 TYR B 2423 1 14
HELIX 50 50 ASP B 2424 ASN B 2435 5 12
HELIX 51 51 LEU B 2493 THR B 2509 1 17
HELIX 52 52 ASP B 2520 SER B 2534 1 15
HELIX 53 53 SER B 2534 CYS B 2539 1 6
HELIX 54 54 GLN B 2540 CYS B 2541 5 2
HELIX 55 55 TYR B 2542 CYS B 2546 5 5
HELIX 56 56 ARG A 1386 GLY A 1407 1 22
HELIX 57 57 THR A 1409 LEU A 1423 1 15
HELIX 58 58 GLN A 1425 PHE A 1440 1 16
HELIX 59 59 ILE A 1445 LEU A 1453 1 9
HELIX 60 60 GLU A 1455 ASN A 1470 1 16
HELIX 61 61 ASP A 1473 GLY A 1488 1 16
HELIX 62 62 GLU A 1489 GLU A 1499 1 11
HELIX 63 63 ASP A 1506 LEU A 1523 1 18
HELIX 64 64 GLN A 1525 CYS A 1534 1 10
HELIX 65 65 THR A 1540 ASP A 1555 1 16
HELIX 66 66 LEU A 1556 MET A 1578 1 23
HELIX 67 67 GLY A 1588 TYR A 1605 1 18
HELIX 68 68 GLU A 1613 GLY A 1625 1 13
HELIX 69 69 ILE A 1629 SER A 1641 1 13
HELIX 70 70 SER A 1645 MET A 1650 1 6
HELIX 71 71 MET A 1650 SER A 1663 1 14
HELIX 72 72 ARG A 1665 GLY A 1678 1 14
HELIX 73 73 HIS A 1693 SER A 1707 1 15
HELIX 74 74 ARG A 1709 HIS A 1730 1 22
HELIX 75 75 GLN A 1737 GLY A 1763 1 27
HELIX 76 76 SER A 1767 ARG A 1784 1 18
HELIX 77 77 TRP A 1786 ASP A 1812 1 27
HELIX 78 78 LYS A 1868 SER A 1893 1 26
HELIX 79 79 ASN A 1899 TYR A 1913 1 15
HELIX 80 80 TRP A 1916 ILE A 1930 1 15
HELIX 81 81 GLN A 1931 GLN A 1937 5 7
HELIX 82 82 VAL A 1938 ALA A 1944 1 7
HELIX 83 83 ARG A 1950 TYR A 1967 1 18
HELIX 84 84 LEU A 1972 LYS A 1981 1 10
HELIX 85 85 THR A 1984 ILE A 2021 1 38
HELIX 86 86 LEU A 2022 GLY A 2040 1 19
HELIX 87 87 ASN A 2043 ARG A 2060 1 18
HELIX 88 88 THR A 2064 GLY A 2092 1 29
HELIX 89 89 LYS A 2095 LEU A 2115 1 21
HELIX 90 90 PRO A 2116 LEU A 2118 5 3
HELIX 91 91 LEU A 2123 SER A 2127 1 5
HELIX 92 92 SER A 2127 CYS A 2133 1 7
HELIX 93 93 LEU A 2192 ASP A 2212 1 21
HELIX 94 94 ASP A 2212 LYS A 2218 1 7
HELIX 95 95 LEU A 2246 LYS A 2257 1 12
HELIX 96 96 ASN A 2262 ALA A 2272 1 11
HELIX 97 97 ASP A 2274 LEU A 2278 5 5
HELIX 98 98 THR A 2279 ASN A 2292 1 14
HELIX 99 99 ASP A 2297 SER A 2307 1 11
HELIX 100 100 SER A 2310 GLY A 2335 1 26
HELIX 101 101 GLU A 2363 ARG A 2368 1 6
HELIX 102 102 THR A 2380 MET A 2387 1 8
HELIX 103 103 GLY A 2394 HIS A 2410 1 17
HELIX 104 104 HIS A 2410 TYR A 2423 1 14
HELIX 105 105 ASP A 2424 ASN A 2435 5 12
HELIX 106 106 LEU A 2493 THR A 2509 1 17
HELIX 107 107 ASP A 2520 SER A 2534 1 15
HELIX 108 108 SER A 2534 CYS A 2539 1 6
HELIX 109 109 GLN A 2540 CYS A 2541 5 2
HELIX 110 110 TYR A 2542 CYS A 2546 5 5
SHEET 1 A 3 SER B2120 GLU B2122 0
SHEET 2 A 3 SER B2159 VAL B2162 -1 O LEU B2160 N LEU B2121
