HEADER LYASE 16-JAN-16 5HMQ
TITLE XYLOSE ISOMERASE-LIKE TIM BARREL/4-HYDROXYPHENYLPYRUVATE DIOXYGENASE
TITLE 2 FUSION PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: 3-DEHYDROSHIKIMATE DEHYDRATASE;
COMPND 5 EC: 4.2.1.118;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 160488;
SOURCE 4 STRAIN: ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440;
SOURCE 5 GENE: QUIC, PP_2554;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE, XYLOSE ISOMERASE-LIKE TIM
KEYWDS 2 BARREL, OXIDOREDUCTASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PEEK,D.CHRISTENDAT
REVDAT 3 08-JAN-20 5HMQ 1 REMARK
REVDAT 2 13-SEP-17 5HMQ 1 REMARK
REVDAT 1 19-OCT-16 5HMQ 0
JRNL AUTH J.PEEK,D.CHRISTENDAT
JRNL TITL STRUCTURE OF A PUTATIVE XYLOSE ISOMERASE-LIKE TIM
JRNL TITL 2 BARREL/4-HYDROXYPHENYLPYRUVATE DIOXYGENASE FUSION PROTEIN
JRNL TITL 3 FROM PSEUDOMONAS PUTIDA AT 2.4 ANGSTROMS RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 436379
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 21648
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 40.4462 - 7.3533 1.00 13814 718 0.1542 0.1706
REMARK 3 2 7.3533 - 5.8421 1.00 13847 694 0.1817 0.2105
REMARK 3 3 5.8421 - 5.1053 1.00 13891 674 0.1779 0.1973
REMARK 3 4 5.1053 - 4.6392 1.00 13730 804 0.1608 0.1774
REMARK 3 5 4.6392 - 4.3071 1.00 13787 730 0.1606 0.1961
REMARK 3 6 4.3071 - 4.0534 1.00 13880 716 0.1653 0.1888
REMARK 3 7 4.0534 - 3.8506 1.00 13824 737 0.1745 0.1972
REMARK 3 8 3.8506 - 3.6831 1.00 13795 708 0.1870 0.2062
REMARK 3 9 3.6831 - 3.5414 1.00 13793 750 0.1996 0.2167
REMARK 3 10 3.5414 - 3.4193 1.00 13855 644 0.2091 0.2372
REMARK 3 11 3.4193 - 3.3124 1.00 13929 666 0.2178 0.2587
REMARK 3 12 3.3124 - 3.2178 1.00 13831 726 0.2276 0.2726
REMARK 3 13 3.2178 - 3.1331 1.00 13763 770 0.2279 0.2590
REMARK 3 14 3.1331 - 3.0567 1.00 13793 772 0.2353 0.2566
REMARK 3 15 3.0567 - 2.9872 1.00 13853 714 0.2378 0.2642
REMARK 3 16 2.9872 - 2.9236 1.00 13780 734 0.2337 0.2536
REMARK 3 17 2.9236 - 2.8652 1.00 13747 834 0.2376 0.2791
REMARK 3 18 2.8652 - 2.8111 1.00 13750 748 0.2403 0.2654
REMARK 3 19 2.8111 - 2.7609 1.00 13909 678 0.2509 0.2902
REMARK 3 20 2.7609 - 2.7141 1.00 13908 648 0.2621 0.2868
REMARK 3 21 2.7141 - 2.6704 1.00 13839 738 0.2691 0.2918
REMARK 3 22 2.6704 - 2.6293 1.00 13783 652 0.2655 0.3159
REMARK 3 23 2.6293 - 2.5906 1.00 13832 706 0.2636 0.2873
REMARK 3 24 2.5906 - 2.5541 1.00 13832 737 0.2646 0.2843
REMARK 3 25 2.5541 - 2.5196 1.00 13894 618 0.2774 0.3024
REMARK 3 26 2.5196 - 2.4869 1.00 13871 720 0.2826 0.2843
REMARK 3 27 2.4869 - 2.4558 1.00 13784 714 0.2882 0.3300
REMARK 3 28 2.4558 - 2.4263 1.00 13778 808 0.3005 0.3286
REMARK 3 29 2.4263 - 2.3980 1.00 13791 764 0.3048 0.3142
REMARK 3 30 2.3980 - 2.3711 1.00 13848 726 0.3107 0.3375
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.004 29739
REMARK 3 ANGLE : 0.744 40275
REMARK 3 CHIRALITY : 0.052 4353
REMARK 3 PLANARITY : 0.004 5376
REMARK 3 DIHEDRAL : 12.027 17689
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 110.3502 133.5949 59.1206
REMARK 3 T TENSOR
REMARK 3 T11: 0.3365 T22: 0.2895
REMARK 3 T33: 0.3538 T12: 0.0456
REMARK 3 T13: -0.0492 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.0693 L22: -0.0010
REMARK 3 L33: 0.2060 L12: 0.0317
REMARK 3 L13: -0.0499 L23: -0.0277
REMARK 3 S TENSOR
REMARK 3 S11: -0.0321 S12: -0.0117 S13: -0.0000
REMARK 3 S21: -0.0015 S22: 0.0055 S23: -0.0079
REMARK 3 S31: -0.0057 S32: 0.0183 S33: 0.0278
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 5HMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97936
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220967
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 39.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 TRIS PH 7.5, 0.1 M LISO4, 25%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.82200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.82200
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.82200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 THR A 416
REMARK 465 ALA A 417
REMARK 465 GLY A 418
REMARK 465 HIS A 419
REMARK 465 ASP A 476
REMARK 465 PRO A 477
REMARK 465 TYR A 478
REMARK 465 SER A 627
REMARK 465 GLY A 628
REMARK 465 ALA A 629
REMARK 465 ALA A 630
REMARK 465 ARG A 631
REMARK 465 LYS A 632
REMARK 465 PRO A 633
REMARK 465 VAL A 634
REMARK 465 LEU A 635
REMARK 465 THR B 416
REMARK 465 ALA B 417
REMARK 465 GLY B 418
REMARK 465 HIS B 419
REMARK 465 ASP B 476
REMARK 465 PRO B 477
REMARK 465 TYR B 478
REMARK 465 PRO B 496
REMARK 465 GLY B 628
REMARK 465 ALA B 629
REMARK 465 ALA B 630
REMARK 465 ARG B 631
REMARK 465 LYS B 632
REMARK 465 PRO B 633
REMARK 465 VAL B 634
REMARK 465 LEU B 635
REMARK 465 LEU C 474
REMARK 465 PRO C 475
REMARK 465 ASP C 476
REMARK 465 PRO C 477
REMARK 465 TYR C 478
REMARK 465 ARG C 626
REMARK 465 SER C 627
REMARK 465 GLY C 628
REMARK 465 ALA C 629
REMARK 465 ALA C 630
REMARK 465 ARG C 631
REMARK 465 LYS C 632
REMARK 465 PRO C 633
REMARK 465 VAL C 634
REMARK 465 LEU C 635
REMARK 465 ALA D 417
REMARK 465 GLY D 418
REMARK 465 ASP D 476
REMARK 465 PRO D 477
REMARK 465 TYR D 478
REMARK 465 GLY D 628
REMARK 465 ALA D 629
REMARK 465 ALA D 630
REMARK 465 ARG D 631
REMARK 465 LYS D 632
REMARK 465 PRO D 633
REMARK 465 VAL D 634
REMARK 465 LEU D 635
REMARK 465 ARG E 246
REMARK 465 THR E 416
REMARK 465 ALA E 417
REMARK 465 GLY E 418
REMARK 465 HIS E 419
REMARK 465 LEU E 474
REMARK 465 PRO E 475
REMARK 465 ASP E 476
REMARK 465 PRO E 477
REMARK 465 TYR E 478
REMARK 465 ALA E 630
REMARK 465 ARG E 631
REMARK 465 LYS E 632
REMARK 465 PRO E 633
REMARK 465 VAL E 634
REMARK 465 LEU E 635
REMARK 465 THR F 416
REMARK 465 ALA F 417
REMARK 465 GLY F 418
REMARK 465 HIS F 419
REMARK 465 ASP F 476
REMARK 465 PRO F 477
REMARK 465 TYR F 478
REMARK 465 ALA F 629
REMARK 465 ALA F 630
REMARK 465 ARG F 631
REMARK 465 LYS F 632
REMARK 465 PRO F 633
REMARK 465 VAL F 634
REMARK 465 LEU F 635
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 246 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU A 421 CB CG CD1 CD2
REMARK 470 ASP A 423 CB CG OD1 OD2
REMARK 470 ASP A 562 CB CG OD1 OD2
REMARK 470 ARG B 246 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP B 559 CG OD1 OD2
REMARK 470 GLU B 563 CG CD OE1 OE2
REMARK 470 ASP C 243 CB CG OD1 OD2
REMARK 470 ARG C 246 CB CG CD NE CZ NH1 NH2
REMARK 470 ALA C 247 CB
REMARK 470 THR C 416 CB OG1 CG2
REMARK 470 ALA C 417 CB
REMARK 470 HIS C 419 CB CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 557 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 558 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP C 559 CB CG OD1 OD2
REMARK 470 PHE C 560 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 246 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 557 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 559 CB CG OD1 OD2
REMARK 470 ASP D 561 CG OD1 OD2
REMARK 470 GLU D 563 CG CD OE1 OE2
REMARK 470 ALA E 247 CB
REMARK 470 ASP E 562 CB CG OD1 OD2
REMARK 470 GLU E 563 CG CD OE1 OE2
REMARK 470 LYS E 624 CG CD CE NZ
REMARK 470 ARG F 246 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG F 515 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 557 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU E 217 NZ LYS E 482 1.94
REMARK 500 NH1 ARG C 70 CG ASP C 72 1.96
