HEADER ISOMERASE 03-AUG-14 4U8I
TITLE STRUCTURE OF ASPERGILLUS FUMIGATUS UDP-GALACTOPYRANOSE MUTASE MUTANT
TITLE 2 F66A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.4.99.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE 3 ORGANISM_TAXID: 746128;
SOURCE 4 GENE: GLF, GLFA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS NUCLEOTIDE BINDING, MUTASE, FLAVIN ADENINE DINUCLEOTIDE BINDING,
KEYWDS 2 ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.A.QURESHI,R.CHAUDHARY,J.J.TANNER
REVDAT 5 27-SEP-23 4U8I 1 REMARK
REVDAT 4 25-DEC-19 4U8I 1 REMARK
REVDAT 3 27-SEP-17 4U8I 1 SOURCE JRNL REMARK
REVDAT 2 24-DEC-14 4U8I 1 JRNL
REVDAT 1 03-DEC-14 4U8I 0
JRNL AUTH I.DA FONSECA,I.A.QURESHI,R.MEHRA-CHAUDHARY,K.KIZJAKINA,
JRNL AUTH 2 J.J.TANNER,P.SOBRADO
JRNL TITL CONTRIBUTIONS OF UNIQUE ACTIVE SITE RESIDUES OF EUKARYOTIC
JRNL TITL 2 UDP-GALACTOPYRANOSE MUTASES TO SUBSTRATE RECOGNITION AND
JRNL TITL 3 ACTIVE SITE DYNAMICS.
JRNL REF BIOCHEMISTRY V. 53 7794 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 25412209
JRNL DOI 10.1021/BI501008Z
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 273034
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 13724
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 48.4019 - 6.3652 0.95 8880 493 0.1469 0.1596
REMARK 3 2 6.3652 - 5.0539 0.98 8768 468 0.1398 0.1576
REMARK 3 3 5.0539 - 4.4156 0.98 8710 454 0.1230 0.1463
REMARK 3 4 4.4156 - 4.0121 0.98 8664 472 0.1334 0.1532
REMARK 3 5 4.0121 - 3.7246 0.99 8690 426 0.1498 0.1689
REMARK 3 6 3.7246 - 3.5051 0.99 8641 442 0.1683 0.1879
REMARK 3 7 3.5051 - 3.3296 0.99 8651 484 0.1912 0.2229
REMARK 3 8 3.3296 - 3.1847 0.99 8641 470 0.1946 0.2293
REMARK 3 9 3.1847 - 3.0621 0.99 8648 448 0.2021 0.2411
REMARK 3 10 3.0621 - 2.9565 0.99 8618 487 0.1973 0.2515
REMARK 3 11 2.9565 - 2.8640 1.00 8659 447 0.2029 0.2487
REMARK 3 12 2.8640 - 2.7822 0.99 8639 424 0.1968 0.2248
REMARK 3 13 2.7822 - 2.7089 1.00 8671 436 0.1977 0.2384
REMARK 3 14 2.7089 - 2.6429 1.00 8648 451 0.2016 0.2474
REMARK 3 15 2.6429 - 2.5828 1.00 8657 438 0.1982 0.2435
REMARK 3 16 2.5828 - 2.5278 1.00 8598 507 0.1988 0.2419
REMARK 3 17 2.5278 - 2.4773 1.00 8647 429 0.1957 0.2299
REMARK 3 18 2.4773 - 2.4305 1.00 8593 491 0.1987 0.2371
REMARK 3 19 2.4305 - 2.3871 1.00 8644 445 0.2040 0.2462
REMARK 3 20 2.3871 - 2.3466 1.00 8652 438 0.2162 0.2595
REMARK 3 21 2.3466 - 2.3088 1.00 8595 441 0.2125 0.2600
REMARK 3 22 2.3088 - 2.2733 1.00 8667 463 0.2096 0.2522
REMARK 3 23 2.2733 - 2.2398 1.00 8539 454 0.2646 0.3117
REMARK 3 24 2.2398 - 2.2083 1.00 8656 441 0.2458 0.2970
REMARK 3 25 2.2083 - 2.1784 1.00 8564 489 0.2260 0.2640
REMARK 3 26 2.1784 - 2.1501 1.00 8564 470 0.2269 0.2713
REMARK 3 27 2.1501 - 2.1233 1.00 8650 455 0.2243 0.2533
REMARK 3 28 2.1233 - 2.0977 1.00 8604 468 0.2402 0.2860
REMARK 3 29 2.0977 - 2.0733 1.00 8569 444 0.2564 0.2961
REMARK 3 30 2.0733 - 2.0500 1.00 8583 449 0.2958 0.3244
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.15
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 : 0.007 16329
REMARK 3 ANGLE : 1.031 22263
REMARK 3 CHIRALITY : 0.038 2432
REMARK 3 PLANARITY : 0.006 2855
REMARK 3 DIHEDRAL : 15.200 5924
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND NOT RESNAME FDA
REMARK 3 ORIGIN FOR THE GROUP (A): 71.2405 77.5640 159.7759
REMARK 3 T TENSOR
REMARK 3 T11: 0.1980 T22: 0.3209
REMARK 3 T33: 0.2909 T12: 0.0256
REMARK 3 T13: 0.0272 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.7233 L22: 0.2565
REMARK 3 L33: 0.6091 L12: -0.0626
REMARK 3 L13: -0.1259 L23: -0.0371
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: 0.2304 S13: -0.0097
REMARK 3 S21: -0.0354 S22: -0.0155 S23: -0.0446
REMARK 3 S31: -0.0146 S32: -0.0431 S33: -0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND NOT RESNAME FDA
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3808 102.9092 212.1161
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.2146
REMARK 3 T33: 0.2776 T12: 0.0465
REMARK 3 T13: 0.0137 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.5263 L22: 0.4317
REMARK 3 L33: 0.4739 L12: -0.2162
REMARK 3 L13: 0.0212 L23: -0.0057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: -0.0867 S13: 0.0209
REMARK 3 S21: 0.1384 S22: 0.0510 S23: 0.0570
REMARK 3 S31: -0.0206 S32: -0.0065 S33: 0.0436
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C AND NOT RESNAME FDA
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5657 67.8367 149.8603
REMARK 3 T TENSOR
REMARK 3 T11: 0.1996 T22: 0.3665
REMARK 3 T33: 0.2979 T12: 0.0102
REMARK 3 T13: -0.0360 T23: -0.0835
REMARK 3 L TENSOR
REMARK 3 L11: 0.9794 L22: 0.2556
REMARK 3 L33: 0.6676 L12: 0.0274
REMARK 3 L13: -0.0915 L23: 0.1040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.3458 S13: -0.2205
REMARK 3 S21: -0.0687 S22: 0.0362 S23: 0.0022
REMARK 3 S31: 0.0860 S32: 0.0477 S33: -0.0333
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D AND NOT RESNAME FDA
