HEADER OXIDOREDUCTASE 17-APR-15 5A02
TITLE CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER
TITLE 2 CRESCENTUS COMPLEXED WITH GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE-ALDOSE OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 1.1.99.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULOBACTER CRESCENTUS CB15;
SOURCE 3 ORGANISM_TAXID: 190650;
SOURCE 4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TABERMAN,J.ROUVINEN,T.PARKKINEN
REVDAT 4 10-JAN-24 5A02 1 REMARK
REVDAT 3 09-DEC-15 5A02 1 JRNL
REVDAT 2 25-NOV-15 5A02 1 SOURCE
REVDAT 1 21-OCT-15 5A02 0
JRNL AUTH H.TABERMAN,M.ANDBERG,A.KOIVULA,N.HAKULINEN,M.PENTTILA,
JRNL AUTH 2 J.ROUVINEN,T.PARKKINEN
JRNL TITL STRUCTURE AND FUNCTION OF CAULOBACTER CRESCENTUS
JRNL TITL 2 ALDOSE-ALDOSE OXIDOREDUCTASE.
JRNL REF BIOCHEM.J. V. 472 297 2015
JRNL REFN ISSN 0264-6021
JRNL PMID 26438878
JRNL DOI 10.1042/BJ20150681
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 208065
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10403
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.2403 - 6.2102 0.99 6700 353 0.1676 0.1745
REMARK 3 2 6.2102 - 4.9308 0.99 6619 348 0.1724 0.1859
REMARK 3 3 4.9308 - 4.3079 1.00 6622 348 0.1327 0.1477
REMARK 3 4 4.3079 - 3.9142 1.00 6606 348 0.1266 0.1368
REMARK 3 5 3.9142 - 3.6338 0.99 6608 348 0.1300 0.1545
REMARK 3 6 3.6338 - 3.4196 1.00 6592 347 0.1362 0.1722
REMARK 3 7 3.4196 - 3.2484 1.00 6609 348 0.1412 0.1606
REMARK 3 8 3.2484 - 3.1070 1.00 6610 348 0.1442 0.1682
REMARK 3 9 3.1070 - 2.9874 1.00 6587 346 0.1508 0.1762
REMARK 3 10 2.9874 - 2.8843 1.00 6596 348 0.1613 0.2028
REMARK 3 11 2.8843 - 2.7942 1.00 6594 347 0.1595 0.1844
REMARK 3 12 2.7942 - 2.7143 0.99 6603 347 0.1581 0.2117
REMARK 3 13 2.7143 - 2.6429 1.00 6549 345 0.1675 0.2133
REMARK 3 14 2.6429 - 2.5784 1.00 6629 349 0.1646 0.2057
REMARK 3 15 2.5784 - 2.5198 1.00 6567 345 0.1646 0.1862
REMARK 3 16 2.5198 - 2.4661 1.00 6577 346 0.1714 0.2221
REMARK 3 17 2.4661 - 2.4168 1.00 6594 348 0.1739 0.2145
REMARK 3 18 2.4168 - 2.3712 1.00 6610 347 0.1727 0.2057
REMARK 3 19 2.3712 - 2.3289 1.00 6568 346 0.1722 0.2105
REMARK 3 20 2.3289 - 2.2894 1.00 6579 346 0.1774 0.2112
REMARK 3 21 2.2894 - 2.2525 1.00 6572 346 0.1734 0.2180
REMARK 3 22 2.2525 - 2.2178 0.99 6619 349 0.1817 0.2154
REMARK 3 23 2.2178 - 2.1852 1.00 6526 343 0.1814 0.2029
REMARK 3 24 2.1852 - 2.1544 1.00 6578 346 0.1826 0.2211
REMARK 3 25 2.1544 - 2.1253 1.00 6649 350 0.1923 0.2355
REMARK 3 26 2.1253 - 2.0977 1.00 6548 345 0.1974 0.2267
REMARK 3 27 2.0977 - 2.0715 1.00 6530 344 0.2054 0.2470
REMARK 3 28 2.0715 - 2.0465 1.00 6623 348 0.2067 0.2513
REMARK 3 29 2.0465 - 2.0227 1.00 6556 345 0.2215 0.2505
REMARK 3 30 2.0227 - 2.0000 0.98 6442 339 0.2369 0.2502
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.11
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 : 0.008 16326
REMARK 3 ANGLE : 1.073 22158
REMARK 3 CHIRALITY : 0.045 2384
REMARK 3 PLANARITY : 0.005 2884
REMARK 3 DIHEDRAL : 13.392 6076
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 5A02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208164
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1H6A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, MAGNESIUM SULPHATE,
REMARK 280 GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 76.79500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 7140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 ALA A 1
REMARK 465 GLN A 2
REMARK 465 PRO A 3
REMARK 465 GLY A 4
REMARK 465 ALA B 1
REMARK 465 GLN B 2
REMARK 465 PRO B 3
REMARK 465 GLY B 4
REMARK 465 ALA C 1
REMARK 465 GLN C 2
REMARK 465 PRO C 3
REMARK 465 GLY C 4
REMARK 465 ALA D 1
REMARK 465 GLN D 2