REMARK 500 OD1 ASN C 502 N THR C 505 2.05
REMARK 500 NH2 ARG B 603 O GLY B 609 2.07
REMARK 500 O ALA E 104 NH1 ARG E 140 2.14
REMARK 500 NH2 ARG C 327 O ASP C 423 2.16
REMARK 500 O ASP D 94 O HOH D 801 2.18
REMARK 500 O HOH A 934 O HOH F 942 2.18
REMARK 500 OD2 ASP B 338 NH2 ARG B 368 2.18
REMARK 500 NH2 ARG D 515 OE1 GLU E 204 2.18
REMARK 500 O ARG E 64 NH2 ARG E 80 2.19
REMARK 500 O ASP D 562 N PHE D 564 2.19
REMARK 500 OE2 GLU A 395 O HOH A 801 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 511 CB - CG - CD2 ANGL. DEV. = 15.2 DEGREES
REMARK 500 VAL D 472 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU D 511 CB - CG - CD1 ANGL. DEV. = -17.5 DEGREES
REMARK 500 ARG D 515 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 VAL E 473 CG1 - CB - CG2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU E 511 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 VAL F 481 CG1 - CB - CG2 ANGL. DEV. = 10.0 DEGREES
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 ASP A 65 73.51 44.87
REMARK 500 PHE A 66 -64.90 -109.21
REMARK 500 ASP A 243 -54.29 162.61
REMARK 500 ARG A 246 -157.65 51.67
REMARK 500 ALA A 247 -143.83 51.49
REMARK 500 ALA A 248 90.74 53.37
REMARK 500 ALA A 432 -85.23 -25.26
REMARK 500 THR A 433 122.03 53.07
REMARK 500 ASP A 469 54.38 -151.17
REMARK 500 HIS A 509 -147.30 -86.34
REMARK 500 ASP A 561 -176.05 -65.68
REMARK 500 ASP A 562 -155.22 61.32
REMARK 500 GLU A 563 -32.62 80.08
REMARK 500 ARG A 595 -123.89 -127.04
REMARK 500 LYS A 604 -76.41 -120.94
REMARK 500 ALA A 605 52.97 -96.11
REMARK 500 ALA A 625 10.81 -65.42
REMARK 500 ASP B 65 74.33 44.54
REMARK 500 PHE B 66 -63.63 -109.16
REMARK 500 ARG B 246 -142.96 61.42
REMARK 500 ALA B 247 -160.33 54.95
REMARK 500 ALA B 248 87.82 56.23
REMARK 500 LEU B 421 -67.95 53.28
REMARK 500 ASP B 469 53.32 -148.94
REMARK 500 SER B 513 41.62 -94.01
REMARK 500 ASP B 561 -81.21 -49.03
REMARK 500 ASP B 562 -51.87 156.95
REMARK 500 ARG B 595 -109.81 -119.93
REMARK 500 ASP C 65 73.16 44.36
REMARK 500 PHE C 66 -65.09 -108.27
REMARK 500 ASP C 243 169.24 67.82
REMARK 500 ARG C 246 113.41 -176.18
REMARK 500 ALA C 247 51.28 70.12
REMARK 500 GLN C 336 119.63 -160.50
REMARK 500 LEU C 390 29.71 47.07
REMARK 500 ASP C 405 -145.79 -85.94
REMARK 500 THR C 416 -93.62 66.77
REMARK 500 ALA C 417 -26.79 115.91
REMARK 500 THR C 420 -155.00 48.19
REMARK 500 ALA C 432 -82.26 -56.84
REMARK 500 THR C 433 134.84 52.65
REMARK 500 ASP C 469 54.75 -150.89
REMARK 500 SER C 512 -7.47 -154.28
REMARK 500 ASP C 559 67.22 63.58
REMARK 500 ARG C 595 -113.60 -125.50
REMARK 500 ASP D 65 73.15 44.70
REMARK 500 PHE D 66 -64.19 -108.15
REMARK 500 ARG D 246 -149.60 51.58
REMARK 500 ALA D 247 -152.87 57.61
REMARK 500 ALA D 248 105.05 52.04
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU B 471 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH F 954 DISTANCE = 5.93 ANGSTROMS
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 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 134 OE2
REMARK 620 2 ASP A 165 OD2 99.5
REMARK 620 3 GLN A 191 OE1 82.9 106.4
REMARK 620 4 GLU A 239 OE1 172.4 88.0 96.2
REMARK 620 5 HOH A 832 O 85.7 167.5 85.5 86.7
REMARK 620 6 HOH A 837 O 79.6 102.7 148.1 97.6 66.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 599 OE1
REMARK 620 2 HOH A 916 O 172.6
REMARK 620 3 HOH A 819 O 92.8 85.5
REMARK 620 4 HOH A 897 O 102.5 70.1 78.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 134 OE1
REMARK 620 2 ASP B 165 OD2 90.1
REMARK 620 3 GLN B 191 OE1 76.1 98.5
REMARK 620 4 GLU B 239 OE1 165.7 87.9 90.2
REMARK 620 5 HOH B 909 O 95.7 105.4 154.7 98.5
REMARK 620 6 HOH B 811 O 93.3 173.1 76.6 87.2 80.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 599 OE1
REMARK 620 2 HOH B 865 O 81.3
REMARK 620 3 HOH B 880 O 163.2 83.5
REMARK 620 4 HOH B 941 O 108.1 78.8 75.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 134 OE1
REMARK 620 2 ASP C 165 OD2 97.7
REMARK 620 3 GLN C 191 OE1 88.4 89.8
REMARK 620 4 GLU C 239 OE1 170.0 88.4 83.7
REMARK 620 5 HOH C 832 O 85.9 174.8 86.5 87.5
REMARK 620 6 HOH C 823 O 96.0 96.5 171.8 91.1 86.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 599 OE1
REMARK 620 2 HOH C 843 O 87.5
REMARK 620 3 HOH C 882 O 95.3 86.8
REMARK 620 4 HOH C 919 O 178.8 93.2 83.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 134 OE1
REMARK 620 2 ASP D 165 OD2 92.3
REMARK 620 3 GLN D 191 OE1 86.5 100.2
REMARK 620 4 GLU D 239 OE1 170.9 93.6 85.7
REMARK 620 5 HOH D 814 O 93.7 172.8 84.3 81.0
REMARK 620 6 HOH D 923 O 91.5 103.2 156.5 93.8 72.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 599 OE1
REMARK 620 2 HOH D 846 O 99.3
REMARK 620 3 HOH D 885 O 86.8 84.6
REMARK 620 4 HOH D 984 O 175.1 83.3 89.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 134 OE2
REMARK 620 2 ASP E 165 OD2 91.6
REMARK 620 3 GLU E 239 OE1 171.6 91.5
REMARK 620 4 HOH E 846 O 92.1 173.8 84.2
REMARK 620 5 HOH E 889 O 90.7 104.9 96.1 80.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 599 OE1
REMARK 620 2 HOH E 851 O 91.2
REMARK 620 3 HOH E 981 O 112.1 87.5
REMARK 620 4 HOH E1003 O 175.3 86.5 72.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 134 OE1
REMARK 620 2 ASP F 165 OD2 92.7
REMARK 620 3 GLN F 191 OE1 83.1 94.4
REMARK 620 4 GLU F 239 OE1 169.9 92.2 87.8
REMARK 620 5 HOH F 896 O 88.2 108.1 156.2 98.7
REMARK 620 6 HOH F 831 O 90.2 177.0 85.2 84.8 72.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 599 OE1
REMARK 620 2 HOH F 821 O 88.8
REMARK 620 3 HOH F 887 O 103.6 83.3
REMARK 620 4 HOH F 929 O 171.2 98.1 71.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG C 70 and ASP C
REMARK 800 72
DBREF 5HMQ A 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
DBREF 5HMQ B 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
DBREF 5HMQ C 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
DBREF 5HMQ D 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
DBREF 5HMQ E 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
DBREF 5HMQ F 1 635 UNP Q88JU3 Q88JU3_PSEPK 1 635
SEQADV 5HMQ ALA A -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS A 0 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ ALA B -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS B 0 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ ALA C -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS C 0 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ ALA D -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS D 0 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ ALA E -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS E 0 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ ALA F -1 UNP Q88JU3 EXPRESSION TAG
SEQADV 5HMQ LYS F 0 UNP Q88JU3 EXPRESSION TAG