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7610 59.5650 222.4000
REMARK 3 T TENSOR
REMARK 3 T11: 0.3117 T22: 0.2440
REMARK 3 T33: 0.2957 T12: 0.0739
REMARK 3 T13: 0.0436 T23: 0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 0.5623 L22: 0.8746
REMARK 3 L33: 0.5958 L12: -0.4433
REMARK 3 L13: -0.1127 L23: 0.1550
REMARK 3 S TENSOR
REMARK 3 S11: -0.1393 S12: -0.1339 S13: -0.1233
REMARK 3 S21: 0.3181 S22: 0.1567 S23: 0.1875
REMARK 3 S31: 0.0423 S32: -0.0627 S33: -0.0126
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 4U8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000202895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 273170
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 48.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 1.08100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3UTF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 - 1.4 M AMMONIUM SULFATE AND 0.1 M
REMARK 280 SODIUM ACETATE AT PH 4.5., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 213.56533
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 106.78267
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 160.17400
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 53.39133
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 266.95667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 213.56533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 106.78267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 53.39133
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 160.17400
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 266.95667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -278.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A -2
REMARK 465 ILE A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 LYS A 508
REMARK 465 ALA A 509
REMARK 465 GLN A 510
REMARK 465 ALA B -2
REMARK 465 ILE B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 LYS B 508
REMARK 465 ALA B 509
REMARK 465 GLN B 510
REMARK 465 ALA C -2
REMARK 465 ILE C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 LYS C 508
REMARK 465 ALA C 509
REMARK 465 GLN C 510
REMARK 465 ALA D -2
REMARK 465 ILE D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 LYS D 508
REMARK 465 ALA D 509
REMARK 465 GLN D 510
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 HIS A 3 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 82 CE NZ
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 LYS A 138 CE NZ
REMARK 470 LYS A 140 CD CE NZ
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 ARG A 182 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 231 CG CD CE NZ
REMARK 470 GLU A 238 CD OE1 OE2
REMARK 470 LYS A 244 CE NZ
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 ARG A 356 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 358 CG CD OE1 NE2
REMARK 470 GLU A 361 CG CD OE1 OE2
REMARK 470 GLU A 385 CG CD OE1 OE2
REMARK 470 LYS A 506 CG CD CE NZ
REMARK 470 SER A 507 OG
REMARK 470 HIS B 3 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 41 CG CD OE1 OE2
REMARK 470 LYS B 82 CE NZ
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 ASP B 84 CG OD1 OD2
REMARK 470 LYS B 138 CE NZ
REMARK 470 LYS B 140 CE NZ
REMARK 470 GLU B 181 CG CD OE1 OE2
REMARK 470 ARG B 182 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 231 CG CD CE NZ
REMARK 470 LYS B 244 CE NZ
REMARK 470 GLU B 282 CG CD OE1 OE2
REMARK 470 GLU B 308 CD OE1 OE2
REMARK 470 GLU B 341 CG CD OE1 OE2
REMARK 470 ARG B 356 NE CZ NH1 NH2
REMARK 470 GLN B 358 CG CD OE1 NE2
REMARK 470 GLU B 385 CG CD OE1 OE2
REMARK 470 LYS B 506 CG CD CE NZ
REMARK 470 SER B 507 OG
REMARK 470 HIS C 3 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 41 CG CD OE1 OE2
REMARK 470 LYS C 82 CG CD CE NZ
REMARK 470 GLU C 83 CG CD OE1 OE2
REMARK 470 ASP C 84 CG OD1 OD2
REMARK 470 LYS C 115 CE NZ
REMARK 470 GLU C 116 CG CD OE1 OE2
REMARK 470 LYS C 138 CE NZ
REMARK 470 LYS C 140 CD CE NZ
REMARK 470 LYS C 173 NZ
REMARK 470 GLU C 181 CG CD OE1 OE2
REMARK 470 ARG C 182 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 231 CG CD CE NZ
REMARK 470 LYS C 241 NZ
REMARK 470 LYS C 244 CD CE NZ
REMARK 470 GLN C 281 CG CD OE1 NE2
REMARK 470 GLU C 308 CG CD OE1 OE2
REMARK 470 ASP C 321 CG OD1 OD2
REMARK 470 GLU C 341 CG CD OE1 OE2
REMARK 470 ARG C 356 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 361 CG CD OE1 OE2
REMARK 470 GLU C 385 CG CD OE1 OE2
REMARK 470 LYS C 506 CG CD CE NZ
REMARK 470 SER C 507 OG
REMARK 470 HIS D 3 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 41 CG CD OE1 OE2
REMARK 470 LYS D 82 CE NZ
REMARK 470 ASP D 84 CG OD1 OD2
REMARK 470 GLU D 116 CG CD OE1 OE2
REMARK 470 LYS D 138 CE NZ
REMARK 470 LYS D 140 CG CD CE NZ
REMARK 470 LYS D 173 CE NZ
REMARK 470 GLU D 181 CG CD OE1 OE2
REMARK 470 ARG D 182 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 231 CG CD CE NZ
