HEADER RECOMBINATION 06-MAY-17 5NWL
TITLE CRYSTAL STRUCTURE OF A HUMAN RAD51-ATP FILAMENT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPAIR PROTEIN RAD51 HOMOLOG 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;
COMPND 4 SYNONYM: HRAD51,RAD51 HOMOLOG A;
COMPND 5 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: RAD51, RAD51A, RECA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA
KEYWDS ATPASE, DNA-STRAND EXCHANGE, HOMOLOGOUS RECOMBINATION, DOUBLE-STRAND
KEYWDS 2 DNA BREAK REPAIR, RECOMBINATION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PELLEGRINI,T.MOSCHETTI
REVDAT 3 17-JAN-24 5NWL 1 LINK
REVDAT 2 18-APR-18 5NWL 1 JRNL
REVDAT 1 07-MAR-18 5NWL 0
JRNL AUTH I.BROUWER,T.MOSCHETTI,A.CANDELLI,E.B.GARCIN,M.MODESTI,
JRNL AUTH 2 L.PELLEGRINI,G.J.WUITE,E.J.PETERMAN
JRNL TITL TWO DISTINCT CONFORMATIONAL STATES DEFINE THE INTERACTION OF
JRNL TITL 2 HUMAN RAD51-ATP WITH SINGLE-STRANDED DNA.
JRNL REF EMBO J. V. 37 2018
JRNL REFN ESSN 1460-2075
JRNL PMID 29507080
JRNL DOI 10.15252/EMBJ.201798162
REMARK 2
REMARK 2 RESOLUTION. 3.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 61077
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.271
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 5960
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1434 - 12.1517 0.98 3721 172 0.2243 0.2529
REMARK 3 2 12.1517 - 9.6692 0.99 3714 215 0.1682 0.2149
REMARK 3 3 9.6692 - 8.4540 0.99 3754 178 0.1801 0.2308
REMARK 3 4 8.4540 - 7.6842 0.99 3780 206 0.2192 0.3186
REMARK 3 5 7.6842 - 7.1352 0.99 3749 210 0.2322 0.2734
REMARK 3 6 7.1352 - 6.7157 0.99 3692 214 0.2541 0.2969
REMARK 3 7 6.7157 - 6.3801 0.99 3738 209 0.2624 0.3236
REMARK 3 8 6.3801 - 6.1029 0.99 3761 214 0.2782 0.3059
REMARK 3 9 6.1029 - 5.8683 0.99 3678 188 0.2925 0.3215
REMARK 3 10 5.8683 - 5.6661 0.99 3828 201 0.2729 0.3204
REMARK 3 11 5.6661 - 5.4892 0.99 3755 189 0.2812 0.3333
REMARK 3 12 5.4892 - 5.3325 0.99 3733 176 0.3073 0.3382
REMARK 3 13 5.3325 - 5.1923 0.98 3746 194 0.3132 0.3754
REMARK 3 14 5.1923 - 5.0657 0.98 3690 185 0.3085 0.3876
REMARK 3 15 5.0657 - 4.9507 0.99 3809 152 0.2954 0.3314
REMARK 3 16 4.9507 - 4.8454 0.99 3785 200 0.2797 0.3283
REMARK 3 17 4.8454 - 4.7486 0.99 3780 182 0.2813 0.3119
REMARK 3 18 4.7486 - 4.6590 0.99 3724 212 0.2850 0.3628
REMARK 3 19 4.6590 - 4.5759 0.98 3683 179 0.2985 0.3336
REMARK 3 20 4.5759 - 4.4984 0.99 3815 194 0.3029 0.3412
REMARK 3 21 4.4984 - 4.4259 0.99 3676 231 0.3252 0.3911
REMARK 3 22 4.4259 - 4.3578 0.99 3692 204 0.3165 0.3873
REMARK 3 23 4.3578 - 4.2938 0.99 3841 191 0.3164 0.3456
REMARK 3 24 4.2938 - 4.2333 0.98 3617 227 0.3362 0.3941
REMARK 3 25 4.2333 - 4.1761 0.96 3653 194 0.3374 0.3542
REMARK 3 26 4.1761 - 4.1219 0.97 3670 206 0.3557 0.4053
REMARK 3 27 4.1219 - 4.0704 0.97 3634 225 0.3569 0.3878
REMARK 3 28 4.0704 - 4.0214 0.96 3615 240 0.3564 0.3879
REMARK 3 29 4.0214 - 3.9747 0.94 3565 194 0.3632 0.3583
REMARK 3 30 3.9747 - 3.9300 0.92 3475 178 0.3609 0.4006
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.760
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 128.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 33271
REMARK 3 ANGLE : 0.429 44908
REMARK 3 CHIRALITY : 0.038 5121
REMARK 3 PLANARITY : 0.002 5774
REMARK 3 DIHEDRAL : 9.358 20132
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95373
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61077
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.930
REMARK 200 RESOLUTION RANGE LOW (A) : 49.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.28700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 2.88800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1N0W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MES PH 5.2 MPD, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 64.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -193.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -192.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, K, L, M, N
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 MET A 3
REMARK 465 GLN A 4
REMARK 465 MET A 5
REMARK 465 GLN A 6
REMARK 465 LEU A 7
REMARK 465 GLU A 8
REMARK 465 ALA A 9
REMARK 465 ASN A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 THR A 13
REMARK 465 SER A 14
REMARK 465 VAL A 15
REMARK 465 GLU A 16
REMARK 465 GLU A 17
REMARK 465 GLU A 18
REMARK 465 SER A 19
REMARK 465 PHE A 20
REMARK 465 ALA A 271
REMARK 465 GLN A 272
REMARK 465 VAL A 273
REMARK 465 ASP A 274
REMARK 465 GLY A 275
REMARK 465 ALA A 276
REMARK 465 ALA A 277
REMARK 465 MET A 278
REMARK 465 PHE A 279
REMARK 465 ALA A 280
REMARK 465 ALA A 281
REMARK 465 ASP A 282
REMARK 465 PRO A 283
REMARK 465 LYS A 284
REMARK 465 LYS A 285
REMARK 465 PRO A 286
REMARK 465 ILE A 287
REMARK 465 GLY A 288
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 MET B 3
REMARK 465 GLN B 4
REMARK 465 MET B 5
REMARK 465 GLN B 6
REMARK 465 LEU B 7
REMARK 465 GLU B 8
REMARK 465 ALA B 9
REMARK 465 ASN B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 THR B 13
REMARK 465 SER B 14
REMARK 465 VAL B 15
REMARK 465 GLU B 16
REMARK 465 GLU B 17
REMARK 465 GLU B 18
REMARK 465 SER B 19
REMARK 465 PHE B 20
REMARK 465 ALA B 271
REMARK 465 GLN B 272
REMARK 465 VAL B 273
REMARK 465 ASP B 274
REMARK 465 GLY B 275
REMARK 465 ALA B 276
REMARK 465 ALA B 277
REMARK 465 MET B 278
REMARK 465 PHE B 279
REMARK 465 ALA B 280
REMARK 465 ALA B 281
REMARK 465 ASP B 282
REMARK 465 PRO B 283
REMARK 465 LYS B 284
REMARK 465 LYS B 285
REMARK 465 PRO B 286
REMARK 465 ILE B 287
REMARK 465 GLY B 288
REMARK 465 GLY B 289
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 MET C 3
REMARK 465 GLN C 4
REMARK 465 MET C 5
REMARK 465 GLN C 6
REMARK 465 LEU C 7
REMARK 465 GLU C 8
REMARK 465 ALA C 9
REMARK 465 ASN C 10
REMARK 465 ALA C 11
REMARK 465 ASP C 12
REMARK 465 THR C 13
REMARK 465 SER C 14
REMARK 465 VAL C 15
REMARK 465 GLU C 16
REMARK 465 GLU C 17
REMARK 465 GLU C 18
REMARK 465 SER C 19
REMARK 465 PHE C 20
REMARK 465 ALA C 271
REMARK 465 GLN C 272
REMARK 465 VAL C 273
REMARK 465 ASP C 274
REMARK 465 GLY C 275
REMARK 465 ALA C 276
REMARK 465 ALA C 277
REMARK 465 MET C 278
REMARK 465 PHE C 279
REMARK 465 ALA C 280
REMARK 465 ALA C 281
REMARK 465 ASP C 282
REMARK 465 PRO C 283
REMARK 465 LYS C 284
REMARK 465 LYS C 285
REMARK 465 PRO C 286
REMARK 465 ILE C 287
REMARK 465 GLY C 288
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 MET D 3
REMARK 465 GLN D 4
REMARK 465 MET D 5
REMARK 465 GLN D 6
REMARK 465 LEU D 7
REMARK 465 GLU D 8
REMARK 465 ALA D 9
REMARK 465 ASN D 10
REMARK 465 ALA D 11
REMARK 465 ASP D 12
REMARK 465 THR D 13
REMARK 465 SER D 14
REMARK 465 VAL D 15
REMARK 465 GLU D 16
REMARK 465 GLU D 17
REMARK 465 GLU D 18
REMARK 465 SER D 19
REMARK 465 PHE D 20
REMARK 465 ALA D 271
REMARK 465 GLN D 272
REMARK 465 VAL D 273
REMARK 465 ASP D 274
REMARK 465 GLY D 275
REMARK 465 ALA D 276
REMARK 465 ALA D 277
REMARK 465 MET D 278
REMARK 465 PHE D 279
REMARK 465 ALA D 280
REMARK 465 ALA D 281
REMARK 465 ASP D 282
REMARK 465 PRO D 283
REMARK 465 LYS D 284
REMARK 465 LYS D 285
REMARK 465 PRO D 286
REMARK 465 ILE D 287
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 MET E 3
REMARK 465 GLN E 4
REMARK 465 MET E 5
REMARK 465 GLN E 6
REMARK 465 LEU E 7
REMARK 465 GLU E 8
REMARK 465 ALA E 9
REMARK 465 ASN E 10
REMARK 465 ALA E 11
REMARK 465 ASP E 12
REMARK 465 THR E 13
REMARK 465 SER E 14
REMARK 465 VAL E 15
REMARK 465 GLU E 16
REMARK 465 GLU E 17
REMARK 465 GLU E 18
REMARK 465 SER E 19
REMARK 465 PHE E 20
REMARK 465 ALA E 271
REMARK 465 GLN E 272
REMARK 465 VAL E 273
REMARK 465 ASP E 274
REMARK 465 GLY E 275
REMARK 465 ALA E 276
REMARK 465 ALA E 277
REMARK 465 MET E 278
REMARK 465 PHE E 279
REMARK 465 ALA E 280
REMARK 465 ALA E 281
REMARK 465 ASP E 282
REMARK 465 PRO E 283
REMARK 465 LYS E 284
REMARK 465 LYS E 285
REMARK 465 PRO E 286
REMARK 465 ILE E 287
REMARK 465 GLY E 288
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 MET F 3
REMARK 465 GLN F 4
REMARK 465 MET F 5
REMARK 465 GLN F 6
REMARK 465 LEU F 7
REMARK 465 GLU F 8
REMARK 465 ALA F 9
REMARK 465 ASN F 10
REMARK 465 ALA F 11
REMARK 465 ASP F 12
REMARK 465 THR F 13
REMARK 465 SER F 14
REMARK 465 VAL F 15
REMARK 465 GLU F 16
REMARK 465 GLU F 17
REMARK 465 GLU F 18
