HEADER OXIDOREDUCTASE 30-MAY-14 4TM3
TITLE KUTZNERIA SP. 744 ORNITHINE N-HYDROXYLASE, KTZI-FADOX-BR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KTZI;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PEPTIDE MONOOXYGENASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KUTZNERIA SP. 744;
SOURCE 3 ORGANISM_TAXID: 345341;
SOURCE 4 GENE: KTZI, KUTG_08917;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROXYLASE, FLAVIN, ORNITHINE, MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SETSER,C.L.DRENNAN
REVDAT 3 27-SEP-23 4TM3 1 SOURCE KEYWDS JRNL REMARK
REVDAT 2 10-DEC-14 4TM3 1 JRNL
REVDAT 1 17-SEP-14 4TM3 0
JRNL AUTH J.W.SETSER,J.R.HEEMSTRA,C.T.WALSH,C.L.DRENNAN
JRNL TITL CRYSTALLOGRAPHIC EVIDENCE OF DRASTIC CONFORMATIONAL CHANGES
JRNL TITL 2 IN THE ACTIVE SITE OF A FLAVIN-DEPENDENT N-HYDROXYLASE.
JRNL REF BIOCHEMISTRY V. 53 6063 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 25184411
JRNL DOI 10.1021/BI500655Q
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 116327
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5814
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 45.5171 - 6.4852 0.99 3955 211 0.1674 0.1836
REMARK 3 2 6.4852 - 5.1498 0.99 3791 192 0.1834 0.2209
REMARK 3 3 5.1498 - 4.4995 0.99 3759 190 0.1525 0.1828
REMARK 3 4 4.4995 - 4.0884 1.00 3745 203 0.1543 0.1806
REMARK 3 5 4.0884 - 3.7955 1.00 3711 198 0.1760 0.1712
REMARK 3 6 3.7955 - 3.5718 0.99 3721 196 0.1906 0.2328
REMARK 3 7 3.5718 - 3.3930 0.99 3678 201 0.2027 0.2257
REMARK 3 8 3.3930 - 3.2453 1.00 3688 199 0.2121 0.2303
REMARK 3 9 3.2453 - 3.1204 1.00 3687 216 0.2309 0.2408
REMARK 3 10 3.1204 - 3.0128 1.00 3695 201 0.2463 0.2831
REMARK 3 11 3.0128 - 2.9186 1.00 3711 197 0.2422 0.2607
REMARK 3 12 2.9186 - 2.8352 1.00 3673 200 0.2346 0.3062
REMARK 3 13 2.8352 - 2.7606 0.99 3653 201 0.2380 0.2826
REMARK 3 14 2.7606 - 2.6932 1.00 3691 189 0.2523 0.2766
REMARK 3 15 2.6932 - 2.6320 0.99 3675 184 0.2368 0.2868
REMARK 3 16 2.6320 - 2.5760 1.00 3617 187 0.2397 0.2779
REMARK 3 17 2.5760 - 2.5245 1.00 3721 188 0.2400 0.2968
REMARK 3 18 2.5245 - 2.4768 1.00 3667 198 0.2431 0.3079
REMARK 3 19 2.4768 - 2.4326 1.00 3664 202 0.2367 0.3033
REMARK 3 20 2.4326 - 2.3914 1.00 3681 196 0.2375 0.2513
REMARK 3 21 2.3914 - 2.3528 1.00 3645 191 0.2357 0.3106
REMARK 3 22 2.3528 - 2.3166 1.00 3656 199 0.2415 0.2733
REMARK 3 23 2.3166 - 2.2825 0.99 3648 183 0.2325 0.2768
REMARK 3 24 2.2825 - 2.2504 0.99 3657 186 0.2536 0.3017
REMARK 3 25 2.2504 - 2.2200 0.98 3611 172 0.2638 0.3222
REMARK 3 26 2.2200 - 2.1911 1.00 3705 195 0.2348 0.2766
REMARK 3 27 2.1911 - 2.1637 1.00 3615 190 0.2458 0.2795
REMARK 3 28 2.1637 - 2.1377 1.00 3697 177 0.2480 0.2948
REMARK 3 29 2.1377 - 2.1128 1.00 3654 193 0.2514 0.2787
REMARK 3 30 2.1128 - 2.0900 0.94 3442 179 0.2599 0.3090
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 13282
REMARK 3 ANGLE : 1.657 18150
REMARK 3 CHIRALITY : 0.270 2008
REMARK 3 PLANARITY : 0.006 2372
REMARK 3 DIHEDRAL : 13.684 4610
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 4TM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201849.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: 3S5W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9-1.2 M SODIUM BROMIDE, 22-25% PEG
REMARK 280 3350, 0.1 M BIS-TRIS PROPANE PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 39.90700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.93500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.97150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.93500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.90700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.97150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 28890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 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 MET A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 HIS A 1
REMARK 465 MET A 2
REMARK 465 VAL A 3
REMARK 465 ALA A 4
REMARK 465 HIS A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 GLU A 8
REMARK 465 SER A 9
REMARK 465 SER A 424
REMARK 465 MET B -18
REMARK 465 GLY B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 SER B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 LEU B -5
REMARK 465 VAL B -4
REMARK 465 PRO B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 HIS B 1
REMARK 465 MET B 2
REMARK 465 VAL B 3
REMARK 465 ALA B 4
REMARK 465 HIS B 5
REMARK 465 ALA B 6
REMARK 465 GLY B 7
REMARK 465 GLU B 8
