HEADER OXIDOREDUCTASE 16-DEC-13 4O1Q
TITLE CRYSTAL STRUCTURE OF THE Q103N-MAUG/PRE-METHYLAMINE DEHYDROGENASE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLAMINE UTILIZATION PROTEIN MAUG;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 21-387;
COMPND 5 EC: 1.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: METHYLAMINE DEHYDROGENASE LIGHT CHAIN;
COMPND 10 CHAIN: C, E;
COMPND 11 FRAGMENT: UNP RESIDUES 58-188;
COMPND 12 EC: 1.4.99.3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: METHYLAMINE DEHYDROGENASE HEAVY CHAIN;
COMPND 16 CHAIN: D, F;
COMPND 17 FRAGMENT: UNP RESIDUES 33-417;
COMPND 18 EC: 1.4.99.3;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 3 ORGANISM_TAXID: 318586;
SOURCE 4 STRAIN: PD 1222;
SOURCE 5 GENE: MAUG, PDEN_4736;
SOURCE 6 EXPRESSION_SYSTEM: PARACOCCUS DENITRIFICANS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 10 ORGANISM_TAXID: 318586;
SOURCE 11 STRAIN: PD 1222;
SOURCE 12 GENE: PDEN_4733;
SOURCE 13 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 17 ORGANISM_TAXID: 318586;
SOURCE 18 STRAIN: PD 1222;
SOURCE 19 GENE: PDEN_4730;
SOURCE 20 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 1063
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.T.YUKL,C.W.WILMOT
REVDAT 3 06-DEC-23 4O1Q 1 REMARK
REVDAT 2 20-SEP-23 4O1Q 1 REMARK SEQADV LINK
REVDAT 1 30-APR-14 4O1Q 0
JRNL AUTH S.SHIN,E.T.YUKL,E.SEHANOBISH,C.M.WILMOT,V.L.DAVIDSON
JRNL TITL SITE-DIRECTED MUTAGENESIS OF GLN103 REVEALS THE INFLUENCE OF
JRNL TITL 2 THIS RESIDUE ON THE REDOX PROPERTIES AND STABILITY OF MAUG.
JRNL REF BIOCHEMISTRY V. 53 1342 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24517455
JRNL DOI 10.1021/BI5000349
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 50437
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2653
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3621
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13231
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 226
REMARK 3 SOLVENT ATOMS : 397
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.80000
REMARK 3 B22 (A**2) : 4.28000
REMARK 3 B33 (A**2) : -2.58000
REMARK 3 B12 (A**2) : 1.05000
REMARK 3 B13 (A**2) : -0.50000
REMARK 3 B23 (A**2) : 2.30000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.354
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.306
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.950
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13877 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12614 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18973 ; 1.400 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 29022 ; 0.763 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1715 ; 5.680 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 670 ;33.860 ;23.791
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2044 ;13.861 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 106 ;14.377 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1991 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16081 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3245 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 359
REMARK 3 RESIDUE RANGE : A 401 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7454 28.0068 -76.7039
REMARK 3 T TENSOR
REMARK 3 T11: 0.6191 T22: 0.2130
REMARK 3 T33: 0.5418 T12: 0.1022
REMARK 3 T13: 0.0529 T23: -0.2999
REMARK 3 L TENSOR
REMARK 3 L11: 1.4530 L22: 0.7306
REMARK 3 L33: 3.0347 L12: 0.3710
REMARK 3 L13: -0.4236 L23: -0.6516
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.2048 S13: -0.0934
REMARK 3 S21: -0.0845 S22: 0.0288 S23: -0.0295
REMARK 3 S31: 0.2569 S32: 0.1301 S33: -0.0414
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 360
REMARK 3 RESIDUE RANGE : B 401 B 403
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9776 29.2943 23.6824
REMARK 3 T TENSOR
REMARK 3 T11: 0.4069 T22: 0.1310
REMARK 3 T33: 0.4109 T12: -0.0277
REMARK 3 T13: 0.1006 T23: -0.2145
REMARK 3 L TENSOR
REMARK 3 L11: 0.9357 L22: 1.2891
REMARK 3 L33: 3.0503 L12: 0.1678
REMARK 3 L13: -0.2203 L23: -1.1955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.0619 S13: 0.0815
REMARK 3 S21: 0.1520 S22: -0.0884 S23: 0.0085
REMARK 3 S31: -0.1335 S32: 0.1766 S33: 0.0780
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 131
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9112 29.0634 -48.2312
REMARK 3 T TENSOR
REMARK 3 T11: 0.5034 T22: 0.1675
REMARK 3 T33: 0.4369 T12: -0.0409
REMARK 3 T13: 0.0069 T23: -0.1856
