HEADER OXIDOREDUCTASE 11-OCT-17 6B9T
TITLE CRYSTAL STRUCTURE OF MPNS WITH SUBSTRATE 2-HYDROXYETHYLPHOSPHONATE (2-
TITLE 2 HEP) AND FE(II) BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLPHOSPHONATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 1.13.11.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NITROSOPUMILUS MARITIMUS (STRAIN SCM1);
SOURCE 3 ORGANISM_TAXID: 436308;
SOURCE 4 STRAIN: SCM1;
SOURCE 5 GENE: MPNS, NMAR_0155;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2 (DE3) PLYSS
KEYWDS PHOSPHONATE, METHYLPHOSPHONATE, IRON, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.BORN,C.L.DRENNAN
REVDAT 3 13-MAR-24 6B9T 1 LINK
REVDAT 2 04-DEC-19 6B9T 1 REMARK
REVDAT 1 20-DEC-17 6B9T 0
JRNL AUTH D.A.BORN,E.C.ULRICH,K.S.JU,S.C.PECK,W.A.VAN DER DONK,
JRNL AUTH 2 C.L.DRENNAN
JRNL TITL STRUCTURAL BASIS FOR METHYLPHOSPHONATE BIOSYNTHESIS.
JRNL REF SCIENCE V. 358 1336 2017
JRNL REFN ESSN 1095-9203
JRNL PMID 29217579
JRNL DOI 10.1126/SCIENCE.AAO3435
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 135624
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 6643
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 46.1077 - 7.2927 0.99 4803 251 0.1286 0.1371
REMARK 3 2 7.2927 - 5.7920 0.98 4707 233 0.1495 0.1933
REMARK 3 3 5.7920 - 5.0609 0.99 4752 217 0.1468 0.1905
REMARK 3 4 5.0609 - 4.5987 1.00 4800 250 0.1414 0.1878
REMARK 3 5 4.5987 - 4.2693 1.00 4795 215 0.1462 0.1709
REMARK 3 6 4.2693 - 4.0178 0.97 4674 210 0.1630 0.2067
REMARK 3 7 4.0178 - 3.8166 0.67 3207 161 0.1786 0.2068
REMARK 3 8 3.8166 - 3.6506 0.98 3161 174 0.1907 0.2338
REMARK 3 9 3.6506 - 3.5101 0.97 4356 242 0.1984 0.2450
REMARK 3 10 3.5101 - 3.3890 0.49 2336 113 0.1962 0.2635
REMARK 3 11 3.3890 - 3.2831 1.00 4780 261 0.2039 0.2636
REMARK 3 12 3.2831 - 3.1892 1.00 4742 257 0.2216 0.2640
REMARK 3 13 3.1892 - 3.1053 0.96 4618 229 0.2270 0.2824
REMARK 3 14 3.1053 - 3.0296 0.97 4631 263 0.2308 0.2873
REMARK 3 15 3.0296 - 2.9607 0.99 4596 240 0.2307 0.2918
REMARK 3 16 2.9607 - 2.8977 0.99 4799 271 0.2292 0.2861
REMARK 3 17 2.8977 - 2.8397 0.99 4670 243 0.2398 0.3261
REMARK 3 18 2.8397 - 2.7862 0.99 4831 240 0.2440 0.3158
REMARK 3 19 2.7862 - 2.7364 0.99 4705 255 0.2467 0.2891
REMARK 3 20 2.7364 - 2.6900 0.92 3531 171 0.2612 0.3231
REMARK 3 21 2.6466 - 2.6059 0.92 4028 196 0.2621 0.3210
REMARK 3 22 2.6059 - 2.5676 0.99 4738 239 0.2521 0.3393
REMARK 3 23 2.5676 - 2.5314 0.94 4476 252 0.2458 0.3207
REMARK 3 24 2.5314 - 2.4972 0.97 4662 252 0.2498 0.3157
REMARK 3 25 2.4972 - 2.4648 0.98 4654 229 0.2570 0.3132
REMARK 3 26 2.4648 - 2.4340 0.99 4740 242 0.2702 0.3293
REMARK 3 27 2.4340 - 2.4047 0.99 4717 240 0.2744 0.3306
REMARK 3 28 2.4047 - 2.3767 0.99 4772 240 0.2756 0.3318
REMARK 3 29 2.3767 - 2.3500 0.99 4700 257 0.2798 0.3536
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.80
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 29032
REMARK 3 ANGLE : 0.627 39357
REMARK 3 CHIRALITY : 0.044 4259
REMARK 3 PLANARITY : 0.005 5127
REMARK 3 DIHEDRAL : 14.929 17330
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 6B9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-16
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 : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 135649
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 220 MM AMMONIUM CHLORIDE, 21% (W/V)
REMARK 280 PEG 3350, 4 MM 2-HYDROXYETHYLPHOSPHONATE, SOAKED IN 220 MM
REMARK 280 AMMONIUM FORMATE, 21% (W/V) PEG 3350, 2 MM IRON(II) CHLORIDE,
REMARK 280 2.5 MM 2-HYDROXYETHYLPHOSPHONATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 297K
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 175.62500
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, 3, 4
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: 16270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 16510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 16230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 4
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: 15850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 GLU A 2
REMARK 465 LYS A 3
REMARK 465 LYS A 4
REMARK 465 ILE A 5
REMARK 465 ASP A 6
REMARK 465 PHE A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 SER A 457
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LYS B 3
REMARK 465 LYS B 4
REMARK 465 ILE B 5
REMARK 465 ASP B 6
REMARK 465 PHE B 7
REMARK 465 LYS B 8
REMARK 465 PRO B 9
REMARK 465 ASN B 456
REMARK 465 SER B 457
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 LYS C 3
REMARK 465 LYS C 4
REMARK 465 ILE C 5
REMARK 465 ASP C 6
REMARK 465 PHE C 7
REMARK 465 LYS C 8
REMARK 465 PRO C 9
REMARK 465 SER C 457
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 LYS D 3
REMARK 465 SER D 457
REMARK 465 MET E 1
REMARK 465 GLU E 2
REMARK 465 LYS E 3
REMARK 465 LYS E 4
REMARK 465 ILE E 5
REMARK 465 ASP E 6
REMARK 465 PHE E 7
REMARK 465 LYS E 8
REMARK 465 PRO E 9
REMARK 465 GLY E 454
REMARK 465 SER E 455
REMARK 465 ASN E 456
REMARK 465 SER E 457
REMARK 465 MET F 1
REMARK 465 GLU F 2
REMARK 465 LYS F 3
REMARK 465 LYS F 4
REMARK 465 ILE F 5
REMARK 465 ASP F 6
REMARK 465 PHE F 7
REMARK 465 LYS F 8
REMARK 465 PRO F 9
REMARK 465 SER F 457
REMARK 465 MET G 1
REMARK 465 GLU G 2
REMARK 465 LYS G 3
REMARK 465 LYS G 4
REMARK 465 ILE G 5
REMARK 465 ASP G 6
REMARK 465 PHE G 7
REMARK 465 LYS G 8
REMARK 465 PRO G 9
REMARK 465 ASN G 456
REMARK 465 SER G 457
REMARK 465 MET H 1
REMARK 465 GLU H 2
REMARK 465 LYS H 3
REMARK 465 LYS H 4
REMARK 465 ILE H 5
REMARK 465 ASP H 6
REMARK 465 PHE H 7
REMARK 465 LYS H 8
REMARK 465 PRO H 9
REMARK 465 PRO H 452
REMARK 465 LYS H 453
REMARK 465 GLY H 454
REMARK 465 SER H 455
REMARK 465 ASN H 456
REMARK 465 SER H 457
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 ASN A 36 CG OD1 ND2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 GLN A 53 CG CD OE1 NE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 LYS A 263 CD CE NZ
REMARK 470 LYS A 278 CD CE NZ
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 LYS A 323 CD CE NZ
REMARK 470 LYS A 453 CE NZ
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 GLN B 53 CG CD OE1 NE2
REMARK 470 GLU B 61 OE1 OE2
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 LYS B 279 CG CD CE NZ
REMARK 470 LYS B 280 CG CD CE NZ
REMARK 470 ASP B 285 CG OD1 OD2
REMARK 470 LYS B 292 CD CE NZ
REMARK 470 GLU B 326 CG CD OE1 OE2
REMARK 470 SER B 354 OG
REMARK 470 LYS B 386 CD CE NZ
REMARK 470 ASP C 10 CG OD1 OD2
REMARK 470 LYS C 52 CE NZ
REMARK 470 LYS C 95 CG CD CE NZ