REMARK 465 PRO D 3
REMARK 465 GLY D 4
REMARK 465 ALA E 1
REMARK 465 GLN E 2
REMARK 465 PRO E 3
REMARK 465 GLY E 4
REMARK 465 ALA F 1
REMARK 465 GLN F 2
REMARK 465 PRO F 3
REMARK 465 GLY F 4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2055 O HOH B 2168 1.95
REMARK 500 O HOH A 2079 O HOH A 2190 1.96
REMARK 500 O HOH C 2066 O HOH C 2180 2.10
REMARK 500 O HOH E 2137 O HOH E 2138 2.12
REMARK 500 O HOH E 2005 O HOH E 2012 2.12
REMARK 500 O HOH F 2069 O HOH F 2203 2.13
REMARK 500 O HOH C 2079 O HOH C 2218 2.13
REMARK 500 O HOH B 2101 O HOH F 2124 2.13
REMARK 500 O HOH B 2266 O HOH F 2010 2.13
REMARK 500 NE ARG F 332 O HOH F 2219 2.15
REMARK 500 O HOH A 2097 O HOH A 2233 2.15
REMARK 500 O HOH F 2183 O HOH F 2206 2.16
REMARK 500 O HOH A 2277 O HOH B 2163 2.17
REMARK 500 O HOH D 2034 O HOH D 2095 2.19
REMARK 500 O HOH B 2212 O HOH B 2213 2.19
REMARK 500 O HOH A 2090 O HOH A 2213 2.19
REMARK 500 O HOH B 2132 O HOH B 2133 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 223 -74.95 -87.46
REMARK 500 ASN A 248 97.01 -164.85
REMARK 500 ASP A 262 105.92 -160.92
REMARK 500 ASP B 167 103.49 -30.63
REMARK 500 ILE B 186 -34.18 -131.25
REMARK 500 ASP B 223 -74.85 -91.73
REMARK 500 ASN B 248 95.54 -160.80
REMARK 500 LEU B 276 57.64 -119.36
REMARK 500 ILE C 186 -37.13 -130.22
REMARK 500 ASP C 223 -73.23 -91.46
REMARK 500 LEU C 276 -85.40 -126.15
REMARK 500 ASP D 223 -75.00 -88.94
REMARK 500 LEU D 276 -84.89 -122.53
REMARK 500 ASP E 223 -76.83 -87.22
REMARK 500 ASN E 248 94.71 -160.75
REMARK 500 ASP F 167 109.27 -45.09
REMARK 500 ASP F 223 -75.79 -86.94
REMARK 500 ASN F 248 95.58 -164.15
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 NAP A 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP F 1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1346
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A03 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER
REMARK 900 CRESCENTUS COMPLEXED WITH XYLOSE
REMARK 900 RELATED ID: 5A04 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER
REMARK 900 CRESCENTUS COMPLEXED WITH GLUCOSE
REMARK 900 RELATED ID: 5A05 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER
REMARK 900 CRESCENTUS COMPLEXED WITH MALTOTRIOSE
REMARK 900 RELATED ID: 5A06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER
REMARK 900 CRESCENTUS COMPLEXED WITH SORBITOL
DBREF 5A02 A 1 339 PDB 5A02 5A02 1 339
DBREF 5A02 B 1 339 PDB 5A02 5A02 1 339
DBREF 5A02 C 1 339 PDB 5A02 5A02 1 339
DBREF 5A02 D 1 339 PDB 5A02 5A02 1 339
DBREF 5A02 E 1 339 PDB 5A02 5A02 1 339
DBREF 5A02 F 1 339 PDB 5A02 5A02 1 339
SEQRES 1 A 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 A 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 A 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 A 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 A 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 A 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 A 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 A 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 A 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 A 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 A 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 A 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 A 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 A 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 A 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 A 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 A 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 A 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 A 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 A 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 A 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 A 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 A 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 A 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 A 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 A 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 A 339 LEU