REMARK 465 SER F 19
REMARK 465 PHE F 20
REMARK 465 VAL F 270
REMARK 465 ALA F 271
REMARK 465 GLN F 272
REMARK 465 VAL F 273
REMARK 465 ASP F 274
REMARK 465 GLY F 275
REMARK 465 ALA F 276
REMARK 465 ALA F 277
REMARK 465 MET F 278
REMARK 465 PHE F 279
REMARK 465 ALA F 280
REMARK 465 ALA F 281
REMARK 465 ASP F 282
REMARK 465 PRO F 283
REMARK 465 LYS F 284
REMARK 465 LYS F 285
REMARK 465 PRO F 286
REMARK 465 ILE F 287
REMARK 465 GLY F 288
REMARK 465 GLY F 289
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 MET G 3
REMARK 465 GLN G 4
REMARK 465 MET G 5
REMARK 465 GLN G 6
REMARK 465 LEU G 7
REMARK 465 GLU G 8
REMARK 465 ALA G 9
REMARK 465 ASN G 10
REMARK 465 ALA G 11
REMARK 465 ASP G 12
REMARK 465 THR G 13
REMARK 465 SER G 14
REMARK 465 VAL G 15
REMARK 465 GLU G 16
REMARK 465 GLU G 17
REMARK 465 GLU G 18
REMARK 465 SER G 19
REMARK 465 PHE G 20
REMARK 465 ALA G 271
REMARK 465 GLN G 272
REMARK 465 VAL G 273
REMARK 465 ASP G 274
REMARK 465 GLY G 275
REMARK 465 ALA G 276
REMARK 465 ALA G 277
REMARK 465 MET G 278
REMARK 465 PHE G 279
REMARK 465 ALA G 280
REMARK 465 ALA G 281
REMARK 465 ASP G 282
REMARK 465 PRO G 283
REMARK 465 LYS G 284
REMARK 465 LYS G 285
REMARK 465 PRO G 286
REMARK 465 ILE G 287
REMARK 465 GLY G 288
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 MET H 3
REMARK 465 GLN H 4
REMARK 465 MET H 5
REMARK 465 GLN H 6
REMARK 465 LEU H 7
REMARK 465 GLU H 8
REMARK 465 ALA H 9
REMARK 465 ASN H 10
REMARK 465 ALA H 11
REMARK 465 ASP H 12
REMARK 465 THR H 13
REMARK 465 SER H 14
REMARK 465 VAL H 15
REMARK 465 GLU H 16
REMARK 465 GLU H 17
REMARK 465 GLU H 18
REMARK 465 SER H 19
REMARK 465 PHE H 20
REMARK 465 ALA H 271
REMARK 465 GLN H 272
REMARK 465 VAL H 273
REMARK 465 ASP H 274
REMARK 465 GLY H 275
REMARK 465 ALA H 276
REMARK 465 ALA H 277
REMARK 465 MET H 278
REMARK 465 PHE H 279
REMARK 465 ALA H 280
REMARK 465 ALA H 281
REMARK 465 ASP H 282
REMARK 465 PRO H 283
REMARK 465 LYS H 284
REMARK 465 LYS H 285
REMARK 465 PRO H 286
REMARK 465 ILE H 287
REMARK 465 GLY H 288
REMARK 465 GLY H 289
REMARK 465 ASN H 290
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 MET I 3
REMARK 465 GLN I 4
REMARK 465 MET I 5
REMARK 465 GLN I 6
REMARK 465 LEU I 7
REMARK 465 GLU I 8
REMARK 465 ALA I 9
REMARK 465 ASN I 10
REMARK 465 ALA I 11
REMARK 465 ASP I 12
REMARK 465 THR I 13
REMARK 465 SER I 14
REMARK 465 VAL I 15
REMARK 465 GLU I 16
REMARK 465 GLU I 17
REMARK 465 GLU I 18
REMARK 465 SER I 19
REMARK 465 PHE I 20
REMARK 465 ALA I 271
REMARK 465 GLN I 272
REMARK 465 VAL I 273
REMARK 465 ASP I 274
REMARK 465 GLY I 275
REMARK 465 ALA I 276
REMARK 465 ALA I 277
REMARK 465 MET I 278
REMARK 465 PHE I 279
REMARK 465 ALA I 280
REMARK 465 ALA I 281
REMARK 465 ASP I 282
REMARK 465 PRO I 283
REMARK 465 LYS I 284
REMARK 465 LYS I 285
REMARK 465 PRO I 286
REMARK 465 ILE I 287
REMARK 465 GLY I 288
REMARK 465 GLY I 289
REMARK 465 MET J 1
REMARK 465 ALA J 2
REMARK 465 MET J 3
REMARK 465 GLN J 4
REMARK 465 MET J 5
REMARK 465 GLN J 6
REMARK 465 LEU J 7
REMARK 465 GLU J 8
REMARK 465 ALA J 9
REMARK 465 ASN J 10
REMARK 465 ALA J 11
REMARK 465 ASP J 12
REMARK 465 THR J 13
REMARK 465 SER J 14
REMARK 465 VAL J 15
REMARK 465 GLU J 16
REMARK 465 GLU J 17
REMARK 465 GLU J 18
REMARK 465 SER J 19
REMARK 465 PHE J 20
REMARK 465 ALA J 271
REMARK 465 GLN J 272
REMARK 465 VAL J 273
REMARK 465 ASP J 274
REMARK 465 GLY J 275
REMARK 465 ALA J 276
REMARK 465 ALA J 277
REMARK 465 MET J 278
REMARK 465 PHE J 279
REMARK 465 ALA J 280
REMARK 465 ALA J 281
REMARK 465 ASP J 282
REMARK 465 PRO J 283
REMARK 465 LYS J 284
REMARK 465 LYS J 285
REMARK 465 PRO J 286
REMARK 465 ILE J 287
REMARK 465 GLY J 288
REMARK 465 GLY J 289
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 MET K 3
REMARK 465 GLN K 4
REMARK 465 MET K 5
REMARK 465 GLN K 6
REMARK 465 LEU K 7
REMARK 465 GLU K 8
REMARK 465 ALA K 9
REMARK 465 ASN K 10
REMARK 465 ALA K 11
REMARK 465 ASP K 12
REMARK 465 THR K 13
REMARK 465 SER K 14
REMARK 465 VAL K 15
REMARK 465 GLU K 16
REMARK 465 GLU K 17
REMARK 465 GLU K 18
REMARK 465 SER K 19
REMARK 465 PHE K 20
REMARK 465 ALA K 271
REMARK 465 GLN K 272
REMARK 465 VAL K 273
REMARK 465 ASP K 274
REMARK 465 GLY K 275
REMARK 465 ALA K 276
REMARK 465 ALA K 277
REMARK 465 MET K 278
REMARK 465 PHE K 279
REMARK 465 ALA K 280
REMARK 465 ALA K 281
REMARK 465 ASP K 282
REMARK 465 PRO K 283
REMARK 465 LYS K 284
REMARK 465 LYS K 285
REMARK 465 PRO K 286
REMARK 465 ILE K 287
REMARK 465 GLY K 288
REMARK 465 MET L 1
REMARK 465 ALA L 2
REMARK 465 MET L 3
REMARK 465 GLN L 4
REMARK 465 MET L 5
REMARK 465 GLN L 6
REMARK 465 LEU L 7
REMARK 465 GLU L 8
REMARK 465 ALA L 9
REMARK 465 ASN L 10
REMARK 465 ALA L 11
REMARK 465 ASP L 12
REMARK 465 THR L 13
REMARK 465 SER L 14
REMARK 465 VAL L 15
REMARK 465 GLU L 16
REMARK 465 GLU L 17
REMARK 465 GLU L 18
REMARK 465 SER L 19
REMARK 465 PHE L 20
REMARK 465 ALA L 271
REMARK 465 GLN L 272
REMARK 465 VAL L 273
REMARK 465 ASP L 274
REMARK 465 GLY L 275
REMARK 465 ALA L 276
REMARK 465 ALA L 277
REMARK 465 MET L 278
REMARK 465 PHE L 279
REMARK 465 ALA L 280
REMARK 465 ALA L 281
REMARK 465 ASP L 282
REMARK 465 PRO L 283
REMARK 465 LYS L 284
REMARK 465 LYS L 285
REMARK 465 PRO L 286
REMARK 465 ILE L 287
REMARK 465 GLY L 288
REMARK 465 MET M 1
REMARK 465 ALA M 2
REMARK 465 MET M 3
REMARK 465 GLN M 4
REMARK 465 MET M 5
REMARK 465 GLN M 6
REMARK 465 LEU M 7
REMARK 465 GLU M 8
REMARK 465 ALA M 9
REMARK 465 ASN M 10
REMARK 465 ALA M 11
REMARK 465 ASP M 12
REMARK 465 THR M 13
REMARK 465 SER M 14
REMARK 465 VAL M 15
REMARK 465 GLU M 16
REMARK 465 GLU M 17
REMARK 465 GLU M 18
REMARK 465 SER M 19
REMARK 465 PHE M 20
REMARK 465 ALA M 271
REMARK 465 GLN M 272
REMARK 465 VAL M 273
REMARK 465 ASP M 274
REMARK 465 GLY M 275
REMARK 465 ALA M 276
REMARK 465 ALA M 277
REMARK 465 MET M 278
REMARK 465 PHE M 279
REMARK 465 ALA M 280
REMARK 465 ALA M 281
REMARK 465 ASP M 282
REMARK 465 PRO M 283
REMARK 465 LYS M 284
REMARK 465 LYS M 285
REMARK 465 PRO M 286
REMARK 465 ILE M 287
REMARK 465 GLY M 288
REMARK 465 GLY M 289
REMARK 465 MET N 1
REMARK 465 ALA N 2
REMARK 465 MET N 3
REMARK 465 GLN N 4
REMARK 465 MET N 5
REMARK 465 GLN N 6
REMARK 465 LEU N 7
REMARK 465 GLU N 8
REMARK 465 ALA N 9
REMARK 465 ASN N 10
REMARK 465 ALA N 11
REMARK 465 ASP N 12
REMARK 465 THR N 13
REMARK 465 SER N 14
REMARK 465 VAL N 15
REMARK 465 GLU N 16
REMARK 465 GLU N 17
REMARK 465 GLU N 18
REMARK 465 SER N 19
REMARK 465 PHE N 20
REMARK 465 ALA N 271
REMARK 465 GLN N 272
REMARK 465 VAL N 273
REMARK 465 ASP N 274
REMARK 465 GLY N 275
REMARK 465 ALA N 276
REMARK 465 ALA N 277
REMARK 465 MET N 278
REMARK 465 PHE N 279
REMARK 465 ALA N 280
REMARK 465 ALA N 281
REMARK 465 ASP N 282
REMARK 465 PRO N 283
REMARK 465 LYS N 284
REMARK 465 LYS N 285
REMARK 465 PRO N 286
REMARK 465 ILE N 287
REMARK 465 GLY N 288
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 229 O GLN A 268 2.00
REMARK 500 NH2 ARG H 229 O GLN H 268 2.07
REMARK 500 NH2 ARG K 229 O GLN K 268 2.15
REMARK 500 NH2 ARG C 229 O GLN C 268 2.19
REMARK 500 NH2 ARG F 229 O GLN F 268 2.19
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 GLN A 23 88.15 58.90
REMARK 500 PRO A 56 -161.52 -72.34
REMARK 500 ALA A 293 -71.33 -66.02
REMARK 500 TYR A 315 -83.03 -96.63
REMARK 500 GLN B 23 88.75 58.99
REMARK 500 PRO B 56 -161.64 -72.17
REMARK 500 ALA B 293 -71.65 -65.45
REMARK 500 TYR B 315 -83.50 -96.89
REMARK 500 GLN C 23 88.70 58.83
REMARK 500 PRO C 56 -161.30 -72.38
REMARK 500 ALA C 293 -70.35 -66.12
REMARK 500 TYR C 315 -83.03 -97.17
REMARK 500 ALA C 337 -76.47 -25.63
REMARK 500 GLN D 23 89.71 59.19
REMARK 500 PRO D 56 -162.54 -72.40
REMARK 500 ALA D 293 -70.88 -65.84
REMARK 500 TYR D 315 -82.95 -96.77
REMARK 500 GLN E 23 88.15 59.16
REMARK 500 PRO E 56 -160.98 -72.63
REMARK 500 TYR E 315 -83.23 -96.54
REMARK 500 GLN F 23 88.85 59.09
REMARK 500 PRO F 56 -162.50 -72.84
REMARK 500 ALA F 293 -71.18 -65.76
REMARK 500 TYR F 315 -83.78 -96.47
REMARK 500 GLN G 23 88.32 59.01
REMARK 500 PRO G 56 -162.47 -72.76
REMARK 500 ALA G 293 -70.86 -66.57
REMARK 500 TYR G 315 -83.74 -97.13
REMARK 500 GLN H 23 89.00 58.87
REMARK 500 PRO H 56 -163.13 -73.06
REMARK 500 ALA H 293 -70.68 -66.10
REMARK 500 TYR H 315 -82.95 -97.31
REMARK 500 GLN I 23 88.09 58.98
REMARK 500 PRO I 56 -161.57 -72.24