REMARK 470 LEU C 226 CG CD1 CD2
REMARK 470 GLU C 270 CG CD OE1 OE2
REMARK 470 LYS C 279 CD CE NZ
REMARK 470 LYS C 292 CD CE NZ
REMARK 470 GLU C 326 CG CD OE1 OE2
REMARK 470 GLU C 355 CG CD OE1 OE2
REMARK 470 ASN C 456 CG OD1 ND2
REMARK 470 LYS D 4 CG CD CE NZ
REMARK 470 GLN D 53 CG CD OE1 NE2
REMARK 470 GLU D 61 CG CD OE1 OE2
REMARK 470 LYS D 95 CG CD CE NZ
REMARK 470 GLU D 270 CG CD OE1 OE2
REMARK 470 ASN D 456 CG OD1 ND2
REMARK 470 LYS E 52 CE NZ
REMARK 470 LYS E 54 CG CD CE NZ
REMARK 470 LYS E 62 CG CD CE NZ
REMARK 470 LYS E 95 CG CD CE NZ
REMARK 470 GLU E 168 CG CD OE1 OE2
REMARK 470 LYS E 263 CD CE NZ
REMARK 470 LYS E 279 CD CE NZ
REMARK 470 GLU E 326 CG CD OE1 OE2
REMARK 470 SER E 354 OG
REMARK 470 GLU E 355 CG CD OE1 OE2
REMARK 470 GLU E 437 CD OE1 OE2
REMARK 470 LYS E 453 CG CD CE NZ
REMARK 470 LYS F 52 CG CD CE NZ
REMARK 470 LYS F 62 CG CD CE NZ
REMARK 470 LYS F 131 CG CD CE NZ
REMARK 470 LYS F 170 CG CD CE NZ
REMARK 470 LYS F 263 CG CD CE NZ
REMARK 470 GLU F 270 CG CD OE1 OE2
REMARK 470 LYS F 279 CG CD CE NZ
REMARK 470 LYS F 280 CG CD CE NZ
REMARK 470 LYS F 292 CD CE NZ
REMARK 470 LYS F 323 CG CD CE NZ
REMARK 470 GLU F 326 CG CD OE1 OE2
REMARK 470 GLU F 355 CG CD OE1 OE2
REMARK 470 LEU F 357 CG CD1 CD2
REMARK 470 LYS F 386 CD CE NZ
REMARK 470 GLU G 32 CG CD OE1 OE2
REMARK 470 ASN G 36 CG OD1 ND2
REMARK 470 ILE G 42 CG1 CG2 CD1
REMARK 470 GLU G 43 CG CD OE1 OE2
REMARK 470 LYS G 52 CG CD CE NZ
REMARK 470 GLN G 53 CG CD OE1 NE2
REMARK 470 LYS G 54 CG CD CE NZ
REMARK 470 LYS G 62 CG CD CE NZ
REMARK 470 LYS G 105 CG CD CE NZ
REMARK 470 LYS G 131 CG CD CE NZ
REMARK 470 LYS G 141 CG CD CE NZ
REMARK 470 LYS G 279 CD CE NZ
REMARK 470 LYS G 280 CG CD CE NZ
REMARK 470 GLU G 326 CG CD OE1 OE2
REMARK 470 LYS G 386 CG CD CE NZ
REMARK 470 LYS G 390 CE NZ
REMARK 470 LYS G 413 CG CD CE NZ
REMARK 470 LYS G 453 CG CD CE NZ
REMARK 470 SER G 455 OG
REMARK 470 LEU H 38 CG CD1 CD2
REMARK 470 GLU H 44 CG CD OE1 OE2
REMARK 470 LYS H 52 CG CD CE NZ
REMARK 470 GLN H 53 CG CD OE1 NE2
REMARK 470 LYS H 54 CG CD CE NZ
REMARK 470 GLU H 61 CG CD OE1 OE2
REMARK 470 LYS H 62 CG CD CE NZ
REMARK 470 LYS H 95 CG CD CE NZ
REMARK 470 LYS H 105 CD CE NZ
REMARK 470 LYS H 170 CG CD CE NZ
REMARK 470 LYS H 292 CD CE NZ
REMARK 470 GLU H 326 CG CD OE1 OE2
REMARK 470 GLU H 355 CG CD OE1 OE2
REMARK 470 LYS H 386 CD CE NZ
REMARK 470 ARG H 441 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 448 CG CD OE1 NE2
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 O4 2HE F 502 O HOH F 601 2.13
REMARK 500 O HOH D 681 O HOH D 716 2.14
REMARK 500 O4 2HE C 502 O HOH C 601 2.14
REMARK 500 O4 2HE H 502 O HOH H 601 2.17
REMARK 500 O HOH G 633 O HOH G 646 2.17
REMARK 500 OE1 GLN H 231 O HOH H 602 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 SER A 211 -91.68 -123.60
REMARK 500 PRO A 325 -152.01 -79.85
REMARK 500 SER A 354 13.48 -141.63
REMARK 500 PRO B 68 49.93 -77.50
REMARK 500 ASP B 196 -168.31 -63.55
REMARK 500 SER B 211 -92.13 -124.85
REMARK 500 PRO B 325 -153.35 -78.78
REMARK 500 PRO C 68 48.97 -77.08
REMARK 500 ASP C 196 -164.80 -64.63
REMARK 500 SER C 211 -91.16 -124.78
REMARK 500 PRO C 325 -154.40 -80.50
REMARK 500 SER C 354 -149.20 -69.26
REMARK 500 PRO D 68 48.32 -78.10
REMARK 500 SER D 211 -91.54 -123.11
REMARK 500 PRO D 325 -153.49 -79.04
REMARK 500 SER D 455 61.56 -118.84
REMARK 500 ASP E 196 -165.03 -63.78
REMARK 500 SER E 211 -89.78 -124.12
REMARK 500 PRO E 325 -154.53 -79.34
REMARK 500 GLU E 355 -132.39 55.46
REMARK 500 ASP E 356 76.80 57.25
REMARK 500 PRO F 68 48.59 -78.19
REMARK 500 SER F 211 -92.28 -122.34
REMARK 500 PRO F 325 -152.90 -78.64
REMARK 500 SER F 354 -147.39 -90.49
REMARK 500 PRO G 68 49.69 -78.15
REMARK 500 ASP G 196 -162.73 -65.69
REMARK 500 SER G 211 -91.19 -123.91
REMARK 500 PRO G 325 -154.42 -79.24
REMARK 500 LEU G 357 -12.53 66.39
REMARK 500 PRO G 452 64.64 -62.88
REMARK 500 PRO H 68 49.46 -77.46
REMARK 500 ASP H 196 -163.79 -64.93
REMARK 500 SER H 211 -90.73 -122.69
REMARK 500 PRO H 325 -155.03 -79.37
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 A 722 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH H 707 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH H 708 DISTANCE = 6.89 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 FE A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 148 NE2
REMARK 620 2 GLN A 152 OE1 91.3
REMARK 620 3 HIS A 190 NE2 97.7 88.6
REMARK 620 4 2HE A 502 O2 89.7 166.7 104.4
REMARK 620 5 2HE A 502 O4 159.1 86.6 103.0 87.8
REMARK 620 6 HOH A 601 O 101.2 77.5 156.7 89.3 58.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 148 NE2
REMARK 620 2 GLN B 152 OE1 78.6
REMARK 620 3 HIS B 190 NE2 94.5 88.1
REMARK 620 4 2HE B 503 O4 164.6 91.6 97.0
REMARK 620 5 2HE B 503 O3 97.2 173.9 96.7 91.5
REMARK 620 6 HOH B 621 O 96.3 77.6 160.0 69.8 98.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 609 O
REMARK 620 2 GLU H 159 OE1 61.1
REMARK 620 3 HOH H 696 O 80.6 136.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 148 NE2
REMARK 620 2 GLN C 152 OE1 90.8
REMARK 620 3 HIS C 190 NE2 99.8 90.0
REMARK 620 4 2HE C 502 O4 155.5 88.8 104.7
REMARK 620 5 2HE C 502 O2 97.4 163.4 102.6 77.8
REMARK 620 6 HOH C 601 O 100.9 79.1 156.6 55.0 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 148 NE2
REMARK 620 2 GLN D 152 OE1 84.6
REMARK 620 3 HIS D 190 NE2 95.1 85.2
REMARK 620 4 2HE D 502 O1 88.4 172.7 97.7
REMARK 620 5 2HE D 502 O4 161.7 91.2 102.3 94.7
REMARK 620 6 HOH D 601 O 99.9 87.3 162.4 91.7 62.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE E 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 148 NE2
REMARK 620 2 GLN E 152 OE1 83.6
REMARK 620 3 HIS E 190 NE2 97.7 88.8
REMARK 620 4 2HE E 502 O2 101.0 174.7 93.2
REMARK 620 5 2HE E 502 O4 169.9 95.1 92.2 79.9
REMARK 620 6 HOH E 608 O 103.3 78.8 154.0 97.4 66.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE F 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 148 NE2
REMARK 620 2 GLN F 152 OE1 81.3
REMARK 620 3 HIS F 190 NE2 100.2 90.4
REMARK 620 4 2HE F 502 O1 95.0 170.1 99.3
REMARK 620 5 2HE F 502 O4 148.7 86.4 108.6 92.3
REMARK 620 6 HOH F 601 O 87.3 88.7 172.2 82.0 63.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE G 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 148 NE2
REMARK 620 2 GLN G 152 OE1 89.2
REMARK 620 3 HIS G 190 NE2 100.6 79.6
REMARK 620 4 2HE G 502 O4 166.6 78.0 73.6
REMARK 620 5 2HE G 502 O2 106.4 164.3 97.2 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE H 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 148 NE2