REMARK 3 L TENSOR
REMARK 3 L11: 1.4950 L22: 1.6686
REMARK 3 L33: 3.2797 L12: -0.0913
REMARK 3 L13: 0.2964 L23: -1.6801
REMARK 3 S TENSOR
REMARK 3 S11: 0.2147 S12: 0.2469 S13: -0.2252
REMARK 3 S21: -0.3646 S22: 0.1023 S23: 0.2375
REMARK 3 S31: 0.4776 S32: -0.3161 S33: -0.3170
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 11 D 386
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8294 10.1442 -30.3745
REMARK 3 T TENSOR
REMARK 3 T11: 0.6232 T22: 0.1422
REMARK 3 T33: 0.5335 T12: -0.1779
REMARK 3 T13: -0.0989 T23: -0.1314
REMARK 3 L TENSOR
REMARK 3 L11: 0.4128 L22: 0.6816
REMARK 3 L33: 2.0026 L12: -0.0690
REMARK 3 L13: 0.0409 L23: -0.6996
REMARK 3 S TENSOR
REMARK 3 S11: 0.1044 S12: 0.0275 S13: -0.2261
REMARK 3 S21: -0.3044 S22: 0.1703 S23: 0.1298
REMARK 3 S31: 0.7729 S32: -0.3525 S33: -0.2747
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 7 E 131
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4735 33.8094 -3.6189
REMARK 3 T TENSOR
REMARK 3 T11: 0.1692 T22: 0.1016
REMARK 3 T33: 0.2607 T12: -0.0372
REMARK 3 T13: 0.0802 T23: -0.1064
REMARK 3 L TENSOR
REMARK 3 L11: 1.7350 L22: 1.0959
REMARK 3 L33: 1.1311 L12: -0.3209
REMARK 3 L13: -0.1626 L23: -0.5747
REMARK 3 S TENSOR
REMARK 3 S11: 0.0880 S12: -0.1876 S13: -0.0177
REMARK 3 S21: 0.0365 S22: 0.0809 S23: 0.1197
REMARK 3 S31: -0.0272 S32: -0.0999 S33: -0.1688
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 11 F 386
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8675 51.7638 -21.7693
REMARK 3 T TENSOR
REMARK 3 T11: 0.3310 T22: 0.1037
REMARK 3 T33: 0.3845 T12: 0.0011
REMARK 3 T13: 0.1222 T23: -0.1731
REMARK 3 L TENSOR
REMARK 3 L11: 0.4828 L22: 0.7625
REMARK 3 L33: 1.6569 L12: -0.0369
REMARK 3 L13: 0.0747 L23: -0.2636
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: -0.0572 S13: 0.1029
REMARK 3 S21: 0.0108 S22: 0.0257 S23: 0.0348
REMARK 3 S31: -0.2512 S32: -0.1576 S33: -0.0724
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4O1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000083931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03324
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : 0.11500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3750
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.59900
REMARK 200 R SYM FOR SHELL (I) : 0.59900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.7.0029
REMARK 200 STARTING MODEL: PDB ENTRY 3L4M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.4, 0.1 M SODIUM
REMARK 280 ACETATE, 24-30% W/V PEG8000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLU A 1
REMARK 465 GLN A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 PRO A 5
REMARK 465 GLU A 360
REMARK 465 SER A 361
REMARK 465 ARG A 362
REMARK 465 ALA A 363
REMARK 465 ALA A 364
REMARK 465 GLN A 365
REMARK 465 LYS A 366
REMARK 465 ASP A 367
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLU B 1
REMARK 465 GLN B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 4
REMARK 465 PRO B 5
REMARK 465 SER B 361
REMARK 465 ARG B 362
REMARK 465 ALA B 363
REMARK 465 ALA B 364
REMARK 465 GLN B 365
REMARK 465 LYS B 366
REMARK 465 ASP B 367
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 ALA C 3
REMARK 465 PRO C 4
REMARK 465 ALA C 5
REMARK 465 GLY C 6
REMARK 465 ASP D 2
REMARK 465 ALA D 3
REMARK 465 PRO D 4
REMARK 465 GLU D 5
REMARK 465 ALA D 6
REMARK 465 GLU D 7
REMARK 465 THR D 8
REMARK 465 GLN D 9
REMARK 465 ALA D 10
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 ALA E 1
REMARK 465 ASP E 2
REMARK 465 ALA E 3
REMARK 465 PRO E 4
REMARK 465 ALA E 5
REMARK 465 GLY E 6
REMARK 465 ASP F 2
REMARK 465 ALA F 3
REMARK 465 PRO F 4
REMARK 465 GLU F 5
REMARK 465 ALA F 6
REMARK 465 GLU F 7
REMARK 465 THR F 8
REMARK 465 GLN F 9
REMARK 465 ALA F 10
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 HIS A 35 70.78 -116.49
REMARK 500 ARG A 39 61.10 -115.05
REMARK 500 PHE A 92 146.34 81.16
REMARK 500 GLU A 113 -114.72 -126.55
REMARK 500 HIS A 205 44.24 -101.88
REMARK 500 GLU A 232 -65.73 -24.42
REMARK 500 ASN A 271 7.38 57.94
REMARK 500 MET A 279 171.08 68.00
REMARK 500 HIS B 35 73.54 -115.59
REMARK 500 PHE B 92 154.13 88.40
REMARK 500 GLU B 113 -112.72 -114.41
REMARK 500 ASP B 257 104.22 -45.06
REMARK 500 ASN B 271 14.39 58.46
REMARK 500 MET B 279 171.16 75.45
REMARK 500 LEU B 358 83.18 -64.02
REMARK 500 ASP C 19 109.84 -166.22
REMARK 500 HIS C 28 31.39 -92.36
REMARK 500 THR C 91 47.38 -144.04
REMARK 500 ARG C 99 74.54 -105.62
REMARK 500 LEU D 80 58.79 37.08