SEQRES 1 B 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 B 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 B 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 B 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 B 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 B 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 B 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 B 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 B 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 B 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 B 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 B 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 B 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 B 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 B 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 B 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 B 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 B 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 B 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 B 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 B 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 B 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 B 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 B 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 B 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 B 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 B 339 LEU
SEQRES 1 C 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 C 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 C 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 C 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 C 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 C 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 C 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 C 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 C 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 C 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 C 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 C 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 C 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 C 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 C 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 C 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 C 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 C 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 C 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 C 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 C 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 C 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 C 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 C 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 C 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 C 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 C 339 LEU
SEQRES 1 D 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 D 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 D 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 D 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 D 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 D 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 D 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 D 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 D 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 D 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 D 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 D 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 D 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 D 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 D 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 D 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 D 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 D 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 D 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 D 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 D 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 D 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 D 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 D 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 D 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 D 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 D 339 LEU
SEQRES 1 E 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 E 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 E 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 E 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 E 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 E 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 E 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 E 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 E 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 E 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 E 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 E 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 E 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 E 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 E 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 E 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 E 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 E 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 E 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 E 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 E 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 E 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 E 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 E 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 E 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 E 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 E 339 LEU
SEQRES 1 F 339 ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY
SEQRES 2 F 339 LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE
SEQRES 3 F 339 ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER
SEQRES 4 F 339 GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR
SEQRES 5 F 339 GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE
SEQRES 6 F 339 ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR
SEQRES 7 F 339 VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU
SEQRES 8 F 339 ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS
SEQRES 9 F 339 PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE
SEQRES 10 F 339 ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY
SEQRES 11 F 339 TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE
SEQRES 12 F 339 LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR
SEQRES 13 F 339 VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS
SEQRES 14 F 339 GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER
SEQRES 15 F 339 LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG
SEQRES 16 F 339 TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL
SEQRES 17 F 339 GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL
SEQRES 18 F 339 GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY
SEQRES 19 F 339 ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS
SEQRES 20 F 339 ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU
SEQRES 21 F 339 ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG
SEQRES 22 F 339 ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA
SEQRES 23 F 339 PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS
SEQRES 24 F 339 LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL
SEQRES 25 F 339 GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU
SEQRES 26 F 339 ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS
SEQRES 27 F 339 LEU
HET NAP A1340 48
HET GOL A1341 6
HET GOL A1342 6
HET SO4 A1343 5
HET NAP B1340 48
HET GOL B1341 6
HET GOL B1342 6
HET NAP C1340 48
HET GOL C1341 6
HET SO4 C1342 5
HET SO4 C1343 5
HET SO4 C1344 5
HET NAP D1340 48
HET GOL D1341 6
HET GOL D1342 6
HET GOL D1343 6
HET SO4 D1344 5
HET SO4 D1345 5
HET NAP E1340 48
HET GOL E1341 6
HET GOL E1342 6
HET GOL E1343 6
HET GOL E1344 6
HET SO4 E1345 5
HET SO4 E1346 5
HET NAP F1340 48
HET GOL F1341 6
HET GOL F1342 6
HET GOL F1343 6
HET GOL F1344 6
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 NAP 6(C21 H28 N7 O17 P3)
FORMUL 8 GOL 16(C3 H8 O3)
FORMUL 10 SO4 8(O4 S 2-)
FORMUL 37 HOH *1550(H2 O)
HELIX 1 1 GLY A 15 ILE A 21 1 7
HELIX 2 2 ILE A 22 CYS A 29 5 8
HELIX 3 3 THR A 41 GLY A 53 1 13
HELIX 4 4 PRO A 55 THR A 57 5 3
HELIX 5 5 THR A 64 ASN A 71 5 8
HELIX 6 6 PRO A 82 SER A 84 5 3
HELIX 7 7 LEU A 85 ALA A 96 1 12
HELIX 8 8 THR A 109 ALA A 123 1 15
HELIX 9 9 TYR A 131 PHE A 135 5 5
HELIX 10 10 GLN A 136 ASP A 148 1 13
HELIX 11 11 GLN A 170 LEU A 173 5 4
HELIX 12 12 ASN A 174 GLY A 179 1 6
HELIX 13 13 GLY A 181 ILE A 186 1 6
HELIX 14 14 ILE A 186 GLY A 199 1 14
HELIX 15 15 ASN A 291 GLY A 307 1 17
HELIX 16 16 GLY A 313 GLY A 334 1 22
HELIX 17 17 GLY B 15 ILE B 21 1 7
HELIX 18 18 ILE B 22 CYS B 29 5 8
HELIX 19 19 THR B 41 GLY B 53 1 13
HELIX 20 20 PRO B 55 THR B 57 5 3
HELIX 21 21 THR B 64 ASN B 71 5 8
HELIX 22 22 PRO B 82 SER B 84 5 3
HELIX 23 23 LEU B 85 ALA B 96 1 12
HELIX 24 24 THR B 109 ALA B 123 1 15
HELIX 25 25 TYR B 131 PHE B 135 5 5
HELIX 26 26 GLN B 136 ASP B 148 1 13
HELIX 27 27 GLN B 170 LEU B 173 5 4
HELIX 28 28 ASN B 174 GLY B 179 1 6
HELIX 29 29 GLY B 181 ILE B 186 1 6
HELIX 30 30 ILE B 186 GLY B 199 1 14
HELIX 31 31 ASN B 291 GLY B 307 1 17
HELIX 32 32 GLY B 313 GLY B 334 1 22
HELIX 33 33 GLY C 15 ILE C 21 1 7
HELIX 34 34 ILE C 22 CYS C 29 5 8
HELIX 35 35 THR C 41 GLY C 53 1 13
HELIX 36 36 PRO C 55 THR C 57 5 3
HELIX 37 37 THR C 64 ASN C 71 5 8
HELIX 38 38 PRO C 82 SER C 84 5 3
HELIX 39 39 LEU C 85 ALA C 96 1 12
HELIX 40 40 THR C 109 ALA C 123 1 15
HELIX 41 41 TYR C 131 PHE C 135 5 5
HELIX 42 42 GLN C 136 ASP C 148 1 13
HELIX 43 43 GLN C 170 LEU C 173 5 4
HELIX 44 44 ASN C 174 GLY C 179 1 6
HELIX 45 45 GLY C 181 ILE C 186 1 6
HELIX 46 46 ILE C 186 GLY C 199 1 14
HELIX 47 47 ASN C 291 GLY C 307 1 17
HELIX 48 48 GLY C 313 GLY C 334 1 22
HELIX 49 49 GLY D 15 ILE D 21 1 7
HELIX 50 50 ILE D 22 CYS D 29 5 8
HELIX 51 51 THR D 41 GLY D 53 1 13
HELIX 52 52 PRO D 55 THR D 57 5 3
HELIX 53 53 THR D 64 ASN D 71 5 8
HELIX 54 54 PRO D 82 SER D 84 5 3
HELIX 55 55 LEU D 85 ALA D 96 1 12
HELIX 56 56 THR D 109 ALA D 123 1 15
HELIX 57 57 TYR D 131 PHE D 135 5 5
HELIX 58 58 GLN D 136 ASP D 148 1 13
HELIX 59 59 GLN D 170 LEU D 173 5 4
HELIX 60 60 ASN D 174 GLY D 179 1 6
HELIX 61 61 GLY D 181 ILE D 186 1 6
HELIX 62 62 ILE D 186 GLY D 199 1 14
HELIX 63 63 ASN D 291 GLY D 307 1 17
HELIX 64 64 GLY D 313 GLY D 334 1 22