SHEET 3 A 3 ARG B2170 LYS B2171 -1 O LYS B2171 N GLN B2161
SHEET 1 B 5 ILE B2153 ILE B2156 0
SHEET 2 B 5 THR B2173 GLY B2176 -1 O MET B2175 N SER B2155
SHEET 3 B 5 GLU B2181 LYS B2187 -1 O PHE B2182 N LEU B2174
SHEET 4 B 5 GLY B2235 GLY B2238 -1 O GLY B2235 N LYS B2187
SHEET 5 B 5 VAL B2227 PRO B2229 -1 N ILE B2228 O LEU B2236
SHEET 1 C 3 CYS B2243 THR B2245 0
SHEET 2 C 3 LEU B2344 ASP B2347 -1 O LEU B2346 N ASP B2244
SHEET 3 C 3 ILE B2353 HIS B2355 -1 O LEU B2354 N MET B2345
SHEET 1 D 4 CYS D 34 GLN D 39 0
SHEET 2 D 4 THR D 23 TRP D 27 -1 N PHE D 26 O ARG D 36
SHEET 3 D 4 VAL D 13 GLY D 19 -1 N LEU D 15 O TRP D 27
SHEET 4 D 4 VAL D 315 ASP D 322 -1 O VAL D 316 N ALA D 18
SHEET 1 E 4 ALA D 47 VAL D 50 0
SHEET 2 E 4 ILE D 57 ALA D 60 -1 O ALA D 58 N GLU D 49
SHEET 3 E 4 ILE D 65 TYR D 68 -1 O ARG D 66 N ALA D 59
SHEET 4 E 4 ILE D 79 TYR D 81 -1 O ILE D 79 N MET D 67
SHEET 1 F 4 ILE D 88 PHE D 93 0
SHEET 2 F 4 TRP D 99 GLY D 104 -1 O TYR D 101 N GLY D 92
SHEET 3 F 4 THR D 108 ASP D 113 -1 O TRP D 112 N MET D 100
SHEET 4 F 4 ARG D 123 GLN D 126 -1 O PHE D 125 N ALA D 109
SHEET 1 G 4 ILE D 131 LEU D 136 0
SHEET 2 G 4 GLU D 142 ASP D 147 -1 O ILE D 144 N CYS D 135
SHEET 3 G 4 ILE D 152 ASP D 156 -1 O HIS D 153 N VAL D 145
SHEET 4 G 4 ASN D 162 LEU D 165 -1 O LEU D 165 N ILE D 152
SHEET 1 H 4 ILE D 173 ILE D 178 0
SHEET 2 H 4 TYR D 184 ASN D 189 -1 O ALA D 186 N HIS D 177
SHEET 3 H 4 CYS D 194 THR D 200 -1 O TYR D 195 N ALA D 187
SHEET 4 H 4 GLN D 209 ILE D 216 -1 O ILE D 211 N ASN D 198
SHEET 1 I 4 ALA D 223 PHE D 228 0
SHEET 2 I 4 LEU D 234 SER D 239 -1 O ALA D 236 N ARG D 227
SHEET 3 I 4 THR D 243 ARG D 248 -1 O TRP D 247 N LEU D 235
SHEET 4 I 4 LEU D 254 SER D 259 -1 O LEU D 258 N CYS D 244
SHEET 1 J 4 MET D 273 PHE D 278 0
SHEET 2 J 4 TYR D 284 SER D 289 -1 O ALA D 288 N GLY D 275
SHEET 3 J 4 LEU D 293 CYS D 298 -1 O TRP D 297 N ILE D 285
SHEET 4 J 4 GLU D 303 GLY D 309 -1 O TYR D 308 N ALA D 294
SHEET 1 K 3 LEU A2121 GLU A2122 0
SHEET 2 K 3 SER A2159 VAL A2162 -1 O LEU A2160 N LEU A2121
SHEET 3 K 3 ARG A2170 LYS A2171 -1 O LYS A2171 N GLN A2161
SHEET 1 L 5 ILE A2153 ILE A2156 0
SHEET 2 L 5 THR A2173 GLY A2176 -1 O MET A2175 N SER A2155
SHEET 3 L 5 GLU A2181 LYS A2187 -1 O PHE A2182 N LEU A2174
SHEET 4 L 5 GLY A2235 GLY A2238 -1 O GLY A2235 N LYS A2187
SHEET 5 L 5 VAL A2227 PRO A2229 -1 N ILE A2228 O LEU A2236
SHEET 1 M 3 CYS A2243 THR A2245 0
SHEET 2 M 3 LEU A2344 ASP A2347 -1 O LEU A2346 N ASP A2244
SHEET 3 M 3 ILE A2353 HIS A2355 -1 O LEU A2354 N MET A2345