SEQRES 1 A 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 A 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 A 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 A 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 A 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 A 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 A 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 A 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 A 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 A 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 A 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 A 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 A 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 A 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 A 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 A 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 A 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 A 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 A 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 A 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 A 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 A 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 A 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 A 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 A 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 A 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 A 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 A 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 A 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 A 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 A 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 A 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 A 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 A 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 A 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 A 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 A 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 A 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 A 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 A 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 A 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 A 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 A 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 A 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 A 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 A 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 A 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 A 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 A 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
SEQRES 1 B 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 B 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 B 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 B 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 B 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 B 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 B 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 B 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 B 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 B 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 B 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 B 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 B 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 B 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 B 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 B 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 B 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 B 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 B 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 B 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 B 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 B 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 B 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 B 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 B 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 B 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 B 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 B 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 B 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 B 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 B 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 B 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 B 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 B 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 B 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 B 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 B 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 B 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 B 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 B 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 B 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 B 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 B 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 B 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 B 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 B 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 B 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 B 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 B 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
SEQRES 1 C 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 C 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 C 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 C 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 C 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 C 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 C 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 C 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 C 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 C 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 C 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 C 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 C 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 C 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 C 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 C 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 C 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 C 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 C 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 C 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 C 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 C 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 C 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 C 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 C 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 C 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 C 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 C 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 C 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 C 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 C 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 C 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 C 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 C 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 C 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 C 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 C 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 C 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 C 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 C 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 C 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 C 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 C 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 C 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 C 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 C 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 C 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 C 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 C 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