REMARK 470 GLU D 238 CG CD OE1 OE2
REMARK 470 LYS D 241 NZ
REMARK 470 LYS D 244 CD CE NZ
REMARK 470 GLN D 281 CG CD OE1 NE2
REMARK 470 GLU D 308 CD OE1 OE2
REMARK 470 GLU D 341 CG CD OE1 OE2
REMARK 470 ARG D 356 NE CZ NH1 NH2
REMARK 470 LYS D 363 CE NZ
REMARK 470 GLU D 385 CG CD OE1 OE2
REMARK 470 LYS D 440 CE NZ
REMARK 470 LYS D 506 CG CD CE NZ
REMARK 470 SER D 507 OG
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 PHE A 158 -72.00 -131.16
REMARK 500 ASN A 203 45.56 -89.74
REMARK 500 CYS A 314 -68.84 -102.14
REMARK 500 PHE B 158 -75.45 -136.70
REMARK 500 ASN B 203 44.71 -84.90
REMARK 500 CYS B 314 -67.92 -101.32
REMARK 500 LYS B 380 86.07 -158.70
REMARK 500 ASP C 59 -179.98 -67.31
REMARK 500 PHE C 158 -76.71 -130.88
REMARK 500 ALA C 201 119.02 -162.40
REMARK 500 ASN C 203 48.23 -87.83
REMARK 500 CYS C 314 -68.39 -102.86
REMARK 500 LYS C 380 81.58 -157.68
REMARK 500 PHE D 158 -71.90 -128.26
REMARK 500 ASN D 203 47.17 -87.23
REMARK 500 CYS D 314 -65.50 -107.19
REMARK 500 LYS D 380 84.31 -165.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDA C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDA D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4U8J RELATED DB: PDB
REMARK 900 RELATED ID: 4U8K RELATED DB: PDB
REMARK 900 RELATED ID: 4U8L RELATED DB: PDB
REMARK 900 RELATED ID: 4U8M RELATED DB: PDB
REMARK 900 RELATED ID: 4U8N RELATED DB: PDB
REMARK 900 RELATED ID: 4U8O RELATED DB: PDB
REMARK 900 RELATED ID: 4U8P RELATED DB: PDB
DBREF 4U8I A 1 510 UNP Q4W1X2 Q4W1X2_ASPFM 1 510
DBREF 4U8I B 1 510 UNP Q4W1X2 Q4W1X2_ASPFM 1 510
DBREF 4U8I C 1 510 UNP Q4W1X2 Q4W1X2_ASPFM 1 510
DBREF 4U8I D 1 510 UNP Q4W1X2 Q4W1X2_ASPFM 1 510
SEQADV 4U8I ALA A -2 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ILE A -1 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA A 0 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA A 66 UNP Q4W1X2 PHE 66 ENGINEERED MUTATION
SEQADV 4U8I ALA A 344 UNP Q4W1X2 LYS 344 ENGINEERED MUTATION
SEQADV 4U8I ALA A 345 UNP Q4W1X2 LYS 345 ENGINEERED MUTATION
SEQADV 4U8I THR A 429 UNP Q4W1X2 ALA 429 ENGINEERED MUTATION
SEQADV 4U8I ALA B -2 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ILE B -1 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA B 0 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA B 66 UNP Q4W1X2 PHE 66 ENGINEERED MUTATION
SEQADV 4U8I ALA B 344 UNP Q4W1X2 LYS 344 ENGINEERED MUTATION
SEQADV 4U8I ALA B 345 UNP Q4W1X2 LYS 345 ENGINEERED MUTATION
SEQADV 4U8I THR B 429 UNP Q4W1X2 ALA 429 ENGINEERED MUTATION
SEQADV 4U8I ALA C -2 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ILE C -1 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA C 0 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA C 66 UNP Q4W1X2 PHE 66 ENGINEERED MUTATION
SEQADV 4U8I ALA C 344 UNP Q4W1X2 LYS 344 ENGINEERED MUTATION
SEQADV 4U8I ALA C 345 UNP Q4W1X2 LYS 345 ENGINEERED MUTATION
SEQADV 4U8I THR C 429 UNP Q4W1X2 ALA 429 ENGINEERED MUTATION
SEQADV 4U8I ALA D -2 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ILE D -1 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA D 0 UNP Q4W1X2 EXPRESSION TAG
SEQADV 4U8I ALA D 66 UNP Q4W1X2 PHE 66 ENGINEERED MUTATION
SEQADV 4U8I ALA D 344 UNP Q4W1X2 LYS 344 ENGINEERED MUTATION
SEQADV 4U8I ALA D 345 UNP Q4W1X2 LYS 345 ENGINEERED MUTATION
SEQADV 4U8I THR D 429 UNP Q4W1X2 ALA 429 ENGINEERED MUTATION
SEQRES 1 A 513 ALA ILE ALA MET THR HIS PRO ASP ILE SER VAL ASP VAL
SEQRES 2 A 513 LEU VAL ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA
SEQRES 3 A 513 LYS ARG LEU ASN GLN ILE ASP GLY PRO SER TRP MET ILE
SEQRES 4 A 513 VAL ASP SER ASN GLU THR PRO GLY GLY LEU ALA SER THR
SEQRES 5 A 513 ASP VAL THR PRO GLU GLY PHE LEU TYR ASP VAL GLY GLY
SEQRES 6 A 513 HIS VAL ILE ALA SER HIS TYR LYS TYR PHE ASP ASP CYS
SEQRES 7 A 513 LEU ASP GLU ALA LEU PRO LYS GLU ASP ASP TRP TYR THR
SEQRES 8 A 513 HIS GLN ARG ILE SER TYR VAL ARG CYS GLN GLY GLN TRP
SEQRES 9 A 513 VAL PRO TYR PRO PHE GLN ASN ASN ILE SER MET LEU PRO
SEQRES 10 A 513 LYS GLU GLU GLN VAL LYS CYS ILE ASP GLY MET ILE ASP
SEQRES 11 A 513 ALA ALA LEU GLU ALA ARG VAL ALA ASN THR LYS PRO LYS
SEQRES 12 A 513 THR PHE ASP GLU TRP ILE VAL ARG MET MET GLY THR GLY
SEQRES 13 A 513 ILE ALA ASP LEU PHE MET ARG PRO TYR ASN PHE LYS VAL
SEQRES 14 A 513 TRP ALA VAL PRO THR THR LYS MET GLN CYS ALA TRP LEU
SEQRES 15 A 513 GLY GLU ARG VAL ALA ALA PRO ASN LEU LYS ALA VAL THR
SEQRES 16 A 513 THR ASN VAL ILE LEU GLY LYS THR ALA GLY ASN TRP GLY
SEQRES 17 A 513 PRO ASN ALA THR PHE ARG PHE PRO ALA ARG GLY GLY THR
SEQRES 18 A 513 GLY GLY ILE TRP ILE ALA VAL ALA ASN THR LEU PRO LYS
SEQRES 19 A 513 GLU LYS THR ARG PHE GLY GLU LYS GLY LYS VAL THR LYS
SEQRES 20 A 513 VAL ASN ALA ASN ASN LYS THR VAL THR LEU GLN ASP GLY
SEQRES 21 A 513 THR THR ILE GLY TYR LYS LYS LEU VAL SER THR MET ALA
SEQRES 22 A 513 VAL ASP PHE LEU ALA GLU ALA MET ASN ASP GLN GLU LEU