REMARK 620 2 GLN H 152 OE1 84.8
REMARK 620 3 HIS H 190 NE2 88.2 93.9
REMARK 620 4 2HE H 502 O2 91.8 164.2 101.4
REMARK 620 5 2HE H 502 O4 154.1 86.3 116.7 90.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT F 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE G 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT G 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2HE H 502
DBREF 6B9T A 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T B 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T C 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T D 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T E 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T F 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T G 1 457 UNP A9A1T2 MPNS_NITMS 1 457
DBREF 6B9T H 1 457 UNP A9A1T2 MPNS_NITMS 1 457
SEQRES 1 A 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 A 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 A 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 A 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 A 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 A 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 A 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 A 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 A 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 A 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 A 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 A 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 A 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 A 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 A 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 A 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 A 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 A 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 A 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 A 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 A 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 A 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 A 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 A 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 A 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 A 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 A 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 A 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 A 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 A 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 A 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 A 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 A 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 A 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 A 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 A 457 ASN SER
SEQRES 1 B 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 B 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 B 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 B 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 B 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 B 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 B 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 B 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 B 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 B 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 B 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 B 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 B 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 B 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 B 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 B 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 B 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 B 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 B 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 B 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 B 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 B 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 B 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 B 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 B 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 B 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 B 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 B 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 B 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 B 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 B 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 B 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 B 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 B 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 B 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 B 457 ASN SER
SEQRES 1 C 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 C 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 C 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 C 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 C 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 C 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 C 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 C 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 C 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 C 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 C 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 C 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 C 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 C 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 C 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 C 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 C 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 C 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 C 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 C 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 C 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 C 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 C 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 C 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 C 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 C 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 C 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 C 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 C 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 C 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 C 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 C 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 C 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 C 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 C 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 C 457 ASN SER