SEQRES 1 D 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 D 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 D 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 D 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 D 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 D 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 D 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 D 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 D 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 D 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 D 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 D 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 D 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 D 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 D 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 D 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 D 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 D 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 D 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 D 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 D 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 D 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 D 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 D 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 D 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 D 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 D 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 D 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 D 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 D 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 D 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 D 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 D 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 D 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 D 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 D 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 D 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 D 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 D 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 D 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 D 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 D 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 D 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 D 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 D 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 D 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 D 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 D 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 D 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
SEQRES 1 E 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 E 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 E 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 E 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 E 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 E 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 E 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 E 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 E 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 E 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 E 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 E 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 E 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 E 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 E 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 E 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 E 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 E 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 E 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 E 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 E 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 E 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 E 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 E 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 E 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 E 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 E 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 E 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 E 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 E 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 E 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 E 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 E 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 E 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 E 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 E 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 E 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 E 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 E 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 E 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 E 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 E 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 E 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 E 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 E 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 E 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 E 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 E 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 E 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
SEQRES 1 F 637 ALA LYS MSE GLN ARG SER ILE ALA THR VAL SER LEU SER
SEQRES 2 F 637 GLY THR LEU PRO GLU LYS LEU GLU ALA ILE ALA ALA ALA
SEQRES 3 F 637 GLY PHE ASP GLY VAL GLU ILE PHE GLU ASN ASP LEU LEU
SEQRES 4 F 637 TYR TYR ALA GLY SER PRO ARG GLN VAL ARG GLN MSE CYS
SEQRES 5 F 637 ALA ASP LEU GLY ILE ALA ILE THR LEU PHE GLN PRO PHE
SEQRES 6 F 637 ARG ASP PHE GLU GLY CYS ARG ARG ASP ARG LEU GLN LYS
SEQRES 7 F 637 ASN LEU ASP ARG ALA GLU ARG LYS PHE ASP LEU MSE GLN
SEQRES 8 F 637 GLU LEU GLY THR ASP LEU VAL LEU VAL CYS SER ASN VAL
SEQRES 9 F 637 GLN ALA ASP ALA LEU GLY ASP GLU GLN LEU LEU VAL ASP
SEQRES 10 F 637 ASP LEU ARG LEU LEU GLY GLU HIS ALA GLY LYS ARG GLY
SEQRES 11 F 637 LEU ARG ILE GLY TYR GLU ALA LEU ALA TRP GLY ARG HIS
SEQRES 12 F 637 VAL ASN THR TYR GLN GLN VAL TRP ASN LEU VAL ARG GLN
SEQRES 13 F 637 ALA ASP HIS PRO ALA LEU GLY VAL ILE LEU ASP SER PHE
SEQRES 14 F 637 HIS THR LEU SER LEU LYS GLY ASP PRO SER ALA ILE ARG
SEQRES 15 F 637 ASP ILE PRO GLY ASP LYS ILE PHE PHE VAL GLN MSE ALA
SEQRES 16 F 637 ASP ALA PRO ILE LEU ALA MSE ASP VAL LEU GLU TRP SER
SEQRES 17 F 637 ARG HIS PHE ARG CYS PHE PRO GLY GLN GLY GLU MSE ASP
SEQRES 18 F 637 MSE ALA GLY PHE LEU ALA PRO ILE LEU ALA THR GLY TYR