REMARK 465 SER B 9
REMARK 465 SER B 424
REMARK 465 MET C -18
REMARK 465 GLY C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 SER C -8
REMARK 465 SER C -7
REMARK 465 GLY C -6
REMARK 465 LEU C -5
REMARK 465 VAL C -4
REMARK 465 PRO C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 HIS C 1
REMARK 465 MET C 2
REMARK 465 VAL C 3
REMARK 465 ALA C 4
REMARK 465 HIS C 5
REMARK 465 ALA C 6
REMARK 465 GLY C 7
REMARK 465 GLU C 8
REMARK 465 SER C 9
REMARK 465 SER C 424
REMARK 465 MET D -18
REMARK 465 GLY D -17
REMARK 465 SER D -16
REMARK 465 SER D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 SER D -8
REMARK 465 SER D -7
REMARK 465 GLY D -6
REMARK 465 LEU D -5
REMARK 465 VAL D -4
REMARK 465 PRO D -3
REMARK 465 ARG D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 HIS D 1
REMARK 465 MET D 2
REMARK 465 VAL D 3
REMARK 465 ALA D 4
REMARK 465 HIS D 5
REMARK 465 ALA D 6
REMARK 465 GLY D 7
REMARK 465 GLU D 8
REMARK 465 SER D 9
REMARK 465 SER D 424
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 GLU A 121 CG CD OE1 OE2
REMARK 470 ARG A 137 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2
REMARK 470 SER A 197 OG
REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 272 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 282 CG CD OE1 OE2
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 ASP A 318 CG OD1 OD2
REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 360 CG CD OE1 OE2
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 ARG A 385 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 422 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 120 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 121 CG CD OE1 OE2
REMARK 470 ASP B 177 CG OD1 OD2
REMARK 470 ASP B 194 CG OD1 OD2
REMARK 470 ARG B 196 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 199 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 261 CG CD CE NZ
REMARK 470 GLN B 262 CG CD OE1 NE2
REMARK 470 ARG B 269 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 272 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 282 CG CD OE1 OE2
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 ASP B 318 CG OD1 OD2
REMARK 470 GLU B 357 CG CD OE1 OE2
REMARK 470 GLU B 360 CG CD OE1 OE2
REMARK 470 GLU B 420 CG CD OE1 OE2
REMARK 470 HIS C 120 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 121 CG CD OE1 OE2
REMARK 470 GLU C 150 CG CD OE1 OE2
REMARK 470 ARG C 153 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 156 CG CD OE1 OE2
REMARK 470 ARG C 158 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 175 CG CD OE1 NE2
REMARK 470 ARG C 191 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 192 CG OD1 OD2
REMARK 470 ARG C 196 CG CD NE CZ NH1 NH2
REMARK 470 SER C 197 OG
REMARK 470 ARG C 199 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 220 CG OD1 ND2
REMARK 470 ARG C 221 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 261 CG CD CE NZ
REMARK 470 GLN C 262 CG CD OE1 NE2
REMARK 470 ARG C 269 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 318 CG OD1 OD2
REMARK 470 GLU C 331 CG CD OE1 OE2
REMARK 470 GLU C 357 CG CD OE1 OE2
REMARK 470 GLU C 367 CG CD OE1 OE2
REMARK 470 ARG C 385 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 420 CG CD OE1 OE2
REMARK 470 ARG C 422 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 120 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 121 CG CD OE1 OE2
REMARK 470 GLU D 150 CG CD OE1 OE2
REMARK 470 GLN D 175 CG CD OE1 NE2
REMARK 470 ARG D 191 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 193 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 ARG D 196 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 199 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 221 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 272 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 314 CG CD CE NZ
REMARK 470 GLU D 331 CG CD OE1 OE2
REMARK 470 GLU D 357 CG CD OE1 OE2
REMARK 470 GLU D 360 CG CD OE1 OE2
REMARK 470 HIS D 361 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 367 CG CD OE1 OE2
REMARK 470 GLU D 420 CG CD OE1 OE2
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 ARG A 45 174.25 -58.22
REMARK 500 ALA A 58 -6.30 70.05
REMARK 500 ASP A 68 -149.73 -101.33
REMARK 500 ALA A 70 -21.84 -150.82
REMARK 500 ALA A 151 -156.13 -145.68
REMARK 500 ASP A 192 40.23 -88.33
REMARK 500 LEU A 198 74.15 -105.36
REMARK 500 ASN A 273 48.46 -83.54
REMARK 500 ASN A 275 -98.56 -143.97
