HEADER OXIDOREDUCTASE 26-MAR-15 4UHW
TITLE HUMAN ALDEHYDE OXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALDEHYDE OXIDASE 1, AZAHETEROCYCLE HYDROXYLASE;
COMPND 5 EC: 1.2.3.1, 1.17.3.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TP1000
KEYWDS OXIDOREDUCTASE, DRUG METABOLISM, MOLYBDENUM ENZYMES, XANTHINE OXIDASE
KEYWDS 2 ENZYMES
EXPDTA X-RAY DIFFRACTION
AUTHOR C.COELHO,M.J.ROMAO,T.SANTOS-SILVA
REVDAT 4 10-JAN-24 4UHW 1 REMARK
REVDAT 3 30-SEP-15 4UHW 1 JRNL
REVDAT 2 09-SEP-15 4UHW 1 JRNL
REVDAT 1 02-SEP-15 4UHW 0
JRNL AUTH C.COELHO,A.FOTI,T.HARTMANN,T.SANTOS-SILVA,S.LEIMKUHLER,
JRNL AUTH 2 M.J.ROMAO
JRNL TITL STRUCTURAL INSIGHTS INTO XENOBIOTIC AND INHIBITOR BINDING TO
JRNL TITL 2 HUMAN ALDEHYDE OXIDASE
JRNL REF NAT.CHEM.BIOL. V. 11 779 2015
JRNL REFN ISSN 1552-4450
JRNL PMID 26322824
JRNL DOI 10.1038/NCHEMBIO.1895
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 105.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 44241
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2359
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3221
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9988
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 103
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.826
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.295
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.157
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10304 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9925 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13937 ; 1.286 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22901 ; 0.897 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1281 ; 6.206 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 428 ;35.827 ;24.182
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1800 ;14.142 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;15.574 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1554 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11511 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2273 ; 0.001 ; 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): 5145 ; 1.122 ; 4.624
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5144 ; 1.122 ; 4.624
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6419 ; 1.957 ; 6.930
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6420 ; 1.957 ; 6.930
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5159 ; 1.169 ; 4.828
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5157 ; 1.169 ; 4.828
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7514 ; 2.009 ; 7.180
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11123 ; 3.713 ;36.875
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11118 ; 3.707 ;36.868
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 1336