REMARK 500 ALA I 293 -70.56 -65.63
REMARK 500 TYR I 315 -82.82 -96.52
REMARK 500 GLN J 23 87.53 58.79
REMARK 500 PRO J 56 -161.86 -72.04
REMARK 500 TYR J 315 -82.38 -97.27
REMARK 500 GLN K 23 89.74 59.02
REMARK 500 PRO K 56 -163.66 -71.88
REMARK 500 TYR K 315 -83.31 -96.71
REMARK 500 GLN L 23 87.29 58.84
REMARK 500 PRO L 56 -161.34 -72.14
REMARK 500 ALA L 293 -70.47 -67.68
REMARK 500 TYR L 315 -83.41 -97.38
REMARK 500 GLN M 23 88.81 58.99
REMARK 500 PRO M 56 -161.60 -72.93
REMARK 500 ALA M 293 -70.73 -65.66
REMARK 500 TYR M 315 -83.26 -96.29
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 134 OG1
REMARK 620 2 ATP A 402 O1G 118.2
REMARK 620 3 ATP A 402 O1B 78.7 65.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 134 OG1
REMARK 620 2 ATP B 402 O3G 135.4
REMARK 620 3 ATP B 402 O1B 77.3 67.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 134 OG1
REMARK 620 2 ATP C 402 O3G 133.2
REMARK 620 3 ATP C 402 O1B 72.0 62.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 134 OG1
REMARK 620 2 ATP D 402 O2B 71.4
REMARK 620 3 ATP D 402 O2G 119.8 63.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 134 OG1
REMARK 620 2 ATP E 402 O2G 108.1
REMARK 620 3 ATP E 402 O2B 70.3 65.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 134 OG1
REMARK 620 2 ATP F 402 O1G 124.8
REMARK 620 3 ATP F 402 O2B 74.6 65.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 134 OG1
REMARK 620 2 ATP G 402 O1G 124.3
REMARK 620 3 ATP G 402 O2B 74.4 64.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR H 134 OG1
REMARK 620 2 ATP H 402 O3G 107.2
REMARK 620 3 ATP H 402 O1B 75.1 64.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 134 OG1
REMARK 620 2 ASP I 222 OD2 60.7
REMARK 620 3 ATP I 402 O3G 122.2 144.1
REMARK 620 4 ATP I 402 O2B 65.8 121.8 59.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR J 134 OG1
REMARK 620 2 ATP J 402 O2G 101.9
REMARK 620 3 ATP J 402 O2B 74.1 64.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 134 OG1
REMARK 620 2 ATP K 402 O2B 74.9
REMARK 620 3 ATP K 402 O2G 116.9 67.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR L 134 OG1
REMARK 620 2 ATP L 402 O2B 73.3
REMARK 620 3 ATP L 402 O1G 119.6 64.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR M 134 OG1
REMARK 620 2 ATP M 402 O1G 111.2
REMARK 620 3 ATP M 402 O1B 70.6 65.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR N 134 OG1
REMARK 620 2 ATP N 402 O1G 124.8
REMARK 620 3 ATP N 402 O1B 74.9 65.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP I 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP J 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP K 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP L 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP M 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP N 402
DBREF 5NWL A 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL B 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL C 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL D 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL E 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL F 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL G 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL H 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL I 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL J 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL K 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL L 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL M 1 339 UNP Q06609 RAD51_HUMAN 1 339
DBREF 5NWL N 1 339 UNP Q06609 RAD51_HUMAN 1 339
SEQRES 1 A 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 A 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 A 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 A 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 A 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 A 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 A 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 A 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 A 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 A 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 A 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 A 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 A 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 A 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 A 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 A 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 A 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 A 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 A 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 A 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 A 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 A 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 A 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 A 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 A 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 A 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 A 339 ASP
SEQRES 1 B 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 B 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 B 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 B 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 B 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 B 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 B 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 B 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 B 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 B 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 B 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 B 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 B 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 B 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 B 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 B 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 B 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 B 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 B 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 B 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 B 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 B 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 B 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 B 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 B 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 B 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 B 339 ASP
SEQRES 1 C 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 C 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 C 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 C 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 C 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 C 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 C 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 C 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 C 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 C 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 C 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 C 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 C 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 C 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 C 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 C 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 C 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 C 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 C 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 C 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 C 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 C 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 C 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 C 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 C 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 C 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 C 339 ASP