REMARK 500 ILE D 102 -80.31 63.13
REMARK 500 ALA D 130 63.98 36.48
REMARK 500 TRP D 140 32.98 -97.27
REMARK 500 LYS D 173 -73.34 -95.57
REMARK 500 PRO D 179 -165.51 -70.79
REMARK 500 HIS D 183 159.60 61.76
REMARK 500 PRO D 189 0.15 -65.24
REMARK 500 ASP D 190 21.70 -151.41
REMARK 500 TRP D 282 -90.73 -103.58
REMARK 500 GLN D 283 80.55 -69.57
REMARK 500 ASP D 384 73.86 -102.41
REMARK 500 ASP E 17 52.31 -114.72
REMARK 500 ASP E 19 116.07 -161.12
REMARK 500 SER E 39 26.95 -140.80
REMARK 500 THR E 91 44.16 -146.15
REMARK 500 ARG E 99 72.49 -107.53
REMARK 500 ILE F 102 -83.11 65.98
REMARK 500 ALA F 130 64.10 36.66
REMARK 500 LYS F 173 -74.71 -91.18
REMARK 500 ASP F 180 72.68 -68.91
REMARK 500 HIS F 183 163.10 66.42
REMARK 500 THR F 187 -54.57 -123.16
REMARK 500 TRP F 282 -95.15 -102.72
REMARK 500 GLN F 283 84.27 -69.84
REMARK 500 ARG F 305 45.89 -108.90
REMARK 500 LEU F 373 58.12 -96.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 35 NE2
REMARK 620 2 HEC A 402 NA 87.7
REMARK 620 3 HEC A 402 NB 90.5 89.4
REMARK 620 4 HEC A 402 NC 94.9 177.4 90.3
REMARK 620 5 HEC A 402 ND 92.4 90.5 177.1 89.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 66 OD1
REMARK 620 2 THR A 275 O 135.9
REMARK 620 3 PRO A 277 O 83.4 83.6
REMARK 620 4 HOH A 534 O 90.6 90.1 163.4
REMARK 620 5 HOH A 550 O 77.0 144.8 90.1 103.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 403 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 205 NE2
REMARK 620 2 HEC A 403 NA 87.5
REMARK 620 3 HEC A 403 NB 91.2 90.5
REMARK 620 4 HEC A 403 NC 90.3 177.8 89.5
REMARK 620 5 HEC A 403 ND 86.5 90.3 177.5 89.5
REMARK 620 6 TYR A 294 OH 165.3 95.1 103.2 87.1 79.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 35 NE2
REMARK 620 2 HEC B 402 NA 88.8
REMARK 620 3 HEC B 402 NB 94.2 89.8
REMARK 620 4 HEC B 402 NC 94.0 177.1 90.2
REMARK 620 5 HEC B 402 ND 88.9 90.1 177.0 89.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 66 OD1
REMARK 620 2 THR B 275 O 131.3
REMARK 620 3 PRO B 277 O 91.2 100.5
REMARK 620 4 HOH B 542 O 84.8 81.9 175.9
REMARK 620 5 HOH B 548 O 140.9 77.6 110.7 72.9
REMARK 620 6 HOH B 551 O 70.8 156.4 85.0 94.1 79.0
REMARK 620 7 HOH B 584 O 72.0 60.1 94.7 83.6 134.1 142.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 403 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 205 NE2
REMARK 620 2 HEC B 403 NA 87.8
REMARK 620 3 HEC B 403 NB 94.3 90.3
REMARK 620 4 HEC B 403 NC 90.1 177.9 89.6
REMARK 620 5 HEC B 403 ND 83.5 89.9 177.8 90.1
REMARK 620 6 TYR B 294 OH 163.8 88.8 101.6 93.4 80.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA F 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 253 O
REMARK 620 2 ASP F 253 OD2 83.1
REMARK 620 3 SER F 256 OG 138.8 136.0
REMARK 620 4 ASP F 258 O 70.2 153.3 69.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L4M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WT MAUG/PRE-METHYLAMINE DEHYDROGENASE
REMARK 900 COMPLEX
DBREF 4O1Q A 1 367 UNP Q51658 MAUG_PARDP 21 387
DBREF 4O1Q B 1 367 UNP Q51658 MAUG_PARDP 21 387
DBREF 4O1Q C 1 131 UNP A1BBA0 A1BBA0_PARDP 58 188
DBREF 4O1Q D 2 386 UNP A1BB97 A1BB97_PARDP 33 417
DBREF 4O1Q E 1 131 UNP A1BBA0 A1BBA0_PARDP 58 188
DBREF 4O1Q F 2 386 UNP A1BB97 A1BB97_PARDP 33 417
SEQADV 4O1Q HIS A -5 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS A -4 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS A -3 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS A -2 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS A -1 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS A 0 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q ASN A 103 UNP Q51658 GLN 123 ENGINEERED MUTATION
SEQADV 4O1Q HIS B -5 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS B -4 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS B -3 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS B -2 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS B -1 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q HIS B 0 UNP Q51658 EXPRESSION TAG
SEQADV 4O1Q ASN B 103 UNP Q51658 GLN 123 ENGINEERED MUTATION
SEQADV 4O1Q HIS C -5 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS C -4 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS C -3 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS C -2 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS C -1 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS C 0 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E -5 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E -4 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E -3 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E -2 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E -1 UNP A1BBA0 EXPRESSION TAG