SEQRES 19 F 637 ARG GLY PRO LEU SER LEU GLU ILE PHE ASN ASP GLY PHE
SEQRES 20 F 637 ARG ALA ALA PRO THR ARG GLN ASN ALA ALA ASP GLY LEU
SEQRES 21 F 637 ARG SER LEU LEU TYR LEU GLU GLU GLN THR ARG LEU ARG
SEQRES 22 F 637 LEU GLU GLN GLU ASN THR PRO ILE GLU PRO GLY VAL LEU
SEQRES 23 F 637 PHE SER PRO PRO PRO ALA SER ALA TYR ASP GLY VAL GLU
SEQRES 24 F 637 PHE LEU GLU PHE ALA VAL ASP GLU ALA VAL GLY ALA ARG
SEQRES 25 F 637 LEU GLY ASN TRP LEU LYS ARG LEU GLY PHE ALA GLU ALA
SEQRES 26 F 637 GLY LYS HIS ARG SER LYS GLU VAL GLN LEU LEU ARG GLN
SEQRES 27 F 637 GLY ASP ILE ASN ILE VAL LEU ASN ALA GLU PRO TYR SER
SEQRES 28 F 637 PHE GLY HIS ASN PHE PHE GLU ALA HIS GLY PRO SER LEU
SEQRES 29 F 637 CYS ALA THR ALA LEU ARG VAL LYS ASP GLN GLN ALA ALA
SEQRES 30 F 637 LEU LYS ARG ALA THR ALA PHE ARG GLY GLN PRO PHE ARG
SEQRES 31 F 637 GLY LEU VAL GLY PRO ASN GLU CYS GLU VAL PRO ALA VAL
SEQRES 32 F 637 ARG ALA PRO ASP GLY SER LEU LEU TYR LEU VAL GLU GLN
SEQRES 33 F 637 GLY THR ALA GLY HIS THR LEU TYR ASP THR ASP PHE SER
SEQRES 34 F 637 LEU ASP ASN ASN ALA THR ALA THR GLY GLY LEU ARG ARG
SEQRES 35 F 637 ILE ASP HIS MSE ALA LEU ALA LEU PRO ALA GLU SER LEU
SEQRES 36 F 637 ASP SER TRP VAL LEU PHE TYR LYS SER LEU PHE ASP PHE
SEQRES 37 F 637 ALA ALA ASP ASP GLU VAL VAL LEU PRO ASP PRO TYR GLY
SEQRES 38 F 637 LEU VAL LYS SER ARG ALA LEU ARG SER GLN CYS GLY THR
SEQRES 39 F 637 LEU ARG LEU PRO LEU ASN ILE SER GLU ASN ARG ASN THR
SEQRES 40 F 637 ALA ILE ALA HIS ALA LEU SER SER TYR ARG GLY SER GLY
SEQRES 41 F 637 VAL HIS HIS ILE ALA PHE ASP CYS ASP ASP ILE PHE ARG
SEQRES 42 F 637 GLU VAL ALA ARG ALA LYS LEU ALA GLY VAL PRO LEU LEU
SEQRES 43 F 637 GLU ILE PRO LEU ASN TYR TYR ASP ASP LEU ALA ALA ARG
SEQRES 44 F 637 PHE ASP PHE ASP ASP GLU PHE LEU SER GLU LEU ALA TYR
SEQRES 45 F 637 TYR ASN VAL LEU TYR ASP ARG ASP ALA GLN GLY GLY GLU
SEQRES 46 F 637 LEU PHE HIS VAL TYR THR GLU PRO PHE GLU GLU ARG PHE
SEQRES 47 F 637 PHE PHE GLU ILE ILE GLN ARG LYS ALA GLY TYR ALA GLY
SEQRES 48 F 637 TYR GLY ALA ALA ASN VAL ALA VAL ARG LEU ALA ALA MSE
SEQRES 49 F 637 ALA LYS ALA ARG SER GLY ALA ALA ARG LYS PRO VAL LEU
MODRES 5HMQ MSE A 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE A 622 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE B 622 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE C 622 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE D 622 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE E 622 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 1 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 49 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 88 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 192 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 200 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 218 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 220 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 444 MET MODIFIED RESIDUE
MODRES 5HMQ MSE F 622 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 49 8
HET MSE A 88 8
HET MSE A 192 8
HET MSE A 200 8
HET MSE A 218 8
HET MSE A 220 8
HET MSE A 444 8
HET MSE A 622 8
HET MSE B 1 8
HET MSE B 49 8
HET MSE B 88 8
HET MSE B 192 8
HET MSE B 200 8
HET MSE B 218 8
HET MSE B 220 8
HET MSE B 444 8
HET MSE B 622 8
HET MSE C 1 8
HET MSE C 49 8
HET MSE C 88 8
HET MSE C 192 8
HET MSE C 200 8
HET MSE C 218 8
HET MSE C 220 8
HET MSE C 444 8
HET MSE C 622 8
HET MSE D 1 8
HET MSE D 49 8
HET MSE D 88 8
HET MSE D 192 8
HET MSE D 200 8
HET MSE D 218 8
HET MSE D 220 8
HET MSE D 444 8
HET MSE D 622 8
HET MSE E 1 8
HET MSE E 49 8
HET MSE E 88 8
HET MSE E 192 8
HET MSE E 200 8
HET MSE E 218 8
HET MSE E 220 8
HET MSE E 444 8
HET MSE E 622 8
HET MSE F 1 8
HET MSE F 49 8
HET MSE F 88 8
HET MSE F 192 8
HET MSE F 200 8
HET MSE F 218 8
HET MSE F 220 8
HET MSE F 444 8
HET MSE F 622 8
HET MG A 701 1
HET MG A 702 1
HET MG B 701 1
HET MG B 702 1
HET MG C 701 1
HET MG C 702 1
HET MG D 701 1
HET MG D 702 1
HET MG E 701 1
HET MG E 702 1
HET MG F 701 1
HET MG F 702 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 54(C5 H11 N O2 SE)
FORMUL 7 MG 12(MG 2+)
FORMUL 19 HOH *1084(H2 O)
HELIX 1 AA1 VAL A 8 LEU A 10 5 3
HELIX 2 AA2 THR A 13 ALA A 24 1 12
HELIX 3 AA3 GLU A 33 TYR A 39 1 7
HELIX 4 AA4 SER A 42 GLY A 54 1 13
HELIX 5 AA5 ARG A 70 ASP A 72 5 3
HELIX 6 AA6 ARG A 73 GLY A 92 1 20
HELIX 7 AA7 ASP A 109 GLY A 128 1 20
HELIX 8 AA8 THR A 144 ASP A 156 1 13
HELIX 9 AA9 SER A 166 SER A 171 1 6
HELIX 10 AB1 ASP A 175 ILE A 182 5 8
HELIX 11 AB2 PRO A 183 ASP A 185 5 3
HELIX 12 AB3 ASP A 201 ARG A 210 1 10
HELIX 13 AB4 ASP A 219 THR A 230 1 12
HELIX 14 AB5 PRO A 249 GLU A 275 1 27
HELIX 15 AB6 ASP A 304 LEU A 318 1 15
HELIX 16 AB7 SER A 349 GLY A 359 1 11
HELIX 17 AB8 ASP A 371 PHE A 382 1 12
HELIX 18 AB9 LEU A 421 ASP A 425 1 5
HELIX 19 AC1 PRO A 449 GLU A 451 5 3
HELIX 20 AC2 SER A 452 PHE A 464 1 13
HELIX 21 AC3 ASN A 502 HIS A 509 1 8
HELIX 22 AC4 ASP A 528 GLY A 540 1 13
HELIX 23 AC5 PRO A 547 PHE A 558 1 12
HELIX 24 AC6 GLU A 563 TYR A 571 1 9
HELIX 25 AC7 GLY A 611 ALA A 613 5 3
HELIX 26 AC8 ASN A 614 ALA A 625 1 12
HELIX 27 AC9 VAL B 8 LEU B 10 5 3
HELIX 28 AD1 THR B 13 ALA B 24 1 12
HELIX 29 AD2 GLU B 33 TYR B 39 1 7
HELIX 30 AD3 SER B 42 GLY B 54 1 13
HELIX 31 AD4 ARG B 70 ASP B 72 5 3
HELIX 32 AD5 ARG B 73 GLY B 92 1 20
HELIX 33 AD6 ASP B 109 ARG B 127 1 19
HELIX 34 AD7 THR B 144 ASP B 156 1 13
HELIX 35 AD8 SER B 166 SER B 171 1 6
HELIX 36 AD9 ASP B 175 ILE B 182 5 8
HELIX 37 AE1 PRO B 183 ASP B 185 5 3
HELIX 38 AE2 ASP B 201 ARG B 210 1 10
HELIX 39 AE3 ASP B 219 THR B 230 1 12
HELIX 40 AE4 PRO B 249 GLU B 275 1 27
HELIX 41 AE5 ASP B 304 LEU B 318 1 15
HELIX 42 AE6 SER B 349 GLY B 359 1 11
HELIX 43 AE7 ASP B 371 PHE B 382 1 12
HELIX 44 AE8 LEU B 421 ASP B 425 1 5
HELIX 45 AE9 PRO B 449 GLU B 451 5 3
HELIX 46 AF1 SER B 452 PHE B 464 1 13
HELIX 47 AF2 ASN B 502 HIS B 509 1 8
HELIX 48 AF3 ASP B 528 GLY B 540 1 13
HELIX 49 AF4 PRO B 547 PHE B 558 1 12
HELIX 50 AF5 ASP B 562 TYR B 571 1 10
HELIX 51 AF6 PRO B 591 ARG B 595 5 5
HELIX 52 AF7 GLY B 611 ALA B 613 5 3
HELIX 53 AF8 ASN B 614 ARG B 626 1 13
HELIX 54 AF9 VAL C 8 LEU C 10 5 3
HELIX 55 AG1 THR C 13 ALA C 24 1 12
HELIX 56 AG2 GLU C 33 TYR C 39 1 7
HELIX 57 AG3 SER C 42 GLY C 54 1 13
HELIX 58 AG4 ARG C 70 ASP C 72 5 3
HELIX 59 AG5 ARG C 73 GLY C 92 1 20
HELIX 60 AG6 ASP C 109 ARG C 127 1 19
HELIX 61 AG7 THR C 144 ASP C 156 1 13
HELIX 62 AG8 SER C 166 SER C 171 1 6
HELIX 63 AG9 ASP C 175 ILE C 182 5 8
HELIX 64 AH1 PRO C 183 ASP C 185 5 3
HELIX 65 AH2 ASP C 201 ARG C 210 1 10
HELIX 66 AH3 ASP C 219 THR C 230 1 12
HELIX 67 AH4 PRO C 249 GLU C 275 1 27
HELIX 68 AH5 ASP C 304 LEU C 318 1 15
HELIX 69 AH6 SER C 349 GLY C 359 1 11
HELIX 70 AH7 ASP C 371 PHE C 382 1 12
HELIX 71 AH8 LEU C 421 ASP C 425 1 5
HELIX 72 AH9 PRO C 449 GLU C 451 5 3
HELIX 73 AI1 SER C 452 PHE C 464 1 13
HELIX 74 AI2 ASN C 502 HIS C 509 1 8
HELIX 75 AI3 ASP C 528 GLY C 540 1 13
HELIX 76 AI4 PRO C 547 PHE C 558 1 12
HELIX 77 AI5 ASP C 561 TYR C 571 1 11
HELIX 78 AI6 PRO C 591 ARG C 595 5 5
HELIX 79 AI7 GLY C 611 ALA C 613 5 3
HELIX 80 AI8 ASN C 614 LYS C 624 1 11
HELIX 81 AI9 VAL D 8 LEU D 10 5 3
HELIX 82 AJ1 THR D 13 ALA D 24 1 12
HELIX 83 AJ2 GLU D 33 TYR D 39 1 7
HELIX 84 AJ3 SER D 42 GLY D 54 1 13
HELIX 85 AJ4 ARG D 70 ASP D 72 5 3