REMARK 500 ARG A 301 -31.09 -130.59
REMARK 500 ALA A 317 -130.73 56.74
REMARK 500 ASP A 375 20.39 -78.84
REMARK 500 PRO A 382 1.50 -62.90
REMARK 500 ALA B 58 -7.20 71.95
REMARK 500 ASP B 68 -148.67 -104.44
REMARK 500 ALA B 70 -20.89 -148.18
REMARK 500 ASP B 192 41.26 -103.75
REMARK 500 ASN B 275 -101.00 -143.12
REMARK 500 ALA B 317 -124.65 52.55
REMARK 500 ASP B 365 -162.45 -101.29
REMARK 500 ALA C 58 -7.41 76.96
REMARK 500 ASP C 68 -150.07 -102.75
REMARK 500 ALA C 70 -21.29 -148.77
REMARK 500 ALA C 151 -152.26 -146.99
REMARK 500 ASP C 177 -165.24 -161.39
REMARK 500 ARG C 191 -77.62 -39.59
REMARK 500 ASP C 192 48.26 -108.61
REMARK 500 ASN C 275 -103.49 -147.20
REMARK 500 ARG C 301 -32.06 -134.32
REMARK 500 ALA C 317 -125.96 56.10
REMARK 500 ASP C 318 34.47 -95.86
REMARK 500 PRO C 382 1.02 -56.04
REMARK 500 ASP D 68 -149.83 -100.36
REMARK 500 ALA D 70 -21.39 -148.59
REMARK 500 ASP D 192 32.12 -92.56
REMARK 500 LEU D 198 68.43 -108.03
REMARK 500 ASN D 275 -99.25 -144.03
REMARK 500 ALA D 317 -127.98 58.74
REMARK 500 GLU D 360 -33.00 -35.26
REMARK 500 ASN D 407 35.33 -140.49
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 FAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR D 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TLX RELATED DB: PDB
REMARK 900 RELATED ID: 4TLZ RELATED DB: PDB
REMARK 900 RELATED ID: 4TM0 RELATED DB: PDB
REMARK 900 RELATED ID: 4TM1 RELATED DB: PDB
REMARK 900 RELATED ID: 4TM4 RELATED DB: PDB
DBREF 4TM3 A 3 424 UNP A8CF85 A8CF85_9PSEU 3 424
DBREF 4TM3 B 3 424 UNP A8CF85 A8CF85_9PSEU 3 424
DBREF 4TM3 C 3 424 UNP A8CF85 A8CF85_9PSEU 3 424
DBREF 4TM3 D 3 424 UNP A8CF85 A8CF85_9PSEU 3 424
SEQADV 4TM3 MET A -18 UNP A8CF85 INITIATING METHIONINE
SEQADV 4TM3 GLY A -17 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER A -16 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER A -15 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -14 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -13 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -12 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -11 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -10 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A -9 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER A -8 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER A -7 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY A -6 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 LEU A -5 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 VAL A -4 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 PRO A -3 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 ARG A -2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY A -1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER A 0 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS A 1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET A 2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET B -18 UNP A8CF85 INITIATING METHIONINE
SEQADV 4TM3 GLY B -17 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER B -16 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER B -15 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -14 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -13 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -12 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -11 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -10 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B -9 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER B -8 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER B -7 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY B -6 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 LEU B -5 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 VAL B -4 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 PRO B -3 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 ARG B -2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY B -1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER B 0 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS B 1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET B 2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET C -18 UNP A8CF85 INITIATING METHIONINE