SEQRES 1 D 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 D 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 D 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 D 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 D 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 D 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 D 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 D 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 D 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 D 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 D 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 D 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 D 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 D 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 D 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 D 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 D 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 D 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 D 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 D 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 D 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 D 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 D 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 D 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 D 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 D 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 D 339 ASP
SEQRES 1 E 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 E 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 E 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 E 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 E 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 E 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 E 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 E 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 E 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 E 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 E 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 E 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 E 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 E 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 E 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 E 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 E 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 E 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 E 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 E 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 E 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 E 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 E 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 E 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 E 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 E 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 E 339 ASP
SEQRES 1 F 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 F 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 F 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 F 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 F 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 F 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 F 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 F 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 F 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 F 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 F 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 F 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 F 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 F 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 F 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 F 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 F 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 F 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 F 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 F 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 F 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 F 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 F 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 F 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 F 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 F 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 F 339 ASP
SEQRES 1 G 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 G 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 G 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 G 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 G 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 G 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 G 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 G 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 G 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 G 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 G 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 G 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 G 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 G 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 G 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 G 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 G 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 G 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 G 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 G 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 G 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 G 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 G 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 G 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 G 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 G 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 G 339 ASP
SEQRES 1 H 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 H 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 H 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 H 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 H 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 H 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 H 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 H 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 H 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 H 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 H 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 H 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 H 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 H 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 H 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 H 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 H 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 H 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 H 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 H 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 H 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 H 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 H 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 H 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 H 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 H 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 H 339 ASP
SEQRES 1 I 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 I 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 I 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 I 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 I 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 I 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 I 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 I 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 I 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 I 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 I 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 I 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 I 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 I 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 I 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 I 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 I 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 I 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 I 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 I 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 I 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 I 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 I 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 I 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 I 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 I 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 I 339 ASP