REMARK 3 ORIGIN FOR THE GROUP (A): -46.7610 -21.5600 -38.4180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1996 T22: 0.1385
REMARK 3 T33: 0.1968 T12: 0.0095
REMARK 3 T13: 0.0613 T23: -0.1186
REMARK 3 L TENSOR
REMARK 3 L11: 0.9255 L22: 0.9253
REMARK 3 L33: 0.8895 L12: 0.0629
REMARK 3 L13: -0.3891 L23: 0.1945
REMARK 3 S TENSOR
REMARK 3 S11: 0.0528 S12: -0.2172 S13: 0.1725
REMARK 3 S21: 0.3672 S22: -0.0847 S23: 0.1411
REMARK 3 S31: -0.0171 S32: -0.0809 S33: 0.0319
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4UHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46600
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 74.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.50
REMARK 200 R MERGE (I) : 0.26000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.80
REMARK 200 R MERGE FOR SHELL (I) : 1.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: PDB ENTRY 3ZYV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 74.46500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 74.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.62500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 74.46500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 74.46500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.62500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 74.46500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.46500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 66.62500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 74.46500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.46500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.62500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 90010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -133.25000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 ARG A 3
REMARK 465 SER A 168
REMARK 465 GLY A 169
REMARK 465 CYS A 170
REMARK 465 CYS A 171
REMARK 465 GLN A 172
REMARK 465 SER A 173
REMARK 465 LYS A 174
REMARK 465 GLU A 175
REMARK 465 ASN A 176
REMARK 465 GLY A 177
REMARK 465 VAL A 178
REMARK 465 CYS A 179
REMARK 465 CYS A 180
REMARK 465 LEU A 181
REMARK 465 ASP A 182
REMARK 465 GLN A 183
REMARK 465 GLY A 184
REMARK 465 ILE A 185
REMARK 465 ASN A 186
REMARK 465 GLY A 187
REMARK 465 LEU A 188
REMARK 465 PRO A 189
REMARK 465 GLU A 190
REMARK 465 PHE A 191
REMARK 465 GLU A 192
REMARK 465 GLU A 193
REMARK 465 GLY A 194
REMARK 465 SER A 195
REMARK 465 LYS A 196
REMARK 465 THR A 197
REMARK 465 SER A 198
REMARK 465 LYS A 559
REMARK 465 ILE A 570
REMARK 465 GLY A 571
REMARK 465 PHE A 655
REMARK 465 PHE A 656
REMARK 465 THR A 657
REMARK 465 GLU A 658
REMARK 465 ALA A 659
REMARK 465 GLU A 660
REMARK 465 HIS A 713
REMARK 465 ASN A 714
REMARK 465 SER A 715
REMARK 465 ASP A 881
REMARK 465 GLU A 882