SEQADV 4TM3 GLY C -17 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER C -16 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER C -15 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -14 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -13 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -12 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -11 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -10 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C -9 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER C -8 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER C -7 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY C -6 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 LEU C -5 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 VAL C -4 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 PRO C -3 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 ARG C -2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY C -1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER C 0 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS C 1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET C 2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET D -18 UNP A8CF85 INITIATING METHIONINE
SEQADV 4TM3 GLY D -17 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER D -16 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER D -15 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -14 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -13 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -12 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -11 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -10 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D -9 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER D -8 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER D -7 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY D -6 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 LEU D -5 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 VAL D -4 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 PRO D -3 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 ARG D -2 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 GLY D -1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 SER D 0 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 HIS D 1 UNP A8CF85 EXPRESSION TAG
SEQADV 4TM3 MET D 2 UNP A8CF85 EXPRESSION TAG
SEQRES 1 A 443 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 443 LEU VAL PRO ARG GLY SER HIS MET VAL ALA HIS ALA GLY
SEQRES 3 A 443 GLU SER PRO THR HIS ASP VAL VAL GLY VAL GLY PHE GLY
SEQRES 4 A 443 PRO ALA ASN LEU SER LEU ALA VAL ALA LEU GLU GLU SER
SEQRES 5 A 443 PRO ALA ALA LEU THR SER ALA PHE PHE GLU ARG ARG ALA
SEQRES 6 A 443 SER ILE SER TRP HIS GLN GLY MET LEU LEU PRO ALA ALA
SEQRES 7 A 443 LYS MET GLN VAL SER PHE LEU LYS ASP LEU ALA THR PHE
SEQRES 8 A 443 ARG ASN PRO ALA SER ARG PHE SER PHE VAL SER PHE LEU
SEQRES 9 A 443 HIS GLU ARG GLY ARG LEU VAL ARG PHE ALA ASN ASN HIS
SEQRES 10 A 443 ASP PHE PHE PRO THR ARG ARG GLU PHE HIS ASP TYR LEU
SEQRES 11 A 443 GLU TRP ALA GLU SER LYS LEU ALA HIS GLU VAL SER TYR
SEQRES 12 A 443 ASP SER GLU VAL THR ALA ILE ARG PRO GLY PRO GLY ARG
SEQRES 13 A 443 PRO VAL ASP SER VAL LEU VAL ASP VAL SER THR PRO GLU
SEQRES 14 A 443 ALA THR ARG THR VAL GLU ALA ARG ASN ILE VAL ILE SER
SEQRES 15 A 443 THR GLY LEU VAL PRO ARG MET PRO ALA GLY VAL GLN SER
SEQRES 16 A 443 ASP GLU PHE VAL TRP HIS SER SER ARG PHE LEU ASP HIS
SEQRES 17 A 443 PHE ARG ASP ARG ASP PRO ARG SER LEU ARG ARG VAL ALA
SEQRES 18 A 443 VAL ALA GLY GLY GLY GLN SER ALA ALA GLU ILE VAL ARG
SEQRES 19 A 443 PHE LEU HIS ASP ASN ARG PRO ASP THR VAL VAL HIS ALA
SEQRES 20 A 443 ILE MET PRO SER TYR GLY TYR VAL VAL ALA ASP ASN THR
SEQRES 21 A 443 PRO PHE ALA ASN GLN ILE PHE ASP PRO ALA ALA VAL ASP
SEQRES 22 A 443 ASP TYR PHE ASP GLY SER LYS GLN ALA LYS ASP ALA PHE
SEQRES 23 A 443 TRP ARG TYR HIS ARG ASN THR ASN TYR SER VAL VAL ASP
SEQRES 24 A 443 ASP GLU VAL ILE ARG ASP LEU TYR ARG ARG GLY TYR ASP
SEQRES 25 A 443 ASP GLU VAL ALA GLY ALA PRO ARG LEU ASN PHE VAL ASN
SEQRES 26 A 443 LEU ALA HIS VAL VAL GLY ALA LYS ARG ILE ALA ASP ASP
SEQRES 27 A 443 THR ARG VAL THR VAL TYR SER MET ALA ARG GLU GLU SER
SEQRES 28 A 443 TYR ASP LEU ASP VAL ASP VAL LEU VAL CYS ALA THR GLY
SEQRES 29 A 443 TYR ASP PRO MET ASP PRO GLY ASP LEU LEU GLY GLU LEU
SEQRES 30 A 443 ALA GLU HIS CYS VAL GLN ASP ALA GLU GLY ARG TRP GLN
SEQRES 31 A 443 VAL ASP ARG ASP TYR ARG MET VAL THR THR PRO ASP LEU
SEQRES 32 A 443 ARG CYS GLY ILE TYR LEU GLN GLY GLY THR GLU HIS THR