SEQRES 23 A 513 VAL GLY LEU THR LYS GLN LEU PHE TYR SER SER THR HIS
SEQRES 24 A 513 VAL ILE GLY VAL GLY VAL ARG GLY SER ARG PRO GLU ARG
SEQRES 25 A 513 ILE GLY ASP LYS CYS TRP LEU TYR PHE PRO GLU ASP ASN
SEQRES 26 A 513 CYS PRO PHE TYR ARG ALA THR ILE PHE SER ASN TYR SER
SEQRES 27 A 513 PRO TYR ASN GLN PRO GLU ALA SER ALA ALA LEU PRO THR
SEQRES 28 A 513 MET GLN LEU ALA ASP GLY SER ARG PRO GLN SER THR GLU
SEQRES 29 A 513 ALA LYS GLU GLY PRO TYR TRP SER ILE MET LEU GLU VAL
SEQRES 30 A 513 SER GLU SER SER MET LYS PRO VAL ASN GLN GLU THR ILE
SEQRES 31 A 513 LEU ALA ASP CYS ILE GLN GLY LEU VAL ASN THR GLU MET
SEQRES 32 A 513 LEU LYS PRO THR ASP GLU ILE VAL SER THR TYR HIS ARG
SEQRES 33 A 513 ARG PHE ASP HIS GLY TYR PRO THR PRO THR LEU GLU ARG
SEQRES 34 A 513 GLU GLY THR LEU THR GLN ILE LEU PRO LYS LEU GLN ASP
SEQRES 35 A 513 LYS ASP ILE TRP SER ARG GLY ARG PHE GLY SER TRP ARG
SEQRES 36 A 513 TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET LEU GLY
SEQRES 37 A 513 VAL GLU ALA VAL ASP ASN ILE VAL ASN GLY ALA VAL GLU
SEQRES 38 A 513 LEU THR LEU ASN TYR PRO ASP PHE VAL ASN GLY ARG GLN
SEQRES 39 A 513 ASN THR GLU ARG ARG LEU VAL ASP GLY ALA GLN VAL PHE
SEQRES 40 A 513 ALA LYS SER LYS ALA GLN
SEQRES 1 B 513 ALA ILE ALA MET THR HIS PRO ASP ILE SER VAL ASP VAL
SEQRES 2 B 513 LEU VAL ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA
SEQRES 3 B 513 LYS ARG LEU ASN GLN ILE ASP GLY PRO SER TRP MET ILE
SEQRES 4 B 513 VAL ASP SER ASN GLU THR PRO GLY GLY LEU ALA SER THR
SEQRES 5 B 513 ASP VAL THR PRO GLU GLY PHE LEU TYR ASP VAL GLY GLY
SEQRES 6 B 513 HIS VAL ILE ALA SER HIS TYR LYS TYR PHE ASP ASP CYS
SEQRES 7 B 513 LEU ASP GLU ALA LEU PRO LYS GLU ASP ASP TRP TYR THR
SEQRES 8 B 513 HIS GLN ARG ILE SER TYR VAL ARG CYS GLN GLY GLN TRP
SEQRES 9 B 513 VAL PRO TYR PRO PHE GLN ASN ASN ILE SER MET LEU PRO
SEQRES 10 B 513 LYS GLU GLU GLN VAL LYS CYS ILE ASP GLY MET ILE ASP
SEQRES 11 B 513 ALA ALA LEU GLU ALA ARG VAL ALA ASN THR LYS PRO LYS
SEQRES 12 B 513 THR PHE ASP GLU TRP ILE VAL ARG MET MET GLY THR GLY
SEQRES 13 B 513 ILE ALA ASP LEU PHE MET ARG PRO TYR ASN PHE LYS VAL
SEQRES 14 B 513 TRP ALA VAL PRO THR THR LYS MET GLN CYS ALA TRP LEU
SEQRES 15 B 513 GLY GLU ARG VAL ALA ALA PRO ASN LEU LYS ALA VAL THR
SEQRES 16 B 513 THR ASN VAL ILE LEU GLY LYS THR ALA GLY ASN TRP GLY
SEQRES 17 B 513 PRO ASN ALA THR PHE ARG PHE PRO ALA ARG GLY GLY THR
SEQRES 18 B 513 GLY GLY ILE TRP ILE ALA VAL ALA ASN THR LEU PRO LYS
SEQRES 19 B 513 GLU LYS THR ARG PHE GLY GLU LYS GLY LYS VAL THR LYS
SEQRES 20 B 513 VAL ASN ALA ASN ASN LYS THR VAL THR LEU GLN ASP GLY
SEQRES 21 B 513 THR THR ILE GLY TYR LYS LYS LEU VAL SER THR MET ALA
SEQRES 22 B 513 VAL ASP PHE LEU ALA GLU ALA MET ASN ASP GLN GLU LEU
SEQRES 23 B 513 VAL GLY LEU THR LYS GLN LEU PHE TYR SER SER THR HIS
SEQRES 24 B 513 VAL ILE GLY VAL GLY VAL ARG GLY SER ARG PRO GLU ARG
SEQRES 25 B 513 ILE GLY ASP LYS CYS TRP LEU TYR PHE PRO GLU ASP ASN
SEQRES 26 B 513 CYS PRO PHE TYR ARG ALA THR ILE PHE SER ASN TYR SER
SEQRES 27 B 513 PRO TYR ASN GLN PRO GLU ALA SER ALA ALA LEU PRO THR
SEQRES 28 B 513 MET GLN LEU ALA ASP GLY SER ARG PRO GLN SER THR GLU
SEQRES 29 B 513 ALA LYS GLU GLY PRO TYR TRP SER ILE MET LEU GLU VAL
SEQRES 30 B 513 SER GLU SER SER MET LYS PRO VAL ASN GLN GLU THR ILE
SEQRES 31 B 513 LEU ALA ASP CYS ILE GLN GLY LEU VAL ASN THR GLU MET
SEQRES 32 B 513 LEU LYS PRO THR ASP GLU ILE VAL SER THR TYR HIS ARG
SEQRES 33 B 513 ARG PHE ASP HIS GLY TYR PRO THR PRO THR LEU GLU ARG
SEQRES 34 B 513 GLU GLY THR LEU THR GLN ILE LEU PRO LYS LEU GLN ASP
SEQRES 35 B 513 LYS ASP ILE TRP SER ARG GLY ARG PHE GLY SER TRP ARG
SEQRES 36 B 513 TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET LEU GLY
SEQRES 37 B 513 VAL GLU ALA VAL ASP ASN ILE VAL ASN GLY ALA VAL GLU
SEQRES 38 B 513 LEU THR LEU ASN TYR PRO ASP PHE VAL ASN GLY ARG GLN
SEQRES 39 B 513 ASN THR GLU ARG ARG LEU VAL ASP GLY ALA GLN VAL PHE
SEQRES 40 B 513 ALA LYS SER LYS ALA GLN
SEQRES 1 C 513 ALA ILE ALA MET THR HIS PRO ASP ILE SER VAL ASP VAL
SEQRES 2 C 513 LEU VAL ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA
SEQRES 3 C 513 LYS ARG LEU ASN GLN ILE ASP GLY PRO SER TRP MET ILE
SEQRES 4 C 513 VAL ASP SER ASN GLU THR PRO GLY GLY LEU ALA SER THR
SEQRES 5 C 513 ASP VAL THR PRO GLU GLY PHE LEU TYR ASP VAL GLY GLY
SEQRES 6 C 513 HIS VAL ILE ALA SER HIS TYR LYS TYR PHE ASP ASP CYS
SEQRES 7 C 513 LEU ASP GLU ALA LEU PRO LYS GLU ASP ASP TRP TYR THR
SEQRES 8 C 513 HIS GLN ARG ILE SER TYR VAL ARG CYS GLN GLY GLN TRP
SEQRES 9 C 513 VAL PRO TYR PRO PHE GLN ASN ASN ILE SER MET LEU PRO
SEQRES 10 C 513 LYS GLU GLU GLN VAL LYS CYS ILE ASP GLY MET ILE ASP
SEQRES 11 C 513 ALA ALA LEU GLU ALA ARG VAL ALA ASN THR LYS PRO LYS
SEQRES 12 C 513 THR PHE ASP GLU TRP ILE VAL ARG MET MET GLY THR GLY
SEQRES 13 C 513 ILE ALA ASP LEU PHE MET ARG PRO TYR ASN PHE LYS VAL
SEQRES 14 C 513 TRP ALA VAL PRO THR THR LYS MET GLN CYS ALA TRP LEU