REMARK 465 PRO A 1337
REMARK 465 ILE A 1338
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 CYS A 44 -16.40 -150.02
REMARK 500 THR A 97 -111.97 -138.45
REMARK 500 GLN A 113 -83.55 -119.68
REMARK 500 TYR A 154 -27.20 70.31
REMARK 500 LYS A 228 82.42 155.78
REMARK 500 GLN A 229 96.80 -69.23
REMARK 500 MET A 266 -74.29 -110.79
REMARK 500 PHE A 277 40.11 -143.63
REMARK 500 ASP A 289 -169.68 -79.71
REMARK 500 ARG A 290 97.77 -67.58
REMARK 500 ALA A 345 -138.10 53.70
REMARK 500 ALA A 431 -162.99 -121.70
REMARK 500 GLU A 451 97.43 39.83
REMARK 500 GLN A 532 -44.51 -162.30
REMARK 500 SER A 648 -119.71 42.57
REMARK 500 THR A 665 -84.18 -91.63
REMARK 500 VAL A 675 -58.33 -124.93
REMARK 500 ALA A 806 -54.11 -146.73
REMARK 500 VAL A 811 -95.56 -129.15
REMARK 500 ASN A 896 -111.99 54.13
REMARK 500 ASN A 913 52.97 -94.76
REMARK 500 ARG A 921 97.63 -35.21
REMARK 500 ALA A 970 36.50 -98.55
REMARK 500 ASN A1117 68.21 -159.68
REMARK 500 GLN A1157 66.35 -119.75
REMARK 500 THR A1230 22.21 -143.38
REMARK 500 SER A1256 36.31 -156.69
REMARK 500 GLN A1257 120.28 65.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2023 DISTANCE = 5.98 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3002 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 FES A3002 S1 104.5
REMARK 620 3 FES A3002 S2 103.1 89.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3002 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 52 SG
REMARK 620 2 FES A3002 S1 106.0
REMARK 620 3 FES A3002 S2 113.2 89.6
REMARK 620 4 CYS A 74 SG 102.3 119.2 125.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3001 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 114 SG
REMARK 620 2 FES A3001 S1 110.6
REMARK 620 3 FES A3001 S2 109.6 94.3
REMARK 620 4 CYS A 151 SG 109.0 111.7 120.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3001 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 117 SG
REMARK 620 2 FES A3001 S1 123.6
REMARK 620 3 FES A3001 S2 115.2 94.9
REMARK 620 4 CYS A 149 SG 106.2 111.8 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS A3004 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE A3003 S2'
REMARK 620 2 MOS A3004 S 140.5
REMARK 620 3 MOS A3004 O1 80.8 84.8
REMARK 620 4 MOS A3004 O2 119.4 99.6 103.2
REMARK 620 5 MTE A3003 S1' 78.5 97.6 150.0 105.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 2337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 2338
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UHX RELATED DB: PDB
REMARK 900 HUMAN ALDEHYDE OXIDASE IN COMPLEX WITH PHTHALAZINE AND THIORIDAZINE
DBREF 4UHW A 1 1338 UNP Q06278 AOXA_HUMAN 1 1338
SEQRES 1 A 1338 MET ASP ARG ALA SER GLU LEU LEU PHE TYR VAL ASN GLY
SEQRES 2 A 1338 ARG LYS VAL ILE GLU LYS ASN VAL ASP PRO GLU THR MET
SEQRES 3 A 1338 LEU LEU PRO TYR LEU ARG LYS LYS LEU ARG LEU THR GLY