SEQRES 33 A 443 HIS GLY LEU SER SER SER LEU LEU SER ASN LEU ALA THR
SEQRES 34 A 443 ARG SER GLY GLU ILE VAL SER SER ILE GLU ARG ARG LYS
SEQRES 35 A 443 SER
SEQRES 1 B 443 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 443 LEU VAL PRO ARG GLY SER HIS MET VAL ALA HIS ALA GLY
SEQRES 3 B 443 GLU SER PRO THR HIS ASP VAL VAL GLY VAL GLY PHE GLY
SEQRES 4 B 443 PRO ALA ASN LEU SER LEU ALA VAL ALA LEU GLU GLU SER
SEQRES 5 B 443 PRO ALA ALA LEU THR SER ALA PHE PHE GLU ARG ARG ALA
SEQRES 6 B 443 SER ILE SER TRP HIS GLN GLY MET LEU LEU PRO ALA ALA
SEQRES 7 B 443 LYS MET GLN VAL SER PHE LEU LYS ASP LEU ALA THR PHE
SEQRES 8 B 443 ARG ASN PRO ALA SER ARG PHE SER PHE VAL SER PHE LEU
SEQRES 9 B 443 HIS GLU ARG GLY ARG LEU VAL ARG PHE ALA ASN ASN HIS
SEQRES 10 B 443 ASP PHE PHE PRO THR ARG ARG GLU PHE HIS ASP TYR LEU
SEQRES 11 B 443 GLU TRP ALA GLU SER LYS LEU ALA HIS GLU VAL SER TYR
SEQRES 12 B 443 ASP SER GLU VAL THR ALA ILE ARG PRO GLY PRO GLY ARG
SEQRES 13 B 443 PRO VAL ASP SER VAL LEU VAL ASP VAL SER THR PRO GLU
SEQRES 14 B 443 ALA THR ARG THR VAL GLU ALA ARG ASN ILE VAL ILE SER
SEQRES 15 B 443 THR GLY LEU VAL PRO ARG MET PRO ALA GLY VAL GLN SER
SEQRES 16 B 443 ASP GLU PHE VAL TRP HIS SER SER ARG PHE LEU ASP HIS
SEQRES 17 B 443 PHE ARG ASP ARG ASP PRO ARG SER LEU ARG ARG VAL ALA
SEQRES 18 B 443 VAL ALA GLY GLY GLY GLN SER ALA ALA GLU ILE VAL ARG
SEQRES 19 B 443 PHE LEU HIS ASP ASN ARG PRO ASP THR VAL VAL HIS ALA
SEQRES 20 B 443 ILE MET PRO SER TYR GLY TYR VAL VAL ALA ASP ASN THR
SEQRES 21 B 443 PRO PHE ALA ASN GLN ILE PHE ASP PRO ALA ALA VAL ASP
SEQRES 22 B 443 ASP TYR PHE ASP GLY SER LYS GLN ALA LYS ASP ALA PHE
SEQRES 23 B 443 TRP ARG TYR HIS ARG ASN THR ASN TYR SER VAL VAL ASP
SEQRES 24 B 443 ASP GLU VAL ILE ARG ASP LEU TYR ARG ARG GLY TYR ASP
SEQRES 25 B 443 ASP GLU VAL ALA GLY ALA PRO ARG LEU ASN PHE VAL ASN
SEQRES 26 B 443 LEU ALA HIS VAL VAL GLY ALA LYS ARG ILE ALA ASP ASP
SEQRES 27 B 443 THR ARG VAL THR VAL TYR SER MET ALA ARG GLU GLU SER
SEQRES 28 B 443 TYR ASP LEU ASP VAL ASP VAL LEU VAL CYS ALA THR GLY
SEQRES 29 B 443 TYR ASP PRO MET ASP PRO GLY ASP LEU LEU GLY GLU LEU
SEQRES 30 B 443 ALA GLU HIS CYS VAL GLN ASP ALA GLU GLY ARG TRP GLN
SEQRES 31 B 443 VAL ASP ARG ASP TYR ARG MET VAL THR THR PRO ASP LEU
SEQRES 32 B 443 ARG CYS GLY ILE TYR LEU GLN GLY GLY THR GLU HIS THR
SEQRES 33 B 443 HIS GLY LEU SER SER SER LEU LEU SER ASN LEU ALA THR
SEQRES 34 B 443 ARG SER GLY GLU ILE VAL SER SER ILE GLU ARG ARG LYS
SEQRES 35 B 443 SER
SEQRES 1 C 443 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 443 LEU VAL PRO ARG GLY SER HIS MET VAL ALA HIS ALA GLY
SEQRES 3 C 443 GLU SER PRO THR HIS ASP VAL VAL GLY VAL GLY PHE GLY
SEQRES 4 C 443 PRO ALA ASN LEU SER LEU ALA VAL ALA LEU GLU GLU SER
SEQRES 5 C 443 PRO ALA ALA LEU THR SER ALA PHE PHE GLU ARG ARG ALA
SEQRES 6 C 443 SER ILE SER TRP HIS GLN GLY MET LEU LEU PRO ALA ALA
SEQRES 7 C 443 LYS MET GLN VAL SER PHE LEU LYS ASP LEU ALA THR PHE
SEQRES 8 C 443 ARG ASN PRO ALA SER ARG PHE SER PHE VAL SER PHE LEU
SEQRES 9 C 443 HIS GLU ARG GLY ARG LEU VAL ARG PHE ALA ASN ASN HIS
SEQRES 10 C 443 ASP PHE PHE PRO THR ARG ARG GLU PHE HIS ASP TYR LEU
SEQRES 11 C 443 GLU TRP ALA GLU SER LYS LEU ALA HIS GLU VAL SER TYR
SEQRES 12 C 443 ASP SER GLU VAL THR ALA ILE ARG PRO GLY PRO GLY ARG
SEQRES 13 C 443 PRO VAL ASP SER VAL LEU VAL ASP VAL SER THR PRO GLU
SEQRES 14 C 443 ALA THR ARG THR VAL GLU ALA ARG ASN ILE VAL ILE SER
SEQRES 15 C 443 THR GLY LEU VAL PRO ARG MET PRO ALA GLY VAL GLN SER
SEQRES 16 C 443 ASP GLU PHE VAL TRP HIS SER SER ARG PHE LEU ASP HIS
SEQRES 17 C 443 PHE ARG ASP ARG ASP PRO ARG SER LEU ARG ARG VAL ALA
SEQRES 18 C 443 VAL ALA GLY GLY GLY GLN SER ALA ALA GLU ILE VAL ARG
SEQRES 19 C 443 PHE LEU HIS ASP ASN ARG PRO ASP THR VAL VAL HIS ALA
SEQRES 20 C 443 ILE MET PRO SER TYR GLY TYR VAL VAL ALA ASP ASN THR
SEQRES 21 C 443 PRO PHE ALA ASN GLN ILE PHE ASP PRO ALA ALA VAL ASP
SEQRES 22 C 443 ASP TYR PHE ASP GLY SER LYS GLN ALA LYS ASP ALA PHE
SEQRES 23 C 443 TRP ARG TYR HIS ARG ASN THR ASN TYR SER VAL VAL ASP
SEQRES 24 C 443 ASP GLU VAL ILE ARG ASP LEU TYR ARG ARG GLY TYR ASP
SEQRES 25 C 443 ASP GLU VAL ALA GLY ALA PRO ARG LEU ASN PHE VAL ASN
SEQRES 26 C 443 LEU ALA HIS VAL VAL GLY ALA LYS ARG ILE ALA ASP ASP
SEQRES 27 C 443 THR ARG VAL THR VAL TYR SER MET ALA ARG GLU GLU SER
SEQRES 28 C 443 TYR ASP LEU ASP VAL ASP VAL LEU VAL CYS ALA THR GLY
SEQRES 29 C 443 TYR ASP PRO MET ASP PRO GLY ASP LEU LEU GLY GLU LEU