SEQRES 15 C 513 GLY GLU ARG VAL ALA ALA PRO ASN LEU LYS ALA VAL THR
SEQRES 16 C 513 THR ASN VAL ILE LEU GLY LYS THR ALA GLY ASN TRP GLY
SEQRES 17 C 513 PRO ASN ALA THR PHE ARG PHE PRO ALA ARG GLY GLY THR
SEQRES 18 C 513 GLY GLY ILE TRP ILE ALA VAL ALA ASN THR LEU PRO LYS
SEQRES 19 C 513 GLU LYS THR ARG PHE GLY GLU LYS GLY LYS VAL THR LYS
SEQRES 20 C 513 VAL ASN ALA ASN ASN LYS THR VAL THR LEU GLN ASP GLY
SEQRES 21 C 513 THR THR ILE GLY TYR LYS LYS LEU VAL SER THR MET ALA
SEQRES 22 C 513 VAL ASP PHE LEU ALA GLU ALA MET ASN ASP GLN GLU LEU
SEQRES 23 C 513 VAL GLY LEU THR LYS GLN LEU PHE TYR SER SER THR HIS
SEQRES 24 C 513 VAL ILE GLY VAL GLY VAL ARG GLY SER ARG PRO GLU ARG
SEQRES 25 C 513 ILE GLY ASP LYS CYS TRP LEU TYR PHE PRO GLU ASP ASN
SEQRES 26 C 513 CYS PRO PHE TYR ARG ALA THR ILE PHE SER ASN TYR SER
SEQRES 27 C 513 PRO TYR ASN GLN PRO GLU ALA SER ALA ALA LEU PRO THR
SEQRES 28 C 513 MET GLN LEU ALA ASP GLY SER ARG PRO GLN SER THR GLU
SEQRES 29 C 513 ALA LYS GLU GLY PRO TYR TRP SER ILE MET LEU GLU VAL
SEQRES 30 C 513 SER GLU SER SER MET LYS PRO VAL ASN GLN GLU THR ILE
SEQRES 31 C 513 LEU ALA ASP CYS ILE GLN GLY LEU VAL ASN THR GLU MET
SEQRES 32 C 513 LEU LYS PRO THR ASP GLU ILE VAL SER THR TYR HIS ARG
SEQRES 33 C 513 ARG PHE ASP HIS GLY TYR PRO THR PRO THR LEU GLU ARG
SEQRES 34 C 513 GLU GLY THR LEU THR GLN ILE LEU PRO LYS LEU GLN ASP
SEQRES 35 C 513 LYS ASP ILE TRP SER ARG GLY ARG PHE GLY SER TRP ARG
SEQRES 36 C 513 TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET LEU GLY
SEQRES 37 C 513 VAL GLU ALA VAL ASP ASN ILE VAL ASN GLY ALA VAL GLU
SEQRES 38 C 513 LEU THR LEU ASN TYR PRO ASP PHE VAL ASN GLY ARG GLN
SEQRES 39 C 513 ASN THR GLU ARG ARG LEU VAL ASP GLY ALA GLN VAL PHE
SEQRES 40 C 513 ALA LYS SER LYS ALA GLN
SEQRES 1 D 513 ALA ILE ALA MET THR HIS PRO ASP ILE SER VAL ASP VAL
SEQRES 2 D 513 LEU VAL ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA
SEQRES 3 D 513 LYS ARG LEU ASN GLN ILE ASP GLY PRO SER TRP MET ILE
SEQRES 4 D 513 VAL ASP SER ASN GLU THR PRO GLY GLY LEU ALA SER THR
SEQRES 5 D 513 ASP VAL THR PRO GLU GLY PHE LEU TYR ASP VAL GLY GLY
SEQRES 6 D 513 HIS VAL ILE ALA SER HIS TYR LYS TYR PHE ASP ASP CYS
SEQRES 7 D 513 LEU ASP GLU ALA LEU PRO LYS GLU ASP ASP TRP TYR THR
SEQRES 8 D 513 HIS GLN ARG ILE SER TYR VAL ARG CYS GLN GLY GLN TRP
SEQRES 9 D 513 VAL PRO TYR PRO PHE GLN ASN ASN ILE SER MET LEU PRO
SEQRES 10 D 513 LYS GLU GLU GLN VAL LYS CYS ILE ASP GLY MET ILE ASP
SEQRES 11 D 513 ALA ALA LEU GLU ALA ARG VAL ALA ASN THR LYS PRO LYS
SEQRES 12 D 513 THR PHE ASP GLU TRP ILE VAL ARG MET MET GLY THR GLY
SEQRES 13 D 513 ILE ALA ASP LEU PHE MET ARG PRO TYR ASN PHE LYS VAL
SEQRES 14 D 513 TRP ALA VAL PRO THR THR LYS MET GLN CYS ALA TRP LEU
SEQRES 15 D 513 GLY GLU ARG VAL ALA ALA PRO ASN LEU LYS ALA VAL THR
SEQRES 16 D 513 THR ASN VAL ILE LEU GLY LYS THR ALA GLY ASN TRP GLY
SEQRES 17 D 513 PRO ASN ALA THR PHE ARG PHE PRO ALA ARG GLY GLY THR
SEQRES 18 D 513 GLY GLY ILE TRP ILE ALA VAL ALA ASN THR LEU PRO LYS
SEQRES 19 D 513 GLU LYS THR ARG PHE GLY GLU LYS GLY LYS VAL THR LYS
SEQRES 20 D 513 VAL ASN ALA ASN ASN LYS THR VAL THR LEU GLN ASP GLY
SEQRES 21 D 513 THR THR ILE GLY TYR LYS LYS LEU VAL SER THR MET ALA
SEQRES 22 D 513 VAL ASP PHE LEU ALA GLU ALA MET ASN ASP GLN GLU LEU
SEQRES 23 D 513 VAL GLY LEU THR LYS GLN LEU PHE TYR SER SER THR HIS
SEQRES 24 D 513 VAL ILE GLY VAL GLY VAL ARG GLY SER ARG PRO GLU ARG
SEQRES 25 D 513 ILE GLY ASP LYS CYS TRP LEU TYR PHE PRO GLU ASP ASN
SEQRES 26 D 513 CYS PRO PHE TYR ARG ALA THR ILE PHE SER ASN TYR SER
SEQRES 27 D 513 PRO TYR ASN GLN PRO GLU ALA SER ALA ALA LEU PRO THR
SEQRES 28 D 513 MET GLN LEU ALA ASP GLY SER ARG PRO GLN SER THR GLU
SEQRES 29 D 513 ALA LYS GLU GLY PRO TYR TRP SER ILE MET LEU GLU VAL
SEQRES 30 D 513 SER GLU SER SER MET LYS PRO VAL ASN GLN GLU THR ILE
SEQRES 31 D 513 LEU ALA ASP CYS ILE GLN GLY LEU VAL ASN THR GLU MET
SEQRES 32 D 513 LEU LYS PRO THR ASP GLU ILE VAL SER THR TYR HIS ARG
SEQRES 33 D 513 ARG PHE ASP HIS GLY TYR PRO THR PRO THR LEU GLU ARG
SEQRES 34 D 513 GLU GLY THR LEU THR GLN ILE LEU PRO LYS LEU GLN ASP
SEQRES 35 D 513 LYS ASP ILE TRP SER ARG GLY ARG PHE GLY SER TRP ARG
SEQRES 36 D 513 TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET LEU GLY
SEQRES 37 D 513 VAL GLU ALA VAL ASP ASN ILE VAL ASN GLY ALA VAL GLU
SEQRES 38 D 513 LEU THR LEU ASN TYR PRO ASP PHE VAL ASN GLY ARG GLN
SEQRES 39 D 513 ASN THR GLU ARG ARG LEU VAL ASP GLY ALA GLN VAL PHE
SEQRES 40 D 513 ALA LYS SER LYS ALA GLN
HET FDA A 601 53
HET EDO A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET SO4 A 607 5
HET SO4 A 608 5
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET SO4 A 613 5
HET SO4 A 614 5
HET FDA B 601 53
HET EDO B 602 4
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HET EDO B 607 4
HET EDO B 608 4
HET EDO B 609 4
HET EDO B 610 4
HET EDO B 611 4
HET EDO B 612 4