HELIX 65 65 GLY E 15 ILE E 21 1 7
HELIX 66 66 ILE E 22 CYS E 29 5 8
HELIX 67 67 THR E 41 TYR E 52 1 12
HELIX 68 68 PRO E 55 THR E 57 5 3
HELIX 69 69 THR E 64 ASN E 71 5 8
HELIX 70 70 PRO E 82 SER E 84 5 3
HELIX 71 71 LEU E 85 ALA E 96 1 12
HELIX 72 72 THR E 109 ALA E 123 1 15
HELIX 73 73 TYR E 131 PHE E 135 5 5
HELIX 74 74 GLN E 136 GLY E 149 1 14
HELIX 75 75 GLN E 170 LEU E 173 5 4
HELIX 76 76 ASN E 174 GLY E 179 1 6
HELIX 77 77 GLY E 181 ILE E 186 1 6
HELIX 78 78 ILE E 186 GLY E 199 1 14
HELIX 79 79 ASN E 291 GLY E 307 1 17
HELIX 80 80 GLY E 313 GLY E 334 1 22
HELIX 81 81 GLY F 15 ILE F 21 1 7
HELIX 82 82 ILE F 22 CYS F 29 5 8
HELIX 83 83 THR F 41 GLY F 53 1 13
HELIX 84 84 PRO F 55 THR F 57 5 3
HELIX 85 85 THR F 64 ASN F 71 5 8
HELIX 86 86 PRO F 82 SER F 84 5 3
HELIX 87 87 LEU F 85 ALA F 96 1 12
HELIX 88 88 THR F 109 GLY F 124 1 16
HELIX 89 89 TYR F 131 PHE F 135 5 5
HELIX 90 90 GLN F 136 ASP F 148 1 13
HELIX 91 91 GLN F 170 LEU F 173 5 4
HELIX 92 92 ASN F 174 GLY F 179 1 6
HELIX 93 93 GLY F 181 ILE F 186 1 6
HELIX 94 94 ILE F 186 GLY F 199 1 14
HELIX 95 95 ASN F 291 GLY F 307 1 17
HELIX 96 96 GLY F 313 GLY F 334 1 22
SHEET 1 AA 6 ARG A 59 TYR A 60 0
SHEET 2 AA 6 SER A 32 VAL A 38 1 O LEU A 37 N TYR A 60
SHEET 3 AA 6 LEU A 7 LEU A 12 1 O LEU A 7 N ARG A 33
SHEET 4 AA 6 ILE A 76 VAL A 79 1 O ILE A 76 N ALA A 10
SHEET 5 AA 6 HIS A 99 CYS A 102 1 O HIS A 99 N VAL A 77
SHEET 6 AA 6 LEU A 127 ILE A 129 1 O MET A 128 N CYS A 102
SHEET 1 AB 9 ALA A 281 PRO A 282 0
SHEET 2 AB 9 MET A 272 GLN A 275 -1 O ALA A 274 N ALA A 281
SHEET 3 AB 9 GLY A 257 ILE A 261 -1 O TRP A 258 N GLN A 275
SHEET 4 AB 9 CYS A 247 GLY A 254 -1 O TYR A 250 N ILE A 261
SHEET 5 AB 9 THR A 156 GLY A 162 -1 O THR A 156 N SER A 253
SHEET 6 AB 9 THR A 236 ALA A 242 1 O THR A 236 N VAL A 157
SHEET 7 AB 9 ILE A 224 LEU A 230 -1 N ILE A 225 O SER A 241
SHEET 8 AB 9 ALA A 204 SER A 210 -1 O ALA A 204 N LEU A 230
SHEET 9 AB 9 VAL A 337 LYS A 338 -1 O VAL A 337 N VAL A 205
SHEET 1 BA 6 ARG B 59 TYR B 60 0
SHEET 2 BA 6 SER B 32 VAL B 38 1 O LEU B 37 N TYR B 60
SHEET 3 BA 6 LEU B 7 LEU B 12 1 O LEU B 7 N ARG B 33
SHEET 4 BA 6 ILE B 76 VAL B 79 1 O ILE B 76 N ALA B 10
SHEET 5 BA 6 HIS B 99 CYS B 102 1 O HIS B 99 N VAL B 77
SHEET 6 BA 6 LEU B 127 ILE B 129 1 O MET B 128 N CYS B 102
SHEET 1 BB 9 ALA B 281 PRO B 282 0
SHEET 2 BB 9 MET B 272 GLN B 275 -1 O ALA B 274 N ALA B 281
SHEET 3 BB 9 GLY B 257 ILE B 261 -1 O TRP B 258 N GLN B 275
SHEET 4 BB 9 CYS B 247 GLY B 254 -1 O TYR B 250 N ILE B 261
SHEET 5 BB 9 THR B 156 GLY B 162 -1 O THR B 156 N SER B 253
SHEET 6 BB 9 THR B 236 ALA B 242 1 O THR B 236 N VAL B 157
SHEET 7 BB 9 ILE B 224 LEU B 230 -1 N ILE B 225 O SER B 241
SHEET 8 BB 9 ALA B 204 SER B 210 -1 O ALA B 204 N LEU B 230
SHEET 9 BB 9 VAL B 337 LYS B 338 -1 O VAL B 337 N VAL B 205
SHEET 1 CA 6 ARG C 59 TYR C 60 0
SHEET 2 CA 6 SER C 32 VAL C 38 1 O LEU C 37 N TYR C 60
SHEET 3 CA 6 LEU C 7 LEU C 12 1 O LEU C 7 N ARG C 33
SHEET 4 CA 6 ILE C 76 VAL C 79 1 O ILE C 76 N ALA C 10
SHEET 5 CA 6 HIS C 99 CYS C 102 1 O HIS C 99 N VAL C 77
SHEET 6 CA 6 LEU C 127 ILE C 129 1 O MET C 128 N CYS C 102
SHEET 1 CB 9 ALA C 281 PRO C 282 0
SHEET 2 CB 9 MET C 272 GLN C 275 -1 O ALA C 274 N ALA C 281
SHEET 3 CB 9 GLY C 257 ILE C 261 -1 O TRP C 258 N GLN C 275
SHEET 4 CB 9 CYS C 247 GLY C 254 -1 O TYR C 250 N ILE C 261
SHEET 5 CB 9 THR C 156 GLY C 162 -1 O THR C 156 N SER C 253
SHEET 6 CB 9 THR C 236 ALA C 242 1 O THR C 236 N VAL C 157
SHEET 7 CB 9 ILE C 224 LEU C 230 -1 N ILE C 225 O SER C 241
SHEET 8 CB 9 ALA C 204 SER C 210 -1 O ALA C 204 N LEU C 230
SHEET 9 CB 9 VAL C 337 LYS C 338 -1 O VAL C 337 N VAL C 205
SHEET 1 DA 6 ARG D 59 TYR D 60 0