SEQRES 30 C 443 ALA GLU HIS CYS VAL GLN ASP ALA GLU GLY ARG TRP GLN
SEQRES 31 C 443 VAL ASP ARG ASP TYR ARG MET VAL THR THR PRO ASP LEU
SEQRES 32 C 443 ARG CYS GLY ILE TYR LEU GLN GLY GLY THR GLU HIS THR
SEQRES 33 C 443 HIS GLY LEU SER SER SER LEU LEU SER ASN LEU ALA THR
SEQRES 34 C 443 ARG SER GLY GLU ILE VAL SER SER ILE GLU ARG ARG LYS
SEQRES 35 C 443 SER
SEQRES 1 D 443 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 443 LEU VAL PRO ARG GLY SER HIS MET VAL ALA HIS ALA GLY
SEQRES 3 D 443 GLU SER PRO THR HIS ASP VAL VAL GLY VAL GLY PHE GLY
SEQRES 4 D 443 PRO ALA ASN LEU SER LEU ALA VAL ALA LEU GLU GLU SER
SEQRES 5 D 443 PRO ALA ALA LEU THR SER ALA PHE PHE GLU ARG ARG ALA
SEQRES 6 D 443 SER ILE SER TRP HIS GLN GLY MET LEU LEU PRO ALA ALA
SEQRES 7 D 443 LYS MET GLN VAL SER PHE LEU LYS ASP LEU ALA THR PHE
SEQRES 8 D 443 ARG ASN PRO ALA SER ARG PHE SER PHE VAL SER PHE LEU
SEQRES 9 D 443 HIS GLU ARG GLY ARG LEU VAL ARG PHE ALA ASN ASN HIS
SEQRES 10 D 443 ASP PHE PHE PRO THR ARG ARG GLU PHE HIS ASP TYR LEU
SEQRES 11 D 443 GLU TRP ALA GLU SER LYS LEU ALA HIS GLU VAL SER TYR
SEQRES 12 D 443 ASP SER GLU VAL THR ALA ILE ARG PRO GLY PRO GLY ARG
SEQRES 13 D 443 PRO VAL ASP SER VAL LEU VAL ASP VAL SER THR PRO GLU
SEQRES 14 D 443 ALA THR ARG THR VAL GLU ALA ARG ASN ILE VAL ILE SER
SEQRES 15 D 443 THR GLY LEU VAL PRO ARG MET PRO ALA GLY VAL GLN SER
SEQRES 16 D 443 ASP GLU PHE VAL TRP HIS SER SER ARG PHE LEU ASP HIS
SEQRES 17 D 443 PHE ARG ASP ARG ASP PRO ARG SER LEU ARG ARG VAL ALA
SEQRES 18 D 443 VAL ALA GLY GLY GLY GLN SER ALA ALA GLU ILE VAL ARG
SEQRES 19 D 443 PHE LEU HIS ASP ASN ARG PRO ASP THR VAL VAL HIS ALA
SEQRES 20 D 443 ILE MET PRO SER TYR GLY TYR VAL VAL ALA ASP ASN THR
SEQRES 21 D 443 PRO PHE ALA ASN GLN ILE PHE ASP PRO ALA ALA VAL ASP
SEQRES 22 D 443 ASP TYR PHE ASP GLY SER LYS GLN ALA LYS ASP ALA PHE
SEQRES 23 D 443 TRP ARG TYR HIS ARG ASN THR ASN TYR SER VAL VAL ASP
SEQRES 24 D 443 ASP GLU VAL ILE ARG ASP LEU TYR ARG ARG GLY TYR ASP
SEQRES 25 D 443 ASP GLU VAL ALA GLY ALA PRO ARG LEU ASN PHE VAL ASN
SEQRES 26 D 443 LEU ALA HIS VAL VAL GLY ALA LYS ARG ILE ALA ASP ASP
SEQRES 27 D 443 THR ARG VAL THR VAL TYR SER MET ALA ARG GLU GLU SER
SEQRES 28 D 443 TYR ASP LEU ASP VAL ASP VAL LEU VAL CYS ALA THR GLY
SEQRES 29 D 443 TYR ASP PRO MET ASP PRO GLY ASP LEU LEU GLY GLU LEU
SEQRES 30 D 443 ALA GLU HIS CYS VAL GLN ASP ALA GLU GLY ARG TRP GLN
SEQRES 31 D 443 VAL ASP ARG ASP TYR ARG MET VAL THR THR PRO ASP LEU
SEQRES 32 D 443 ARG CYS GLY ILE TYR LEU GLN GLY GLY THR GLU HIS THR
SEQRES 33 D 443 HIS GLY LEU SER SER SER LEU LEU SER ASN LEU ALA THR
SEQRES 34 D 443 ARG SER GLY GLU ILE VAL SER SER ILE GLU ARG ARG LYS
SEQRES 35 D 443 SER
HET FAD A 501 53
HET BR A 502 1
HET BR A 503 1
HET BR A 504 1
HET BR A 505 1
HET BR A 506 1
HET BR A 507 1
HET BR A 508 1
HET BR A 509 1
HET BR A 510 1
HET BR A 511 1
HET BR A 512 1
HET BR A 513 1
HET BR A 514 1
HET BR A 515 1
HET FAD B 501 53
HET BR B 502 1
HET BR B 503 1
HET BR B 504 1
HET BR B 505 1
HET BR B 506 1
HET BR B 507 1
HET BR B 508 1
HET BR B 509 1
HET BR B 510 1
HET BR B 511 1
HET BR B 512 1
HET FAD C 501 53
HET BR C 502 1
HET BR C 503 1
HET BR C 504 1
HET BR C 505 1
HET BR C 506 1
HET BR C 507 1
HET BR C 508 1
HET BR C 509 1
HET BR C 510 1
HET FAD D 501 53
HET BR D 502 1
HET BR D 503 1
HET BR D 504 1
HET BR D 505 1
HET BR D 506 1
HET BR D 507 1
HET BR D 508 1
HET BR D 509 1
HET BR D 510 1
HET BR D 511 1
HET BR D 512 1
HET BR D 513 1
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM BR BROMIDE ION
FORMUL 5 FAD 4(C27 H33 N9 O15 P2)
FORMUL 6 BR 46(BR 1-)
FORMUL 55 HOH *465(H2 O)
HELIX 1 AA1 GLY A 20 SER A 33 1 14
HELIX 2 AA2 HIS A 51 LEU A 55 5 5
HELIX 3 AA3 SER A 80 ARG A 88 1 9
HELIX 4 AA4 ARG A 90 HIS A 98 1 9
HELIX 5 AA5 THR A 103 LEU A 118 1 16
HELIX 6 AA6 ARG A 185 ASP A 192 1 8
HELIX 7 AA7 GLY A 207 ARG A 221 1 15
HELIX 8 AA8 THR A 241 ILE A 247 1 7
HELIX 9 AA9 ASP A 249 ASP A 258 1 10
HELIX 10 AB1 SER A 260 ARG A 272 1 13
HELIX 11 AB2 ASP A 280 ALA A 297 1 18
HELIX 12 AB3 ASP A 350 LEU A 355 5 6
HELIX 13 AB4 GLY A 356 CYS A 362 5 7
HELIX 14 AB5 GLY A 399 LEU A 404 5 6
HELIX 15 AB6 ASN A 407 LYS A 423 1 17
HELIX 16 AB7 GLY B 20 SER B 33 1 14
HELIX 17 AB8 HIS B 51 LEU B 55 5 5
HELIX 18 AB9 SER B 80 ARG B 88 1 9
HELIX 19 AC1 ARG B 90 ASN B 96 1 7
HELIX 20 AC2 THR B 103 LEU B 118 1 16
HELIX 21 AC3 ARG B 185 ARG B 191 1 7
HELIX 22 AC4 ASP B 192 ARG B 193 5 2
HELIX 23 AC5 ASP B 194 LEU B 198 5 5
HELIX 24 AC6 GLY B 207 ARG B 221 1 15