SEQADV 4O1Q HIS E 0 UNP A1BBA0 EXPRESSION TAG
SEQRES 1 A 373 HIS HIS HIS HIS HIS HIS GLU GLN ALA ARG PRO ALA ASP
SEQRES 2 A 373 ASP ALA LEU ALA ALA LEU GLY ALA GLN LEU PHE VAL ASP
SEQRES 3 A 373 PRO ALA LEU SER ARG ASN ALA THR GLN SER CYS ALA THR
SEQRES 4 A 373 CYS HIS ASP PRO ALA ARG ALA PHE THR ASP PRO ARG GLU
SEQRES 5 A 373 GLY LYS ALA GLY LEU ALA VAL SER VAL GLY ASP ASP GLY
SEQRES 6 A 373 GLN SER HIS GLY ASP ARG ASN THR PRO THR LEU GLY TYR
SEQRES 7 A 373 ALA ALA LEU VAL PRO ALA PHE HIS ARG ASP ALA ASN GLY
SEQRES 8 A 373 LYS TYR LYS GLY GLY GLN PHE TRP ASP GLY ARG ALA ASP
SEQRES 9 A 373 ASP LEU LYS GLN ASN ALA GLY GLN PRO MET LEU ASN PRO
SEQRES 10 A 373 VAL GLU MET ALA MET PRO ASP ARG ALA ALA VAL ALA ALA
SEQRES 11 A 373 ARG LEU ARG ASP ASP PRO ALA TYR ARG THR GLY PHE GLU
SEQRES 12 A 373 ALA LEU PHE GLY LYS GLY VAL LEU ASP ASP PRO GLU ARG
SEQRES 13 A 373 ALA PHE ASP ALA ALA ALA GLU ALA LEU ALA ALA TYR GLN
SEQRES 14 A 373 ALA THR GLY GLU PHE SER PRO PHE ASP SER LYS TYR ASP
SEQRES 15 A 373 ARG VAL MET ARG GLY GLU GLU LYS PHE THR PRO LEU GLU
SEQRES 16 A 373 GLU PHE GLY TYR THR VAL PHE ILE THR TRP ASN CYS ARG
SEQRES 17 A 373 LEU CYS HIS MET GLN ARG LYS GLN GLY VAL ALA GLU ARG
SEQRES 18 A 373 GLU THR PHE THR ASN PHE GLU TYR HIS ASN ILE GLY LEU
SEQRES 19 A 373 PRO VAL ASN GLU THR ALA ARG GLU ALA SER GLY LEU GLY
SEQRES 20 A 373 ALA ASP HIS VAL ASP HIS GLY LEU LEU ALA ARG PRO GLY
SEQRES 21 A 373 ILE GLU ASP PRO ALA GLN SER GLY ARG PHE LYS VAL PRO
SEQRES 22 A 373 SER LEU ARG ASN VAL ALA VAL THR GLY PRO TYR MET HIS
SEQRES 23 A 373 ASN GLY VAL PHE THR ASP LEU ARG THR ALA ILE LEU PHE
SEQRES 24 A 373 TYR ASN LYS TYR THR SER ARG ARG PRO GLU ALA LYS ILE
SEQRES 25 A 373 ASN PRO GLU THR GLY ALA PRO TRP GLY GLU PRO GLU VAL
SEQRES 26 A 373 ALA ARG ASN LEU SER LEU ALA GLU LEU GLN SER GLY LEU
SEQRES 27 A 373 MET LEU ASP ASP GLY ARG VAL ASP ALA LEU VAL ALA PHE
SEQRES 28 A 373 LEU GLU THR LEU THR ASP ARG ARG TYR GLU PRO LEU LEU
SEQRES 29 A 373 GLU GLU SER ARG ALA ALA GLN LYS ASP
SEQRES 1 B 373 HIS HIS HIS HIS HIS HIS GLU GLN ALA ARG PRO ALA ASP
SEQRES 2 B 373 ASP ALA LEU ALA ALA LEU GLY ALA GLN LEU PHE VAL ASP
SEQRES 3 B 373 PRO ALA LEU SER ARG ASN ALA THR GLN SER CYS ALA THR
SEQRES 4 B 373 CYS HIS ASP PRO ALA ARG ALA PHE THR ASP PRO ARG GLU
SEQRES 5 B 373 GLY LYS ALA GLY LEU ALA VAL SER VAL GLY ASP ASP GLY
SEQRES 6 B 373 GLN SER HIS GLY ASP ARG ASN THR PRO THR LEU GLY TYR
SEQRES 7 B 373 ALA ALA LEU VAL PRO ALA PHE HIS ARG ASP ALA ASN GLY
SEQRES 8 B 373 LYS TYR LYS GLY GLY GLN PHE TRP ASP GLY ARG ALA ASP
SEQRES 9 B 373 ASP LEU LYS GLN ASN ALA GLY GLN PRO MET LEU ASN PRO
SEQRES 10 B 373 VAL GLU MET ALA MET PRO ASP ARG ALA ALA VAL ALA ALA
SEQRES 11 B 373 ARG LEU ARG ASP ASP PRO ALA TYR ARG THR GLY PHE GLU
SEQRES 12 B 373 ALA LEU PHE GLY LYS GLY VAL LEU ASP ASP PRO GLU ARG
SEQRES 13 B 373 ALA PHE ASP ALA ALA ALA GLU ALA LEU ALA ALA TYR GLN
SEQRES 14 B 373 ALA THR GLY GLU PHE SER PRO PHE ASP SER LYS TYR ASP
SEQRES 15 B 373 ARG VAL MET ARG GLY GLU GLU LYS PHE THR PRO LEU GLU
SEQRES 16 B 373 GLU PHE GLY TYR THR VAL PHE ILE THR TRP ASN CYS ARG
SEQRES 17 B 373 LEU CYS HIS MET GLN ARG LYS GLN GLY VAL ALA GLU ARG
SEQRES 18 B 373 GLU THR PHE THR ASN PHE GLU TYR HIS ASN ILE GLY LEU
SEQRES 19 B 373 PRO VAL ASN GLU THR ALA ARG GLU ALA SER GLY LEU GLY
SEQRES 20 B 373 ALA ASP HIS VAL ASP HIS GLY LEU LEU ALA ARG PRO GLY
SEQRES 21 B 373 ILE GLU ASP PRO ALA GLN SER GLY ARG PHE LYS VAL PRO
SEQRES 22 B 373 SER LEU ARG ASN VAL ALA VAL THR GLY PRO TYR MET HIS
SEQRES 23 B 373 ASN GLY VAL PHE THR ASP LEU ARG THR ALA ILE LEU PHE
SEQRES 24 B 373 TYR ASN LYS TYR THR SER ARG ARG PRO GLU ALA LYS ILE
SEQRES 25 B 373 ASN PRO GLU THR GLY ALA PRO TRP GLY GLU PRO GLU VAL
SEQRES 26 B 373 ALA ARG ASN LEU SER LEU ALA GLU LEU GLN SER GLY LEU
SEQRES 27 B 373 MET LEU ASP ASP GLY ARG VAL ASP ALA LEU VAL ALA PHE
SEQRES 28 B 373 LEU GLU THR LEU THR ASP ARG ARG TYR GLU PRO LEU LEU
SEQRES 29 B 373 GLU GLU SER ARG ALA ALA GLN LYS ASP
SEQRES 1 C 137 HIS HIS HIS HIS HIS HIS ALA ASP ALA PRO ALA GLY THR
SEQRES 2 C 137 ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP ILE
SEQRES 3 C 137 GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP GLY
SEQRES 4 C 137 ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN CYS