SEQRES 1 J 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 J 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 J 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 J 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 J 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 J 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 J 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 J 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 J 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 J 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 J 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 J 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 J 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 J 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 J 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 J 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 J 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 J 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 J 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 J 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 J 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 J 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 J 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 J 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 J 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 J 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 J 339 ASP
SEQRES 1 K 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 K 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 K 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 K 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 K 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 K 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 K 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 K 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 K 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 K 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 K 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 K 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 K 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 K 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 K 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 K 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 K 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 K 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 K 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 K 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 K 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 K 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 K 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 K 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 K 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 K 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 K 339 ASP
SEQRES 1 L 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 L 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 L 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 L 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 L 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 L 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 L 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 L 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 L 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 L 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 L 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 L 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 L 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 L 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 L 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 L 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 L 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 L 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 L 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 L 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 L 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 L 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 L 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 L 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 L 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 L 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 L 339 ASP
SEQRES 1 M 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 M 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 M 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 M 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 M 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 M 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 M 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 M 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 M 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 M 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 M 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 M 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 M 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 M 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 M 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 M 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 M 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 M 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 M 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 M 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 M 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 M 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 M 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 M 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 M 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 M 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 M 339 ASP
SEQRES 1 N 339 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR
SEQRES 2 N 339 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER
SEQRES 3 N 339 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS
SEQRES 4 N 339 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL
SEQRES 5 N 339 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY
SEQRES 6 N 339 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA
SEQRES 7 N 339 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU
SEQRES 8 N 339 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR
SEQRES 9 N 339 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE
SEQRES 10 N 339 GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG
SEQRES 11 N 339 THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR
SEQRES 12 N 339 CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS
SEQRES 13 N 339 ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU
SEQRES 14 N 339 ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY
SEQRES 15 N 339 SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE
SEQRES 16 N 339 ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER
SEQRES 17 N 339 ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL
SEQRES 18 N 339 ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY
SEQRES 19 N 339 ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG
SEQRES 20 N 339 PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY
SEQRES 21 N 339 VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL
SEQRES 22 N 339 ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO
SEQRES 23 N 339 ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG
SEQRES 24 N 339 LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS
SEQRES 25 N 339 LYS ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA
SEQRES 26 N 339 MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS
SEQRES 27 N 339 ASP
HET MG A 401 1
HET ATP A 402 31
HET MG B 401 1
HET ATP B 402 31
HET MG C 401 1
HET ATP C 402 31
HET MG D 401 1
HET ATP D 402 31
HET MG E 401 1
HET ATP E 402 31
HET MG F 401 1
HET ATP F 402 31
HET MG G 401 1
HET ATP G 402 31
HET MG H 401 1
HET ATP H 402 31
HET MG I 401 1
HET ATP I 402 31
HET MG J 401 1
HET ATP J 402 31
HET MG K 401 1
HET ATP K 402 31
HET MG L 401 1
HET ATP L 402 31
HET MG M 401 1
HET ATP M 402 31
HET MG N 401 1
HET ATP N 402 31
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 15 MG 14(MG 2+)
FORMUL 16 ATP 14(C10 H16 N5 O13 P3)
HELIX 1 AA1 ILE A 25 GLN A 30 1 6
HELIX 2 AA2 ASN A 34 GLY A 45 1 12
HELIX 3 AA3 THR A 48 ALA A 55 1 8
HELIX 4 AA4 PRO A 56 ASN A 62 1 7
HELIX 5 AA5 SER A 67 VAL A 82 1 16
HELIX 6 AA6 ALA A 89 GLU A 98 1 10
HELIX 7 AA7 SER A 106 LEU A 113 1 8
HELIX 8 AA8 GLY A 132 CYS A 144 1 13
HELIX 9 AA9 GLN A 145 LEU A 146 5 2
HELIX 10 AB1 PRO A 147 GLY A 151 5 5
HELIX 11 AB2 ARG A 167 TYR A 178 1 12
HELIX 12 AB3 SER A 181 ASN A 188 1 8
HELIX 13 AB4 ASN A 196 SER A 214 1 19
HELIX 14 AB5 ALA A 226 ASP A 231 1 6
HELIX 15 AB6 GLU A 237 GLY A 260 1 24
HELIX 16 AB7 GLY A 289 ALA A 293 5 5
HELIX 17 AB8 ILE B 25 GLN B 30 1 6
HELIX 18 AB9 ASN B 34 GLY B 45 1 12
HELIX 19 AC1 THR B 48 ALA B 55 1 8
HELIX 20 AC2 PRO B 56 ASN B 62 1 7
HELIX 21 AC3 SER B 67 VAL B 82 1 16
HELIX 22 AC4 ALA B 89 GLU B 98 1 10
HELIX 23 AC5 SER B 106 LEU B 113 1 8
HELIX 24 AC6 GLY B 132 CYS B 144 1 13
HELIX 25 AC7 GLN B 145 LEU B 146 5 2
HELIX 26 AC8 PRO B 147 GLY B 151 5 5
HELIX 27 AC9 ARG B 167 TYR B 178 1 12
HELIX 28 AD1 SER B 181 ASN B 188 1 8
HELIX 29 AD2 ASN B 196 SER B 214 1 19
HELIX 30 AD3 ALA B 226 ASP B 231 1 6
HELIX 31 AD4 GLU B 237 GLY B 260 1 24
HELIX 32 AD5 ILE C 25 CYS C 31 1 7
HELIX 33 AD6 ASN C 34 GLY C 45 1 12
HELIX 34 AD7 THR C 48 ALA C 55 1 8
HELIX 35 AD8 PRO C 56 ASN C 62 1 7
HELIX 36 AD9 SER C 67 VAL C 82 1 16
HELIX 37 AE1 ALA C 89 GLU C 98 1 10
HELIX 38 AE2 SER C 106 LEU C 113 1 8
HELIX 39 AE3 GLY C 132 CYS C 144 1 13
HELIX 40 AE4 GLN C 145 LEU C 146 5 2
HELIX 41 AE5 PRO C 147 GLY C 151 5 5
HELIX 42 AE6 ARG C 167 TYR C 178 1 12
HELIX 43 AE7 SER C 181 ASN C 188 1 8
HELIX 44 AE8 ASN C 196 SER C 214 1 19
HELIX 45 AE9 ALA C 226 ASP C 231 1 6
HELIX 46 AF1 GLU C 237 GLY C 260 1 24
HELIX 47 AF2 GLY C 289 ALA C 293 5 5
HELIX 48 AF3 ILE D 25 GLN D 30 1 6
HELIX 49 AF4 ASN D 34 GLY D 45 1 12
HELIX 50 AF5 THR D 48 ALA D 55 1 8
HELIX 51 AF6 PRO D 56 ASN D 62 1 7
HELIX 52 AF7 SER D 67 VAL D 82 1 16
HELIX 53 AF8 ALA D 89 GLU D 98 1 10
HELIX 54 AF9 SER D 106 LEU D 113 1 8
HELIX 55 AG1 GLY D 132 CYS D 144 1 13
HELIX 56 AG2 GLN D 145 LEU D 146 5 2
HELIX 57 AG3 PRO D 147 GLY D 151 5 5
HELIX 58 AG4 ARG D 167 TYR D 178 1 12
HELIX 59 AG5 SER D 181 ASN D 188 1 8
HELIX 60 AG6 ASN D 196 SER D 214 1 19
HELIX 61 AG7 ALA D 226 ASP D 231 1 6
HELIX 62 AG8 GLU D 237 GLY D 260 1 24
HELIX 63 AG9 ILE D 291 SER D 296 1 6
HELIX 64 AH1 ILE E 25 GLY E 32 1 8
HELIX 65 AH2 ASN E 34 GLY E 45 1 12
HELIX 66 AH3 THR E 48 ALA E 55 1 8
HELIX 67 AH4 PRO E 56 ILE E 63 1 8
HELIX 68 AH5 SER E 67 VAL E 82 1 16
HELIX 69 AH6 ALA E 89 GLU E 98 1 10
HELIX 70 AH7 SER E 106 LEU E 113 1 8
HELIX 71 AH8 GLY E 132 CYS E 144 1 13
HELIX 72 AH9 GLN E 145 LEU E 146 5 2
HELIX 73 AI1 PRO E 147 GLY E 151 5 5
HELIX 74 AI2 ARG E 167 TYR E 178 1 12
HELIX 75 AI3 SER E 181 ASN E 188 1 8
HELIX 76 AI4 ASN E 196 SER E 214 1 19
HELIX 77 AI5 ALA E 226 ASP E 231 1 6
HELIX 78 AI6 GLU E 237 GLY E 260 1 24
HELIX 79 AI7 ILE E 291 SER E 296 1 6
HELIX 80 AI8 ILE F 25 GLN F 30 1 6
HELIX 81 AI9 ASN F 34 GLY F 45 1 12
HELIX 82 AJ1 THR F 48 ALA F 55 1 8
HELIX 83 AJ2 PRO F 56 ILE F 63 1 8
HELIX 84 AJ3 SER F 67 VAL F 82 1 16
HELIX 85 AJ4 ALA F 89 GLU F 98 1 10
HELIX 86 AJ5 SER F 106 LEU F 113 1 8
HELIX 87 AJ6 GLY F 132 CYS F 144 1 13
HELIX 88 AJ7 GLN F 145 LEU F 146 5 2
HELIX 89 AJ8 PRO F 147 GLY F 151 5 5
HELIX 90 AJ9 ARG F 167 TYR F 178 1 12
HELIX 91 AK1 SER F 181 ASN F 188 1 8
HELIX 92 AK2 ASN F 196 SER F 214 1 19
HELIX 93 AK3 ALA F 226 ASP F 231 1 6
HELIX 94 AK4 GLU F 237 GLY F 260 1 24
HELIX 95 AK5 ILE F 291 SER F 296 1 6
HELIX 96 AK6 ILE G 25 GLN G 30 1 6
HELIX 97 AK7 ASN G 34 GLY G 45 1 12
HELIX 98 AK8 THR G 48 ALA G 55 1 8
HELIX 99 AK9 PRO G 56 ILE G 63 1 8
HELIX 100 AL1 SER G 67 VAL G 82 1 16
HELIX 101 AL2 THR G 88 GLU G 98 1 11
HELIX 102 AL3 SER G 106 LEU G 113 1 8
HELIX 103 AL4 GLY G 132 CYS G 144 1 13
HELIX 104 AL5 GLN G 145 LEU G 146 5 2
HELIX 105 AL6 PRO G 147 GLY G 151 5 5
HELIX 106 AL7 ARG G 167 TYR G 178 1 12
HELIX 107 AL8 SER G 181 ASN G 188 1 8
HELIX 108 AL9 ASN G 196 SER G 214 1 19
HELIX 109 AM1 ALA G 226 ASP G 231 1 6
HELIX 110 AM2 GLU G 237 GLY G 260 1 24
HELIX 111 AM3 ILE G 291 SER G 296 1 6
HELIX 112 AM4 ILE H 25 GLN H 30 1 6
HELIX 113 AM5 ASN H 34 GLY H 45 1 12
HELIX 114 AM6 THR H 48 ALA H 55 1 8
HELIX 115 AM7 PRO H 56 ILE H 63 1 8
HELIX 116 AM8 SER H 67 VAL H 82 1 16
HELIX 117 AM9 ALA H 89 GLU H 98 1 10
HELIX 118 AN1 SER H 106 LEU H 113 1 8
HELIX 119 AN2 GLY H 132 CYS H 144 1 13
HELIX 120 AN3 GLN H 145 LEU H 146 5 2
HELIX 121 AN4 PRO H 147 GLY H 151 5 5
HELIX 122 AN5 ARG H 167 TYR H 178 1 12
HELIX 123 AN6 SER H 181 ASN H 188 1 8
HELIX 124 AN7 ASN H 196 SER H 214 1 19
HELIX 125 AN8 ALA H 226 ASP H 231 1 6
HELIX 126 AN9 GLU H 237 GLY H 260 1 24
HELIX 127 AO1 ILE I 25 GLN I 30 1 6
HELIX 128 AO2 ASN I 34 GLY I 45 1 12
HELIX 129 AO3 THR I 48 ALA I 55 1 8
HELIX 130 AO4 PRO I 56 ASN I 62 1 7
HELIX 131 AO5 SER I 67 VAL I 82 1 16
HELIX 132 AO6 ALA I 89 GLU I 98 1 10
HELIX 133 AO7 SER I 106 LEU I 113 1 8
HELIX 134 AO8 GLY I 132 CYS I 144 1 13
HELIX 135 AO9 GLN I 145 LEU I 146 5 2
HELIX 136 AP1 PRO I 147 GLY I 151 5 5
HELIX 137 AP2 ARG I 167 TYR I 178 1 12
HELIX 138 AP3 SER I 181 ASN I 188 1 8
HELIX 139 AP4 ASN I 196 SER I 214 1 19
HELIX 140 AP5 ALA I 226 ASP I 231 1 6
HELIX 141 AP6 GLU I 237 GLY I 260 1 24
HELIX 142 AP7 ILE J 25 GLY J 32 1 8
HELIX 143 AP8 ASN J 34 GLY J 45 1 12
HELIX 144 AP9 THR J 48 ALA J 55 1 8
HELIX 145 AQ1 PRO J 56 ILE J 63 1 8
HELIX 146 AQ2 SER J 67 VAL J 82 1 16
HELIX 147 AQ3 ALA J 89 GLU J 98 1 10
HELIX 148 AQ4 SER J 106 LEU J 113 1 8
HELIX 149 AQ5 GLY J 132 CYS J 144 1 13
HELIX 150 AQ6 GLN J 145 LEU J 146 5 2
HELIX 151 AQ7 PRO J 147 GLY J 151 5 5
HELIX 152 AQ8 ARG J 167 TYR J 178 1 12
HELIX 153 AQ9 SER J 181 ASN J 188 1 8
HELIX 154 AR1 ASN J 196 SER J 214 1 19
HELIX 155 AR2 ALA J 226 ASP J 231 1 6
HELIX 156 AR3 GLU J 237 GLY J 260 1 24
HELIX 157 AR4 ILE J 291 SER J 296 1 6
HELIX 158 AR5 ILE K 25 GLN K 30 1 6
HELIX 159 AR6 ASN K 34 GLY K 45 1 12
HELIX 160 AR7 THR K 48 ALA K 55 1 8
HELIX 161 AR8 PRO K 56 ASN K 62 1 7
HELIX 162 AR9 SER K 67 VAL K 82 1 16
HELIX 163 AS1 ALA K 89 GLU K 98 1 10
HELIX 164 AS2 SER K 106 LEU K 113 1 8
HELIX 165 AS3 GLY K 132 CYS K 144 1 13
HELIX 166 AS4 GLN K 145 LEU K 146 5 2
HELIX 167 AS5 PRO K 147 GLY K 151 5 5
HELIX 168 AS6 ARG K 167 TYR K 178 1 12
HELIX 169 AS7 SER K 181 ASN K 188 1 8
HELIX 170 AS8 ASN K 196 SER K 214 1 19
HELIX 171 AS9 ALA K 226 ASP K 231 1 6
HELIX 172 AT1 GLU K 237 GLY K 260 1 24
HELIX 173 AT2 ILE K 291 SER K 296 1 6
HELIX 174 AT3 ILE L 25 GLN L 30 1 6
HELIX 175 AT4 ASN L 34 GLY L 45 1 12
HELIX 176 AT5 THR L 48 ALA L 55 1 8
HELIX 177 AT6 PRO L 56 ASN L 62 1 7
HELIX 178 AT7 SER L 67 VAL L 82 1 16
HELIX 179 AT8 ALA L 89 GLU L 98 1 10
HELIX 180 AT9 SER L 106 LEU L 113 1 8
HELIX 181 AU1 GLY L 132 CYS L 144 1 13
HELIX 182 AU2 GLN L 145 LEU L 146 5 2
HELIX 183 AU3 PRO L 147 GLY L 151 5 5
HELIX 184 AU4 ARG L 167 TYR L 178 1 12
HELIX 185 AU5 SER L 181 ASN L 188 1 8
HELIX 186 AU6 ASN L 196 SER L 214 1 19
HELIX 187 AU7 ALA L 226 ASP L 231 1 6
HELIX 188 AU8 GLU L 237 GLY L 260 1 24
HELIX 189 AU9 ILE L 291 SER L 296 1 6
HELIX 190 AV1 ILE M 25 GLN M 30 1 6
HELIX 191 AV2 ASN M 34 GLY M 45 1 12
HELIX 192 AV3 THR M 48 ALA M 55 1 8
HELIX 193 AV4 PRO M 56 ASN M 62 1 7
HELIX 194 AV5 SER M 67 VAL M 82 1 16
HELIX 195 AV6 ALA M 89 GLU M 98 1 10
HELIX 196 AV7 SER M 106 LEU M 113 1 8
HELIX 197 AV8 GLY M 132 CYS M 144 1 13
HELIX 198 AV9 GLN M 145 LEU M 146 5 2
HELIX 199 AW1 PRO M 147 GLY M 151 5 5
HELIX 200 AW2 ARG M 167 TYR M 178 1 12
HELIX 201 AW3 SER M 181 ASN M 188 1 8
HELIX 202 AW4 ASN M 196 SER M 214 1 19
HELIX 203 AW5 ALA M 226 ASP M 231 1 6
HELIX 204 AW6 GLU M 237 GLY M 260 1 24