SHEET 1 N 4 CYS C 34 GLN C 39 0
SHEET 2 N 4 THR C 23 TRP C 27 -1 N PHE C 26 O ARG C 36
SHEET 3 N 4 VAL C 13 GLY C 19 -1 N THR C 17 O ARG C 25
SHEET 4 N 4 VAL C 315 ASP C 322 -1 O VAL C 316 N ALA C 18
SHEET 1 O 4 ALA C 47 VAL C 50 0
SHEET 2 O 4 ILE C 57 ALA C 60 -1 O ALA C 58 N GLU C 49
SHEET 3 O 4 ILE C 65 TYR C 68 -1 O ARG C 66 N ALA C 59
SHEET 4 O 4 ILE C 79 TYR C 81 -1 O ILE C 79 N MET C 67
SHEET 1 P 4 ILE C 88 PHE C 93 0
SHEET 2 P 4 TRP C 99 GLY C 104 -1 O TYR C 101 N GLY C 92
SHEET 3 P 4 THR C 108 ASP C 113 -1 O TRP C 112 N MET C 100
SHEET 4 P 4 ARG C 123 GLN C 126 -1 O PHE C 125 N ALA C 109
SHEET 1 Q 4 ILE C 131 LEU C 136 0
SHEET 2 Q 4 GLU C 142 ASP C 147 -1 O ILE C 144 N CYS C 135
SHEET 3 Q 4 ILE C 152 ASP C 156 -1 O HIS C 153 N VAL C 145
SHEET 4 Q 4 ASN C 162 LEU C 165 -1 O LEU C 165 N ILE C 152
SHEET 1 R 4 ILE C 173 ILE C 178 0
SHEET 2 R 4 TYR C 184 ASN C 189 -1 O ALA C 186 N HIS C 177
SHEET 3 R 4 CYS C 194 THR C 200 -1 O TYR C 195 N ALA C 187
SHEET 4 R 4 GLN C 209 ILE C 216 -1 O ILE C 211 N ASN C 198
SHEET 1 S 4 ALA C 223 PHE C 228 0
SHEET 2 S 4 LEU C 234 SER C 239 -1 O ALA C 236 N ARG C 227
SHEET 3 S 4 THR C 243 ARG C 248 -1 O TRP C 247 N LEU C 235
SHEET 4 S 4 LEU C 254 SER C 259 -1 O LEU C 258 N CYS C 244
SHEET 1 T 4 MET C 273 PHE C 278 0
SHEET 2 T 4 TYR C 284 SER C 289 -1 O VAL C 286 N ALA C 277
SHEET 3 T 4 LEU C 293 CYS C 298 -1 O TRP C 297 N ILE C 285
SHEET 4 T 4 GLU C 303 GLY C 309 -1 O TYR C 308 N ALA C 294
LINK O2G AGS A3000 MG MG A3001 1555 1555 1.85
LINK O2G AGS B3000 MG MG B3001 1555 1555 2.21
LINK O3G AGS B3000 MG MG B3002 1555 1555 2.22
LINK O3G AGS A3000 MG MG A3002 1555 1555 2.53
LINK O1A AGS B3000 MG MG B3001 1555 1555 2.77
LINK O1A AGS A3000 MG MG A3001 1555 1555 2.84
LINK O1B AGS A3000 MG MG A3002 1555 1555 2.86
LINK OD1 ASN B2343 MG MG B3001 1555 1555 2.93
SITE 1 AC1 12 SER B2165 GLN B2167 LEU B2185 LYS B2187
SITE 2 AC1 12 GLU B2190 TYR B2225 ILE B2237 GLY B2238
SITE 3 AC1 12 TRP B2239 VAL B2240 MG B3001 MG B3002
SITE 1 AC2 4 ASN B2343 ASP B2357 AGS B3000 MG B3002
SITE 1 AC3 4 GLU B2190 ASP B2357 AGS B3000 MG B3001
SITE 1 AC4 11 SER A2165 GLN A2167 LEU A2185 LYS A2187
SITE 2 AC4 11 GLU A2190 GLY A2238 TRP A2239 VAL A2240
SITE 3 AC4 11 MET A2345 MG A3001 MG A3002
SITE 1 AC5 2 ASN A2343 AGS A3000
SITE 1 AC6 3 GLU A2190 ASP A2357 AGS A3000
CRYST1 139.400 163.200 207.800 90.00 90.00 90.00 P 2 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 0.007174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