SEQRES 5 C 137 PRO PRO GLY THR LYS LEU ALA THR ALA SER 0AF VAL ALA
SEQRES 6 C 137 SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU ILE
SEQRES 7 C 137 ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY ARG
SEQRES 8 C 137 CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL TYR
SEQRES 9 C 137 ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE GLY
SEQRES 10 C 137 ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE SER
SEQRES 11 C 137 PRO ILE VAL GLY LYS ALA SER
SEQRES 1 D 385 ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR GLN
SEQRES 2 D 385 GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU ALA
SEQRES 3 D 385 ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA PRO
SEQRES 4 D 385 ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO ALA
SEQRES 5 D 385 HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP GLY
SEQRES 6 D 385 GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY PHE
SEQRES 7 D 385 LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE ILE
SEQRES 8 D 385 ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG GLY
SEQRES 9 D 385 GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL THR
SEQRES 10 D 385 LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA PRO
SEQRES 11 D 385 ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER LEU
SEQRES 12 D 385 THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE SER
SEQRES 13 D 385 PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY LYS
SEQRES 14 D 385 ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR HIS
SEQRES 15 D 385 ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS CYS
SEQRES 16 D 385 ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR GLU
SEQRES 17 D 385 GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS PRO
SEQRES 18 D 385 GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER GLN
SEQRES 19 D 385 LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY LYS
SEQRES 20 D 385 ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS PHE
SEQRES 21 D 385 LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG ALA
SEQRES 22 D 385 ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA TYR
SEQRES 23 D 385 HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP GLN
SEQRES 24 D 385 ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE VAL
SEQRES 25 D 385 VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA LYS
SEQRES 26 D 385 PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL SER
SEQRES 27 D 385 GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR GLY
SEQRES 28 D 385 ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY GLU
SEQRES 29 D 385 GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO GLN
SEQRES 30 D 385 VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 E 137 HIS HIS HIS HIS HIS HIS ALA ASP ALA PRO ALA GLY THR
SEQRES 2 E 137 ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP ILE
SEQRES 3 E 137 GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP GLY
SEQRES 4 E 137 ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN CYS
SEQRES 5 E 137 PRO PRO GLY THR LYS LEU ALA THR ALA SER 0AF VAL ALA
SEQRES 6 E 137 SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU ILE
SEQRES 7 E 137 ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY ARG
SEQRES 8 E 137 CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL TYR
SEQRES 9 E 137 ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE GLY
SEQRES 10 E 137 ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE SER
SEQRES 11 E 137 PRO ILE VAL GLY LYS ALA SER
SEQRES 1 F 385 ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR GLN
SEQRES 2 F 385 GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU ALA
SEQRES 3 F 385 ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA PRO
SEQRES 4 F 385 ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO ALA
SEQRES 5 F 385 HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP GLY
SEQRES 6 F 385 GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY PHE
SEQRES 7 F 385 LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE ILE
SEQRES 8 F 385 ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG GLY
SEQRES 9 F 385 GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL THR
SEQRES 10 F 385 LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA PRO
SEQRES 11 F 385 ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER LEU
SEQRES 12 F 385 THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE SER
SEQRES 13 F 385 PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY LYS