HELIX 86 AJ5 ARG D 73 GLY D 92 1 20
HELIX 87 AJ6 ASP D 109 GLY D 128 1 20
HELIX 88 AJ7 THR D 144 ASP D 156 1 13
HELIX 89 AJ8 SER D 166 SER D 171 1 6
HELIX 90 AJ9 ASP D 175 ILE D 182 5 8
HELIX 91 AK1 PRO D 183 ASP D 185 5 3
HELIX 92 AK2 ASP D 201 ARG D 210 1 10
HELIX 93 AK3 ASP D 219 THR D 230 1 12
HELIX 94 AK4 PRO D 249 GLU D 275 1 27
HELIX 95 AK5 ASP D 304 LEU D 318 1 15
HELIX 96 AK6 SER D 349 GLY D 359 1 11
HELIX 97 AK7 ASP D 371 PHE D 382 1 12
HELIX 98 AK8 LEU D 421 ASP D 425 1 5
HELIX 99 AK9 PRO D 449 GLU D 451 5 3
HELIX 100 AL1 SER D 452 PHE D 464 1 13
HELIX 101 AL2 ASN D 502 HIS D 509 1 8
HELIX 102 AL3 ASP D 528 GLY D 540 1 13
HELIX 103 AL4 PRO D 547 PHE D 558 1 12
HELIX 104 AL5 GLU D 563 TYR D 571 1 9
HELIX 105 AL6 PRO D 591 ARG D 595 5 5
HELIX 106 AL7 GLY D 611 ALA D 613 5 3
HELIX 107 AL8 ASN D 614 ALA D 625 1 12
HELIX 108 AL9 VAL E 8 LEU E 10 5 3
HELIX 109 AM1 THR E 13 ALA E 24 1 12
HELIX 110 AM2 GLU E 33 TYR E 39 1 7
HELIX 111 AM3 SER E 42 GLY E 54 1 13
HELIX 112 AM4 ARG E 70 ASP E 72 5 3
HELIX 113 AM5 ARG E 73 GLY E 92 1 20
HELIX 114 AM6 ASP E 109 GLY E 128 1 20
HELIX 115 AM7 THR E 144 ASP E 156 1 13
HELIX 116 AM8 SER E 166 SER E 171 1 6
HELIX 117 AM9 ASP E 175 ILE E 182 5 8
HELIX 118 AN1 PRO E 183 ASP E 185 5 3
HELIX 119 AN2 ASP E 201 ARG E 210 1 10
HELIX 120 AN3 ASP E 219 THR E 230 1 12
HELIX 121 AN4 PRO E 249 GLU E 275 1 27
HELIX 122 AN5 ASP E 304 LEU E 318 1 15
HELIX 123 AN6 SER E 349 GLY E 359 1 11
HELIX 124 AN7 ASP E 371 PHE E 382 1 12
HELIX 125 AN8 LEU E 421 ASP E 425 1 5
HELIX 126 AN9 PRO E 449 GLU E 451 5 3
HELIX 127 AO1 SER E 452 PHE E 464 1 13
HELIX 128 AO2 ASN E 502 HIS E 509 1 8
HELIX 129 AO3 ASP E 528 GLY E 540 1 13
HELIX 130 AO4 PRO E 547 PHE E 558 1 12
HELIX 131 AO5 GLU E 563 TYR E 571 1 9
HELIX 132 AO6 PRO E 591 ARG E 595 5 5
HELIX 133 AO7 GLY E 611 ALA E 613 5 3
HELIX 134 AO8 ASN E 614 SER E 627 1 14
HELIX 135 AO9 VAL F 8 LEU F 10 5 3
HELIX 136 AP1 THR F 13 ALA F 24 1 12
HELIX 137 AP2 GLU F 33 TYR F 39 1 7
HELIX 138 AP3 SER F 42 GLY F 54 1 13
HELIX 139 AP4 ARG F 70 ASP F 72 5 3
HELIX 140 AP5 ARG F 73 GLY F 92 1 20
HELIX 141 AP6 ASP F 109 GLY F 128 1 20
HELIX 142 AP7 THR F 144 ASP F 156 1 13
HELIX 143 AP8 SER F 166 SER F 171 1 6
HELIX 144 AP9 ASP F 175 ILE F 182 5 8
HELIX 145 AQ1 PRO F 183 ASP F 185 5 3
HELIX 146 AQ2 ASP F 201 ARG F 210 1 10
HELIX 147 AQ3 ASP F 219 THR F 230 1 12
HELIX 148 AQ4 PRO F 249 GLU F 275 1 27
HELIX 149 AQ5 ASP F 304 LEU F 318 1 15
HELIX 150 AQ6 SER F 349 GLY F 359 1 11
HELIX 151 AQ7 ASP F 371 PHE F 382 1 12
HELIX 152 AQ8 LEU F 421 ASP F 425 1 5
HELIX 153 AQ9 PRO F 449 GLU F 451 5 3
HELIX 154 AR1 SER F 452 PHE F 464 1 13
HELIX 155 AR2 ASN F 502 HIS F 509 1 8
HELIX 156 AR3 ASP F 528 GLY F 540 1 13
HELIX 157 AR4 PRO F 547 PHE F 558 1 12
HELIX 158 AR5 GLU F 563 TYR F 571 1 9
HELIX 159 AR6 PRO F 591 ARG F 595 5 5
HELIX 160 AR7 GLY F 611 ALA F 613 5 3
HELIX 161 AR8 ASN F 614 SER F 627 1 14
SHEET 1 AA1 8 SER A 4 ALA A 6 0
SHEET 2 AA1 8 GLY A 28 PHE A 32 1 O GLU A 30 N ILE A 5
SHEET 3 AA1 8 ALA A 56 ARG A 64 1 O LEU A 59 N ILE A 31
SHEET 4 AA1 8 LEU A 95 CYS A 99 1 O LEU A 95 N PHE A 60
SHEET 5 AA1 8 ARG A 130 GLU A 134 1 O GLY A 132 N VAL A 98
SHEET 6 AA1 8 LEU A 160 ASP A 165 1 O GLY A 161 N ILE A 131
SHEET 7 AA1 8 ILE A 187 MSE A 192 1 O GLN A 191 N LEU A 164
SHEET 8 AA1 8 LEU A 236 LEU A 238 1 O SER A 237 N MSE A 192
SHEET 1 AA2 9 PRO A 386 PHE A 387 0
SHEET 2 AA2 9 ALA A 400 ARG A 402 -1 O ALA A 400 N PHE A 387
SHEET 3 AA2 9 LEU A 408 GLU A 413 -1 O LEU A 409 N VAL A 401
SHEET 4 AA2 9 SER A 361 VAL A 369 1 N LEU A 367 O TYR A 410
SHEET 5 AA2 9 TYR A 293 ALA A 302 -1 N ALA A 302 O SER A 361
SHEET 6 AA2 9 ILE A 339 ASN A 344 1 O VAL A 342 N LEU A 299
SHEET 7 AA2 9 VAL A 331 GLN A 336 -1 N GLN A 332 O LEU A 343
SHEET 8 AA2 9 ALA A 321 HIS A 326 -1 N ALA A 321 O ARG A 335
SHEET 9 AA2 9 PHE A 426 LEU A 428 -1 O SER A 427 N LYS A 325
SHEET 1 AA3 3 ALA A 467 ALA A 468 0
SHEET 2 AA3 3 LYS A 482 ARG A 487 -1 O ARG A 487 N ALA A 467
SHEET 3 AA3 3 GLU A 471 VAL A 472 -1 N GLU A 471 O SER A 483
SHEET 1 AA4 8 ALA A 467 ALA A 468 0
SHEET 2 AA4 8 LYS A 482 ARG A 487 -1 O ARG A 487 N ALA A 467
SHEET 3 AA4 8 ARG A 494 ILE A 499 -1 O LEU A 495 N LEU A 486
SHEET 4 AA4 8 ARG A 440 LEU A 448 1 N LEU A 446 O ASN A 498
SHEET 5 AA4 8 GLY A 518 ASP A 525 -1 O HIS A 520 N ALA A 445
SHEET 6 AA4 8 PHE A 597 ARG A 603 1 O GLU A 599 N PHE A 524
SHEET 7 AA4 8 GLU A 583 TYR A 588 -1 N PHE A 585 O GLN A 602
SHEET 8 AA4 8 LEU A 574 ARG A 577 -1 N LEU A 574 O HIS A 586
SHEET 1 AA5 8 SER B 4 ALA B 6 0
SHEET 2 AA5 8 GLY B 28 PHE B 32 1 O GLU B 30 N ILE B 5
SHEET 3 AA5 8 ALA B 56 ARG B 64 1 O LEU B 59 N ILE B 31
SHEET 4 AA5 8 LEU B 95 CYS B 99 1 O LEU B 97 N PHE B 60
SHEET 5 AA5 8 ARG B 130 GLU B 134 1 O GLY B 132 N VAL B 98
SHEET 6 AA5 8 LEU B 160 ASP B 165 1 O GLY B 161 N ILE B 131
SHEET 7 AA5 8 ILE B 187 MSE B 192 1 O GLN B 191 N LEU B 164
SHEET 8 AA5 8 LEU B 236 LEU B 238 1 O SER B 237 N MSE B 192
SHEET 1 AA6 9 PRO B 386 PHE B 387 0
SHEET 2 AA6 9 ALA B 400 ARG B 402 -1 O ALA B 400 N PHE B 387
SHEET 3 AA6 9 LEU B 408 GLU B 413 -1 O LEU B 409 N VAL B 401
SHEET 4 AA6 9 SER B 361 VAL B 369 1 N LEU B 367 O TYR B 410
SHEET 5 AA6 9 TYR B 293 ALA B 302 -1 N ALA B 302 O SER B 361
SHEET 6 AA6 9 ILE B 339 ASN B 344 1 O VAL B 342 N LEU B 299
SHEET 7 AA6 9 VAL B 331 GLN B 336 -1 N GLN B 332 O LEU B 343
SHEET 8 AA6 9 ALA B 321 HIS B 326 -1 N ALA B 321 O ARG B 335
SHEET 9 AA6 9 PHE B 426 LEU B 428 -1 O SER B 427 N LYS B 325
SHEET 1 AA7 6 ASN B 498 ILE B 499 0
SHEET 2 AA7 6 ILE B 441 LEU B 448 1 N LEU B 446 O ASN B 498
SHEET 3 AA7 6 GLY B 518 ASP B 525 -1 O GLY B 518 N ALA B 447
SHEET 4 AA7 6 PHE B 597 LYS B 604 1 O GLU B 599 N PHE B 524
SHEET 5 AA7 6 GLU B 583 TYR B 588 -1 N GLU B 583 O LYS B 604
SHEET 6 AA7 6 LEU B 574 ARG B 577 -1 N ASP B 576 O LEU B 584
SHEET 1 AA8 2 ALA B 467 ALA B 468 0
SHEET 2 AA8 2 LEU B 486 ARG B 487 -1 O ARG B 487 N ALA B 467
SHEET 1 AA9 2 GLU B 471 VAL B 472 0
SHEET 2 AA9 2 LYS B 482 SER B 483 -1 O SER B 483 N GLU B 471
SHEET 1 AB1 8 SER C 4 ALA C 6 0
SHEET 2 AB1 8 GLY C 28 PHE C 32 1 O GLU C 30 N ILE C 5
SHEET 3 AB1 8 ALA C 56 ARG C 64 1 O LEU C 59 N ILE C 31
SHEET 4 AB1 8 LEU C 95 CYS C 99 1 O LEU C 95 N PHE C 60
SHEET 5 AB1 8 ARG C 130 GLU C 134 1 O GLY C 132 N VAL C 98
SHEET 6 AB1 8 LEU C 160 ASP C 165 1 O GLY C 161 N ILE C 131
SHEET 7 AB1 8 ILE C 187 MSE C 192 1 O GLN C 191 N LEU C 164
SHEET 8 AB1 8 LEU C 236 LEU C 238 1 O SER C 237 N MSE C 192
SHEET 1 AB2 9 PRO C 386 PHE C 387 0
SHEET 2 AB2 9 ALA C 400 ARG C 402 -1 O ALA C 400 N PHE C 387
SHEET 3 AB2 9 LEU C 408 VAL C 412 -1 O LEU C 409 N VAL C 401
SHEET 4 AB2 9 SER C 361 VAL C 369 1 N LEU C 367 O TYR C 410
SHEET 5 AB2 9 TYR C 293 ALA C 302 -1 N ALA C 302 O SER C 361
SHEET 6 AB2 9 ILE C 339 ASN C 344 1 O VAL C 342 N LEU C 299
SHEET 7 AB2 9 VAL C 331 GLN C 336 -1 N GLN C 332 O LEU C 343
SHEET 8 AB2 9 ALA C 321 HIS C 326 -1 N HIS C 326 O VAL C 331
SHEET 9 AB2 9 PHE C 426 LEU C 428 -1 O SER C 427 N LYS C 325
SHEET 1 AB3 3 ALA C 467 ALA C 468 0
SHEET 2 AB3 3 LYS C 482 ARG C 487 -1 O ARG C 487 N ALA C 467
SHEET 3 AB3 3 GLU C 471 VAL C 472 -1 N GLU C 471 O SER C 483
SHEET 1 AB4 8 ALA C 467 ALA C 468 0
SHEET 2 AB4 8 LYS C 482 ARG C 487 -1 O ARG C 487 N ALA C 467
SHEET 3 AB4 8 ARG C 494 ILE C 499 -1 O LEU C 497 N ARG C 484