SHEET 2 DA 6 SER D 32 VAL D 38 1 O LEU D 37 N TYR D 60
SHEET 3 DA 6 LEU D 7 LEU D 12 1 O LEU D 7 N ARG D 33
SHEET 4 DA 6 ILE D 76 VAL D 79 1 O ILE D 76 N ALA D 10
SHEET 5 DA 6 HIS D 99 CYS D 102 1 O HIS D 99 N VAL D 77
SHEET 6 DA 6 LEU D 127 ILE D 129 1 O MET D 128 N CYS D 102
SHEET 1 DB 9 ALA D 281 PRO D 282 0
SHEET 2 DB 9 MET D 272 GLN D 275 -1 O ALA D 274 N ALA D 281
SHEET 3 DB 9 GLY D 257 ILE D 261 -1 O TRP D 258 N GLN D 275
SHEET 4 DB 9 CYS D 247 GLY D 254 -1 O TYR D 250 N ILE D 261
SHEET 5 DB 9 THR D 156 GLY D 162 -1 O THR D 156 N SER D 253
SHEET 6 DB 9 THR D 236 ALA D 242 1 O THR D 236 N VAL D 157
SHEET 7 DB 9 ILE D 224 LEU D 230 -1 N ILE D 225 O SER D 241
SHEET 8 DB 9 ALA D 204 SER D 210 -1 O ALA D 204 N LEU D 230
SHEET 9 DB 9 VAL D 337 LYS D 338 -1 O VAL D 337 N VAL D 205
SHEET 1 EA 6 ARG E 59 TYR E 60 0
SHEET 2 EA 6 SER E 32 VAL E 38 1 O LEU E 37 N TYR E 60
SHEET 3 EA 6 LEU E 7 LEU E 12 1 O LEU E 7 N ARG E 33
SHEET 4 EA 6 ILE E 76 VAL E 79 1 O ILE E 76 N ALA E 10
SHEET 5 EA 6 HIS E 99 CYS E 102 1 O HIS E 99 N VAL E 77
SHEET 6 EA 6 LEU E 127 ILE E 129 1 O MET E 128 N CYS E 102
SHEET 1 EB 9 ALA E 281 ARG E 283 0
SHEET 2 EB 9 MET E 272 LEU E 276 -1 O MET E 272 N ARG E 283
SHEET 3 EB 9 GLY E 257 ILE E 261 -1 O TRP E 258 N GLN E 275
SHEET 4 EB 9 CYS E 247 GLY E 254 -1 O TYR E 250 N ILE E 261
SHEET 5 EB 9 THR E 156 GLY E 162 -1 O THR E 156 N SER E 253
SHEET 6 EB 9 THR E 236 ALA E 242 1 O THR E 236 N VAL E 157
SHEET 7 EB 9 ILE E 224 LEU E 230 -1 N ILE E 225 O SER E 241
SHEET 8 EB 9 ALA E 204 SER E 210 -1 O ALA E 204 N LEU E 230
SHEET 9 EB 9 VAL E 337 LYS E 338 -1 O VAL E 337 N VAL E 205
SHEET 1 FA 6 ARG F 59 TYR F 60 0
SHEET 2 FA 6 SER F 32 VAL F 38 1 O LEU F 37 N TYR F 60
SHEET 3 FA 6 LEU F 7 LEU F 12 1 O LEU F 7 N ARG F 33
SHEET 4 FA 6 ILE F 76 VAL F 79 1 O ILE F 76 N ALA F 10
SHEET 5 FA 6 HIS F 99 CYS F 102 1 O HIS F 99 N VAL F 77
SHEET 6 FA 6 LEU F 127 ILE F 129 1 O MET F 128 N CYS F 102
SHEET 1 FB 9 ALA F 281 PRO F 282 0
SHEET 2 FB 9 MET F 272 LEU F 276 -1 O ALA F 274 N ALA F 281
SHEET 3 FB 9 GLY F 257 ILE F 261 -1 O TRP F 258 N GLN F 275
SHEET 4 FB 9 CYS F 247 GLY F 254 -1 O TYR F 250 N ILE F 261
SHEET 5 FB 9 THR F 156 GLY F 162 -1 O THR F 156 N SER F 253
SHEET 6 FB 9 THR F 236 ALA F 242 1 O THR F 236 N VAL F 157
SHEET 7 FB 9 ILE F 224 LEU F 230 -1 N ILE F 225 O SER F 241
SHEET 8 FB 9 ALA F 204 SER F 210 -1 O ALA F 204 N LEU F 230
SHEET 9 FB 9 VAL F 337 LYS F 338 -1 O VAL F 337 N VAL F 205
CISPEP 1 LYS A 104 PRO A 105 0 -15.60
CISPEP 2 ASP A 262 PRO A 263 0 0.62
CISPEP 3 LYS B 104 PRO B 105 0 -12.89
CISPEP 4 ASP B 262 PRO B 263 0 -1.05
CISPEP 5 LYS C 104 PRO C 105 0 -13.01
CISPEP 6 ASP C 262 PRO C 263 0 0.59
CISPEP 7 LYS D 104 PRO D 105 0 -15.62
CISPEP 8 ASP D 262 PRO D 263 0 -0.35
CISPEP 9 LYS E 104 PRO E 105 0 -13.98
CISPEP 10 ASP E 262 PRO E 263 0 1.14
CISPEP 11 LYS F 104 PRO F 105 0 -11.93
CISPEP 12 ASP F 262 PRO F 263 0 2.12
SITE 1 AC1 36 GLY A 13 LEU A 14 GLY A 15 TYR A 16
SITE 2 AC1 36 TYR A 17 SER A 39 GLY A 40 THR A 41
SITE 3 AC1 36 LYS A 44 TYR A 62 ILE A 80 THR A 81
SITE 4 AC1 36 PRO A 82 ASN A 83 LEU A 85 HIS A 86
SITE 5 AC1 36 GLU A 103 LYS A 104 GLY A 130 ARG A 132
SITE 6 AC1 36 TRP A 171 ARG A 172 TYR A 189 TYR A 267
SITE 7 AC1 36 GOL A1341 HOH A2002 HOH A2009 HOH A2045
SITE 8 AC1 36 HOH A2101 HOH A2147 HOH A2191 HOH A2193
SITE 9 AC1 36 HOH A2311 HOH A2312 HOH A2313 HOH A2314
SITE 1 AC2 38 GLY B 13 LEU B 14 GLY B 15 TYR B 16
SITE 2 AC2 38 TYR B 17 SER B 39 GLY B 40 THR B 41
SITE 3 AC2 38 LYS B 44 TYR B 62 ILE B 80 THR B 81
SITE 4 AC2 38 PRO B 82 ASN B 83 LEU B 85 HIS B 86
SITE 5 AC2 38 GLU B 103 LYS B 104 GLY B 130 ARG B 132
SITE 6 AC2 38 TRP B 171 ARG B 172 TYR B 189 TYR B 267