SEQRES 1 D 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 D 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 D 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 D 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 D 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 D 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 D 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 D 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 D 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 D 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 D 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 D 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 D 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 D 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 D 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 D 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 D 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 D 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 D 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 D 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 D 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 D 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 D 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 D 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 D 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 D 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 D 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 D 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 D 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 D 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 D 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 D 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 D 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 D 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 D 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 D 457 ASN SER
SEQRES 1 E 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 E 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 E 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 E 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 E 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 E 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 E 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 E 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 E 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 E 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 E 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 E 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 E 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 E 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 E 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 E 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 E 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 E 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 E 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 E 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 E 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 E 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 E 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 E 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 E 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 E 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 E 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 E 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 E 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 E 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 E 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 E 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 E 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 E 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 E 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 E 457 ASN SER
SEQRES 1 F 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 F 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 F 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 F 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 F 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 F 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 F 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 F 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 F 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 F 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 F 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 F 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 F 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 F 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 F 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 F 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 F 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 F 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 F 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 F 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 F 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 F 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 F 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 F 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 F 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 F 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 F 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 F 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 F 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 F 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 F 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 F 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 F 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 F 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 F 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 F 457 ASN SER
SEQRES 1 G 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 G 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 G 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 G 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 G 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 G 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 G 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 G 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 G 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 G 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 G 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 G 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 G 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 G 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 G 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 G 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 G 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 G 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 G 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 G 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 G 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 G 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 G 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 G 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 G 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 G 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 G 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 G 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 G 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 G 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 G 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 G 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 G 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 G 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 G 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 G 457 ASN SER
SEQRES 1 H 457 MET GLU LYS LYS ILE ASP PHE LYS PRO ASP SER TYR LEU
SEQRES 2 H 457 ILE ARG SER GLY ASN ASN PHE LEU GLY ILE LEU ASN ASP
SEQRES 3 H 457 ILE LYS ARG ARG PRO GLU ASP ALA ALA ASN GLU LEU GLY
SEQRES 4 H 457 VAL SER ILE GLU GLU ILE ASN SER ILE ILE SER GLY LYS
SEQRES 5 H 457 GLN LYS ILE SER PRO SER LEU ILE GLU LYS ALA VAL ASN
SEQRES 6 H 457 ILE TRP PRO VAL ASN GLU ARG ASP PHE TYR ILE VAL SER
SEQRES 7 H 457 ASP ASP CYS SER SER GLY ILE LEU ILE MET THR SER GLN
SEQRES 8 H 457 ASP SER ILE LYS SER SER ARG ILE MET GLU ARG ALA GLY
SEQRES 9 H 457 LYS PRO TYR TYR GLU TYR ARG ASP THR ALA MET SER LYS
SEQRES 10 H 457 THR ALA PRO PHE ARG PRO GLU TRP ILE LEU GLU LEU CYS
SEQRES 11 H 457 LYS VAL GLU ASN ASN ASP PRO GLU ASN PRO LYS ALA GLN
SEQRES 12 H 457 TRP ASN ASN GLY HIS PHE MET HIS GLN PHE THR TYR PHE
SEQRES 13 H 457 ILE GLY GLU VAL ASN PHE TYR TYR LYS ASP PRO GLU GLY
SEQRES 14 H 457 LYS LYS HIS VAL ALA ILE MET ASN THR GLY ASP SER MET
SEQRES 15 H 457 TYR ILE THR PRO PHE THR PRO HIS THR PHE THR THR ARG
SEQRES 16 H 457 ASP GLY ALA SER GLN ASN GLY LEU ILE LEU ALA LEU THR
SEQRES 17 H 457 TYR GLY SER LYS LEU THR GLY ASP ILE GLN GLN GLU LEU
SEQRES 18 H 457 SER SER LEU SER LEU ASP CYS GLY SER GLN TYR ALA LEU
SEQRES 19 H 457 ASP PHE THR ASN HIS GLU ASN ALA SER LEU SER LEU LEU
SEQRES 20 H 457 GLU TYR TYR PHE GLU LEU SER ASN LEU THR LYS GLU LYS
SEQRES 21 H 457 PHE ALA LYS ARG THR ASN PHE SER MET GLU THR LEU ALA
SEQRES 22 H 457 ASP PHE PHE THR LYS LYS LYS LEU PRO THR PHE ASP GLU
SEQRES 23 H 457 LEU LYS ILE ILE ALA LYS ALA LEU ASN VAL ASN SER ARG
SEQRES 24 H 457 ASP LEU MET PRO ASN ASP LEU THR GLU SER LYS VAL ILE
SEQRES 25 H 457 VAL LYS THR HIS ASP GLN CYS ASP HIS TRP LYS TYR PRO
SEQRES 26 H 457 GLU SER GLY ASN TYR GLU PHE TYR GLU LEU ALA SER THR
SEQRES 27 H 457 THR ALA LEU PRO HIS SER LYS ALA PHE GLU ILE ASP VAL
SEQRES 28 H 457 SER SER SER GLU ASP LEU ASN LEU ASP LEU LYS VAL GLY
SEQRES 29 H 457 LEU HIS GLN TYR VAL TYR ASN ILE GLY ASP SER ALA LEU
SEQRES 30 H 457 THR ILE ASN TRP ASN TYR GLU ASN LYS THR TYR GLN LYS
SEQRES 31 H 457 SER LEU ASN PRO GLY ASP SER ALA TYR ILE LYS PRO PHE
SEQRES 32 H 457 VAL PRO HIS ASN PHE ARG GLY ASN GLY LYS ILE LEU ILE
SEQRES 33 H 457 LEU ARG ILE GLY GLY LYS ILE SER GLY ASP SER GLN ARG
SEQRES 34 H 457 GLU LEU SER PHE VAL GLY ARG GLU ASN THR GLN ARG ALA
SEQRES 35 H 457 ILE SER GLU THR MET GLN TRP PHE ASP PRO LYS GLY SER
SEQRES 36 H 457 ASN SER
HET FE A 501 1
HET 2HE A 502 7
HET FE B 501 1
HET FE B 502 1
HET 2HE B 503 7
HET FMT B 504 3
HET FE C 501 1
HET 2HE C 502 7
HET FMT C 503 3
HET FE D 501 1
HET 2HE D 502 7
HET FMT D 503 3
HET FE E 501 1
HET 2HE E 502 7
HET FMT E 503 3
HET FE F 501 1
HET 2HE F 502 7
HET FMT F 503 3
HET FE G 501 1
HET 2HE G 502 7
HET FMT G 503 3
HET FE H 501 1
HET 2HE H 502 7
HETNAM FE FE (III) ION
HETNAM 2HE (2-HYDROXYETHYL)PHOSPHONIC ACID
HETNAM FMT FORMIC ACID
FORMUL 9 FE 9(FE 3+)
FORMUL 10 2HE 8(C2 H7 O4 P)
FORMUL 14 FMT 6(C H2 O2)
FORMUL 32 HOH *987(H2 O)
HELIX 1 AA1 ASP A 10 ILE A 27 1 18
HELIX 2 AA2 ARG A 30 GLY A 39 1 10
HELIX 3 AA3 SER A 41 SER A 50 1 10
HELIX 4 AA4 SER A 56 TRP A 67 1 12
HELIX 5 AA5 ASN A 70 TYR A 75 5 6
HELIX 6 AA6 THR A 89 SER A 96 1 8
HELIX 7 AA7 GLY A 215 SER A 223 1 9
HELIX 8 AA8 SER A 225 GLN A 231 1 7
HELIX 9 AA9 ASN A 238 ASN A 255 1 18
HELIX 10 AB1 THR A 257 ASN A 266 1 10
HELIX 11 AB2 SER A 268 THR A 277 1 10
HELIX 12 AB3 THR A 283 LEU A 294 1 12
HELIX 13 AB4 ASN A 297 MET A 302 1 6
HELIX 14 AB5 THR A 315 CYS A 319 5 5
HELIX 15 AB6 GLY A 425 GLY A 435 1 11
HELIX 16 AB7 ASN A 438 SER A 444 1 7
HELIX 17 AB8 SER B 11 ILE B 27 1 17
HELIX 18 AB9 ARG B 30 GLY B 39 1 10
HELIX 19 AC1 SER B 41 SER B 50 1 10
HELIX 20 AC2 SER B 56 TRP B 67 1 12
HELIX 21 AC3 ASN B 70 TYR B 75 5 6
HELIX 22 AC4 THR B 89 SER B 96 1 8
HELIX 23 AC5 GLY B 215 SER B 223 1 9
HELIX 24 AC6 SER B 225 GLN B 231 1 7
HELIX 25 AC7 ASN B 238 ASN B 255 1 18
HELIX 26 AC8 THR B 257 ASN B 266 1 10
HELIX 27 AC9 SER B 268 THR B 277 1 10
HELIX 28 AD1 THR B 283 ASN B 295 1 13
HELIX 29 AD2 ASN B 297 MET B 302 1 6
HELIX 30 AD3 THR B 315 CYS B 319 5 5
HELIX 31 AD4 GLY B 425 GLY B 435 1 11
HELIX 32 AD5 ASN B 438 SER B 444 1 7
HELIX 33 AD6 SER C 11 ILE C 27 1 17
HELIX 34 AD7 ARG C 30 GLY C 39 1 10
HELIX 35 AD8 SER C 41 SER C 50 1 10
HELIX 36 AD9 SER C 56 TRP C 67 1 12
HELIX 37 AE1 ASN C 70 PHE C 74 5 5
HELIX 38 AE2 THR C 89 SER C 96 1 8
HELIX 39 AE3 GLY C 215 SER C 223 1 9
HELIX 40 AE4 SER C 225 GLN C 231 1 7
HELIX 41 AE5 ASN C 238 ASN C 255 1 18
HELIX 42 AE6 THR C 257 ASN C 266 1 10
HELIX 43 AE7 SER C 268 THR C 277 1 10
HELIX 44 AE8 THR C 283 LEU C 294 1 12
HELIX 45 AE9 ASN C 297 MET C 302 1 6