SEQRES 4 A 1338 THR LYS TYR GLY CYS GLY GLY GLY GLY CYS GLY ALA CYS
SEQRES 5 A 1338 THR VAL MET ILE SER ARG TYR ASN PRO ILE THR LYS ARG
SEQRES 6 A 1338 ILE ARG HIS HIS PRO ALA ASN ALA CYS LEU ILE PRO ILE
SEQRES 7 A 1338 CYS SER LEU TYR GLY ALA ALA VAL THR THR VAL GLU GLY
SEQRES 8 A 1338 ILE GLY SER THR HIS THR ARG ILE HIS PRO VAL GLN GLU
SEQRES 9 A 1338 ARG ILE ALA LYS CYS HIS GLY THR GLN CYS GLY PHE CYS
SEQRES 10 A 1338 THR PRO GLY MET VAL MET SER ILE TYR THR LEU LEU ARG
SEQRES 11 A 1338 ASN HIS PRO GLU PRO THR LEU ASP GLN LEU THR ASP ALA
SEQRES 12 A 1338 LEU GLY GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO
SEQRES 13 A 1338 ILE ILE ASP ALA CYS LYS THR PHE CYS LYS THR SER GLY
SEQRES 14 A 1338 CYS CYS GLN SER LYS GLU ASN GLY VAL CYS CYS LEU ASP
SEQRES 15 A 1338 GLN GLY ILE ASN GLY LEU PRO GLU PHE GLU GLU GLY SER
SEQRES 16 A 1338 LYS THR SER PRO LYS LEU PHE ALA GLU GLU GLU PHE LEU
SEQRES 17 A 1338 PRO LEU ASP PRO THR GLN GLU LEU ILE PHE PRO PRO GLU
SEQRES 18 A 1338 LEU MET ILE MET ALA GLU LYS GLN SER GLN ARG THR ARG
SEQRES 19 A 1338 VAL PHE GLY SER GLU ARG MET MET TRP PHE SER PRO VAL
SEQRES 20 A 1338 THR LEU LYS GLU LEU LEU GLU PHE LYS PHE LYS TYR PRO
SEQRES 21 A 1338 GLN ALA PRO VAL ILE MET GLY ASN THR SER VAL GLY PRO
SEQRES 22 A 1338 GLU VAL LYS PHE LYS GLY VAL PHE HIS PRO VAL ILE ILE
SEQRES 23 A 1338 SER PRO ASP ARG ILE GLU GLU LEU SER VAL VAL ASN HIS
SEQRES 24 A 1338 ALA TYR ASN GLY LEU THR LEU GLY ALA GLY LEU SER LEU
SEQRES 25 A 1338 ALA GLN VAL LYS ASP ILE LEU ALA ASP VAL VAL GLN LYS
SEQRES 26 A 1338 LEU PRO GLU GLU LYS THR GLN MET TYR HIS ALA LEU LEU
SEQRES 27 A 1338 LYS HIS LEU GLY THR LEU ALA GLY SER GLN ILE ARG ASN
SEQRES 28 A 1338 MET ALA SER LEU GLY GLY HIS ILE ILE SER ARG HIS PRO
SEQRES 29 A 1338 ASP SER ASP LEU ASN PRO ILE LEU ALA VAL GLY ASN CYS
SEQRES 30 A 1338 THR LEU ASN LEU LEU SER LYS GLU GLY LYS ARG GLN ILE
SEQRES 31 A 1338 PRO LEU ASN GLU GLN PHE LEU SER LYS CYS PRO ASN ALA
SEQRES 32 A 1338 ASP LEU LYS PRO GLN GLU ILE LEU VAL SER VAL ASN ILE
SEQRES 33 A 1338 PRO TYR SER ARG LYS TRP GLU PHE VAL SER ALA PHE ARG
SEQRES 34 A 1338 GLN ALA GLN ARG GLN GLU ASN ALA LEU ALA ILE VAL ASN
SEQRES 35 A 1338 SER GLY MET ARG VAL PHE PHE GLY GLU GLY ASP GLY ILE
SEQRES 36 A 1338 ILE ARG GLU LEU CYS ILE SER TYR GLY GLY VAL GLY PRO
SEQRES 37 A 1338 ALA THR ILE CYS ALA LYS ASN SER CYS GLN LYS LEU ILE
SEQRES 38 A 1338 GLY ARG HIS TRP ASN GLU GLN MET LEU ASP ILE ALA CYS
SEQRES 39 A 1338 ARG LEU ILE LEU ASN GLU VAL SER LEU LEU GLY SER ALA
SEQRES 40 A 1338 PRO GLY GLY LYS VAL GLU PHE LYS ARG THR LEU ILE ILE
SEQRES 41 A 1338 SER PHE LEU PHE LYS PHE TYR LEU GLU VAL SER GLN ILE
SEQRES 42 A 1338 LEU LYS LYS MET ASP PRO VAL HIS TYR PRO SER LEU ALA
SEQRES 43 A 1338 ASP LYS TYR GLU SER ALA LEU GLU ASP LEU HIS SER LYS