SHEET 4 AB4 8 LEU C 438 LEU C 448 1 N LEU C 446 O ASN C 498
SHEET 5 AB4 8 GLY C 518 CYS C 526 -1 O HIS C 520 N ALA C 445
SHEET 6 AB4 8 PHE C 597 LYS C 604 1 O GLU C 599 N PHE C 524
SHEET 7 AB4 8 GLU C 583 TYR C 588 -1 N GLU C 583 O LYS C 604
SHEET 8 AB4 8 LEU C 574 ARG C 577 -1 N ASP C 576 O LEU C 584
SHEET 1 AB5 8 SER D 4 ALA D 6 0
SHEET 2 AB5 8 GLY D 28 PHE D 32 1 O GLU D 30 N ILE D 5
SHEET 3 AB5 8 ALA D 56 ARG D 64 1 O LEU D 59 N ILE D 31
SHEET 4 AB5 8 LEU D 95 CYS D 99 1 O LEU D 97 N PHE D 60
SHEET 5 AB5 8 ARG D 130 GLU D 134 1 O GLY D 132 N VAL D 98
SHEET 6 AB5 8 LEU D 160 ASP D 165 1 O GLY D 161 N ILE D 131
SHEET 7 AB5 8 ILE D 187 MSE D 192 1 O GLN D 191 N LEU D 164
SHEET 8 AB5 8 LEU D 236 LEU D 238 1 O SER D 237 N MSE D 192
SHEET 1 AB6 9 PRO D 386 PHE D 387 0
SHEET 2 AB6 9 ALA D 400 ARG D 402 -1 O ALA D 400 N PHE D 387
SHEET 3 AB6 9 LEU D 408 VAL D 412 -1 O LEU D 409 N VAL D 401
SHEET 4 AB6 9 SER D 361 VAL D 369 1 N LEU D 367 O TYR D 410
SHEET 5 AB6 9 TYR D 293 ALA D 302 -1 N ALA D 302 O SER D 361
SHEET 6 AB6 9 ILE D 339 ASN D 344 1 O VAL D 342 N LEU D 299
SHEET 7 AB6 9 VAL D 331 GLN D 336 -1 N GLN D 332 O LEU D 343
SHEET 8 AB6 9 ALA D 321 HIS D 326 -1 N ALA D 321 O ARG D 335
SHEET 9 AB6 9 PHE D 426 LEU D 428 -1 O SER D 427 N LYS D 325
SHEET 1 AB7 8 ALA D 467 ALA D 468 0
SHEET 2 AB7 8 ALA D 485 ARG D 487 -1 O ARG D 487 N ALA D 467
SHEET 3 AB7 8 ARG D 494 ILE D 499 -1 O LEU D 495 N LEU D 486
SHEET 4 AB7 8 ILE D 441 LEU D 448 1 N LEU D 446 O ASN D 498
SHEET 5 AB7 8 GLY D 518 ASP D 525 -1 O GLY D 518 N ALA D 447
SHEET 6 AB7 8 PHE D 597 LYS D 604 1 O GLU D 599 N PHE D 524
SHEET 7 AB7 8 GLU D 583 TYR D 588 -1 N GLU D 583 O LYS D 604
SHEET 8 AB7 8 LEU D 574 ARG D 577 -1 N ASP D 576 O LEU D 584
SHEET 1 AB8 2 GLU D 471 VAL D 472 0
SHEET 2 AB8 2 LYS D 482 SER D 483 -1 O SER D 483 N GLU D 471
SHEET 1 AB9 8 SER E 4 ALA E 6 0
SHEET 2 AB9 8 GLY E 28 PHE E 32 1 O GLU E 30 N ILE E 5
SHEET 3 AB9 8 ALA E 56 ARG E 64 1 O LEU E 59 N ILE E 31
SHEET 4 AB9 8 LEU E 95 CYS E 99 1 O LEU E 97 N PHE E 60
SHEET 5 AB9 8 ARG E 130 GLU E 134 1 O GLY E 132 N VAL E 98
SHEET 6 AB9 8 LEU E 160 ASP E 165 1 O GLY E 161 N ILE E 131
SHEET 7 AB9 8 ILE E 187 MSE E 192 1 O PHE E 188 N VAL E 162
SHEET 8 AB9 8 LEU E 236 LEU E 238 1 O SER E 237 N MSE E 192
SHEET 1 AC1 9 PRO E 386 PHE E 387 0
SHEET 2 AC1 9 ALA E 400 ARG E 402 -1 O ALA E 400 N PHE E 387
SHEET 3 AC1 9 LEU E 408 VAL E 412 -1 O LEU E 409 N VAL E 401
SHEET 4 AC1 9 SER E 361 VAL E 369 1 N LEU E 367 O TYR E 410
SHEET 5 AC1 9 TYR E 293 ALA E 302 -1 N ALA E 302 O SER E 361
SHEET 6 AC1 9 ILE E 339 ASN E 344 1 O VAL E 342 N LEU E 299
SHEET 7 AC1 9 VAL E 331 GLN E 336 -1 N GLN E 332 O LEU E 343
SHEET 8 AC1 9 ALA E 321 HIS E 326 -1 N HIS E 326 O VAL E 331
SHEET 9 AC1 9 PHE E 426 LEU E 428 -1 O SER E 427 N LYS E 325
SHEET 1 AC2 3 ALA E 467 ALA E 468 0
SHEET 2 AC2 3 LYS E 482 ARG E 487 -1 O ARG E 487 N ALA E 467
SHEET 3 AC2 3 GLU E 471 VAL E 472 -1 N GLU E 471 O SER E 483
SHEET 1 AC3 8 ALA E 467 ALA E 468 0
SHEET 2 AC3 8 LYS E 482 ARG E 487 -1 O ARG E 487 N ALA E 467
SHEET 3 AC3 8 ARG E 494 ILE E 499 -1 O LEU E 495 N LEU E 486
SHEET 4 AC3 8 ILE E 441 LEU E 448 1 N LEU E 446 O ASN E 498
SHEET 5 AC3 8 GLY E 518 ASP E 525 -1 O HIS E 520 N ALA E 445
SHEET 6 AC3 8 PHE E 597 LYS E 604 1 O GLU E 599 N PHE E 524
SHEET 7 AC3 8 GLU E 583 TYR E 588 -1 N GLU E 583 O LYS E 604
SHEET 8 AC3 8 LEU E 574 ARG E 577 -1 N ASP E 576 O LEU E 584
SHEET 1 AC4 8 SER F 4 ALA F 6 0
SHEET 2 AC4 8 GLY F 28 PHE F 32 1 O GLU F 30 N ILE F 5
SHEET 3 AC4 8 ALA F 56 ARG F 64 1 O LEU F 59 N ILE F 31
SHEET 4 AC4 8 LEU F 95 CYS F 99 1 O LEU F 97 N PHE F 60
SHEET 5 AC4 8 ARG F 130 GLU F 134 1 O GLY F 132 N VAL F 98
SHEET 6 AC4 8 LEU F 160 ASP F 165 1 O GLY F 161 N ILE F 131
SHEET 7 AC4 8 ILE F 187 MSE F 192 1 O PHE F 188 N VAL F 162
SHEET 8 AC4 8 LEU F 236 LEU F 238 1 O SER F 237 N MSE F 192
SHEET 1 AC5 9 PRO F 386 PHE F 387 0
SHEET 2 AC5 9 ALA F 400 ARG F 402 -1 O ALA F 400 N PHE F 387
SHEET 3 AC5 9 LEU F 408 VAL F 412 -1 O LEU F 409 N VAL F 401
SHEET 4 AC5 9 SER F 361 VAL F 369 1 N LEU F 367 O TYR F 410
SHEET 5 AC5 9 TYR F 293 ALA F 302 -1 N ALA F 302 O SER F 361
SHEET 6 AC5 9 ILE F 339 ASN F 344 1 O VAL F 342 N LEU F 299
SHEET 7 AC5 9 VAL F 331 GLN F 336 -1 N GLN F 332 O LEU F 343
SHEET 8 AC5 9 ALA F 321 HIS F 326 -1 N ALA F 321 O ARG F 335
SHEET 9 AC5 9 PHE F 426 LEU F 428 -1 O SER F 427 N LYS F 325
SHEET 1 AC6 3 ALA F 467 ALA F 468 0
SHEET 2 AC6 3 LYS F 482 ARG F 487 -1 O ARG F 487 N ALA F 467
SHEET 3 AC6 3 GLU F 471 VAL F 472 -1 N GLU F 471 O SER F 483
SHEET 1 AC7 8 ALA F 467 ALA F 468 0
SHEET 2 AC7 8 LYS F 482 ARG F 487 -1 O ARG F 487 N ALA F 467
SHEET 3 AC7 8 ARG F 494 ILE F 499 -1 O LEU F 495 N LEU F 486
SHEET 4 AC7 8 ARG F 440 LEU F 448 1 N LEU F 446 O ASN F 498
SHEET 5 AC7 8 GLY F 518 ASP F 525 -1 O GLY F 518 N ALA F 447
SHEET 6 AC7 8 PHE F 597 LYS F 604 1 O GLU F 599 N PHE F 524
SHEET 7 AC7 8 GLU F 583 TYR F 588 -1 N GLU F 583 O LYS F 604
SHEET 8 AC7 8 LEU F 574 ARG F 577 -1 N LEU F 574 O HIS F 586
LINK C LYS A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N GLN A 2 1555 1555 1.33
LINK C GLN A 48 N MSE A 49 1555 1555 1.33
LINK C MSE A 49 N CYS A 50 1555 1555 1.34
LINK C LEU A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N GLN A 89 1555 1555 1.33
LINK OE2 GLU A 134 MG MG A 701 1555 1555 2.03
LINK OD2 ASP A 165 MG MG A 701 1555 1555 2.08
LINK C GLN A 191 N MSE A 192 1555 1555 1.33
LINK OE1 GLN A 191 MG MG A 701 1555 1555 2.16
LINK C MSE A 192 N ALA A 193 1555 1555 1.33
LINK C ALA A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N ASP A 201 1555 1555 1.33
LINK C GLU A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N ASP A 219 1555 1555 1.33
LINK C ASP A 219 N MSE A 220 1555 1555 1.33
LINK C MSE A 220 N ALA A 221 1555 1555 1.34
LINK OE1 GLU A 239 MG MG A 701 1555 1555 2.08
LINK C HIS A 443 N MSE A 444 1555 1555 1.33
LINK C MSE A 444 N ALA A 445 1555 1555 1.33
LINK OE1 GLU A 599 MG MG A 702 1555 1555 2.16
LINK C ALA A 621 N MSE A 622 1555 1555 1.33
LINK C MSE A 622 N ALA A 623 1555 1555 1.33
LINK C LYS B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C GLN B 48 N MSE B 49 1555 1555 1.33
LINK C MSE B 49 N CYS B 50 1555 1555 1.34
LINK C LEU B 87 N MSE B 88 1555 1555 1.33
LINK C MSE B 88 N GLN B 89 1555 1555 1.34
LINK OE1 GLU B 134 MG MG B 701 1555 1555 2.14
LINK OD2 ASP B 165 MG MG B 701 1555 1555 2.22
LINK C GLN B 191 N MSE B 192 1555 1555 1.33
LINK OE1 GLN B 191 MG MG B 701 1555 1555 2.41
LINK C MSE B 192 N ALA B 193 1555 1555 1.33
LINK C ALA B 199 N MSE B 200 1555 1555 1.33
LINK C MSE B 200 N ASP B 201 1555 1555 1.33
LINK C GLU B 217 N MSE B 218 1555 1555 1.33
LINK C MSE B 218 N ASP B 219 1555 1555 1.33
LINK C ASP B 219 N MSE B 220 1555 1555 1.33
LINK C MSE B 220 N ALA B 221 1555 1555 1.34
LINK OE1 GLU B 239 MG MG B 701 1555 1555 1.95
LINK C HIS B 443 N MSE B 444 1555 1555 1.33
LINK C MSE B 444 N ALA B 445 1555 1555 1.33
LINK OE1 GLU B 599 MG MG B 702 1555 1555 2.14
LINK C ALA B 621 N MSE B 622 1555 1555 1.33
LINK C MSE B 622 N ALA B 623 1555 1555 1.34
LINK C LYS C 0 N MSE C 1 1555 1555 1.33
LINK C MSE C 1 N GLN C 2 1555 1555 1.33
LINK C GLN C 48 N MSE C 49 1555 1555 1.33
LINK C MSE C 49 N CYS C 50 1555 1555 1.34
LINK NH1 ARG C 70 OD1 ASP C 72 1555 1555 1.30