SEQRES 14 F 385 ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR HIS
SEQRES 15 F 385 ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS CYS
SEQRES 16 F 385 ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR GLU
SEQRES 17 F 385 GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS PRO
SEQRES 18 F 385 GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER GLN
SEQRES 19 F 385 LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY LYS
SEQRES 20 F 385 ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS PHE
SEQRES 21 F 385 LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG ALA
SEQRES 22 F 385 ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA TYR
SEQRES 23 F 385 HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP GLN
SEQRES 24 F 385 ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE VAL
SEQRES 25 F 385 VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA LYS
SEQRES 26 F 385 PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL SER
SEQRES 27 F 385 GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR GLY
SEQRES 28 F 385 ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY GLU
SEQRES 29 F 385 GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO GLN
SEQRES 30 F 385 VAL ILE THR THR ALA ASP MET GLY
MODRES 4O1Q 0AF C 57 TRP 7-HYDROXY-L-TRYPTOPHAN
MODRES 4O1Q 0AF E 57 TRP 7-HYDROXY-L-TRYPTOPHAN
HET 0AF C 57 15
HET 0AF E 57 15
HET CA A 401 1
HET HEC A 402 43
HET HEC A 403 43
HET EDO A 404 4
HET EDO A 405 4
HET CA B 401 1
HET HEC B 402 43
HET HEC B 403 43
HET EDO B 404 4
HET PO4 B 405 5
HET PGE C 201 10
HET MES D 401 12
HET MES F 401 12
HET NA F 402 1
HETNAM 0AF 7-HYDROXY-L-TRYPTOPHAN
HETNAM CA CALCIUM ION
HETNAM HEC HEME C
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 0AF 2(C11 H12 N2 O3)
FORMUL 7 CA 2(CA 2+)
FORMUL 8 HEC 4(C34 H34 FE N4 O4)
FORMUL 10 EDO 3(C2 H6 O2)
FORMUL 16 PO4 O4 P 3-
FORMUL 17 PGE C6 H14 O4
FORMUL 18 MES 2(C6 H13 N O4 S)
FORMUL 20 NA NA 1+
FORMUL 21 HOH *397(H2 O)
HELIX 1 1 ALA A 6 VAL A 19 1 14
HELIX 2 2 ASP A 20 SER A 24 5 5
HELIX 3 3 SER A 30 HIS A 35 1 6
HELIX 4 4 ASP A 36 ALA A 40 5 5
HELIX 5 5 TYR A 72 VAL A 76 5 5
HELIX 6 6 ASP A 99 ASN A 110 1 12
HELIX 7 7 ASP A 118 ASP A 129 1 12
HELIX 8 8 ASP A 129 GLY A 141 1 13
HELIX 9 9 GLY A 143 ASP A 146 5 4
HELIX 10 10 ASP A 147 ALA A 164 1 18
HELIX 11 11 SER A 173 ARG A 180 1 8
HELIX 12 12 THR A 186 ILE A 197 1 12
HELIX 13 13 ASN A 200 HIS A 205 1 6
HELIX 14 14 ASN A 231 GLY A 239 1 9
HELIX 15 15 HIS A 247 ARG A 252 5 6
HELIX 16 16 ASP A 257 SER A 261 5 5
HELIX 17 17 ASN A 271 THR A 275 5 5
HELIX 18 18 ASP A 286 PHE A 293 1 8
HELIX 19 19 TYR A 294 THR A 298 5 5
HELIX 20 20 ARG A 301 ALA A 304 5 4
HELIX 21 21 SER A 324 GLN A 329 1 6
HELIX 22 22 ASP A 335 THR A 348 1 14
HELIX 23 23 LEU A 349 THR A 350 5 2
HELIX 24 24 ASP A 351 GLU A 355 5 5
HELIX 25 25 ASP B 7 VAL B 19 1 13
HELIX 26 26 ASP B 20 SER B 24 5 5
HELIX 27 27 SER B 30 HIS B 35 1 6
HELIX 28 28 ASP B 36 ALA B 40 5 5
HELIX 29 29 TYR B 72 VAL B 76 5 5
HELIX 30 30 ASP B 99 ASN B 110 1 12
HELIX 31 31 ASP B 118 ASP B 128 1 11
HELIX 32 32 ASP B 129 PHE B 140 1 12
HELIX 33 33 GLY B 143 ASP B 146 5 4
HELIX 34 34 ASP B 147 ALA B 164 1 18
HELIX 35 35 SER B 173 GLY B 181 1 9
HELIX 36 36 THR B 186 ILE B 197 1 12
HELIX 37 37 ASN B 200 HIS B 205 1 6
HELIX 38 38 ASN B 231 GLY B 239 1 9
HELIX 39 39 HIS B 247 ARG B 252 5 6
HELIX 40 40 ASP B 257 SER B 261 5 5
HELIX 41 41 ASN B 271 THR B 275 5 5
HELIX 42 42 ASP B 286 PHE B 293 1 8
HELIX 43 43 TYR B 294 THR B 298 5 5
HELIX 44 44 ARG B 301 ILE B 306 5 6
HELIX 45 45 SER B 324 GLN B 329 1 6
HELIX 46 46 ASP B 335 THR B 348 1 14
HELIX 47 47 LEU B 349 THR B 350 5 2
HELIX 48 48 ASP B 351 GLU B 355 5 5
HELIX 49 49 TYR C 25 CYS C 29 5 5
HELIX 50 50 CYS C 36 SER C 39 5 4
HELIX 51 51 ARG C 99 ALA C 103 5 5
HELIX 52 52 ALA C 112 ALA C 116 5 5
HELIX 53 53 THR D 13 GLY D 29 1 17
HELIX 54 54 PRO D 52 ALA D 56 5 5
HELIX 55 55 TYR D 138 TRP D 140 5 3
HELIX 56 56 THR D 269 ASP D 275 1 7
HELIX 57 57 TYR E 25 CYS E 29 5 5
HELIX 58 58 CYS E 36 GLY E 40 5 5
HELIX 59 59 ARG E 99 ALA E 103 5 5
HELIX 60 60 ALA E 112 ALA E 116 5 5
HELIX 61 61 THR F 13 GLY F 29 1 17
HELIX 62 62 TYR F 138 TRP F 140 5 3
HELIX 63 63 THR F 269 ASP F 275 1 7
SHEET 1 A 2 HIS A 80 ARG A 81 0
SHEET 2 A 2 TYR A 87 LYS A 88 -1 O LYS A 88 N HIS A 80
SHEET 1 B 2 TYR A 223 HIS A 224 0
SHEET 2 B 2 PHE A 264 LYS A 265 -1 O PHE A 264 N HIS A 224
SHEET 1 C 2 ILE A 306 ASN A 307 0