SEQRES 44 A 1338 HIS HIS CYS SER THR LEU LYS TYR GLN ASN ILE GLY PRO
SEQRES 45 A 1338 LYS GLN HIS PRO GLU ASP PRO ILE GLY HIS PRO ILE MET
SEQRES 46 A 1338 HIS LEU SER GLY VAL LYS HIS ALA THR GLY GLU ALA ILE
SEQRES 47 A 1338 TYR CYS ASP ASP MET PRO LEU VAL ASP GLN GLU LEU PHE
SEQRES 48 A 1338 LEU THR PHE VAL THR SER SER ARG ALA HIS ALA LYS ILE
SEQRES 49 A 1338 VAL SER ILE ASP LEU SER GLU ALA LEU SER MET PRO GLY
SEQRES 50 A 1338 VAL VAL ASP ILE MET THR ALA GLU HIS LEU SER ASP VAL
SEQRES 51 A 1338 ASN SER PHE CYS PHE PHE THR GLU ALA GLU LYS PHE LEU
SEQRES 52 A 1338 ALA THR ASP LYS VAL PHE CYS VAL GLY GLN LEU VAL CYS
SEQRES 53 A 1338 ALA VAL LEU ALA ASP SER GLU VAL GLN ALA LYS ARG ALA
SEQRES 54 A 1338 ALA LYS ARG VAL LYS ILE VAL TYR GLN ASP LEU GLU PRO
SEQRES 55 A 1338 LEU ILE LEU THR ILE GLU GLU SER ILE GLN HIS ASN SER
SEQRES 56 A 1338 SER PHE LYS PRO GLU ARG LYS LEU GLU TYR GLY ASN VAL
SEQRES 57 A 1338 ASP GLU ALA PHE LYS VAL VAL ASP GLN ILE LEU GLU GLY
SEQRES 58 A 1338 GLU ILE HIS MET GLY GLY GLN GLU HIS PHE TYR MET GLU
SEQRES 59 A 1338 THR GLN SER MET LEU VAL VAL PRO LYS GLY GLU ASP GLN
SEQRES 60 A 1338 GLU MET ASP VAL TYR VAL SER THR GLN PHE PRO LYS TYR
SEQRES 61 A 1338 ILE GLN ASP ILE VAL ALA SER THR LEU LYS LEU PRO ALA
SEQRES 62 A 1338 ASN LYS VAL MET CYS HIS VAL ARG ARG VAL GLY GLY ALA
SEQRES 63 A 1338 PHE GLY GLY LYS VAL LEU LYS THR GLY ILE ILE ALA ALA
SEQRES 64 A 1338 VAL THR ALA PHE ALA ALA ASN LYS HIS GLY ARG ALA VAL
SEQRES 65 A 1338 ARG CYS VAL LEU GLU ARG GLY GLU ASP MET LEU ILE THR
SEQRES 66 A 1338 GLY GLY ARG HIS PRO TYR LEU GLY LYS TYR LYS ALA GLY
SEQRES 67 A 1338 PHE MET ASN ASP GLY ARG ILE LEU ALA LEU ASP MET GLU
SEQRES 68 A 1338 HIS TYR SER ASN ALA GLY ALA SER LEU ASP GLU SER LEU
SEQRES 69 A 1338 PHE VAL ILE GLU MET GLY LEU LEU LYS MET ASP ASN ALA
SEQRES 70 A 1338 TYR LYS PHE PRO ASN LEU ARG CYS ARG GLY TRP ALA CYS
SEQRES 71 A 1338 ARG THR ASN LEU PRO SER ASN THR ALA PHE ARG GLY PHE
SEQRES 72 A 1338 GLY PHE PRO GLN ALA ALA LEU ILE THR GLU SER CYS ILE
SEQRES 73 A 1338 THR GLU VAL ALA ALA LYS CYS GLY LEU SER PRO GLU LYS
SEQRES 74 A 1338 VAL ARG ILE ILE ASN MET TYR LYS GLU ILE ASP GLN THR
SEQRES 75 A 1338 PRO TYR LYS GLN GLU ILE ASN ALA LYS ASN LEU ILE GLN
SEQRES 76 A 1338 CYS TRP ARG GLU CYS MET ALA MET SER SER TYR SER LEU
SEQRES 77 A 1338 ARG LYS VAL ALA VAL GLU LYS PHE ASN ALA GLU ASN TYR
SEQRES 78 A 1338 TRP LYS LYS LYS GLY LEU ALA MET VAL PRO LEU LYS PHE
SEQRES 79 A 1338 PRO VAL GLY LEU GLY SER ARG ALA ALA GLY GLN ALA ALA
SEQRES 80 A 1338 ALA LEU VAL HIS ILE TYR LEU ASP GLY SER VAL LEU VAL
SEQRES 81 A 1338 THR HIS GLY GLY ILE GLU MET GLY GLN GLY VAL HIS THR
SEQRES 82 A 1338 LYS MET ILE GLN VAL VAL SER ARG GLU LEU ARG MET PRO
SEQRES 83 A 1338 MET SER ASN VAL HIS LEU ARG GLY THR SER THR GLU THR