HELIX 46 AF1 THR C 315 CYS C 319 5 5
HELIX 47 AF2 GLY C 425 GLY C 435 1 11
HELIX 48 AF3 ASN C 438 SER C 444 1 7
HELIX 49 AF4 ASP D 10 ILE D 27 1 18
HELIX 50 AF5 ARG D 30 GLY D 39 1 10
HELIX 51 AF6 SER D 41 SER D 50 1 10
HELIX 52 AF7 SER D 56 TRP D 67 1 12
HELIX 53 AF8 ASN D 70 TYR D 75 5 6
HELIX 54 AF9 THR D 89 SER D 96 1 8
HELIX 55 AG1 GLY D 215 SER D 223 1 9
HELIX 56 AG2 SER D 225 SER D 230 1 6
HELIX 57 AG3 GLN D 231 ALA D 233 5 3
HELIX 58 AG4 ASN D 238 ASN D 255 1 18
HELIX 59 AG5 THR D 257 ASN D 266 1 10
HELIX 60 AG6 SER D 268 THR D 277 1 10
HELIX 61 AG7 THR D 283 LEU D 294 1 12
HELIX 62 AG8 ASN D 297 MET D 302 1 6
HELIX 63 AG9 THR D 315 CYS D 319 5 5
HELIX 64 AH1 GLY D 425 GLY D 435 1 11
HELIX 65 AH2 ASN D 438 SER D 444 1 7
HELIX 66 AH3 SER E 11 ILE E 27 1 17
HELIX 67 AH4 ARG E 30 GLY E 39 1 10
HELIX 68 AH5 SER E 41 SER E 50 1 10
HELIX 69 AH6 SER E 56 TRP E 67 1 12
HELIX 70 AH7 ASN E 70 TYR E 75 5 6
HELIX 71 AH8 THR E 89 SER E 96 1 8
HELIX 72 AH9 GLY E 215 SER E 223 1 9
HELIX 73 AI1 SER E 225 GLN E 231 1 7
HELIX 74 AI2 ASN E 238 ASN E 255 1 18
HELIX 75 AI3 THR E 257 ASN E 266 1 10
HELIX 76 AI4 SER E 268 THR E 277 1 10
HELIX 77 AI5 THR E 283 LEU E 294 1 12
HELIX 78 AI6 ASN E 297 MET E 302 1 6
HELIX 79 AI7 THR E 315 CYS E 319 5 5
HELIX 80 AI8 GLY E 425 GLY E 435 1 11
HELIX 81 AI9 ASN E 438 SER E 444 1 7
HELIX 82 AJ1 SER F 11 ILE F 27 1 17
HELIX 83 AJ2 ARG F 30 GLY F 39 1 10
HELIX 84 AJ3 SER F 41 SER F 50 1 10
HELIX 85 AJ4 SER F 56 TRP F 67 1 12
HELIX 86 AJ5 ASN F 70 PHE F 74 5 5
HELIX 87 AJ6 THR F 89 SER F 96 1 8
HELIX 88 AJ7 GLY F 215 SER F 223 1 9
HELIX 89 AJ8 SER F 225 GLN F 231 1 7
HELIX 90 AJ9 ASN F 238 ASN F 255 1 18
HELIX 91 AK1 THR F 257 ASN F 266 1 10
HELIX 92 AK2 SER F 268 THR F 277 1 10
HELIX 93 AK3 THR F 283 LEU F 294 1 12
HELIX 94 AK4 ASN F 297 MET F 302 1 6
HELIX 95 AK5 THR F 315 CYS F 319 5 5
HELIX 96 AK6 GLY F 425 GLY F 435 1 11
HELIX 97 AK7 ASN F 438 SER F 444 1 7
HELIX 98 AK8 SER G 11 ILE G 27 1 17
HELIX 99 AK9 ARG G 30 GLY G 39 1 10
HELIX 100 AL1 SER G 41 SER G 50 1 10
HELIX 101 AL2 SER G 56 TRP G 67 1 12
HELIX 102 AL3 ASN G 70 TYR G 75 5 6
HELIX 103 AL4 THR G 89 SER G 96 1 8
HELIX 104 AL5 GLY G 215 SER G 223 1 9
HELIX 105 AL6 SER G 225 GLN G 231 1 7
HELIX 106 AL7 ASN G 238 ASN G 255 1 18
HELIX 107 AL8 THR G 257 ASN G 266 1 10
HELIX 108 AL9 SER G 268 THR G 277 1 10
HELIX 109 AM1 THR G 283 LEU G 294 1 12
HELIX 110 AM2 ASN G 297 MET G 302 1 6
HELIX 111 AM3 THR G 315 CYS G 319 5 5
HELIX 112 AM4 GLY G 425 GLY G 435 1 11
HELIX 113 AM5 ASN G 438 SER G 444 1 7
HELIX 114 AM6 SER H 11 ILE H 27 1 17
HELIX 115 AM7 ARG H 30 GLY H 39 1 10
HELIX 116 AM8 SER H 41 SER H 50 1 10
HELIX 117 AM9 SER H 56 TRP H 67 1 12
HELIX 118 AN1 ASN H 70 TYR H 75 5 6
HELIX 119 AN2 THR H 89 SER H 96 1 8
HELIX 120 AN3 GLY H 215 SER H 223 1 9
HELIX 121 AN4 SER H 225 GLN H 231 1 7
HELIX 122 AN5 ASN H 238 ASN H 255 1 18
HELIX 123 AN6 THR H 257 ASN H 266 1 10
HELIX 124 AN7 SER H 268 THR H 277 1 10
HELIX 125 AN8 THR H 283 LEU H 294 1 12
HELIX 126 AN9 ASN H 297 MET H 302 1 6
HELIX 127 AO1 THR H 315 CYS H 319 5 5
HELIX 128 AO2 GLY H 425 GLY H 435 1 11
HELIX 129 AO3 ASN H 438 SER H 444 1 7
SHEET 1 AA1 7 ILE A 85 MET A 88 0
SHEET 2 AA1 7 SER A 397 ILE A 400 -1 O TYR A 399 N LEU A 86
SHEET 3 AA1 7 HIS A 366 ASN A 371 -1 N VAL A 369 O ALA A 398
SHEET 4 AA1 7 HIS A 406 ILE A 419 -1 O LEU A 415 N TYR A 370
SHEET 5 AA1 7 LYS A 345 SER A 353 -1 N LYS A 345 O ARG A 418
SHEET 6 AA1 7 TYR A 330 GLU A 334 -1 N TYR A 333 O GLU A 348
SHEET 7 AA1 7 HIS A 321 TYR A 324 -1 N TYR A 324 O TYR A 330
SHEET 1 AA2 6 ILE A 85 MET A 88 0
SHEET 2 AA2 6 SER A 397 ILE A 400 -1 O TYR A 399 N LEU A 86
SHEET 3 AA2 6 HIS A 366 ASN A 371 -1 N VAL A 369 O ALA A 398
SHEET 4 AA2 6 HIS A 406 ILE A 419 -1 O LEU A 415 N TYR A 370
SHEET 5 AA2 6 LEU A 377 ASN A 382 -1 N THR A 378 O ARG A 409
SHEET 6 AA2 6 THR A 387 LEU A 392 -1 O LEU A 392 N LEU A 377
SHEET 1 AA3 7 ARG A 98 ARG A 102 0
SHEET 2 AA3 7 LYS A 105 ASP A 112 -1 O TYR A 110 N ARG A 98
SHEET 3 AA3 7 PHE A 121 GLU A 128 -1 O TRP A 125 N ARG A 111
SHEET 4 AA3 7 LEU A 203 TYR A 209 -1 O THR A 208 N ARG A 122
SHEET 5 AA3 7 HIS A 151 ILE A 157 -1 N ILE A 157 O LEU A 203
SHEET 6 AA3 7 SER A 181 ILE A 184 -1 O MET A 182 N THR A 154
SHEET 7 AA3 7 VAL A 311 LYS A 314 -1 O ILE A 312 N TYR A 183
SHEET 1 AA4 4 LYS A 131 VAL A 132 0
SHEET 2 AA4 4 HIS A 190 ARG A 195 1 O THR A 194 N VAL A 132
SHEET 3 AA4 4 VAL A 160 LYS A 165 -1 N TYR A 163 O THR A 191
SHEET 4 AA4 4 LYS A 171 MET A 176 -1 O HIS A 172 N TYR A 164
SHEET 1 AA5 7 ILE B 85 MET B 88 0
SHEET 2 AA5 7 SER B 397 ILE B 400 -1 O SER B 397 N MET B 88
SHEET 3 AA5 7 HIS B 366 ASN B 371 -1 N GLN B 367 O ILE B 400
SHEET 4 AA5 7 HIS B 406 ILE B 419 -1 O LEU B 415 N TYR B 370
SHEET 5 AA5 7 LYS B 345 SER B 353 -1 N SER B 353 O GLY B 410
SHEET 6 AA5 7 TYR B 330 GLU B 334 -1 N GLU B 331 O ASP B 350
SHEET 7 AA5 7 HIS B 321 TYR B 324 -1 N TYR B 324 O TYR B 330
SHEET 1 AA6 6 ILE B 85 MET B 88 0
SHEET 2 AA6 6 SER B 397 ILE B 400 -1 O SER B 397 N MET B 88
SHEET 3 AA6 6 HIS B 366 ASN B 371 -1 N GLN B 367 O ILE B 400
SHEET 4 AA6 6 HIS B 406 ILE B 419 -1 O LEU B 415 N TYR B 370
SHEET 5 AA6 6 LEU B 377 ASN B 382 -1 N THR B 378 O ARG B 409
SHEET 6 AA6 6 THR B 387 LEU B 392 -1 O LEU B 392 N LEU B 377
SHEET 1 AA7 7 ARG B 98 ARG B 102 0
SHEET 2 AA7 7 LYS B 105 ASP B 112 -1 O TYR B 107 N MET B 100
SHEET 3 AA7 7 PHE B 121 GLU B 128 -1 O TRP B 125 N ARG B 111
SHEET 4 AA7 7 LEU B 203 TYR B 209 -1 O THR B 208 N ARG B 122
SHEET 5 AA7 7 HIS B 151 ILE B 157 -1 N ILE B 157 O LEU B 203
SHEET 6 AA7 7 SER B 181 ILE B 184 -1 O ILE B 184 N GLN B 152
SHEET 7 AA7 7 VAL B 311 LYS B 314 -1 O ILE B 312 N TYR B 183
SHEET 1 AA8 4 LYS B 131 VAL B 132 0
SHEET 2 AA8 4 HIS B 190 ARG B 195 1 O THR B 194 N VAL B 132
SHEET 3 AA8 4 VAL B 160 LYS B 165 -1 N TYR B 163 O THR B 191
SHEET 4 AA8 4 LYS B 171 ILE B 175 -1 O HIS B 172 N TYR B 164
SHEET 1 AA9 7 ILE C 85 MET C 88 0
SHEET 2 AA9 7 SER C 397 ILE C 400 -1 O TYR C 399 N LEU C 86
SHEET 3 AA9 7 HIS C 366 ASN C 371 -1 N VAL C 369 O ALA C 398
SHEET 4 AA9 7 HIS C 406 ILE C 419 -1 O LEU C 415 N TYR C 370
SHEET 5 AA9 7 LYS C 345 SER C 352 -1 N LYS C 345 O ARG C 418
SHEET 6 AA9 7 TYR C 330 GLU C 334 -1 N TYR C 333 O GLU C 348
SHEET 7 AA9 7 HIS C 321 TYR C 324 -1 N TYR C 324 O TYR C 330
SHEET 1 AB1 6 ILE C 85 MET C 88 0
SHEET 2 AB1 6 SER C 397 ILE C 400 -1 O TYR C 399 N LEU C 86
SHEET 3 AB1 6 HIS C 366 ASN C 371 -1 N VAL C 369 O ALA C 398
SHEET 4 AB1 6 HIS C 406 ILE C 419 -1 O LEU C 415 N TYR C 370