LINK C LEU C 87 N MSE C 88 1555 1555 1.33
LINK C MSE C 88 N GLN C 89 1555 1555 1.33
LINK OE1 GLU C 134 MG MG C 701 1555 1555 2.06
LINK OD2 ASP C 165 MG MG C 701 1555 1555 2.10
LINK C GLN C 191 N MSE C 192 1555 1555 1.33
LINK OE1 GLN C 191 MG MG C 701 1555 1555 2.04
LINK C MSE C 192 N ALA C 193 1555 1555 1.33
LINK C ALA C 199 N MSE C 200 1555 1555 1.33
LINK C MSE C 200 N ASP C 201 1555 1555 1.33
LINK C GLU C 217 N MSE C 218 1555 1555 1.33
LINK C MSE C 218 N ASP C 219 1555 1555 1.33
LINK C ASP C 219 N MSE C 220 1555 1555 1.33
LINK C MSE C 220 N ALA C 221 1555 1555 1.34
LINK OE1 GLU C 239 MG MG C 701 1555 1555 2.08
LINK C HIS C 443 N MSE C 444 1555 1555 1.33
LINK C MSE C 444 N ALA C 445 1555 1555 1.33
LINK OE1 GLU C 599 MG MG C 702 1555 1555 2.29
LINK C ALA C 621 N MSE C 622 1555 1555 1.33
LINK C MSE C 622 N ALA C 623 1555 1555 1.34
LINK C LYS D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N GLN D 2 1555 1555 1.33
LINK C GLN D 48 N MSE D 49 1555 1555 1.33
LINK C MSE D 49 N CYS D 50 1555 1555 1.34
LINK C LEU D 87 N MSE D 88 1555 1555 1.33
LINK C MSE D 88 N GLN D 89 1555 1555 1.34
LINK OE1 GLU D 134 MG MG D 701 1555 1555 2.12
LINK OD2 ASP D 165 MG MG D 701 1555 1555 2.09
LINK C GLN D 191 N MSE D 192 1555 1555 1.33
LINK OE1 GLN D 191 MG MG D 701 1555 1555 2.04
LINK C MSE D 192 N ALA D 193 1555 1555 1.33
LINK C ALA D 199 N MSE D 200 1555 1555 1.33
LINK C MSE D 200 N ASP D 201 1555 1555 1.33
LINK C GLU D 217 N MSE D 218 1555 1555 1.33
LINK C MSE D 218 N ASP D 219 1555 1555 1.33
LINK C ASP D 219 N MSE D 220 1555 1555 1.33
LINK C MSE D 220 N ALA D 221 1555 1555 1.34
LINK OE1 GLU D 239 MG MG D 701 1555 1555 2.05
LINK C HIS D 443 N MSE D 444 1555 1555 1.33
LINK C MSE D 444 N ALA D 445 1555 1555 1.33
LINK OE1 GLU D 599 MG MG D 702 1555 1555 2.33
LINK C ALA D 621 N MSE D 622 1555 1555 1.33
LINK C MSE D 622 N ALA D 623 1555 1555 1.34
LINK C LYS E 0 N MSE E 1 1555 1555 1.33
LINK C MSE E 1 N GLN E 2 1555 1555 1.33
LINK C GLN E 48 N MSE E 49 1555 1555 1.33
LINK C MSE E 49 N CYS E 50 1555 1555 1.33
LINK C LEU E 87 N MSE E 88 1555 1555 1.33
LINK C MSE E 88 N GLN E 89 1555 1555 1.33
LINK OE2 GLU E 134 MG MG E 701 1555 1555 2.13
LINK OD2 ASP E 165 MG MG E 701 1555 1555 2.04
LINK C GLN E 191 N MSE E 192 1555 1555 1.33
LINK C MSE E 192 N ALA E 193 1555 1555 1.33
LINK C ALA E 199 N MSE E 200 1555 1555 1.33
LINK C MSE E 200 N ASP E 201 1555 1555 1.33
LINK C GLU E 217 N MSE E 218 1555 1555 1.33
LINK C MSE E 218 N ASP E 219 1555 1555 1.33
LINK C ASP E 219 N MSE E 220 1555 1555 1.33
LINK C MSE E 220 N ALA E 221 1555 1555 1.34
LINK OE1 GLU E 239 MG MG E 701 1555 1555 2.07
LINK C HIS E 443 N MSE E 444 1555 1555 1.33
LINK C MSE E 444 N ALA E 445 1555 1555 1.33
LINK OE1 GLU E 599 MG MG E 702 1555 1555 2.22
LINK C ALA E 621 N MSE E 622 1555 1555 1.33
LINK C MSE E 622 N ALA E 623 1555 1555 1.34
LINK C LYS F 0 N MSE F 1 1555 1555 1.33
LINK C MSE F 1 N GLN F 2 1555 1555 1.33
LINK C GLN F 48 N MSE F 49 1555 1555 1.33
LINK C MSE F 49 N CYS F 50 1555 1555 1.34
LINK C LEU F 87 N MSE F 88 1555 1555 1.33
LINK C MSE F 88 N GLN F 89 1555 1555 1.34
LINK OE1 GLU F 134 MG MG F 701 1555 1555 2.15
LINK OD2 ASP F 165 MG MG F 701 1555 1555 2.12
LINK C GLN F 191 N MSE F 192 1555 1555 1.33
LINK OE1 GLN F 191 MG MG F 701 1555 1555 2.06
LINK C MSE F 192 N ALA F 193 1555 1555 1.33
LINK C ALA F 199 N MSE F 200 1555 1555 1.33
LINK C MSE F 200 N ASP F 201 1555 1555 1.33
LINK C GLU F 217 N MSE F 218 1555 1555 1.33
LINK C MSE F 218 N ASP F 219 1555 1555 1.33
LINK C ASP F 219 N MSE F 220 1555 1555 1.33
LINK C MSE F 220 N ALA F 221 1555 1555 1.34
LINK OE1 GLU F 239 MG MG F 701 1555 1555 2.00
LINK C HIS F 443 N MSE F 444 1555 1555 1.33
LINK C MSE F 444 N ALA F 445 1555 1555 1.33
LINK OE1 GLU F 599 MG MG F 702 1555 1555 2.12
LINK C ALA F 621 N MSE F 622 1555 1555 1.33
LINK C MSE F 622 N ALA F 623 1555 1555 1.34
LINK MG MG A 701 O HOH A 832 1555 1555 2.42
LINK MG MG A 701 O HOH A 837 1555 1555 2.56
LINK MG MG A 702 O HOH A 916 1555 1555 2.11
LINK MG MG A 702 O HOH A 819 1555 1555 2.05
LINK MG MG A 702 O HOH A 897 1555 1555 2.23
LINK MG MG B 701 O HOH B 909 1555 1555 2.23
LINK MG MG B 701 O HOH B 811 1555 1555 2.28
LINK MG MG B 702 O HOH B 865 1555 1555 2.14
LINK MG MG B 702 O HOH B 880 1555 1555 2.18
LINK MG MG B 702 O HOH B 941 1555 1555 2.05
LINK MG MG C 701 O HOH C 832 1555 1555 2.03
LINK MG MG C 701 O HOH C 823 1555 1555 1.98
LINK MG MG C 702 O HOH C 843 1555 1555 2.07
LINK MG MG C 702 O HOH C 882 1555 1555 2.07
LINK MG MG C 702 O HOH C 919 1555 1555 2.37
LINK MG MG D 701 O HOH D 814 1555 1555 2.31
LINK MG MG D 701 O HOH D 923 1555 1555 2.21
LINK MG MG D 702 O HOH D 846 1555 1555 2.07
LINK MG MG D 702 O HOH D 885 1555 1555 2.06
LINK MG MG D 702 O HOH D 984 1555 1555 2.30
LINK MG MG E 701 O HOH E 846 1555 1555 2.13
LINK MG MG E 701 O HOH E 889 1555 1555 2.30
LINK MG MG E 702 O HOH E 851 1555 1555 2.12
LINK MG MG E 702 O HOH E 981 1555 1555 2.05
LINK MG MG E 702 O HOH E1003 1555 1555 2.18
LINK MG MG F 701 O HOH F 896 1555 1555 2.28
LINK MG MG F 701 O HOH F 831 1555 1555 2.13
LINK MG MG F 702 O HOH F 821 1555 1555 2.04
LINK MG MG F 702 O HOH F 887 1555 1555 2.00
LINK MG MG F 702 O HOH F 929 1555 1555 2.34
CISPEP 1 GLN A 61 PRO A 62 0 -2.15
CISPEP 2 ASN A 242 ASP A 243 0 3.19
CISPEP 3 GLY A 436 GLY A 437 0 0.79
CISPEP 4 ASP A 562 GLU A 563 0 -3.14
CISPEP 5 GLN B 61 PRO B 62 0 -2.27
CISPEP 6 GLN C 61 PRO C 62 0 -2.50
CISPEP 7 ASP C 243 GLY C 244 0 -2.94
CISPEP 8 PHE C 245 ARG C 246 0 -1.38
CISPEP 9 GLN C 414 GLY C 415 0 2.30
CISPEP 10 GLY C 418 HIS C 419 0 3.94
CISPEP 11 GLN D 61 PRO D 62 0 -1.92
CISPEP 12 GLY D 436 GLY D 437 0 3.39
CISPEP 13 GLN E 61 PRO E 62 0 -2.57
CISPEP 14 GLY E 389 LEU E 390 0 -2.02
CISPEP 15 SER E 427 LEU E 428 0 6.63
CISPEP 16 GLY E 436 GLY E 437 0 -5.25
CISPEP 17 GLN F 61 PRO F 62 0 -2.51
CISPEP 18 ALA F 247 ALA F 248 0 -10.50
CISPEP 19 ALA F 432 THR F 433 0 -9.61
CISPEP 20 GLY F 436 GLY F 437 0 5.46
SITE 1 AC1 6 GLU A 134 ASP A 165 GLN A 191 GLU A 239
SITE 2 AC1 6 HOH A 832 HOH A 837
SITE 1 AC2 6 HIS A 443 HIS A 521 GLU A 599 HOH A 819
SITE 2 AC2 6 HOH A 897 HOH A 916
SITE 1 AC3 6 GLU B 134 ASP B 165 GLN B 191 GLU B 239
SITE 2 AC3 6 HOH B 811 HOH B 909
SITE 1 AC4 6 HIS B 443 HIS B 521 GLU B 599 HOH B 865
SITE 2 AC4 6 HOH B 880 HOH B 941
SITE 1 AC5 6 GLU C 134 ASP C 165 GLN C 191 GLU C 239
SITE 2 AC5 6 HOH C 823 HOH C 832
SITE 1 AC6 6 HIS C 443 HIS C 521 GLU C 599 HOH C 843
SITE 2 AC6 6 HOH C 882 HOH C 919
SITE 1 AC7 6 GLU D 134 ASP D 165 GLN D 191 GLU D 239
SITE 2 AC7 6 HOH D 814 HOH D 923
SITE 1 AC8 6 HIS D 443 HIS D 521 GLU D 599 HOH D 846
SITE 2 AC8 6 HOH D 885 HOH D 984
SITE 1 AC9 6 GLU E 134 ASP E 165 GLN E 191 GLU E 239
SITE 2 AC9 6 HOH E 846 HOH E 889
SITE 1 AD1 6 HIS E 443 HIS E 521 GLU E 599 HOH E 851
SITE 2 AD1 6 HOH E 981 HOH E1003
SITE 1 AD2 6 GLU F 134 ASP F 165 GLN F 191 GLU F 239
SITE 2 AD2 6 HOH F 831 HOH F 896
SITE 1 AD3 6 HIS F 443 HIS F 521 GLU F 599 HOH F 821
SITE 2 AD3 6 HOH F 887 HOH F 929
SITE 1 AD4 7 CYS C 69 ARG C 71 ARG C 73 LEU C 74
SITE 2 AD4 7 HOH C 808 HOH C 870 HOH C 893
CRYST1 262.503 262.503 139.644 90.00 90.00 120.00 P 63 36
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 0.003809 0.002199 0.000000 0.00000
SCALE2 0.000000 0.004399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