HET EDO B 613 4
HET SO4 B 614 5
HET SO4 B 615 5
HET SO4 B 616 5
HET SO4 B 617 5
HET SO4 B 618 5
HET SO4 B 619 5
HET SO4 B 620 5
HET FDA C 601 53
HET EDO C 602 4
HET EDO C 603 4
HET EDO C 604 4
HET EDO C 605 4
HET EDO C 606 4
HET EDO C 607 4
HET SO4 C 608 5
HET SO4 C 609 5
HET SO4 C 610 5
HET SO4 C 611 5
HET SO4 C 612 5
HET SO4 C 613 5
HET SO4 C 614 5
HET FDA D 601 53
HET EDO D 602 4
HET EDO D 603 4
HET EDO D 604 4
HET EDO D 605 4
HET SO4 D 606 5
HET SO4 D 607 5
HET SO4 D 608 5
HET SO4 D 609 5
HET SO4 D 610 5
HETNAM FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 FDA 4(C27 H35 N9 O15 P2)
FORMUL 6 EDO 27(C2 H6 O2)
FORMUL 11 SO4 27(O4 S 2-)
FORMUL 63 HOH *1014(H2 O)
HELIX 1 AA1 GLY A 16 ASP A 30 1 15
HELIX 2 AA2 GLY A 44 ALA A 47 5 4
HELIX 3 AA3 TYR A 69 LEU A 80 1 12
HELIX 4 AA4 LYS A 82 ASP A 84 5 3
HELIX 5 AA5 PRO A 105 LEU A 113 5 9
HELIX 6 AA6 PRO A 114 ALA A 135 1 22
HELIX 7 AA7 THR A 141 PHE A 158 1 18
HELIX 8 AA8 PHE A 158 ALA A 168 1 11
HELIX 9 AA9 PRO A 170 MET A 174 5 5
HELIX 10 AB1 CYS A 176 GLY A 180 5 5
HELIX 11 AB2 ASN A 187 GLY A 198 1 12
HELIX 12 AB3 THR A 218 THR A 228 1 11
HELIX 13 AB4 LEU A 229 GLU A 232 5 4
HELIX 14 AB5 GLU A 238 GLY A 240 5 3
HELIX 15 AB6 ALA A 270 ASN A 279 1 10
HELIX 16 AB7 ASP A 280 GLN A 289 1 10
HELIX 17 AB8 SER A 332 TYR A 334 5 3
HELIX 18 AB9 SER A 335 GLN A 339 5 5
HELIX 19 AC1 THR A 386 THR A 398 1 13
HELIX 20 AC2 GLU A 425 LYS A 440 1 16
HELIX 21 AC3 ARG A 452 GLY A 456 5 5
HELIX 22 AC4 ASN A 457 GLY A 475 1 19
HELIX 23 AC5 GLU A 478 TYR A 483 1 6
HELIX 24 AC6 TYR A 483 GLY A 489 1 7
HELIX 25 AC7 ASP A 499 SER A 507 1 9
HELIX 26 AC8 GLY B 16 ASP B 30 1 15
HELIX 27 AC9 GLY B 44 ALA B 47 5 4
HELIX 28 AD1 TYR B 69 LEU B 80 1 12
HELIX 29 AD2 LYS B 82 ASP B 84 5 3
HELIX 30 AD3 PRO B 105 LEU B 113 5 9
HELIX 31 AD4 PRO B 114 ALA B 135 1 22
HELIX 32 AD5 THR B 141 PHE B 158 1 18
HELIX 33 AD6 PHE B 158 ALA B 168 1 11
HELIX 34 AD7 PRO B 170 MET B 174 5 5
HELIX 35 AD8 CYS B 176 GLY B 180 5 5
HELIX 36 AD9 ASN B 187 GLY B 198 1 12
HELIX 37 AE1 THR B 218 ASN B 227 1 10
HELIX 38 AE2 THR B 228 LEU B 229 5 2
HELIX 39 AE3 PRO B 230 GLU B 232 5 3
HELIX 40 AE4 GLU B 238 GLY B 240 5 3
HELIX 41 AE5 ALA B 270 MET B 278 1 9
HELIX 42 AE6 ASP B 280 GLN B 289 1 10
HELIX 43 AE7 PHE B 331 TYR B 334 5 4
HELIX 44 AE8 SER B 335 GLN B 339 5 5
HELIX 45 AE9 THR B 386 THR B 398 1 13
HELIX 46 AF1 GLU B 425 ASP B 439 1 15
HELIX 47 AF2 ARG B 452 GLY B 456 5 5
HELIX 48 AF3 ASN B 457 GLY B 475 1 19
HELIX 49 AF4 GLU B 478 TYR B 483 1 6
HELIX 50 AF5 TYR B 483 GLY B 489 1 7
HELIX 51 AF6 ASP B 499 SER B 507 1 9
HELIX 52 AF7 GLY C 16 ASP C 30 1 15
HELIX 53 AF8 GLY C 44 ALA C 47 5 4
HELIX 54 AF9 TYR C 69 LEU C 80 1 12
HELIX 55 AG1 LYS C 82 ASP C 84 5 3
HELIX 56 AG2 PRO C 105 LEU C 113 5 9
HELIX 57 AG3 PRO C 114 ALA C 135 1 22
HELIX 58 AG4 THR C 141 GLY C 151 1 11
HELIX 59 AG5 GLY C 151 PHE C 158 1 8
HELIX 60 AG6 PHE C 158 ALA C 168 1 11
HELIX 61 AG7 PRO C 170 MET C 174 5 5
HELIX 62 AG8 CYS C 176 GLY C 180 5 5
HELIX 63 AG9 ASN C 187 GLY C 198 1 12
HELIX 64 AH1 GLY C 217 THR C 228 1 12
HELIX 65 AH2 LEU C 229 GLU C 232 5 4
HELIX 66 AH3 GLU C 238 GLY C 240 5 3
HELIX 67 AH4 ALA C 270 MET C 278 1 9
HELIX 68 AH5 ASP C 280 LYS C 288 1 9
HELIX 69 AH6 SER C 332 TYR C 334 5 3
HELIX 70 AH7 SER C 335 GLN C 339 5 5
HELIX 71 AH8 THR C 386 THR C 398 1 13
HELIX 72 AH9 GLU C 425 ASP C 439 1 15
HELIX 73 AI1 ARG C 452 GLY C 456 5 5
HELIX 74 AI2 ASN C 457 GLY C 475 1 19
HELIX 75 AI3 GLU C 478 TYR C 483 1 6
HELIX 76 AI4 TYR C 483 GLY C 489 1 7
HELIX 77 AI5 ASP C 499 SER C 507 1 9
HELIX 78 AI6 GLY D 16 ASP D 30 1 15
HELIX 79 AI7 GLY D 44 ALA D 47 5 4
HELIX 80 AI8 TYR D 69 LEU D 80 1 12
HELIX 81 AI9 LYS D 82 ASP D 84 5 3
HELIX 82 AJ1 PRO D 105 LEU D 113 5 9
HELIX 83 AJ2 PRO D 114 VAL D 134 1 21
HELIX 84 AJ3 THR D 141 GLY D 151 1 11
HELIX 85 AJ4 GLY D 151 PHE D 158 1 8
HELIX 86 AJ5 PHE D 158 ALA D 168 1 11
HELIX 87 AJ6 PRO D 170 MET D 174 5 5
HELIX 88 AJ7 CYS D 176 GLY D 180 5 5
HELIX 89 AJ8 ASN D 187 GLY D 198 1 12
HELIX 90 AJ9 GLY D 217 ASN D 227 1 11
HELIX 91 AK1 THR D 228 LEU D 229 5 2
HELIX 92 AK2 PRO D 230 GLU D 232 5 3
HELIX 93 AK3 GLU D 238 GLY D 240 5 3
HELIX 94 AK4 ALA D 270 MET D 278 1 9
HELIX 95 AK5 ASP D 280 GLN D 289 1 10
HELIX 96 AK6 PHE D 331 TYR D 334 5 4
HELIX 97 AK7 THR D 386 THR D 398 1 13
HELIX 98 AK8 GLU D 425 ASP D 439 1 15
HELIX 99 AK9 ARG D 452 GLY D 456 5 5
HELIX 100 AL1 ASN D 457 GLY D 475 1 19
HELIX 101 AL2 GLU D 478 TYR D 483 1 6
HELIX 102 AL3 TYR D 483 GLY D 489 1 7
HELIX 103 AL4 ASP D 499 SER D 507 1 9
SHEET 1 AA1 4 ILE A 6 SER A 7 0
SHEET 2 AA1 4 THR A 259 GLY A 261 1 O GLY A 261 N ILE A 6
SHEET 3 AA1 4 THR A 251 LEU A 254 -1 N VAL A 252 O ILE A 260
SHEET 4 AA1 4 VAL A 242 ASN A 246 -1 N ASN A 246 O THR A 251
SHEET 1 AA2 5 THR A 234 PHE A 236 0
SHEET 2 AA2 5 TRP A 34 ASP A 38 1 N ASP A 38 O ARG A 235
SHEET 3 AA2 5 VAL A 10 ILE A 13 1 N VAL A 12 O MET A 35