SEQRES 84 A 1338 VAL PRO ASN ALA ASN ILE SER GLY GLY SER VAL VAL ALA
SEQRES 85 A 1338 ASP LEU ASN GLY LEU ALA VAL LYS ASP ALA CYS GLN THR
SEQRES 86 A 1338 LEU LEU LYS ARG LEU GLU PRO ILE ILE SER LYS ASN PRO
SEQRES 87 A 1338 LYS GLY THR TRP LYS ASP TRP ALA GLN THR ALA PHE ASP
SEQRES 88 A 1338 GLU SER ILE ASN LEU SER ALA VAL GLY TYR PHE ARG GLY
SEQRES 89 A 1338 TYR GLU SER ASP MET ASN TRP GLU LYS GLY GLU GLY GLN
SEQRES 90 A 1338 PRO PHE GLU TYR PHE VAL TYR GLY ALA ALA CYS SER GLU
SEQRES 91 A 1338 VAL GLU ILE ASP CYS LEU THR GLY ASP HIS LYS ASN ILE
SEQRES 92 A 1338 ARG THR ASP ILE VAL MET ASP VAL GLY CYS SER ILE ASN
SEQRES 93 A 1338 PRO ALA ILE ASP ILE GLY GLN ILE GLU GLY ALA PHE ILE
SEQRES 94 A 1338 GLN GLY MET GLY LEU TYR THR ILE GLU GLU LEU ASN TYR
SEQRES 95 A 1338 SER PRO GLN GLY ILE LEU HIS THR ARG GLY PRO ASP GLN
SEQRES 96 A 1338 TYR LYS ILE PRO ALA ILE CYS ASP MET PRO THR GLU LEU
SEQRES 97 A 1338 HIS ILE ALA LEU LEU PRO PRO SER GLN ASN SER ASN THR
SEQRES 98 A 1338 LEU TYR SER SER LYS GLY LEU GLY GLU SER GLY VAL PHE
SEQRES 99 A 1338 LEU GLY CYS SER VAL PHE PHE ALA ILE HIS ASP ALA VAL
SEQRES 100 A 1338 SER ALA ALA ARG GLN GLU ARG GLY LEU HIS GLY PRO LEU
SEQRES 101 A 1338 THR LEU ASN SER PRO LEU THR PRO GLU LYS ILE ARG MET
SEQRES 102 A 1338 ALA CYS GLU ASP LYS PHE THR LYS MET ILE PRO ARG ASP
SEQRES 103 A 1338 GLU PRO GLY SER TYR VAL PRO TRP ASN VAL PRO ILE
HET MLI A2337 7
HET MLI A2338 7
HET FES A3001 4
HET FES A3002 4
HET MTE A3003 24
HET MOS A3004 4
HET FAD A3006 53
HETNAM MLI MALONATE ION
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,
HETNAM 2 MTE 8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-
HETNAM 3 MTE ANTHRACEN-7-YLMETHYL)ESTER
HETNAM MOS DIOXOTHIOMOLYBDENUM(VI) ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 MLI 2(C3 H2 O4 2-)
FORMUL 4 FES 2(FE2 S2)
FORMUL 6 MTE C10 H14 N5 O6 P S2
FORMUL 7 MOS H MO O2 S
FORMUL 8 FAD C27 H33 N9 O15 P2
FORMUL 9 HOH *43(H2 O)
HELIX 1 1 MET A 26 LYS A 34 1 9
HELIX 2 2 CYS A 74 ILE A 76 5 3
HELIX 3 3 ILE A 78 TYR A 82 5 5
HELIX 4 4 THR A 88 GLY A 93 1 6
HELIX 5 5 HIS A 100 CYS A 109 1 10
HELIX 6 6 CYS A 117 HIS A 132 1 16
HELIX 7 7 THR A 136 LEU A 144 1 9
HELIX 8 8 GLY A 145 ASN A 147 5 3
HELIX 9 9 TYR A 154 THR A 163 1 10
HELIX 10 10 ALA A 203 PHE A 207 5 5
HELIX 11 11 PRO A 219 GLU A 227 1 9
HELIX 12 12 THR A 248 TYR A 259 1 12
HELIX 13 13 SER A 270 LYS A 278 1 9
HELIX 14 14 ILE A 291 SER A 295 5 5
HELIX 15 15 SER A 311 LEU A 326 1 16
HELIX 16 16 THR A 331 LEU A 344 1 14
HELIX 17 17 GLY A 346 ALA A 353 1 8
HELIX 18 18 SER A 354 ARG A 362 1 9
HELIX 19 19 LEU A 368 GLY A 375 1 8
HELIX 20 20 ASN A 393 SER A 398 1 6
HELIX 21 21 ALA A 473 ILE A 481 1 9
HELIX 22 22 ASN A 486 ASN A 499 1 14
HELIX 23 23 LYS A 511 ASP A 538 1 28
HELIX 24 24 TYR A 549 LEU A 553 5 5
HELIX 25 25 SER A 588 THR A 594 1 7