HELIX 25 AC7 THR B 241 GLN B 246 1 6
HELIX 26 AC8 ASP B 249 GLY B 259 1 11
HELIX 27 AC9 SER B 260 ARG B 272 1 13
HELIX 28 AD1 ASP B 280 ALA B 297 1 18
HELIX 29 AD2 PRO B 351 GLY B 356 1 6
HELIX 30 AD3 GLU B 357 CYS B 362 5 6
HELIX 31 AD4 THR B 394 GLY B 399 1 6
HELIX 32 AD5 LEU B 400 LEU B 404 5 5
HELIX 33 AD6 ASN B 407 LYS B 423 1 17
HELIX 34 AD7 GLY C 20 SER C 33 1 14
HELIX 35 AD8 HIS C 51 LEU C 55 5 5
HELIX 36 AD9 SER C 80 ARG C 88 1 9
HELIX 37 AE1 ARG C 90 ASN C 97 1 8
HELIX 38 AE2 THR C 103 LEU C 118 1 16
HELIX 39 AE3 ARG C 185 ARG C 191 1 7
HELIX 40 AE4 ASP C 194 LEU C 198 5 5
HELIX 41 AE5 GLY C 207 ARG C 221 1 15
HELIX 42 AE6 THR C 241 ILE C 247 1 7
HELIX 43 AE7 ASP C 249 ASP C 258 1 10
HELIX 44 AE8 SER C 260 ARG C 272 1 13
HELIX 45 AE9 ASP C 280 GLY C 298 1 19
HELIX 46 AF1 PRO C 351 GLY C 356 1 6
HELIX 47 AF2 GLU C 357 CYS C 362 5 6
HELIX 48 AF3 THR C 394 GLY C 399 1 6
HELIX 49 AF4 LEU C 400 LEU C 404 5 5
HELIX 50 AF5 ASN C 407 LYS C 423 1 17
HELIX 51 AF6 GLY D 20 SER D 33 1 14
HELIX 52 AF7 HIS D 51 LEU D 55 5 5
HELIX 53 AF8 SER D 80 ARG D 88 1 9
HELIX 54 AF9 ARG D 90 ASN D 97 1 8
HELIX 55 AG1 THR D 103 LEU D 118 1 16
HELIX 56 AG2 ARG D 185 ASP D 192 1 8
HELIX 57 AG3 ARG D 193 LEU D 198 5 6
HELIX 58 AG4 GLY D 207 ARG D 221 1 15
HELIX 59 AG5 THR D 241 GLN D 246 1 6
HELIX 60 AG6 ASP D 249 GLY D 259 1 11
HELIX 61 AG7 SER D 260 ARG D 272 1 13
HELIX 62 AG8 ASP D 280 GLY D 298 1 19
HELIX 63 AG9 PRO D 351 GLY D 356 1 6
HELIX 64 AH1 GLU D 357 CYS D 362 5 6
HELIX 65 AH2 THR D 394 GLY D 399 1 6
HELIX 66 AH3 ASN D 407 ARG D 422 1 16
SHEET 1 AA1 4 THR A 11 HIS A 12 0
SHEET 2 AA1 4 THR A 152 ALA A 157 1 O GLU A 156 N HIS A 12
SHEET 3 AA1 4 VAL A 142 SER A 147 -1 N VAL A 144 O VAL A 155
SHEET 4 AA1 4 GLU A 127 PRO A 133 -1 N ARG A 132 O LEU A 143
SHEET 1 AA2 4 SER A 39 PHE A 42 0
SHEET 2 AA2 4 VAL A 14 VAL A 17 1 N GLY A 16 O ALA A 40
SHEET 3 AA2 4 ASN A 159 ILE A 162 1 O VAL A 161 N VAL A 17
SHEET 4 AA2 4 GLY A 387 LEU A 390 1 O TYR A 389 N ILE A 160
SHEET 1 AA3 2 VAL A 167 PRO A 168 0
SHEET 2 AA3 2 TYR A 346 ASP A 347 -1 O ASP A 347 N VAL A 167
SHEET 1 AA4 5 VAL A 180 HIS A 182 0
SHEET 2 AA4 5 VAL A 339 CYS A 342 1 O CYS A 342 N TRP A 181
SHEET 3 AA4 5 ARG A 200 ALA A 204 1 N ALA A 202 O VAL A 341
SHEET 4 AA4 5 VAL A 225 ILE A 229 1 O HIS A 227 N VAL A 203
SHEET 5 AA4 5 LEU A 302 VAL A 305 1 O ASN A 303 N VAL A 226
SHEET 1 AA5 3 ALA A 308 ILE A 316 0
SHEET 2 AA5 3 ASP A 319 SER A 326 -1 O ARG A 321 N LYS A 314
SHEET 3 AA5 3 GLU A 331 VAL A 337 -1 O VAL A 337 N THR A 320
SHEET 1 AA6 5 SER B 39 PHE B 42 0
SHEET 2 AA6 5 THR B 11 VAL B 17 1 N GLY B 16 O ALA B 40
SHEET 3 AA6 5 THR B 152 ILE B 162 1 O VAL B 161 N VAL B 17
SHEET 4 AA6 5 VAL B 142 SER B 147 -1 N VAL B 144 O VAL B 155
SHEET 5 AA6 5 GLU B 127 PRO B 133 -1 N GLU B 127 O SER B 147
SHEET 1 AA7 4 SER B 39 PHE B 42 0
SHEET 2 AA7 4 THR B 11 VAL B 17 1 N GLY B 16 O ALA B 40
SHEET 3 AA7 4 THR B 152 ILE B 162 1 O VAL B 161 N VAL B 17
SHEET 4 AA7 4 GLY B 387 LEU B 390 1 O TYR B 389 N ILE B 160
SHEET 1 AA8 2 VAL B 167 PRO B 168 0
SHEET 2 AA8 2 TYR B 346 ASP B 347 -1 O ASP B 347 N VAL B 167
SHEET 1 AA9 5 VAL B 180 HIS B 182 0
SHEET 2 AA9 5 VAL B 339 CYS B 342 1 O CYS B 342 N TRP B 181
SHEET 3 AA9 5 ARG B 200 ALA B 204 1 N ALA B 202 O VAL B 341
SHEET 4 AA9 5 VAL B 225 ILE B 229 1 O HIS B 227 N VAL B 203
SHEET 5 AA9 5 LEU B 302 VAL B 305 1 O ASN B 303 N VAL B 226
SHEET 1 AB1 3 ALA B 308 ILE B 316 0
SHEET 2 AB1 3 ASP B 319 SER B 326 -1 O ARG B 321 N LYS B 314
SHEET 3 AB1 3 GLU B 331 VAL B 337 -1 O LEU B 335 N VAL B 322
SHEET 1 AB2 4 THR C 11 HIS C 12 0
SHEET 2 AB2 4 THR C 152 ALA C 157 1 O GLU C 156 N HIS C 12
SHEET 3 AB2 4 VAL C 142 SER C 147 -1 N VAL C 144 O VAL C 155
SHEET 4 AB2 4 GLU C 127 PRO C 133 -1 N ARG C 132 O LEU C 143
SHEET 1 AB3 4 SER C 39 PHE C 42 0
SHEET 2 AB3 4 VAL C 14 VAL C 17 1 N GLY C 16 O ALA C 40
SHEET 3 AB3 4 ASN C 159 ILE C 162 1 O VAL C 161 N VAL C 17
SHEET 4 AB3 4 GLY C 387 LEU C 390 1 O TYR C 389 N ILE C 160
SHEET 1 AB4 2 VAL C 167 PRO C 168 0
SHEET 2 AB4 2 TYR C 346 ASP C 347 -1 O ASP C 347 N VAL C 167
SHEET 1 AB5 5 VAL C 180 HIS C 182 0
SHEET 2 AB5 5 VAL C 339 CYS C 342 1 O CYS C 342 N TRP C 181
SHEET 3 AB5 5 ARG C 200 ALA C 204 1 N ALA C 202 O VAL C 341
SHEET 4 AB5 5 VAL C 225 ILE C 229 1 O HIS C 227 N VAL C 203
SHEET 5 AB5 5 LEU C 302 VAL C 305 1 O ASN C 303 N VAL C 226
SHEET 1 AB6 3 ALA C 308 ILE C 316 0
SHEET 2 AB6 3 ASP C 319 SER C 326 -1 O ASP C 319 N ILE C 316