SHEET 5 AB1 6 LEU C 377 TYR C 383 -1 N THR C 378 O ARG C 409
SHEET 6 AB1 6 LYS C 386 LEU C 392 -1 O LEU C 392 N LEU C 377
SHEET 1 AB2 7 ARG C 98 ARG C 102 0
SHEET 2 AB2 7 LYS C 105 ASP C 112 -1 O LYS C 105 N ARG C 102
SHEET 3 AB2 7 PHE C 121 GLU C 128 -1 O TRP C 125 N ARG C 111
SHEET 4 AB2 7 LEU C 203 TYR C 209 -1 O THR C 208 N ARG C 122
SHEET 5 AB2 7 HIS C 151 ILE C 157 -1 N ILE C 157 O LEU C 203
SHEET 6 AB2 7 SER C 181 ILE C 184 -1 O MET C 182 N THR C 154
SHEET 7 AB2 7 VAL C 311 LYS C 314 -1 O ILE C 312 N TYR C 183
SHEET 1 AB3 4 LYS C 131 VAL C 132 0
SHEET 2 AB3 4 HIS C 190 ARG C 195 1 O THR C 194 N VAL C 132
SHEET 3 AB3 4 VAL C 160 LYS C 165 -1 N TYR C 163 O THR C 191
SHEET 4 AB3 4 LYS C 171 MET C 176 -1 O HIS C 172 N TYR C 164
SHEET 1 AB4 7 ILE D 85 MET D 88 0
SHEET 2 AB4 7 SER D 397 ILE D 400 -1 O SER D 397 N MET D 88
SHEET 3 AB4 7 HIS D 366 ASN D 371 -1 N VAL D 369 O ALA D 398
SHEET 4 AB4 7 HIS D 406 ILE D 419 -1 O LEU D 415 N TYR D 370
SHEET 5 AB4 7 LYS D 345 SER D 353 -1 N LYS D 345 O ARG D 418
SHEET 6 AB4 7 TYR D 330 GLU D 334 -1 N GLU D 331 O ASP D 350
SHEET 7 AB4 7 HIS D 321 TYR D 324 -1 N TRP D 322 O PHE D 332
SHEET 1 AB5 6 ILE D 85 MET D 88 0
SHEET 2 AB5 6 SER D 397 ILE D 400 -1 O SER D 397 N MET D 88
SHEET 3 AB5 6 HIS D 366 ASN D 371 -1 N VAL D 369 O ALA D 398
SHEET 4 AB5 6 HIS D 406 ILE D 419 -1 O LEU D 415 N TYR D 370
SHEET 5 AB5 6 LEU D 377 TYR D 383 -1 N THR D 378 O ARG D 409
SHEET 6 AB5 6 LYS D 386 LEU D 392 -1 O LEU D 392 N LEU D 377
SHEET 1 AB6 7 ARG D 98 ARG D 102 0
SHEET 2 AB6 7 LYS D 105 ASP D 112 -1 O TYR D 107 N MET D 100
SHEET 3 AB6 7 PHE D 121 GLU D 128 -1 O TRP D 125 N ARG D 111
SHEET 4 AB6 7 LEU D 203 TYR D 209 -1 O THR D 208 N ARG D 122
SHEET 5 AB6 7 HIS D 151 ILE D 157 -1 N ILE D 157 O LEU D 203
SHEET 6 AB6 7 SER D 181 ILE D 184 -1 O MET D 182 N THR D 154
SHEET 7 AB6 7 VAL D 311 LYS D 314 -1 O ILE D 312 N TYR D 183
SHEET 1 AB7 4 LYS D 131 VAL D 132 0
SHEET 2 AB7 4 HIS D 190 ARG D 195 1 O THR D 194 N VAL D 132
SHEET 3 AB7 4 VAL D 160 LYS D 165 -1 N TYR D 163 O THR D 191
SHEET 4 AB7 4 LYS D 171 ILE D 175 -1 O HIS D 172 N TYR D 164
SHEET 1 AB8 7 ILE E 85 MET E 88 0
SHEET 2 AB8 7 SER E 397 ILE E 400 -1 O SER E 397 N MET E 88
SHEET 3 AB8 7 HIS E 366 ASN E 371 -1 N VAL E 369 O ALA E 398
SHEET 4 AB8 7 HIS E 406 ILE E 419 -1 O LEU E 415 N TYR E 370
SHEET 5 AB8 7 LYS E 345 SER E 353 -1 N LYS E 345 O ARG E 418
SHEET 6 AB8 7 TYR E 330 GLU E 334 -1 N TYR E 333 O GLU E 348
SHEET 7 AB8 7 HIS E 321 TYR E 324 -1 N TYR E 324 O TYR E 330
SHEET 1 AB9 6 ILE E 85 MET E 88 0
SHEET 2 AB9 6 SER E 397 ILE E 400 -1 O SER E 397 N MET E 88
SHEET 3 AB9 6 HIS E 366 ASN E 371 -1 N VAL E 369 O ALA E 398
SHEET 4 AB9 6 HIS E 406 ILE E 419 -1 O LEU E 415 N TYR E 370
SHEET 5 AB9 6 LEU E 377 TYR E 383 -1 N THR E 378 O ARG E 409
SHEET 6 AB9 6 LYS E 386 LEU E 392 -1 O LEU E 392 N LEU E 377
SHEET 1 AC1 7 ARG E 98 ARG E 102 0
SHEET 2 AC1 7 LYS E 105 ASP E 112 -1 O TYR E 107 N MET E 100
SHEET 3 AC1 7 PHE E 121 GLU E 128 -1 O TRP E 125 N ARG E 111
SHEET 4 AC1 7 LEU E 203 TYR E 209 -1 O THR E 208 N ARG E 122
SHEET 5 AC1 7 HIS E 151 ILE E 157 -1 N ILE E 157 O LEU E 203
SHEET 6 AC1 7 SER E 181 ILE E 184 -1 O MET E 182 N THR E 154
SHEET 7 AC1 7 VAL E 311 LYS E 314 -1 O ILE E 312 N TYR E 183
SHEET 1 AC2 4 LYS E 131 VAL E 132 0
SHEET 2 AC2 4 HIS E 190 ARG E 195 1 O THR E 194 N VAL E 132
SHEET 3 AC2 4 VAL E 160 LYS E 165 -1 N TYR E 163 O THR E 191
SHEET 4 AC2 4 LYS E 171 MET E 176 -1 O HIS E 172 N TYR E 164
SHEET 1 AC3 7 ILE F 85 MET F 88 0
SHEET 2 AC3 7 SER F 397 ILE F 400 -1 O SER F 397 N MET F 88
SHEET 3 AC3 7 HIS F 366 ASN F 371 -1 N VAL F 369 O ALA F 398
SHEET 4 AC3 7 HIS F 406 ILE F 419 -1 O LEU F 415 N TYR F 370
SHEET 5 AC3 7 LYS F 345 SER F 352 -1 N LYS F 345 O ARG F 418
SHEET 6 AC3 7 TYR F 330 GLU F 334 -1 N GLU F 331 O ASP F 350
SHEET 7 AC3 7 HIS F 321 TYR F 324 -1 N TYR F 324 O TYR F 330
SHEET 1 AC4 6 ILE F 85 MET F 88 0
SHEET 2 AC4 6 SER F 397 ILE F 400 -1 O SER F 397 N MET F 88
SHEET 3 AC4 6 HIS F 366 ASN F 371 -1 N VAL F 369 O ALA F 398
SHEET 4 AC4 6 HIS F 406 ILE F 419 -1 O LEU F 415 N TYR F 370
SHEET 5 AC4 6 LEU F 377 TYR F 383 -1 N THR F 378 O ARG F 409
SHEET 6 AC4 6 LYS F 386 LEU F 392 -1 O LEU F 392 N LEU F 377
SHEET 1 AC5 7 ARG F 98 ARG F 102 0
SHEET 2 AC5 7 LYS F 105 ASP F 112 -1 O TYR F 107 N MET F 100
SHEET 3 AC5 7 PHE F 121 GLU F 128 -1 O TRP F 125 N ARG F 111
SHEET 4 AC5 7 LEU F 203 TYR F 209 -1 O THR F 208 N ARG F 122
SHEET 5 AC5 7 HIS F 151 ILE F 157 -1 N ILE F 157 O LEU F 203
SHEET 6 AC5 7 SER F 181 ILE F 184 -1 O MET F 182 N THR F 154
SHEET 7 AC5 7 VAL F 311 LYS F 314 -1 O ILE F 312 N TYR F 183
SHEET 1 AC6 4 LYS F 131 VAL F 132 0
SHEET 2 AC6 4 HIS F 190 ARG F 195 1 O THR F 194 N VAL F 132
SHEET 3 AC6 4 VAL F 160 LYS F 165 -1 N TYR F 163 O THR F 191
SHEET 4 AC6 4 LYS F 171 ILE F 175 -1 O HIS F 172 N TYR F 164
SHEET 1 AC7 7 ILE G 85 MET G 88 0
SHEET 2 AC7 7 SER G 397 ILE G 400 -1 O SER G 397 N MET G 88
SHEET 3 AC7 7 HIS G 366 ASN G 371 -1 N VAL G 369 O ALA G 398
SHEET 4 AC7 7 HIS G 406 ILE G 419 -1 O LEU G 415 N TYR G 370
SHEET 5 AC7 7 LYS G 345 SER G 353 -1 N LYS G 345 O ARG G 418
SHEET 6 AC7 7 TYR G 330 GLU G 334 -1 N GLU G 331 O ASP G 350
SHEET 7 AC7 7 HIS G 321 TYR G 324 -1 N TYR G 324 O TYR G 330
SHEET 1 AC8 6 ILE G 85 MET G 88 0
SHEET 2 AC8 6 SER G 397 ILE G 400 -1 O SER G 397 N MET G 88
SHEET 3 AC8 6 HIS G 366 ASN G 371 -1 N VAL G 369 O ALA G 398
SHEET 4 AC8 6 HIS G 406 ILE G 419 -1 O LEU G 415 N TYR G 370
SHEET 5 AC8 6 LEU G 377 TYR G 383 -1 N THR G 378 O ARG G 409
SHEET 6 AC8 6 LYS G 386 LEU G 392 -1 O LEU G 392 N LEU G 377
SHEET 1 AC9 7 ARG G 98 ARG G 102 0
SHEET 2 AC9 7 LYS G 105 ASP G 112 -1 O TYR G 108 N MET G 100
SHEET 3 AC9 7 PHE G 121 GLU G 128 -1 O TRP G 125 N ARG G 111
SHEET 4 AC9 7 LEU G 203 TYR G 209 -1 O ALA G 206 N GLU G 124
SHEET 5 AC9 7 HIS G 151 ILE G 157 -1 N ILE G 157 O LEU G 203
SHEET 6 AC9 7 SER G 181 ILE G 184 -1 O MET G 182 N THR G 154
SHEET 7 AC9 7 VAL G 311 LYS G 314 -1 O LYS G 314 N SER G 181
SHEET 1 AD1 4 LYS G 131 VAL G 132 0
SHEET 2 AD1 4 HIS G 190 ARG G 195 1 O THR G 194 N VAL G 132
SHEET 3 AD1 4 VAL G 160 LYS G 165 -1 N TYR G 163 O THR G 191
SHEET 4 AD1 4 LYS G 171 MET G 176 -1 O ALA G 174 N PHE G 162
SHEET 1 AD2 7 ILE H 85 MET H 88 0
SHEET 2 AD2 7 SER H 397 ILE H 400 -1 O SER H 397 N MET H 88
SHEET 3 AD2 7 HIS H 366 ASN H 371 -1 N VAL H 369 O ALA H 398
SHEET 4 AD2 7 ASN H 411 ILE H 419 -1 O LEU H 415 N TYR H 370
SHEET 5 AD2 7 LYS H 345 SER H 352 -1 N LYS H 345 O ARG H 418