HELIX 26 26 TYR A 599 MET A 603 5 5
HELIX 27 27 LEU A 629 SER A 634 1 6
HELIX 28 28 THR A 643 LEU A 647 5 5
HELIX 29 29 LEU A 647 ASN A 651 5 5
HELIX 30 30 SER A 682 LYS A 691 1 10
HELIX 31 31 GLU A 708 GLN A 712 5 5
HELIX 32 32 ASN A 727 PHE A 732 1 6
HELIX 33 33 LYS A 733 VAL A 735 5 3
HELIX 34 34 PHE A 777 LYS A 790 1 14
HELIX 35 35 PRO A 792 ASN A 794 5 3
HELIX 36 36 VAL A 811 GLY A 829 1 19
HELIX 37 37 GLU A 837 THR A 845 1 9
HELIX 38 38 SER A 883 MET A 894 1 12
HELIX 39 39 GLY A 924 GLY A 944 1 21
HELIX 40 40 SER A 946 MET A 955 1 10
HELIX 41 41 ALA A 970 SER A 985 1 16
HELIX 42 42 SER A 985 ASN A 1000 1 16
HELIX 43 43 ARG A 1021 GLN A 1025 5 5
HELIX 44 44 GLY A 1050 LEU A 1063 1 14
HELIX 45 45 PRO A 1066 SER A 1068 5 3
HELIX 46 46 VAL A 1090 LYS A 1116 1 27
HELIX 47 47 THR A 1121 GLU A 1132 1 12
HELIX 48 48 ASN A 1196 THR A 1216 1 21
HELIX 49 49 ARG A 1231 GLN A 1235 5 5
HELIX 50 50 ALA A 1240 MET A 1244 5 5
HELIX 51 51 THR A 1261 SER A 1264 5 4
HELIX 52 52 GLU A 1270 LEU A 1275 5 6
HELIX 53 53 GLY A 1276 ARG A 1294 1 19
HELIX 54 54 THR A 1307 CYS A 1315 1 9
HELIX 55 55 ASP A 1317 ILE A 1323 1 7
HELIX 56 56 GLU A 1327 TYR A 1331 5 5
SHEET 1 AA 5 ARG A 14 LYS A 19 0
SHEET 2 AA 5 GLU A 6 VAL A 11 -1 O LEU A 7 N GLU A 18
SHEET 3 AA 5 ALA A 85 THR A 87 1 N VAL A 86 O TYR A 10
SHEET 4 AA 5 THR A 53 ASN A 60 -1 O MET A 55 N THR A 87
SHEET 5 AA 5 ARG A 65 ASN A 72 -1 O ARG A 65 N ASN A 60
SHEET 1 AB 3 ARG A 234 GLY A 237 0
SHEET 2 AB 3 MET A 242 SER A 245 -1 O TRP A 243 N PHE A 236
SHEET 3 AB 3 VAL A 284 ILE A 286 1 O ILE A 285 N PHE A 244
SHEET 1 AC 5 VAL A 297 HIS A 299 0
SHEET 2 AC 5 GLY A 303 GLY A 307 -1 O THR A 305 N ASN A 298
SHEET 3 AC 5 ILE A 410 PRO A 417 -1 O VAL A 414 N LEU A 306
SHEET 4 AC 5 THR A 378 LEU A 382 -1 O THR A 378 N ASN A 415
SHEET 5 AC 5 LYS A 387 PRO A 391 -1 O ARG A 388 N LEU A 381
SHEET 1 AD 4 GLU A 423 GLN A 430 0
SHEET 2 AD 4 VAL A 441 PHE A 448 -1 O VAL A 441 N GLN A 430
SHEET 3 AD 4 GLU A 458 GLY A 464 -1 O GLU A 458 N PHE A 448
SHEET 4 AD 4 ILE A 471 CYS A 472 -1 O ILE A 471 N TYR A 463
SHEET 1 AE 5 CYS A 562 LYS A 566 0
SHEET 2 AE 5 GLU A1247 LEU A1252 1 O LEU A1248 N THR A 564
SHEET 3 AE 5 HIS A1180 ASP A1190 1 O ILE A1183 N GLU A1247
SHEET 4 AE 5 TYR A1161 ASP A1174 -1 O TYR A1164 N ASP A1190
SHEET 5 AE 5 LYS A1003 VAL A1016 -1 O LYS A1004 N ILE A1173
SHEET 1 AF 8 VAL A 638 MET A 642 0
SHEET 2 AF 8 LEU A 674 ALA A 680 -1 O ALA A 677 N MET A 642
SHEET 3 AF 8 LEU A 610 THR A 616 -1 O PHE A 611 N ALA A 680
SHEET 4 AF 8 VAL A 832 VAL A 835 1 O ARG A 833 N LEU A 612
SHEET 5 AF 8 SER A 757 PRO A 762 -1 O MET A 758 N CYS A 834
SHEET 6 AF 8 MET A 769 VAL A 773 -1 O ASP A 770 N VAL A 761
SHEET 7 AF 8 VAL A 796 VAL A 800 1 O MET A 797 N VAL A 771
SHEET 8 AF 8 THR A1075 SER A1076 -1 O THR A1075 N VAL A 800