SHEET 3 AB6 3 GLU C 331 VAL C 337 -1 O TYR C 333 N VAL C 324
SHEET 1 AB7 4 THR D 11 HIS D 12 0
SHEET 2 AB7 4 THR D 152 ALA D 157 1 O GLU D 156 N HIS D 12
SHEET 3 AB7 4 VAL D 142 SER D 147 -1 N VAL D 144 O VAL D 155
SHEET 4 AB7 4 GLU D 127 PRO D 133 -1 N ARG D 132 O LEU D 143
SHEET 1 AB8 4 SER D 39 PHE D 42 0
SHEET 2 AB8 4 VAL D 14 VAL D 17 1 N GLY D 16 O ALA D 40
SHEET 3 AB8 4 ASN D 159 ILE D 162 1 O VAL D 161 N VAL D 17
SHEET 4 AB8 4 GLY D 387 LEU D 390 1 O TYR D 389 N ILE D 160
SHEET 1 AB9 2 VAL D 167 PRO D 168 0
SHEET 2 AB9 2 TYR D 346 ASP D 347 -1 O ASP D 347 N VAL D 167
SHEET 1 AC1 5 VAL D 180 HIS D 182 0
SHEET 2 AC1 5 VAL D 339 CYS D 342 1 O CYS D 342 N TRP D 181
SHEET 3 AC1 5 ARG D 200 ALA D 204 1 N ALA D 202 O VAL D 341
SHEET 4 AC1 5 VAL D 225 ILE D 229 1 O HIS D 227 N VAL D 203
SHEET 5 AC1 5 LEU D 302 VAL D 305 1 O ASN D 303 N VAL D 226
SHEET 1 AC2 3 ALA D 308 ILE D 316 0
SHEET 2 AC2 3 ASP D 319 SER D 326 -1 O ARG D 321 N LYS D 314
SHEET 3 AC2 3 GLU D 331 VAL D 337 -1 O TYR D 333 N VAL D 324
CISPEP 1 ARG A 137 PRO A 138 0 -5.04
CISPEP 2 ARG B 137 PRO B 138 0 3.64
CISPEP 3 ARG C 137 PRO C 138 0 0.50
CISPEP 4 ARG D 137 PRO D 138 0 3.29
SITE 1 AC1 30 GLY A 18 GLY A 20 PRO A 21 ALA A 22
SITE 2 AC1 30 PHE A 42 GLU A 43 ARG A 44 ARG A 45
SITE 3 AC1 30 TRP A 50 HIS A 51 MET A 54 SER A 126
SITE 4 AC1 30 GLU A 127 VAL A 128 SER A 163 THR A 164
SITE 5 AC1 30 GLY A 165 LEU A 166 TYR A 276 TYR A 346
SITE 6 AC1 30 SER A 403 LEU A 405 BR A 503 HOH A 604
SITE 7 AC1 30 HOH A 625 HOH A 629 HOH A 643 HOH A 648
SITE 8 AC1 30 HOH A 651 HOH A 694
SITE 1 AC2 1 LEU A 91
SITE 1 AC3 4 SER A 183 SER A 209 TYR A 346 FAD A 501
SITE 1 AC4 3 SER A 64 LYS A 67 HIS B 98
SITE 1 AC5 2 TYR A 276 LEU A 405
SITE 1 AC6 4 ARG A 374 TYR A 376 ASN A 407 GLU A 414
SITE 1 AC7 2 HIS A 182 HIS A 189
SITE 1 AC8 1 GLY A 413
SITE 1 AC9 1 ARG A 78
SITE 1 AD1 2 ARG A 105 ARG A 191
SITE 1 AD2 2 PHE A 100 HOH B 690
SITE 1 AD3 2 ASP A 177 PHE A 179
SITE 1 AD4 1 LEU A 307
SITE 1 AD5 3 ASP A 249 PRO A 250 ALA A 251
SITE 1 AD6 1 GLU A 295
SITE 1 AD7 28 GLY B 18 GLY B 20 PRO B 21 ALA B 22
SITE 2 AD7 28 PHE B 42 GLU B 43 ARG B 44 ARG B 45
SITE 3 AD7 28 TRP B 50 HIS B 51 MET B 54 SER B 126
SITE 4 AD7 28 VAL B 128 SER B 163 THR B 164 GLY B 165
SITE 5 AD7 28 LEU B 166 TYR B 276 TYR B 346 SER B 403
SITE 6 AD7 28 LEU B 404 LEU B 405 BR B 503 BR B 505
SITE 7 AD7 28 HOH B 611 HOH B 618 HOH B 662 HOH B 682
SITE 1 AD8 3 GLY B 89 LEU B 91 VAL B 92
SITE 1 AD9 3 TYR B 276 LEU B 405 FAD B 501
SITE 1 AE1 1 HOH B 703
SITE 1 AE2 4 SER B 183 SER B 209 TYR B 346 FAD B 501
SITE 1 AE3 3 HIS A 98 SER B 64 LYS B 67
SITE 1 AE4 4 ARG B 374 TYR B 376 ASN B 407 GLU B 414
SITE 1 AE5 3 ASN A 303 TYR A 333 ARG B 385
SITE 1 AE6 4 SER B 176 HIS B 182 ARG B 185 HIS B 189
SITE 1 AE7 2 PHE B 100 HOH B 690
SITE 1 AE8 1 LEU B 307
SITE 1 AE9 3 THR B 164 ASP B 350 LEU B 354
SITE 1 AF1 29 GLY C 18 GLY C 20 PRO C 21 ALA C 22
SITE 2 AF1 29 PHE C 42 GLU C 43 ARG C 44 ARG C 45
SITE 3 AF1 29 TRP C 50 HIS C 51 MET C 54 SER C 126
SITE 4 AF1 29 GLU C 127 VAL C 128 SER C 163 THR C 164
SITE 5 AF1 29 GLY C 165 LEU C 166 TYR C 276 TYR C 346
SITE 6 AF1 29 SER C 403 LEU C 405 BR C 502 HOH C 616
SITE 7 AF1 29 HOH C 618 HOH C 625 HOH C 651 HOH C 691
SITE 8 AF1 29 HOH C 692
SITE 1 AF2 3 TYR C 276 LEU C 405 FAD C 501
SITE 1 AF3 2 LEU C 91 VAL C 92
SITE 1 AF4 3 SER C 183 SER C 209 TYR C 346
SITE 1 AF5 3 SER C 64 LYS C 67 HIS D 98
SITE 1 AF6 4 ARG C 374 TYR C 376 ASN C 407 GLU C 414
SITE 1 AF7 1 TYR C 333
SITE 1 AF8 2 ASP C 99 PHE C 100
SITE 1 AF9 29 GLY D 18 GLY D 20 PRO D 21 ALA D 22
SITE 2 AF9 29 PHE D 42 GLU D 43 ARG D 44 ARG D 45
SITE 3 AF9 29 TRP D 50 HIS D 51 MET D 54 SER D 126
SITE 4 AF9 29 VAL D 128 SER D 163 THR D 164 GLY D 165
SITE 5 AF9 29 LEU D 166 TYR D 276 TYR D 346 SER D 403
SITE 6 AF9 29 LEU D 405 BR D 504 HOH D 622 HOH D 637
SITE 7 AF9 29 HOH D 646 HOH D 657 HOH D 675 HOH D 691
SITE 8 AF9 29 HOH D 707
SITE 1 AG1 3 SER D 183 SER D 209 TYR D 346
SITE 1 AG2 3 GLY D 89 LEU D 91 VAL D 92
SITE 1 AG3 3 TYR D 276 LEU D 405 FAD D 501
SITE 1 AG4 3 HIS C 98 SER D 64 LYS D 67
SITE 1 AG5 4 SER D 176 TRP D 181 HIS D 182 HIS D 189
SITE 1 AG6 4 ARG D 374 TYR D 376 ASN D 407 GLU D 414
SITE 1 AG7 2 PRO D 250 ALA D 251
SITE 1 AG8 1 PHE D 100
SITE 1 AG9 1 PHE D 179
CRYST1 79.814 151.943 161.870 90.00 90.00 90.00 P 21 21 21 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 0.012529 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