HELIX 205 AW7 ILE M 291 SER M 296 1 6
HELIX 206 AW8 ILE N 25 GLY N 32 1 8
HELIX 207 AW9 ASN N 34 GLY N 45 1 12
HELIX 208 AX1 THR N 48 ALA N 55 1 8
HELIX 209 AX2 PRO N 56 ASN N 62 1 7
HELIX 210 AX3 SER N 67 VAL N 82 1 16
HELIX 211 AX4 THR N 88 GLU N 98 1 11
HELIX 212 AX5 SER N 106 LEU N 113 1 8
HELIX 213 AX6 GLY N 132 CYS N 144 1 13
HELIX 214 AX7 GLN N 145 LEU N 146 5 2
HELIX 215 AX8 PRO N 147 GLY N 151 5 5
HELIX 216 AX9 ARG N 167 TYR N 178 1 12
HELIX 217 AY1 SER N 181 ASN N 188 1 8
HELIX 218 AY2 ASN N 196 SER N 214 1 19
HELIX 219 AY3 ALA N 226 ASP N 231 1 6
HELIX 220 AY4 GLU N 237 GLY N 260 1 24
HELIX 221 AY5 ILE N 291 SER N 296 1 6
SHEET 1 AA110 THR A 87 THR A 88 0
SHEET 2 AA110 VAL B 189 ARG B 193 -1 O TYR B 191 N THR A 87
SHEET 3 AA110 LYS B 156 ASP B 161 1 N TYR B 159 O ALA B 190
SHEET 4 AA110 TYR B 216 ASP B 222 1 O ALA B 217 N LYS B 156
SHEET 5 AA110 ALA B 262 GLN B 268 1 O VAL B 264 N LEU B 219
SHEET 6 AA110 ILE B 122 GLY B 127 1 N THR B 123 O VAL B 263
SHEET 7 AA110 THR B 298 LYS B 304 1 O THR B 298 N GLU B 124
SHEET 8 AA110 THR B 309 ILE B 314 -1 O LYS B 313 N TYR B 301
SHEET 9 AA110 GLU B 324 ASN B 330 -1 O PHE B 327 N ARG B 310
SHEET 10 AA110 GLY B 333 GLY B 335 -1 O GLY B 335 N ALA B 328
SHEET 1 AA2 2 GLN A 101 ILE A 102 0
SHEET 2 AA2 2 ILE A 117 GLU A 118 -1 O ILE A 117 N ILE A 102
SHEET 1 AA3 9 VAL A 189 ARG A 193 0
SHEET 2 AA3 9 LYS A 156 ASP A 161 1 N TYR A 159 O ALA A 190
SHEET 3 AA3 9 TYR A 216 ASP A 222 1 O ILE A 220 N ILE A 160
SHEET 4 AA3 9 ALA A 262 GLN A 268 1 O VAL A 264 N LEU A 219
SHEET 5 AA3 9 ILE A 122 GLY A 127 1 N THR A 123 O VAL A 263
SHEET 6 AA3 9 THR A 298 LYS A 304 1 O THR A 298 N GLU A 124
SHEET 7 AA3 9 THR A 309 ILE A 314 -1 O LYS A 313 N TYR A 301
SHEET 8 AA3 9 GLU A 324 ASN A 330 -1 O PHE A 327 N ARG A 310
SHEET 9 AA3 9 GLY A 333 GLY A 335 -1 O GLY A 333 N ASN A 330
SHEET 1 AA410 THR B 87 THR B 88 0
SHEET 2 AA410 VAL C 189 ARG C 193 -1 O TYR C 191 N THR B 87
SHEET 3 AA410 LYS C 156 ASP C 161 1 N TYR C 159 O ALA C 190
SHEET 4 AA410 TYR C 216 ASP C 222 1 O ILE C 220 N ILE C 160
SHEET 5 AA410 ALA C 262 GLN C 268 1 O VAL C 264 N LEU C 219
SHEET 6 AA410 ILE C 122 GLY C 127 1 N THR C 123 O VAL C 263
SHEET 7 AA410 THR C 298 LYS C 304 1 O LEU C 300 N GLU C 124
SHEET 8 AA410 THR C 309 ILE C 314 -1 O LYS C 313 N TYR C 301
SHEET 9 AA410 GLU C 324 ASN C 330 -1 O PHE C 327 N ARG C 310
SHEET 10 AA410 GLY C 333 GLY C 335 -1 O GLY C 335 N ALA C 328
SHEET 1 AA5 2 GLN B 101 ILE B 102 0
SHEET 2 AA5 2 ILE B 117 GLU B 118 -1 O ILE B 117 N ILE B 102
SHEET 1 AA610 THR C 87 THR C 88 0
SHEET 2 AA610 VAL D 189 ARG D 193 -1 O TYR D 191 N THR C 87
SHEET 3 AA610 LYS D 156 ASP D 161 1 N TYR D 159 O ALA D 190
SHEET 4 AA610 TYR D 216 ASP D 222 1 O ILE D 220 N ILE D 160
SHEET 5 AA610 ALA D 262 GLN D 268 1 O VAL D 264 N LEU D 219
SHEET 6 AA610 ILE D 122 GLY D 127 1 N THR D 123 O VAL D 263
SHEET 7 AA610 THR D 298 LYS D 304 1 O THR D 298 N GLU D 124
SHEET 8 AA610 THR D 309 ILE D 314 -1 O LYS D 313 N TYR D 301
SHEET 9 AA610 GLU D 324 ASN D 330 -1 O PHE D 327 N ARG D 310
SHEET 10 AA610 GLY D 333 ASP D 336 -1 O GLY D 333 N ASN D 330
SHEET 1 AA7 2 GLN C 101 ILE C 102 0
SHEET 2 AA7 2 ILE C 117 GLU C 118 -1 O ILE C 117 N ILE C 102
SHEET 1 AA810 THR D 87 THR D 88 0
SHEET 2 AA810 VAL E 189 ARG E 193 -1 O TYR E 191 N THR D 87
SHEET 3 AA810 LYS E 156 ASP E 161 1 N TYR E 159 O ALA E 190
SHEET 4 AA810 TYR E 216 ASP E 222 1 O ILE E 220 N ILE E 160
SHEET 5 AA810 ALA E 262 GLN E 268 1 O VAL E 264 N LEU E 219
SHEET 6 AA810 ILE E 122 GLY E 127 1 N THR E 123 O VAL E 263
SHEET 7 AA810 THR E 298 LYS E 304 1 O LEU E 300 N GLU E 124
SHEET 8 AA810 THR E 309 ILE E 314 -1 O LYS E 313 N TYR E 301
SHEET 9 AA810 GLU E 324 ASN E 330 -1 O PHE E 327 N ARG E 310
SHEET 10 AA810 GLY E 333 ASP E 336 -1 O GLY E 333 N ASN E 330
SHEET 1 AA9 2 GLN D 101 ILE D 102 0
SHEET 2 AA9 2 ILE D 117 GLU D 118 -1 O ILE D 117 N ILE D 102
SHEET 1 AB110 THR E 87 THR E 88 0
SHEET 2 AB110 VAL F 189 ARG F 193 -1 O TYR F 191 N THR E 87
SHEET 3 AB110 LYS F 156 ASP F 161 1 N TYR F 159 O ALA F 190
SHEET 4 AB110 TYR F 216 ASP F 222 1 O ILE F 220 N ILE F 160
SHEET 5 AB110 ALA F 262 GLN F 268 1 O ALA F 262 N LEU F 219
SHEET 6 AB110 ILE F 122 GLY F 127 1 N THR F 123 O VAL F 263
SHEET 7 AB110 THR F 298 LYS F 304 1 O THR F 298 N GLU F 124
SHEET 8 AB110 THR F 309 ILE F 314 -1 O LYS F 313 N TYR F 301
SHEET 9 AB110 GLU F 324 ASN F 330 -1 O PHE F 327 N ARG F 310
SHEET 10 AB110 GLY F 333 GLY F 335 -1 O GLY F 333 N ASN F 330
SHEET 1 AB2 2 GLN E 101 ILE E 102 0
SHEET 2 AB2 2 ILE E 117 GLU E 118 -1 O ILE E 117 N ILE E 102
SHEET 1 AB310 THR F 87 THR F 88 0
SHEET 2 AB310 VAL G 189 ARG G 193 -1 O TYR G 191 N THR F 87
SHEET 3 AB310 LYS G 156 ASP G 161 1 N TYR G 159 O ALA G 190
SHEET 4 AB310 TYR G 216 ASP G 222 1 O ILE G 220 N ILE G 160
SHEET 5 AB310 ALA G 262 GLN G 268 1 O ALA G 262 N LEU G 219
SHEET 6 AB310 ILE G 122 GLY G 127 1 N THR G 123 O VAL G 263
SHEET 7 AB310 THR G 298 LYS G 304 1 O THR G 298 N GLU G 124
SHEET 8 AB310 THR G 309 ILE G 314 -1 O LYS G 313 N TYR G 301
SHEET 9 AB310 GLU G 324 ASN G 330 -1 O PHE G 327 N ARG G 310
SHEET 10 AB310 GLY G 333 GLY G 335 -1 O GLY G 335 N ALA G 328
SHEET 1 AB4 2 GLN F 101 ILE F 102 0
SHEET 2 AB4 2 ILE F 117 GLU F 118 -1 O ILE F 117 N ILE F 102
SHEET 1 AB5 2 GLN G 101 ILE G 102 0
SHEET 2 AB5 2 ILE G 117 GLU G 118 -1 O ILE G 117 N ILE G 102
SHEET 1 AB610 THR H 87 THR H 88 0
SHEET 2 AB610 VAL I 189 ARG I 193 -1 O TYR I 191 N THR H 87
SHEET 3 AB610 LYS I 156 ASP I 161 1 N TYR I 159 O ALA I 190
SHEET 4 AB610 TYR I 216 ASP I 222 1 O ILE I 220 N ILE I 160
SHEET 5 AB610 ALA I 262 GLN I 268 1 O VAL I 264 N LEU I 219
SHEET 6 AB610 ILE I 122 GLY I 127 1 N THR I 123 O VAL I 263
SHEET 7 AB610 THR I 298 LYS I 304 1 O THR I 298 N GLU I 124
SHEET 8 AB610 THR I 309 ILE I 314 -1 O LYS I 313 N TYR I 301
SHEET 9 AB610 GLU I 324 ASN I 330 -1 O PHE I 327 N ARG I 310
SHEET 10 AB610 GLY I 333 GLY I 335 -1 O GLY I 333 N ASN I 330
SHEET 1 AB7 2 GLN H 101 ILE H 102 0
SHEET 2 AB7 2 ILE H 117 GLU H 118 -1 O ILE H 117 N ILE H 102
SHEET 1 AB8 9 VAL H 189 ARG H 193 0
SHEET 2 AB8 9 LYS H 156 ASP H 161 1 N TYR H 159 O ALA H 190
SHEET 3 AB8 9 TYR H 216 ASP H 222 1 O ILE H 220 N ILE H 160
SHEET 4 AB8 9 ALA H 262 GLN H 268 1 O VAL H 264 N LEU H 219
SHEET 5 AB8 9 ILE H 122 GLY H 127 1 N THR H 123 O VAL H 263
SHEET 6 AB8 9 THR H 298 LYS H 304 1 O THR H 298 N GLU H 124
SHEET 7 AB8 9 THR H 309 ILE H 314 -1 O LYS H 313 N TYR H 301
SHEET 8 AB8 9 GLU H 324 ASN H 330 -1 O PHE H 327 N ARG H 310
SHEET 9 AB8 9 GLY H 333 GLY H 335 -1 O GLY H 333 N ASN H 330
SHEET 1 AB910 THR I 87 THR I 88 0
SHEET 2 AB910 VAL J 189 ARG J 193 -1 O TYR J 191 N THR I 87
SHEET 3 AB910 LYS J 156 ASP J 161 1 N TYR J 159 O ALA J 190
SHEET 4 AB910 TYR J 216 ASP J 222 1 O ILE J 220 N ILE J 160
SHEET 5 AB910 ALA J 262 GLN J 268 1 O ALA J 262 N LEU J 219
SHEET 6 AB910 ILE J 122 GLY J 127 1 N THR J 123 O VAL J 263
SHEET 7 AB910 THR J 298 LYS J 304 1 O THR J 298 N GLU J 124
SHEET 8 AB910 THR J 309 ILE J 314 -1 O LYS J 313 N TYR J 301
SHEET 9 AB910 GLU J 324 ASN J 330 -1 O PHE J 327 N ARG J 310
SHEET 10 AB910 GLY J 333 ASP J 336 -1 O GLY J 333 N ASN J 330
SHEET 1 AC1 2 GLN I 101 ILE I 102 0
SHEET 2 AC1 2 ILE I 117 GLU I 118 -1 O ILE I 117 N ILE I 102
SHEET 1 AC210 THR J 87 THR J 88 0
SHEET 2 AC210 VAL K 189 ARG K 193 -1 O TYR K 191 N THR J 87
SHEET 3 AC210 LYS K 156 ASP K 161 1 N TYR K 159 O ALA K 190
SHEET 4 AC210 TYR K 216 ASP K 222 1 O ALA K 217 N LYS K 156
SHEET 5 AC210 ALA K 262 GLN K 268 1 O VAL K 264 N LEU K 219
SHEET 6 AC210 ILE K 122 GLY K 127 1 N THR K 123 O VAL K 263
SHEET 7 AC210 THR K 298 LYS K 304 1 O THR K 298 N GLU K 124
SHEET 8 AC210 THR K 309 ILE K 314 -1 O LYS K 313 N TYR K 301
SHEET 9 AC210 GLU K 324 ASN K 330 -1 O PHE K 327 N ARG K 310
SHEET 10 AC210 GLY K 333 GLY K 335 -1 O GLY K 335 N ALA K 328
SHEET 1 AC3 2 GLN J 101 ILE J 102 0
SHEET 2 AC3 2 ILE J 117 GLU J 118 -1 O ILE J 117 N ILE J 102
SHEET 1 AC410 THR K 87 THR K 88 0
SHEET 2 AC410 VAL L 189 ARG L 193 -1 O TYR L 191 N THR K 87
SHEET 3 AC410 LYS L 156 ASP L 161 1 N TYR L 159 O ALA L 190
SHEET 4 AC410 TYR L 216 ASP L 222 1 O ILE L 220 N ILE L 160
SHEET 5 AC410 ALA L 262 GLN L 268 1 O ALA L 262 N LEU L 219
SHEET 6 AC410 ILE L 122 GLY L 127 1 N THR L 123 O VAL L 263