SHEET 2 C 2 ALA A 312 PRO A 313 -1 O ALA A 312 N ASN A 307
SHEET 1 D 2 HIS B 80 ARG B 81 0
SHEET 2 D 2 TYR B 87 LYS B 88 -1 O LYS B 88 N HIS B 80
SHEET 1 E 2 TYR B 223 HIS B 224 0
SHEET 2 E 2 PHE B 264 LYS B 265 -1 O PHE B 264 N HIS B 224
SHEET 1 F 2 ASP C 32 ASN C 34 0
SHEET 2 F 2 PRO C 87 LEU C 89 -1 O CYS C 88 N GLY C 33
SHEET 1 G 3 LYS C 51 LEU C 52 0
SHEET 2 G 3 SER C 69 CYS C 78 -1 O CYS C 78 N LYS C 51
SHEET 3 G 3 TYR C 119 ILE C 123 -1 O CYS C 121 N CYS C 77
SHEET 1 H 3 0AF C 57 TYR C 62 0
SHEET 2 H 3 SER C 69 CYS C 78 -1 O ILE C 72 N ALA C 59
SHEET 3 H 3 ILE C 126 LYS C 129 -1 O VAL C 127 N LEU C 71
SHEET 1 I 4 ARG D 70 GLY D 77 0
SHEET 2 I 4 THR D 59 ASP D 65 -1 N VAL D 63 O GLY D 73
SHEET 3 I 4 ARG D 46 ASP D 51 -1 N VAL D 47 O ILE D 64
SHEET 4 I 4 VAL D 379 THR D 382 -1 O THR D 381 N TYR D 48
SHEET 1 J 4 ASN D 82 VAL D 85 0
SHEET 2 J 4 ILE D 92 PHE D 99 -1 O ALA D 93 N VAL D 84
SHEET 3 J 4 ARG D 107 PHE D 114 -1 O PHE D 114 N ILE D 92
SHEET 4 J 4 PRO D 121 LEU D 127 -1 O LEU D 127 N ASP D 109
SHEET 1 K 4 THR D 142 LEU D 144 0
SHEET 2 K 4 THR D 150 GLN D 155 -1 O LEU D 152 N SER D 143
SHEET 3 K 4 ALA D 161 ASP D 166 -1 O GLY D 163 N PHE D 153
SHEET 4 K 4 ALA D 171 ASP D 177 -1 O ALA D 171 N ASP D 166
SHEET 1 L 4 CYS D 181 ALA D 188 0
SHEET 2 L 4 THR D 191 CYS D 196 -1 O HIS D 195 N TYR D 182
SHEET 3 L 4 LEU D 201 ALA D 205 -1 O ALA D 202 N MET D 194
SHEET 4 L 4 GLU D 213 HIS D 216 -1 O THR D 215 N LYS D 203
SHEET 1 M 4 ALA D 232 SER D 234 0
SHEET 2 M 4 ARG D 239 PRO D 243 -1 O VAL D 241 N ALA D 232
SHEET 3 M 4 LYS D 248 ASP D 253 -1 O HIS D 250 N TRP D 242
SHEET 4 M 4 LYS D 260 PHE D 261 -1 O LYS D 260 N ASP D 253
SHEET 1 N 4 ALA D 232 SER D 234 0
SHEET 2 N 4 ARG D 239 PRO D 243 -1 O VAL D 241 N ALA D 232
SHEET 3 N 4 LYS D 248 ASP D 253 -1 O HIS D 250 N TRP D 242
SHEET 4 N 4 VAL D 265 GLU D 266 -1 O VAL D 265 N ILE D 249
SHEET 1 O 3 TRP D 277 PRO D 279 0
SHEET 2 O 3 ARG D 293 GLN D 300 -1 O ASP D 299 N ARG D 278
SHEET 3 O 3 VAL D 285 HIS D 288 -1 N ALA D 286 O TYR D 295
SHEET 1 P 4 TRP D 277 PRO D 279 0
SHEET 2 P 4 ARG D 293 GLN D 300 -1 O ASP D 299 N ARG D 278
SHEET 3 P 4 SER D 310 ASP D 317 -1 O LEU D 316 N ILE D 294
SHEET 4 P 4 ARG D 323 ILE D 333 -1 O ALA D 325 N VAL D 315
SHEET 1 Q 4 SER D 335 VAL D 338 0
SHEET 2 Q 4 LEU D 345 SER D 350 -1 O LEU D 349 N SER D 335
SHEET 3 Q 4 THR D 355 ASP D 360 -1 O TYR D 357 N ALA D 348
SHEET 4 Q 4 GLU D 366 VAL D 370 -1 O VAL D 370 N LEU D 356
SHEET 1 R 2 ASP E 32 ASN E 34 0
SHEET 2 R 2 PRO E 87 LEU E 89 -1 O CYS E 88 N GLY E 33
SHEET 1 S 3 LYS E 51 LEU E 52 0
SHEET 2 S 3 SER E 69 CYS E 78 -1 O CYS E 78 N LYS E 51
SHEET 3 S 3 TYR E 119 ILE E 123 -1 O ILE E 123 N ARG E 75
SHEET 1 T 3 0AF E 57 TYR E 62 0
SHEET 2 T 3 SER E 69 CYS E 78 -1 O TYR E 70 N CYS E 61
SHEET 3 T 3 ILE E 126 LYS E 129 -1 O VAL E 127 N LEU E 71
SHEET 1 U 4 ARG F 70 GLY F 77 0
SHEET 2 U 4 THR F 59 ASP F 65 -1 N THR F 59 O GLY F 77
SHEET 3 U 4 ARG F 46 ASP F 51 -1 N VAL F 49 O PHE F 62
SHEET 4 U 4 VAL F 379 THR F 382 -1 O VAL F 379 N ASN F 50
SHEET 1 V 3 ASN F 82 VAL F 85 0
SHEET 2 V 3 ILE F 92 PHE F 114 -1 O ALA F 93 N VAL F 84
SHEET 3 V 3 PRO F 121 LEU F 127 -1 O LEU F 127 N ASP F 109
SHEET 1 W 4 THR F 142 LEU F 144 0
SHEET 2 W 4 THR F 150 GLN F 155 -1 O LEU F 152 N SER F 143
SHEET 3 W 4 ALA F 161 ASP F 166 -1 O ALA F 161 N GLN F 155
SHEET 4 W 4 ALA F 171 ASP F 177 -1 O ARG F 174 N VAL F 164
SHEET 1 X 4 CYS F 181 ALA F 188 0
SHEET 2 X 4 THR F 191 CYS F 196 -1 O HIS F 195 N TYR F 182
SHEET 3 X 4 LEU F 201 ALA F 205 -1 O ALA F 202 N MET F 194
SHEET 4 X 4 GLU F 213 HIS F 216 -1 O THR F 215 N LYS F 203
SHEET 1 Y 4 ALA F 232 SER F 234 0
SHEET 2 Y 4 ARG F 239 PRO F 243 -1 O VAL F 241 N ALA F 232
SHEET 3 Y 4 LYS F 248 ASP F 253 -1 O HIS F 250 N TRP F 242
SHEET 4 Y 4 LYS F 260 PHE F 261 -1 O LYS F 260 N ASP F 253
SHEET 1 Z 4 ALA F 232 SER F 234 0
SHEET 2 Z 4 ARG F 239 PRO F 243 -1 O VAL F 241 N ALA F 232
SHEET 3 Z 4 LYS F 248 ASP F 253 -1 O HIS F 250 N TRP F 242
SHEET 4 Z 4 VAL F 265 GLU F 266 -1 O VAL F 265 N ILE F 249
SHEET 1 AA 3 TRP F 277 PRO F 279 0
SHEET 2 AA 3 ARG F 293 GLN F 300 -1 O ASP F 299 N ARG F 278
SHEET 3 AA 3 VAL F 285 HIS F 288 -1 N ALA F 286 O TYR F 295
SHEET 1 AB 4 TRP F 277 PRO F 279 0
SHEET 2 AB 4 ARG F 293 GLN F 300 -1 O ASP F 299 N ARG F 278
SHEET 3 AB 4 SER F 310 ASP F 317 -1 O LEU F 316 N ILE F 294
SHEET 4 AB 4 ARG F 323 ILE F 333 -1 O LEU F 324 N VAL F 315
SHEET 1 AC 4 SER F 335 VAL F 338 0
SHEET 2 AC 4 LEU F 345 SER F 350 -1 O TYR F 347 N ASN F 337