SHEET 1 AG 3 LYS A 667 VAL A 668 0
SHEET 2 AG 3 ALA A 622 ASP A 628 -1 O ALA A 622 N VAL A 668
SHEET 3 AG 3 LYS A 694 ASP A 699 -1 O LYS A 694 N ASP A 628
SHEET 1 AH 5 ARG A 721 TYR A 725 0
SHEET 2 AH 5 ASN A 902 ARG A 911 -1 O LEU A 903 N TYR A 725
SHEET 3 AH 5 ILE A 865 GLY A 877 1 O LEU A 866 N ASN A 902
SHEET 4 AH 5 TYR A 851 PHE A 859 -1 O LEU A 852 N TYR A 873
SHEET 5 AH 5 GLN A 737 MET A 745 -1 O GLN A 737 N PHE A 859
SHEET 1 AI 2 ILE A 959 GLN A 961 0
SHEET 2 AI 2 GLU A 967 ASN A 969 -1 O ILE A 968 N ASP A 960
SHEET 1 AJ 4 VAL A1070 HIS A1071 0
SHEET 2 AJ 4 VAL A1038 HIS A1042 1 O VAL A1038 N HIS A1071
SHEET 3 AJ 4 ALA A1026 ILE A1032 -1 O LEU A1029 N THR A1041
SHEET 4 AJ 4 SER A1137 PHE A1142 -1 O ALA A1138 N VAL A1030
SHEET 1 AK 2 ASP A1148 ASN A1150 0
SHEET 2 AK 2 GLU A1155 GLN A1157 -1 O GLU A1155 N ASN A1150
SHEET 1 AL 2 ASN A1221 TYR A1222 0
SHEET 2 AL 2 LEU A1228 HIS A1229 -1 O HIS A1229 N ASN A1221
LINK SG CYS A 49 FE1 FES A3002 1555 1555 2.32
LINK SG CYS A 52 FE2 FES A3002 1555 1555 2.08
LINK SG CYS A 74 FE2 FES A3002 1555 1555 2.52
LINK SG CYS A 114 FE2 FES A3001 1555 1555 2.41
LINK SG CYS A 117 FE1 FES A3001 1555 1555 2.09
LINK SG CYS A 149 FE1 FES A3001 1555 1555 2.42
LINK SG CYS A 151 FE2 FES A3001 1555 1555 2.44
LINK S2' MTE A3003 MO MOS A3004 1555 1555 2.46
LINK S1' MTE A3003 MO MOS A3004 1555 1555 2.43
CISPEP 1 GLU A 701 PRO A 702 0 1.35
CISPEP 2 SER A 1304 PRO A 1305 0 1.27
SITE 1 AC1 8 GLN A 113 CYS A 114 GLY A 115 CYS A 117
SITE 2 AC1 8 CYS A 149 ARG A 150 CYS A 151 MET A 753
SITE 1 AC2 8 GLY A 43 CYS A 44 GLY A 45 GLY A 47
SITE 2 AC2 8 CYS A 49 GLY A 50 CYS A 52 CYS A 74
SITE 1 AC3 18 GLN A 113 CYS A 151 GLY A 805 ALA A 806
SITE 2 AC3 18 PHE A 807 ARG A 921 MET A1047 GLY A1048
SITE 3 AC3 18 GLN A1049 GLY A1087 GLY A1088 SER A1089
SITE 4 AC3 18 VAL A1090 VAL A1091 ALA A1092 GLN A1203
SITE 5 AC3 18 LEU A1268 MOS A3004
SITE 1 AC4 8 GLN A 776 GLY A 808 PHE A 920 ARG A 921
SITE 2 AC4 8 GLY A1087 GLY A1088 GLU A1270 MTE A3003
SITE 1 AC5 24 GLY A 46 GLY A 47 PRO A 263 VAL A 264
SITE 2 AC5 24 MET A 266 GLY A 267 ASN A 268 THR A 269
SITE 3 AC5 24 SER A 270 VAL A 271 LEU A 344 ALA A 345
SITE 4 AC5 24 ALA A 353 SER A 354 GLY A 357 HIS A 358
SITE 5 AC5 24 ILE A 360 SER A 361 HIS A 363 SER A 366
SITE 6 AC5 24 ASP A 367 ILE A 410 LEU A 411 LEU A 438
SITE 1 AC6 8 ARG A 32 LYS A 33 THR A 38 ASP A 601
SITE 2 AC6 8 MET A 603 LEU A 605 ARG A 833 HOH A2019
SITE 1 AC7 9 CYS A 44 GLY A 48 CYS A 49 LEU A 148
SITE 2 AC7 9 ARG A 433 PHE A 751 TYR A1236 LYS A1237
SITE 3 AC7 9 ILE A1238
CRYST1 148.930 148.930 133.250 90.00 90.00 90.00 P 42 21 2 8
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 0.006715 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007505 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