SHEET 7 AC410 THR L 298 LYS L 304 1 O THR L 298 N GLU L 124
SHEET 8 AC410 THR L 309 ILE L 314 -1 O LYS L 313 N TYR L 301
SHEET 9 AC410 GLU L 324 ASN L 330 -1 O PHE L 327 N ARG L 310
SHEET 10 AC410 GLY L 333 ASP L 336 -1 O GLY L 333 N ASN L 330
SHEET 1 AC5 2 GLN K 101 ILE K 102 0
SHEET 2 AC5 2 ILE K 117 GLU K 118 -1 O ILE K 117 N ILE K 102
SHEET 1 AC610 THR L 87 THR L 88 0
SHEET 2 AC610 VAL M 189 ARG M 193 -1 O TYR M 191 N THR L 87
SHEET 3 AC610 LYS M 156 ASP M 161 1 N TYR M 159 O ALA M 190
SHEET 4 AC610 TYR M 216 ASP M 222 1 O ILE M 220 N ILE M 160
SHEET 5 AC610 ALA M 262 GLN M 268 1 O VAL M 264 N LEU M 219
SHEET 6 AC610 ILE M 122 GLY M 127 1 N THR M 123 O VAL M 263
SHEET 7 AC610 THR M 298 LYS M 304 1 O THR M 298 N GLU M 124
SHEET 8 AC610 THR M 309 ILE M 314 -1 O LYS M 313 N TYR M 301
SHEET 9 AC610 GLU M 324 ASN M 330 -1 O PHE M 327 N ARG M 310
SHEET 10 AC610 GLY M 333 GLY M 335 -1 O GLY M 333 N ASN M 330
SHEET 1 AC7 2 GLN L 101 ILE L 102 0
SHEET 2 AC7 2 ILE L 117 GLU L 118 -1 O ILE L 117 N ILE L 102
SHEET 1 AC810 THR M 87 THR M 88 0
SHEET 2 AC810 VAL N 189 ARG N 193 -1 O TYR N 191 N THR M 87
SHEET 3 AC810 LYS N 156 ASP N 161 1 N TYR N 159 O ALA N 190
SHEET 4 AC810 TYR N 216 ASP N 222 1 O ALA N 217 N LYS N 156
SHEET 5 AC810 ALA N 262 GLN N 268 1 O VAL N 264 N LEU N 219
SHEET 6 AC810 ILE N 122 GLY N 127 1 N THR N 123 O VAL N 263
SHEET 7 AC810 THR N 298 LYS N 304 1 O THR N 298 N GLU N 124
SHEET 8 AC810 THR N 309 ILE N 314 -1 O LYS N 313 N TYR N 301
SHEET 9 AC810 GLU N 324 ASN N 330 -1 O PHE N 327 N ARG N 310
SHEET 10 AC810 GLY N 333 ASP N 336 -1 O GLY N 335 N ALA N 328
SHEET 1 AC9 2 GLN M 101 ILE M 102 0
SHEET 2 AC9 2 ILE M 117 GLU M 118 -1 O ILE M 117 N ILE M 102
SHEET 1 AD1 2 GLN N 101 ILE N 102 0
SHEET 2 AD1 2 ILE N 117 GLU N 118 -1 O ILE N 117 N ILE N 102
LINK OG1 THR A 134 MG MG A 401 1555 1555 2.08
LINK MG MG A 401 O1G ATP A 402 1555 1555 2.19
LINK MG MG A 401 O1B ATP A 402 1555 1555 2.04
LINK OG1 THR B 134 MG MG B 401 1555 1555 2.07
LINK MG MG B 401 O3G ATP B 402 1555 1555 2.08
LINK MG MG B 401 O1B ATP B 402 1555 1555 2.05
LINK OG1 THR C 134 MG MG C 401 1555 1555 2.05
LINK MG MG C 401 O3G ATP C 402 1555 1555 1.95
LINK MG MG C 401 O1B ATP C 402 1555 1555 2.18
LINK OG1 THR D 134 MG MG D 401 1555 1555 2.06
LINK MG MG D 401 O2B ATP D 402 1555 1555 2.17
LINK MG MG D 401 O2G ATP D 402 1555 1555 1.95
LINK OG1 THR E 134 MG MG E 401 1555 1555 2.08
LINK MG MG E 401 O2G ATP E 402 1555 1555 2.17
LINK MG MG E 401 O2B ATP E 402 1555 1555 2.04
LINK OG1 THR F 134 MG MG F 401 1555 1555 2.07
LINK MG MG F 401 O1G ATP F 402 1555 1555 2.09
LINK MG MG F 401 O2B ATP F 402 1555 1555 2.14
LINK OG1 THR G 134 MG MG G 401 1555 1555 2.07
LINK MG MG G 401 O1G ATP G 402 1555 1555 2.13
LINK MG MG G 401 O2B ATP G 402 1555 1555 2.13
LINK OG1 THR H 134 MG MG H 401 1555 1555 2.08
LINK MG MG H 401 O3G ATP H 402 1555 1555 2.24
LINK MG MG H 401 O1B ATP H 402 1555 1555 1.98
LINK OG1 THR I 134 MG MG I 401 1555 1555 2.04
LINK OD2 ASP I 222 MG MG I 401 1555 1555 2.95
LINK MG MG I 401 O3G ATP I 402 1555 1555 1.87
LINK MG MG I 401 O2B ATP I 402 1555 1555 2.30
LINK OG1 THR J 134 MG MG J 401 1555 1555 2.07
LINK MG MG J 401 O2G ATP J 402 1555 1555 2.18
LINK MG MG J 401 O2B ATP J 402 1555 1555 2.05
LINK OG1 THR K 134 MG MG K 401 1555 1555 2.08
LINK MG MG K 401 O2B ATP K 402 1555 1555 2.01
LINK MG MG K 401 O2G ATP K 402 1555 1555 2.16
LINK OG1 THR L 134 MG MG L 401 1555 1555 2.06
LINK MG MG L 401 O2B ATP L 402 1555 1555 2.14
LINK MG MG L 401 O1G ATP L 402 1555 1555 2.07
LINK OG1 THR M 134 MG MG M 401 1555 1555 2.07
LINK MG MG M 401 O1G ATP M 402 1555 1555 2.14
LINK MG MG M 401 O1B ATP M 402 1555 1555 2.09
LINK OG1 THR N 134 MG MG N 401 1555 1555 2.07
LINK MG MG N 401 O1G ATP N 402 1555 1555 2.08
LINK MG MG N 401 O1B ATP N 402 1555 1555 2.08
CISPEP 1 ASP A 222 SER A 223 0 0.00
CISPEP 2 ASP B 222 SER B 223 0 0.06
CISPEP 3 ASP C 222 SER C 223 0 -0.33
CISPEP 4 ASP D 222 SER D 223 0 -0.18
CISPEP 5 ASP E 222 SER E 223 0 -0.25
CISPEP 6 ASP F 222 SER F 223 0 0.30
CISPEP 7 ASP G 222 SER G 223 0 -0.37
CISPEP 8 ASP H 222 SER H 223 0 0.12
CISPEP 9 ASP I 222 SER I 223 0 -0.13
CISPEP 10 ASP J 222 SER J 223 0 -0.33
CISPEP 11 ASP K 222 SER K 223 0 0.05
CISPEP 12 ASP L 222 SER L 223 0 -0.12
CISPEP 13 ASP M 222 SER M 223 0 -0.25
CISPEP 14 ASP N 222 SER N 223 0 0.10
SITE 1 AC1 4 THR A 134 THR A 165 ASP A 222 ATP A 402
SITE 1 AC2 15 PHE A 129 ARG A 130 THR A 131 GLY A 132
SITE 2 AC2 15 LYS A 133 THR A 134 GLN A 135 ARG A 170
SITE 3 AC2 15 GLN A 268 ARG A 310 ILE A 329 ASN A 330
SITE 4 AC2 15 ALA A 331 MG A 401 PRO G 318
SITE 1 AC3 4 THR B 134 THR B 165 ASP B 222 ATP B 402
SITE 1 AC4 18 SER A 317 CYS A 319 LEU A 320 PRO A 321
SITE 2 AC4 18 GLU A 322 PHE B 129 ARG B 130 GLY B 132
SITE 3 AC4 18 LYS B 133 THR B 134 GLN B 135 ARG B 170
SITE 4 AC4 18 GLN B 268 ARG B 310 ILE B 329 ASN B 330
SITE 5 AC4 18 ALA B 331 MG B 401
SITE 1 AC5 4 THR C 134 THR C 165 ASP C 222 ATP C 402
SITE 1 AC6 16 SER B 317 CYS B 319 LEU B 320 PRO B 321
SITE 2 AC6 16 GLU B 322 ARG C 130 GLY C 132 LYS C 133
SITE 3 AC6 16 THR C 134 GLN C 135 ARG C 170 GLN C 268
SITE 4 AC6 16 ARG C 310 ILE C 329 ASN C 330 MG C 401
SITE 1 AC7 3 THR D 134 ASP D 222 ATP D 402
SITE 1 AC8 15 SER C 317 LEU C 320 PRO C 321 GLU C 322
SITE 2 AC8 15 PHE D 129 ARG D 130 GLY D 132 LYS D 133
SITE 3 AC8 15 THR D 134 GLN D 135 ARG D 170 GLN D 268
SITE 4 AC8 15 ARG D 310 ILE D 329 MG D 401
SITE 1 AC9 3 THR E 134 THR E 165 ATP E 402
SITE 1 AD1 14 SER D 317 CYS D 319 LEU D 320 PRO D 321
SITE 2 AD1 14 GLU D 322 ARG E 130 GLY E 132 LYS E 133
SITE 3 AD1 14 THR E 134 GLN E 135 ARG E 170 GLN E 268
SITE 4 AD1 14 ARG E 310 MG E 401
SITE 1 AD2 4 THR F 134 THR F 165 ASP F 222 ATP F 402
SITE 1 AD3 16 SER E 317 CYS E 319 LEU E 320 PRO E 321
SITE 2 AD3 16 GLU E 322 PHE F 129 ARG F 130 GLY F 132
SITE 3 AD3 16 LYS F 133 THR F 134 GLN F 135 ARG F 170
SITE 4 AD3 16 GLN F 268 ARG F 310 ILE F 329 MG F 401
SITE 1 AD4 4 THR G 134 THR G 165 ASP G 222 ATP G 402
SITE 1 AD5 16 SER F 317 CYS F 319 LEU F 320 PRO F 321
SITE 2 AD5 16 GLU F 322 PHE G 129 ARG G 130 GLY G 132
SITE 3 AD5 16 LYS G 133 THR G 134 GLN G 135 ARG G 170
SITE 4 AD5 16 GLN G 268 ARG G 310 ILE G 329 MG G 401
SITE 1 AD6 3 THR H 134 THR H 165 ATP H 402
SITE 1 AD7 13 PHE H 129 ARG H 130 THR H 131 GLY H 132
SITE 2 AD7 13 LYS H 133 THR H 134 GLN H 135 ARG H 170
SITE 3 AD7 13 GLN H 268 ARG H 310 ILE H 329 MG H 401
SITE 4 AD7 13 SER N 317
SITE 1 AD8 4 THR I 134 THR I 165 ASP I 222 ATP I 402
SITE 1 AD9 14 SER H 317 CYS H 319 LEU H 320 PRO H 321
SITE 2 AD9 14 GLU H 322 ARG I 130 GLY I 132 LYS I 133
SITE 3 AD9 14 THR I 134 GLN I 135 ARG I 170 GLN I 268
SITE 4 AD9 14 ARG I 310 MG I 401
SITE 1 AE1 3 THR J 134 THR J 165 ATP J 402
SITE 1 AE2 18 TYR I 315 SER I 317 CYS I 319 LEU I 320
SITE 2 AE2 18 PRO I 321 GLU I 322 ARG J 130 THR J 131
SITE 3 AE2 18 GLY J 132 LYS J 133 THR J 134 GLN J 135
SITE 4 AE2 18 ARG J 170 GLN J 268 ARG J 310 ASN J 330
SITE 5 AE2 18 ALA J 331 MG J 401
SITE 1 AE3 3 THR K 134 THR K 165 ATP K 402
SITE 1 AE4 15 SER J 317 LEU J 320 PRO J 321 GLU J 322
SITE 2 AE4 15 PHE K 129 ARG K 130 GLY K 132 LYS K 133
SITE 3 AE4 15 THR K 134 GLN K 135 ARG K 170 GLN K 268
SITE 4 AE4 15 ARG K 310 ILE K 329 MG K 401
SITE 1 AE5 4 THR L 134 THR L 165 ASP L 222 ATP L 402
SITE 1 AE6 16 CYS K 319 LEU K 320 PRO K 321 GLU K 322
SITE 2 AE6 16 ARG L 130 GLY L 132 LYS L 133 THR L 134
SITE 3 AE6 16 GLN L 135 ARG L 170 GLN L 268 ARG L 310
SITE 4 AE6 16 ILE L 329 ASN L 330 ALA L 331 MG L 401
SITE 1 AE7 4 THR M 134 THR M 165 ASP M 222 ATP M 402
SITE 1 AE8 14 SER L 317 CYS L 319 LEU L 320 PRO L 321
SITE 2 AE8 14 GLU L 322 ARG M 130 GLY M 132 LYS M 133
SITE 3 AE8 14 THR M 134 GLN M 135 ARG M 170 GLN M 268
SITE 4 AE8 14 ARG M 310 MG M 401
SITE 1 AE9 4 THR N 134 THR N 165 ASP N 222 ATP N 402
SITE 1 AF1 16 SER M 317 CYS M 319 LEU M 320 PRO M 321
SITE 2 AF1 16 GLU M 322 ARG N 130 GLY N 132 LYS N 133
SITE 3 AF1 16 THR N 134 GLN N 135 ARG N 170 GLN N 268
SITE 4 AF1 16 ARG N 310 ILE N 329 ASN N 330 MG N 401
CRYST1 117.700 128.000 230.100 90.00 90.30 90.00 P 1 21 1 28
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 0.008496 0.000000 0.000044 0.00000
SCALE2 0.000000 0.007812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