SHEET 6 AD2 7 TYR H 330 GLU H 334 -1 N GLU H 331 O ASP H 350
SHEET 7 AD2 7 HIS H 321 TYR H 324 -1 N TRP H 322 O PHE H 332
SHEET 1 AD3 7 ARG H 98 ARG H 102 0
SHEET 2 AD3 7 LYS H 105 ASP H 112 -1 O TYR H 107 N MET H 100
SHEET 3 AD3 7 PHE H 121 GLU H 128 -1 O TRP H 125 N ARG H 111
SHEET 4 AD3 7 LEU H 203 TYR H 209 -1 O ALA H 206 N GLU H 124
SHEET 5 AD3 7 HIS H 151 ILE H 157 -1 N ILE H 157 O LEU H 203
SHEET 6 AD3 7 SER H 181 ILE H 184 -1 O MET H 182 N THR H 154
SHEET 7 AD3 7 VAL H 311 LYS H 314 -1 O ILE H 312 N TYR H 183
SHEET 1 AD4 4 LYS H 131 VAL H 132 0
SHEET 2 AD4 4 HIS H 190 ARG H 195 1 O THR H 194 N VAL H 132
SHEET 3 AD4 4 VAL H 160 LYS H 165 -1 N TYR H 163 O THR H 191
SHEET 4 AD4 4 LYS H 171 ILE H 175 -1 O HIS H 172 N TYR H 164
SHEET 1 AD5 3 LYS H 386 LEU H 392 0
SHEET 2 AD5 3 LEU H 377 TYR H 383 -1 N LEU H 377 O LEU H 392
SHEET 3 AD5 3 HIS H 406 ARG H 409 -1 O ARG H 409 N THR H 378
LINK NE2 HIS A 148 FE FE A 501 1555 1555 2.07
LINK OE1 GLN A 152 FE FE A 501 1555 1555 2.28
LINK NE2 HIS A 190 FE FE A 501 1555 1555 2.15
LINK FE FE A 501 O2 2HE A 502 1555 1555 1.85
LINK FE FE A 501 O4 2HE A 502 1555 1555 1.89
LINK FE FE A 501 O HOH A 601 1555 1555 2.56
LINK NE2 HIS B 148 FE FE B 501 1555 1555 2.17
LINK OE1 GLN B 152 FE FE B 501 1555 1555 2.08
LINK NE2 HIS B 190 FE FE B 501 1555 1555 2.21
LINK FE FE B 501 O4 2HE B 503 1555 1555 2.00
LINK FE FE B 501 O3 2HE B 503 1555 1555 2.05
LINK FE FE B 501 O HOH B 621 1555 1555 2.38
LINK FE FE B 502 O HOH B 609 1555 1555 2.01
LINK FE FE B 502 OE1 GLU H 159 1455 1555 2.50
LINK FE FE B 502 O HOH H 696 1555 1655 2.18
LINK NE2 HIS C 148 FE FE C 501 1555 1555 2.06
LINK OE1 GLN C 152 FE FE C 501 1555 1555 2.14
LINK NE2 HIS C 190 FE FE C 501 1555 1555 2.17
LINK FE FE C 501 O4 2HE C 502 1555 1555 1.99
LINK FE FE C 501 O2 2HE C 502 1555 1555 2.21
LINK FE FE C 501 O HOH C 601 1555 1555 2.52
LINK NE2 HIS D 148 FE FE D 501 1555 1555 2.17
LINK OE1 GLN D 152 FE FE D 501 1555 1555 2.24
LINK NE2 HIS D 190 FE FE D 501 1555 1555 2.18
LINK FE FE D 501 O1 2HE D 502 1555 1555 1.99
LINK FE FE D 501 O4 2HE D 502 1555 1555 2.12
LINK FE FE D 501 O HOH D 601 1555 1555 2.17
LINK NE2 HIS E 148 FE FE E 501 1555 1555 2.08
LINK OE1 GLN E 152 FE FE E 501 1555 1555 2.21
LINK NE2 HIS E 190 FE FE E 501 1555 1555 2.23
LINK FE FE E 501 O2 2HE E 502 1555 1555 2.02
LINK FE FE E 501 O4 2HE E 502 1555 1555 1.91
LINK FE FE E 501 O HOH E 608 1555 1555 2.38
LINK NE2 HIS F 148 FE FE F 501 1555 1555 2.20
LINK OE1 GLN F 152 FE FE F 501 1555 1555 2.18
LINK NE2 HIS F 190 FE FE F 501 1555 1555 2.03
LINK FE FE F 501 O1 2HE F 502 1555 1555 2.15
LINK FE FE F 501 O4 2HE F 502 1555 1555 2.09
LINK FE FE F 501 O HOH F 601 1555 1555 1.94
LINK NE2 HIS G 148 FE FE G 501 1555 1555 1.98
LINK OE1 GLN G 152 FE FE G 501 1555 1555 2.41
LINK NE2 HIS G 190 FE FE G 501 1555 1555 2.36
LINK FE FE G 501 O4 2HE G 502 1555 1555 2.08
LINK FE FE G 501 O2 2HE G 502 1555 1555 2.15
LINK NE2 HIS H 148 FE FE H 501 1555 1555 2.14
LINK OE1 GLN H 152 FE FE H 501 1555 1555 2.20
LINK NE2 HIS H 190 FE FE H 501 1555 1555 2.13
LINK FE FE H 501 O2 2HE H 502 1555 1555 2.06
LINK FE FE H 501 O4 2HE H 502 1555 1555 1.92
CISPEP 1 TYR A 324 PRO A 325 0 -9.19
CISPEP 2 TYR B 324 PRO B 325 0 -7.66
CISPEP 3 TYR C 324 PRO C 325 0 -7.72
CISPEP 4 TYR D 324 PRO D 325 0 -8.11
CISPEP 5 TYR E 324 PRO E 325 0 -7.42
CISPEP 6 TYR F 324 PRO F 325 0 -7.87
CISPEP 7 TYR G 324 PRO G 325 0 -7.29
CISPEP 8 TYR H 324 PRO H 325 0 -7.21
SITE 1 AC1 5 HIS A 148 GLN A 152 HIS A 190 2HE A 502
SITE 2 AC1 5 HOH A 601
SITE 1 AC2 14 ARG A 102 TYR A 108 TYR A 110 ILE A 126
SITE 2 AC2 14 ASN A 145 HIS A 148 GLN A 152 HIS A 190
SITE 3 AC2 14 PHE A 192 FE A 501 HOH A 601 HOH A 653
SITE 4 AC2 14 LYS B 28 TRP B 449
SITE 1 AC3 6 LYS A 28 HIS B 148 GLN B 152 HIS B 190
SITE 2 AC3 6 2HE B 503 HOH B 621
SITE 1 AC4 4 GLU B 159 HOH B 609 GLU H 159 HOH H 696
SITE 1 AC5 13 LYS A 28 TRP A 449 ARG B 102 TYR B 108
SITE 2 AC5 13 TYR B 110 ILE B 126 ASN B 145 HIS B 148
SITE 3 AC5 13 GLN B 152 HIS B 190 PHE B 192 FE B 501
SITE 4 AC5 13 HOH B 621
SITE 1 AC6 7 PHE A 433 PHE B 236 ALA B 242 PRO B 303
SITE 2 AC6 7 ASN B 304 HOH B 615 HOH B 650
SITE 1 AC7 5 HIS C 148 GLN C 152 HIS C 190 2HE C 502
SITE 2 AC7 5 HOH C 601
SITE 1 AC8 14 ARG C 102 TYR C 108 TYR C 110 ILE C 126
SITE 2 AC8 14 ASN C 145 HIS C 148 GLN C 152 HIS C 190
SITE 3 AC8 14 PHE C 192 FE C 501 HOH C 601 HOH C 635
SITE 4 AC8 14 LYS D 28 TRP D 449
SITE 1 AC9 8 PHE C 236 ALA C 242 PRO C 303 ASN C 304
SITE 2 AC9 8 HOH C 631 HOH C 688 HOH C 697 PHE D 433
SITE 1 AD1 5 HIS D 148 GLN D 152 HIS D 190 2HE D 502
SITE 2 AD1 5 HOH D 601
SITE 1 AD2 14 LYS C 28 TRP C 449 ARG D 102 TYR D 108
SITE 2 AD2 14 TYR D 110 ILE D 126 ASN D 145 HIS D 148
SITE 3 AD2 14 GLN D 152 HIS D 190 PHE D 192 FE D 501
SITE 4 AD2 14 HOH D 601 HOH D 665
SITE 1 AD3 7 PHE C 433 PHE D 236 ALA D 242 PRO D 303
SITE 2 AD3 7 ASN D 304 HOH D 634 HOH D 683
SITE 1 AD4 6 HIS E 148 GLN E 152 HIS E 190 2HE E 502
SITE 2 AD4 6 HOH E 608 LYS F 28
SITE 1 AD5 14 ARG E 102 TYR E 108 TYR E 110 ILE E 126
SITE 2 AD5 14 ASN E 145 HIS E 148 GLN E 152 HIS E 190
SITE 3 AD5 14 PHE E 192 FE E 501 HOH E 608 HOH E 655
SITE 4 AD5 14 LYS F 28 TRP F 449
SITE 1 AD6 8 PHE E 236 ALA E 242 PRO E 303 ASN E 304
SITE 2 AD6 8 HOH E 623 HOH E 625 HOH E 654 PHE F 433
SITE 1 AD7 5 HIS F 148 GLN F 152 HIS F 190 2HE F 502
SITE 2 AD7 5 HOH F 601
SITE 1 AD8 13 LYS E 28 TRP E 449 ARG F 102 TYR F 110
SITE 2 AD8 13 ILE F 126 ASN F 145 HIS F 148 GLN F 152
SITE 3 AD8 13 HIS F 190 PHE F 192 FE F 501 HOH F 601
SITE 4 AD8 13 HOH F 616
SITE 1 AD9 6 PHE E 433 PHE F 236 PRO F 303 ASN F 304
SITE 2 AD9 6 HOH F 608 HOH F 656
SITE 1 AE1 5 HIS G 148 GLN G 152 HIS G 190 2HE G 502
SITE 2 AE1 5 LYS H 28
SITE 1 AE2 12 ARG G 102 TYR G 108 TYR G 110 ILE G 126
SITE 2 AE2 12 ASN G 145 HIS G 148 GLN G 152 HIS G 190
SITE 3 AE2 12 PHE G 192 FE G 501 LYS H 28 TRP H 449
SITE 1 AE3 5 PHE G 236 PRO G 303 ASN G 304 HOH G 617
SITE 2 AE3 5 PHE H 433
SITE 1 AE4 6 LYS G 28 HIS H 148 GLN H 152 HIS H 190
SITE 2 AE4 6 2HE H 502 HOH H 601
SITE 1 AE5 13 LYS G 28 TRP G 449 ARG H 102 TYR H 110
SITE 2 AE5 13 ILE H 126 ASN H 145 HIS H 148 GLN H 152
SITE 3 AE5 13 HIS H 190 PHE H 192 FE H 501 HOH H 601
SITE 4 AE5 13 HOH H 654
CRYST1 70.850 351.250 76.870 90.00 103.36 90.00 P 1 21 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014114 0.000000 0.003352 0.00000
SCALE2 0.000000 0.002847 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013371 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