SHEET 3 AC 4 THR F 355 ASP F 360 -1 O HIS F 359 N LEU F 346
SHEET 4 AC 4 GLU F 366 VAL F 370 -1 O VAL F 370 N LEU F 356
SSBOND 1 CYS C 23 CYS C 88 1555 1555 2.03
SSBOND 2 CYS C 29 CYS C 61 1555 1555 2.02
SSBOND 3 CYS C 36 CYS C 121 1555 1555 2.04
SSBOND 4 CYS C 38 CYS C 86 1555 1555 2.02
SSBOND 5 CYS C 46 CYS C 77 1555 1555 2.01
SSBOND 6 CYS C 78 CYS C 109 1555 1555 2.02
SSBOND 7 CYS D 181 CYS D 196 1555 1555 2.03
SSBOND 8 CYS E 23 CYS E 88 1555 1555 2.03
SSBOND 9 CYS E 29 CYS E 61 1555 1555 2.03
SSBOND 10 CYS E 36 CYS E 121 1555 1555 2.03
SSBOND 11 CYS E 38 CYS E 86 1555 1555 2.03
SSBOND 12 CYS E 46 CYS E 77 1555 1555 2.02
SSBOND 13 CYS E 78 CYS E 109 1555 1555 2.02
SSBOND 14 CYS F 181 CYS F 196 1555 1555 2.04
LINK SG CYS A 31 CAB HEC A 402 1555 1555 1.76
LINK SG CYS A 34 CAC HEC A 402 1555 1555 1.78
LINK SG CYS A 201 CAB HEC A 403 1555 1555 1.76
LINK SG CYS A 204 CAC HEC A 403 1555 1555 1.77
LINK SG CYS B 31 CAB HEC B 402 1555 1555 1.76
LINK SG CYS B 34 CAC HEC B 402 1555 1555 1.80
LINK SG CYS B 201 CAB HEC B 403 1555 1555 1.76
LINK SG CYS B 204 CAC HEC B 403 1555 1555 1.78
LINK C SER C 56 N 0AF C 57 1555 1555 1.33
LINK C 0AF C 57 N VAL C 58 1555 1555 1.33
LINK C SER E 56 N 0AF E 57 1555 1555 1.33
LINK C 0AF E 57 N VAL E 58 1555 1555 1.33
LINK NE2 HIS A 35 FE HEC A 402 1555 1555 2.29
LINK OD1 ASN A 66 CA CA A 401 1555 1555 2.51
LINK NE2 HIS A 205 FE HEC A 403 1555 1555 2.37
LINK O THR A 275 CA CA A 401 1555 1555 2.27
LINK O PRO A 277 CA CA A 401 1555 1555 2.46
LINK OH TYR A 294 FE HEC A 403 1555 1555 1.86
LINK CA CA A 401 O HOH A 534 1555 1555 2.41
LINK CA CA A 401 O HOH A 550 1555 1555 2.12
LINK NE2 HIS B 35 FE HEC B 402 1555 1555 2.24
LINK OD1 ASN B 66 CA CA B 401 1555 1555 2.27
LINK NE2 HIS B 205 FE HEC B 403 1555 1555 2.30
LINK O THR B 275 CA CA B 401 1555 1555 2.35
LINK O PRO B 277 CA CA B 401 1555 1555 2.33
LINK OH TYR B 294 FE HEC B 403 1555 1555 1.89
LINK CA CA B 401 O HOH B 542 1555 1555 2.18
LINK CA CA B 401 O HOH B 548 1555 1555 2.26
LINK CA CA B 401 O HOH B 551 1555 1555 2.48
LINK CA CA B 401 O HOH B 584 1555 1555 2.80
LINK O ASP F 253 NA NA F 402 1555 1555 2.82
LINK OD2 ASP F 253 NA NA F 402 1555 1555 2.90
LINK OG SER F 256 NA NA F 402 1555 1555 2.59
LINK O ASP F 258 NA NA F 402 1555 1555 2.61
CISPEP 1 GLY A 276 PRO A 277 0 -7.64
CISPEP 2 GLY B 276 PRO B 277 0 -5.90
CISPEP 3 SER D 157 PRO D 158 0 -0.85
CISPEP 4 SER F 157 PRO F 158 0 -4.61
SITE 1 AC1 5 ASN A 66 THR A 275 PRO A 277 HOH A 534
SITE 2 AC1 5 HOH A 550
SITE 1 AC2 26 GLN A 29 SER A 30 CYS A 31 CYS A 34
SITE 2 AC2 26 HIS A 35 VAL A 55 ARG A 65 ASN A 66
SITE 3 AC2 26 THR A 67 PRO A 68 LEU A 70 GLN A 91
SITE 4 AC2 26 PHE A 92 TRP A 93 ARG A 96 LEU A 100
SITE 5 AC2 26 ASN A 103 ALA A 104 PRO A 107 GLU A 113
SITE 6 AC2 26 MET A 114 LEU A 159 GLN A 163 LYS A 265
SITE 7 AC2 26 HOH A 535 HOH A 563
SITE 1 AC3 20 TRP A 93 ASN A 200 CYS A 201 CYS A 204
SITE 2 AC3 20 HIS A 205 HIS A 224 LEU A 228 PHE A 264
SITE 3 AC3 20 LYS A 265 PRO A 267 LEU A 269 VAL A 272
SITE 4 AC3 20 TYR A 278 MET A 279 HIS A 280 LEU A 287
SITE 5 AC3 20 TYR A 294 GLU A 327 LEU A 334 HOH A 550
SITE 1 AC4 4 LYS A 48 GLN A 60 ALA A 237 HOH A 507
SITE 1 AC5 3 LYS A 296 SER A 299 ARG A 300
SITE 1 AC6 7 ASN B 66 THR B 275 PRO B 277 HOH B 542
SITE 2 AC6 7 HOH B 548 HOH B 551 HOH B 584
SITE 1 AC7 25 GLN B 29 SER B 30 CYS B 31 CYS B 34
SITE 2 AC7 25 HIS B 35 ARG B 65 ASN B 66 THR B 67
SITE 3 AC7 25 PRO B 68 LEU B 70 GLN B 91 PHE B 92
SITE 4 AC7 25 TRP B 93 ARG B 96 LEU B 100 ASN B 103
SITE 5 AC7 25 PRO B 107 GLU B 113 MET B 114 GLN B 163
SITE 6 AC7 25 LYS B 265 HOH B 573 HOH B 587 HOH B 588
SITE 7 AC7 25 HOH B 596
SITE 1 AC8 22 ASN B 200 CYS B 201 CYS B 204 HIS B 205
SITE 2 AC8 22 HIS B 224 LEU B 228 PHE B 264 VAL B 266
SITE 3 AC8 22 PRO B 267 TYR B 278 MET B 279 HIS B 280
SITE 4 AC8 22 LEU B 287 TYR B 294 SER B 324 GLU B 327
SITE 5 AC8 22 LEU B 334 HOH B 510 HOH B 548 HOH B 551
SITE 6 AC8 22 HOH B 590 HOH B 595
SITE 1 AC9 3 LEU B 75 ALA B 164 ARG B 215
SITE 1 BC1 1 HOH B 577
SITE 1 BC2 4 SER C 60 GLU C 92 GLY C 93 HOH C 320
SITE 1 BC3 4 ALA A 138 ARG D 35 LEU D 37 GLU D 38
SITE 1 BC4 6 ALA B 138 LEU B 139 GLY B 141 ARG F 35
SITE 2 BC4 6 LEU F 37 GLU F 38
SITE 1 BC5 3 ASP F 253 SER F 256 ASP F 258
CRYST1 55.530 83.520 107.780 109.94 91.54 105.78 P 1 2
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 0.018008 0.005089 0.002496 0.00000
SCALE2 0.000000 0.012442 0.004834 0.00000
SCALE3 0.000000 0.000000 0.009957 0.00000
(ATOM LINES ARE NOT SHOWN.)
END