SHEET 4 AA2 5 LYS A 264 SER A 267 1 O VAL A 266 N LEU A 11
SHEET 5 AA2 5 ILE A 442 SER A 444 1 O TRP A 443 N LEU A 265
SHEET 1 AA3 2 THR A 49 VAL A 51 0
SHEET 2 AA3 2 LEU A 57 ASP A 59 -1 O TYR A 58 N ASP A 50
SHEET 1 AA4 2 TRP A 86 GLN A 90 0
SHEET 2 AA4 2 THR A 209 PRO A 213 -1 O PHE A 212 N TYR A 87
SHEET 1 AA5 8 GLN A 100 PRO A 103 0
SHEET 2 AA5 8 SER A 93 CYS A 97 -1 N VAL A 95 O VAL A 102
SHEET 3 AA5 8 TRP A 315 TYR A 317 1 O TYR A 317 N ARG A 96
SHEET 4 AA5 8 ARG A 327 ILE A 330 -1 O ALA A 328 N LEU A 316
SHEET 5 AA5 8 TYR A 367 GLU A 376 -1 O MET A 371 N THR A 329
SHEET 6 AA5 8 TYR A 292 ARG A 303 -1 N ILE A 298 O LEU A 372
SHEET 7 AA5 8 GLU A 406 PRO A 420 -1 O PHE A 415 N THR A 295
SHEET 8 AA5 8 GLN A 350 LEU A 351 -1 N GLN A 350 O ILE A 407
SHEET 1 AA6 6 THR B 234 PHE B 236 0
SHEET 2 AA6 6 TRP B 34 ASP B 38 1 N ASP B 38 O ARG B 235
SHEET 3 AA6 6 ILE B 6 ILE B 13 1 N VAL B 12 O MET B 35
SHEET 4 AA6 6 THR B 259 SER B 267 1 O GLY B 261 N ILE B 6
SHEET 5 AA6 6 THR B 251 LEU B 254 -1 N VAL B 252 O ILE B 260
SHEET 6 AA6 6 VAL B 242 ASN B 246 -1 N ASN B 246 O THR B 251
SHEET 1 AA7 5 THR B 234 PHE B 236 0
SHEET 2 AA7 5 TRP B 34 ASP B 38 1 N ASP B 38 O ARG B 235
SHEET 3 AA7 5 ILE B 6 ILE B 13 1 N VAL B 12 O MET B 35
SHEET 4 AA7 5 THR B 259 SER B 267 1 O GLY B 261 N ILE B 6
SHEET 5 AA7 5 ILE B 442 SER B 444 1 O TRP B 443 N LEU B 265
SHEET 1 AA8 2 THR B 49 VAL B 51 0
SHEET 2 AA8 2 LEU B 57 ASP B 59 -1 O TYR B 58 N ASP B 50
SHEET 1 AA9 2 TRP B 86 GLN B 90 0
SHEET 2 AA9 2 THR B 209 PRO B 213 -1 O PHE B 212 N TYR B 87
SHEET 1 AB1 8 GLN B 100 PRO B 103 0
SHEET 2 AB1 8 SER B 93 CYS B 97 -1 N VAL B 95 O VAL B 102
SHEET 3 AB1 8 TRP B 315 TYR B 317 1 O TYR B 317 N ARG B 96
SHEET 4 AB1 8 ARG B 327 THR B 329 -1 O ALA B 328 N LEU B 316
SHEET 5 AB1 8 TYR B 367 GLU B 376 -1 O MET B 371 N THR B 329
SHEET 6 AB1 8 TYR B 292 ARG B 303 -1 N ILE B 298 O LEU B 372
SHEET 7 AB1 8 GLU B 406 PRO B 420 -1 O PHE B 415 N THR B 295
SHEET 8 AB1 8 GLN B 350 LEU B 351 -1 N GLN B 350 O ILE B 407
SHEET 1 AB2 2 LEU B 346 PRO B 347 0
SHEET 2 AB2 2 ALA B 362 LYS B 363 -1 O LYS B 363 N LEU B 346
SHEET 1 AB3 6 THR C 234 PHE C 236 0
SHEET 2 AB3 6 TRP C 34 ASP C 38 1 N ILE C 36 O ARG C 235
SHEET 3 AB3 6 ILE C 6 ILE C 13 1 N VAL C 12 O MET C 35
SHEET 4 AB3 6 THR C 259 SER C 267 1 O GLY C 261 N ILE C 6
SHEET 5 AB3 6 THR C 251 LEU C 254 -1 N VAL C 252 O ILE C 260
SHEET 6 AB3 6 VAL C 242 ASN C 246 -1 N ASN C 246 O THR C 251
SHEET 1 AB4 5 THR C 234 PHE C 236 0
SHEET 2 AB4 5 TRP C 34 ASP C 38 1 N ILE C 36 O ARG C 235
SHEET 3 AB4 5 ILE C 6 ILE C 13 1 N VAL C 12 O MET C 35
SHEET 4 AB4 5 THR C 259 SER C 267 1 O GLY C 261 N ILE C 6
SHEET 5 AB4 5 ILE C 442 SER C 444 1 O TRP C 443 N LEU C 265
SHEET 1 AB5 2 THR C 49 VAL C 51 0
SHEET 2 AB5 2 LEU C 57 ASP C 59 -1 O TYR C 58 N ASP C 50
SHEET 1 AB6 2 TRP C 86 GLN C 90 0
SHEET 2 AB6 2 THR C 209 PRO C 213 -1 O PHE C 212 N TYR C 87
SHEET 1 AB7 8 GLN C 100 PRO C 103 0
SHEET 2 AB7 8 SER C 93 CYS C 97 -1 N VAL C 95 O VAL C 102
SHEET 3 AB7 8 TRP C 315 TYR C 317 1 O TYR C 317 N ARG C 96
SHEET 4 AB7 8 ARG C 327 ILE C 330 -1 O ALA C 328 N LEU C 316
SHEET 5 AB7 8 TYR C 367 GLU C 376 -1 O MET C 371 N THR C 329
SHEET 6 AB7 8 TYR C 292 ARG C 303 -1 N ILE C 298 O LEU C 372
SHEET 7 AB7 8 GLU C 406 PRO C 420 -1 O VAL C 408 N GLY C 301
SHEET 8 AB7 8 GLN C 350 LEU C 351 -1 N GLN C 350 O ILE C 407
SHEET 1 AB8 4 ILE D 6 SER D 7 0
SHEET 2 AB8 4 THR D 259 GLY D 261 1 O GLY D 261 N ILE D 6
SHEET 3 AB8 4 THR D 251 LEU D 254 -1 N VAL D 252 O ILE D 260
SHEET 4 AB8 4 VAL D 242 ASN D 246 -1 N LYS D 244 O THR D 253
SHEET 1 AB9 5 THR D 234 PHE D 236 0
SHEET 2 AB9 5 TRP D 34 ASP D 38 1 N ASP D 38 O ARG D 235
SHEET 3 AB9 5 VAL D 10 ILE D 13 1 N VAL D 12 O MET D 35
SHEET 4 AB9 5 LYS D 264 SER D 267 1 O VAL D 266 N LEU D 11
SHEET 5 AB9 5 ILE D 442 SER D 444 1 O TRP D 443 N LEU D 265
SHEET 1 AC1 2 THR D 49 VAL D 51 0
SHEET 2 AC1 2 LEU D 57 ASP D 59 -1 O TYR D 58 N ASP D 50
SHEET 1 AC2 2 TRP D 86 GLN D 90 0
SHEET 2 AC2 2 THR D 209 PRO D 213 -1 O PHE D 210 N HIS D 89
SHEET 1 AC3 8 GLN D 100 PRO D 103 0
SHEET 2 AC3 8 SER D 93 CYS D 97 -1 N VAL D 95 O VAL D 102
SHEET 3 AC3 8 TRP D 315 TYR D 317 1 O TYR D 317 N ARG D 96
SHEET 4 AC3 8 ARG D 327 THR D 329 -1 O ALA D 328 N LEU D 316
SHEET 5 AC3 8 TYR D 367 GLU D 376 -1 O MET D 371 N THR D 329
SHEET 6 AC3 8 TYR D 292 ARG D 303 -1 N ILE D 298 O LEU D 372
SHEET 7 AC3 8 GLU D 406 PRO D 420 -1 O GLU D 406 N ARG D 303
SHEET 8 AC3 8 GLN D 350 LEU D 351 -1 N GLN D 350 O ILE D 407
CISPEP 1 TYR A 104 PRO A 105 0 3.05
CISPEP 2 GLY A 365 PRO A 366 0 4.17
CISPEP 3 TYR B 104 PRO B 105 0 -0.23
CISPEP 4 GLY B 365 PRO B 366 0 2.97
CISPEP 5 TYR C 104 PRO C 105 0 2.20
CISPEP 6 GLY C 365 PRO C 366 0 3.22
CISPEP 7 TYR D 104 PRO D 105 0 5.10
CISPEP 8 GLY D 365 PRO D 366 0 1.49
SITE 1 AC1 31 GLY A 14 GLY A 16 PRO A 17 THR A 18
SITE 2 AC1 31 ASP A 38 SER A 39 GLY A 44 GLY A 45
SITE 3 AC1 31 LEU A 46 ALA A 47 VAL A 60 GLY A 62
SITE 4 AC1 31 HIS A 63 VAL A 64 GLY A 240 VAL A 242
SITE 5 AC1 31 THR A 295 GLU A 373 GLY A 418 GLY A 446
SITE 6 AC1 31 ARG A 447 GLY A 456 ASN A 457 GLN A 458
SITE 7 AC1 31 SER A 461 HOH A 719 HOH A 729 HOH A 738
SITE 8 AC1 31 HOH A 770 HOH A 798 HOH A 942
SITE 1 AC2 3 ASN A 471 GLU C 494 HOH C 831
SITE 1 AC3 6 TRP A 178 LEU A 179 GLY A 180 PRO A 484
SITE 2 AC3 6 ASP A 485 ASN A 488
SITE 1 AC4 4 ARG A 452 ASN A 482 PRO A 484 HOH A 845
SITE 1 AC5 4 LYS A 115 GLU A 116 ASP A 390 HOH A 704
SITE 1 AC6 4 ARG A 306 ASP A 312 HOH A 873 HOH A 914
SITE 1 AC7 5 PRO A 307 GLU A 308 ARG A 309 LYS A 402
SITE 2 AC7 5 HOH A 726
SITE 1 AC8 2 ASN A 40 ARG A 413
SITE 1 AC9 2 LYS A 70 ARG A 496
SITE 1 AD1 3 TRP A 86 TYR A 87 THR A 88
SITE 1 AD2 3 THR A 152 ARG A 160 HOH A 787
SITE 1 AD3 6 ARG A 91 TYR A 104 ASN A 203 HOH A 788
SITE 2 AD3 6 HOH A 793 HOH A 903
SITE 1 AD4 2 LYS A 82 GLU A 83
SITE 1 AD5 2 THR A 137 LYS A 138
SITE 1 AD6 31 GLY B 14 GLY B 16 PRO B 17 THR B 18
SITE 2 AD6 31 ASP B 38 SER B 39 GLY B 45 LEU B 46
SITE 3 AD6 31 ALA B 47 VAL B 60 GLY B 62 HIS B 63
SITE 4 AD6 31 VAL B 64 GLY B 240 VAL B 242 MET B 269
SITE 5 AD6 31 GLU B 373 GLY B 418 GLY B 446 ARG B 447
SITE 6 AD6 31 GLY B 456 ASN B 457 GLN B 458 SER B 461
SITE 7 AD6 31 EDO B 605 HOH B 762 HOH B 775 HOH B 783
SITE 8 AD6 31 HOH B 785 HOH B 816 HOH B 842
SITE 1 AD7 5 ASN B 322 CYS B 323 ASP B 390 EDO B 607
SITE 2 AD7 5 HOH B 709
SITE 1 AD8 5 GLU B 494 HOH B 861 HOH B 907 TRP D 443
SITE 2 AD8 5 ASN D 471
SITE 1 AD9 3 TRP B 443 ASN B 471 GLU D 494
SITE 1 AE1 5 GLY B 62 TRP B 315 ARG B 327 FDA B 601
SITE 2 AE1 5 HOH B 741
SITE 1 AE2 9 GLN B 98 GLU B 116 GLU B 117 ASP B 321
SITE 2 AE2 9 CYS B 323 PRO B 324 EDO B 607 HOH B 714
SITE 3 AE2 9 HOH B 726
SITE 1 AE3 7 PRO B 114 GLU B 116 PRO B 324 ASP B 390
SITE 2 AE3 7 EDO B 602 EDO B 606 HOH B 718
SITE 1 AE4 3 GLU B 117 LYS B 120 HOH B 714
SITE 1 AE5 6 GLU B 427 ARG B 452 LEU B 481 ASN B 482
SITE 2 AE5 6 PRO B 484 HOH B 935
SITE 1 AE6 2 LYS B 189 ASP C 123
SITE 1 AE7 5 GLN B 107 MET B 125 MET B 149 ASN B 187
SITE 2 AE7 5 HOH B 803
SITE 1 AE8 3 GLY B 202 TRP B 204 HOH B 996
SITE 1 AE9 5 ARG B 96 ASN B 397 GLU B 399 HOH B 716
SITE 2 AE9 5 HOH B 771
SITE 1 AF1 5 PRO B 307 GLU B 308 ARG B 309 LYS B 402
SITE 2 AF1 5 HOH B 780
SITE 1 AF2 6 PRO B 114 LYS B 115 ASN B 383 THR B 386
SITE 2 AF2 6 ASP B 390 HOH B 702
SITE 1 AF3 3 ASN B 40 ASP B 50 ARG B 413
SITE 1 AF4 3 TYR B 87 THR B 88 HOH B 849
SITE 1 AF5 2 LYS B 70 ARG B 496
SITE 1 AF6 2 THR B 152 ARG B 160
SITE 1 AF7 6 ARG B 91 TYR B 104 ASN B 203 HOH B 815
SITE 2 AF7 6 HOH B 828 HOH B 851
SITE 1 AF8 32 GLY C 14 GLY C 16 PRO C 17 THR C 18
SITE 2 AF8 32 ASP C 38 SER C 39 GLY C 45 LEU C 46
SITE 3 AF8 32 ALA C 47 VAL C 60 GLY C 62 HIS C 63
SITE 4 AF8 32 VAL C 64 GLY C 240 VAL C 242 MET C 269
SITE 5 AF8 32 GLU C 373 GLY C 418 TYR C 419 GLY C 446
SITE 6 AF8 32 ARG C 447 GLY C 456 ASN C 457 GLN C 458
SITE 7 AF8 32 SER C 461 EDO C 603 HOH C 746 HOH C 754
SITE 8 AF8 32 HOH C 792 HOH C 813 HOH C 820 HOH C 912
SITE 1 AF9 2 GLU A 494 ASN C 471
SITE 1 AG1 4 VAL C 64 ALA C 66 ARG C 91 FDA C 601
SITE 1 AG2 5 TRP C 178 GLY C 180 PRO C 484 ASP C 485
SITE 2 AG2 5 ASN C 488
SITE 1 AG3 6 GLN C 107 MET C 149 ALA C 185 PRO C 186
SITE 2 AG3 6 ASN C 187 HOH C 882
SITE 1 AG4 3 ALA C 201 GLY C 202 TRP C 204
SITE 1 AG5 3 ARG C 306 ASP C 312 HOH C 772
SITE 1 AG6 5 PRO C 307 GLU C 308 ARG C 309 LYS C 402
SITE 2 AG6 5 HOH C 837
SITE 1 AG7 3 VAL C 147 THR C 152 ARG C 160
SITE 1 AG8 3 ASN B 248 LYS C 70 ARG C 496
SITE 1 AG9 3 ASN C 40 ASP C 50 ARG C 413
SITE 1 AH1 2 PRO C 114 LYS C 115
SITE 1 AH2 5 ARG C 91 TYR C 104 ASN C 203 HOH C 763
SITE 2 AH2 5 HOH C 765
SITE 1 AH3 3 TRP C 86 TYR C 87 THR C 88
SITE 1 AH4 30 GLY D 14 GLY D 16 PRO D 17 THR D 18
SITE 2 AH4 30 ASP D 38 SER D 39 GLY D 45 LEU D 46
SITE 3 AH4 30 ALA D 47 VAL D 60 GLY D 62 HIS D 63
SITE 4 AH4 30 VAL D 64 GLY D 240 VAL D 242 MET D 269
SITE 5 AH4 30 GLU D 373 GLY D 418 GLY D 446 ARG D 447
SITE 6 AH4 30 GLY D 456 ASN D 457 GLN D 458 SER D 461
SITE 7 AH4 30 HOH D 749 HOH D 751 HOH D 775 HOH D 780
SITE 8 AH4 30 HOH D 794 HOH D 829
SITE 1 AH5 5 TRP D 178 LEU D 179 PRO D 484 ASP D 485
SITE 2 AH5 5 ASN D 488
SITE 1 AH6 3 MET D 149 ALA D 185 ASN D 187
SITE 1 AH7 4 HOH B 750 GLN D 438 ASN D 471 GLU D 478
SITE 1 AH8 3 ARG D 452 ASN D 482 HOH D 798
SITE 1 AH9 5 PRO D 307 GLU D 308 ARG D 309 LYS D 402
SITE 2 AH9 5 HOH D 917
SITE 1 AI1 6 VAL A 382 ASN A 383 GLN A 384 GLU A 385
SITE 2 AI1 6 LYS D 199 THR D 200
SITE 1 AI2 4 PRO D 114 LYS D 115 HOH D 827 HOH D 887
SITE 1 AI3 2 THR D 152 ARG D 160
SITE 1 AI4 2 ASN D 40 ARG D 413
CRYST1 217.126 217.126 320.348 90.00 90.00 120.00 P 65 2 2 48
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 0.004606 0.002659 0.000000 0.00000
SCALE2 0.000000 0.005318 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