SITE 7 AC2 38 GOL B1342 HOH B2002 HOH B2005 HOH B2025
SITE 8 AC2 38 HOH B2076 HOH B2169 HOH B2172 HOH B2288
SITE 9 AC2 38 HOH B2289 HOH B2290 HOH B2291 ASP C 66
SITE 10 AC2 38 HOH C2054 HOH C2056
SITE 1 AC3 37 GLU B 63 HOH B2059 HOH B2061 GLY C 13
SITE 2 AC3 37 LEU C 14 GLY C 15 TYR C 16 TYR C 17
SITE 3 AC3 37 SER C 39 GLY C 40 THR C 41 LYS C 44
SITE 4 AC3 37 TYR C 62 ILE C 80 THR C 81 PRO C 82
SITE 5 AC3 37 ASN C 83 LEU C 85 HIS C 86 GLU C 103
SITE 6 AC3 37 LYS C 104 PRO C 105 GLY C 130 ARG C 132
SITE 7 AC3 37 TRP C 171 ARG C 172 TYR C 189 TYR C 267
SITE 8 AC3 37 GOL C1341 SO4 C1344 HOH C2003 HOH C2006
SITE 9 AC3 37 HOH C2025 HOH C2070 HOH C2152 HOH C2273
SITE 10 AC3 37 HOH C2274
SITE 1 AC4 31 LEU D 14 GLY D 15 TYR D 16 TYR D 17
SITE 2 AC4 31 SER D 39 GLY D 40 THR D 41 LYS D 44
SITE 3 AC4 31 TYR D 62 ILE D 80 THR D 81 PRO D 82
SITE 4 AC4 31 ASN D 83 LEU D 85 HIS D 86 GLU D 103
SITE 5 AC4 31 LYS D 104 GLY D 130 ARG D 132 TRP D 171
SITE 6 AC4 31 ARG D 172 TYR D 189 TYR D 267 GOL D1341
SITE 7 AC4 31 HOH D2002 HOH D2006 HOH D2060 HOH D2135
SITE 8 AC4 31 HOH D2138 HOH D2211 HOH D2212
SITE 1 AC5 34 GLY E 13 LEU E 14 GLY E 15 TYR E 16
SITE 2 AC5 34 TYR E 17 SER E 39 GLY E 40 THR E 41
SITE 3 AC5 34 LYS E 44 TYR E 62 ILE E 80 THR E 81
SITE 4 AC5 34 PRO E 82 ASN E 83 LEU E 85 HIS E 86
SITE 5 AC5 34 GLU E 103 LYS E 104 GLY E 130 ARG E 132
SITE 6 AC5 34 TRP E 171 ARG E 172 TYR E 189 TYR E 267
SITE 7 AC5 34 GOL E1341 SO4 E1346 HOH E2001 HOH E2006
SITE 8 AC5 34 HOH E2052 HOH E2129 HOH E2131 HOH E2214
SITE 9 AC5 34 HOH E2215 HOH E2216
SITE 1 AC6 37 LEU F 14 GLY F 15 TYR F 16 TYR F 17
SITE 2 AC6 37 SER F 39 GLY F 40 THR F 41 LYS F 44
SITE 3 AC6 37 TYR F 62 ILE F 80 THR F 81 PRO F 82
SITE 4 AC6 37 ASN F 83 LEU F 85 HIS F 86 GLU F 103
SITE 5 AC6 37 LYS F 104 GLY F 130 ARG F 132 TRP F 171
SITE 6 AC6 37 ARG F 172 TYR F 189 TYR F 267 GOL F1342
SITE 7 AC6 37 HOH F2002 HOH F2005 HOH F2025 HOH F2055
SITE 8 AC6 37 HOH F2090 HOH F2133 HOH F2136 HOH F2223
SITE 9 AC6 37 HOH F2224 HOH F2225 HOH F2226 HOH F2227
SITE 10 AC6 37 HOH F2228
SITE 1 AC7 6 HIS F 138 MET F 272 ARG F 283 GLU F 284
SITE 2 AC7 6 HOH F2192 HOH F2230
SITE 1 AC8 7 LYS F 104 PHE F 163 ARG F 172 ASP F 185
SITE 2 AC8 7 TYR F 189 NAP F1340 HOH F2135
SITE 1 AC9 9 HIS B 138 GLN B 270 ALA B 271 MET B 272
SITE 2 AC9 9 PRO B 282 ARG B 283 GLU B 284 HOH B2248
SITE 3 AC9 9 PRO C 279
SITE 1 BC1 7 LYS C 104 PHE C 163 ARG C 172 ASP C 185
SITE 2 BC1 7 TYR C 189 NAP C1340 HOH C2275
SITE 1 BC2 7 LYS A 104 PHE A 163 ARG A 172 ASP A 185
SITE 2 BC2 7 TYR A 189 NAP A1340 HOH A2315
SITE 1 BC3 7 LYS D 104 PHE D 163 ARG D 172 ASP D 185
SITE 2 BC3 7 TYR D 189 NAP D1340 HOH D2137
SITE 1 BC4 7 LYS E 104 PHE E 163 ARG E 172 ASP E 185
SITE 2 BC4 7 TYR E 189 NAP E1340 HOH E2217
SITE 1 BC5 6 LEU A 230 LYS A 338 HOH A2308 GLU E 209
SITE 2 BC5 6 ALA E 331 HOH E2218
SITE 1 BC6 7 LYS B 104 PHE B 163 ARG B 172 ASP B 185
SITE 2 BC6 7 TYR B 189 NAP B1340 HOH B2171
SITE 1 BC7 7 TYR A 48 GLN A 51 HOH A2010 HOH A2011
SITE 2 BC7 7 HOH A2316 HOH A2317 PRO F 282
SITE 1 BC8 6 GLN E 136 ALA E 137 TYR E 267 GLN E 292
SITE 2 BC8 6 HOH E2095 HOH E2219
SITE 1 BC9 7 ARG A 155 PRO A 255 HOH A2174 ASP E 212
SITE 2 BC9 7 ASP E 215 SER E 244 HOH E2164
SITE 1 CC1 6 ARG B 155 HOH B2156 ASP D 212 ASP D 215
SITE 2 CC1 6 SER D 244 HOH D2167
SITE 1 CC2 8 ARG C 155 PRO C 255 HOH C2138 ASP F 212
SITE 2 CC2 8 ASP F 215 ARG F 217 SER F 244 HOH F2232
SITE 1 CC3 6 LYS C 338 HOH C2272 VAL F 208 GLU F 209
SITE 2 CC3 6 ALA F 331 HOH F2233
SITE 1 CC4 6 ARG B 251 TRP B 258 GLU B 260 ARG B 273
SITE 2 CC4 6 ASP D 262 PRO D 263
SITE 1 CC5 5 ILE E 165 GLY E 166 ASP E 167 GLN E 170
SITE 2 CC5 5 HOH E2128
SITE 1 CC6 3 LYS D 290 ASN D 291 HOH D2185
SITE 1 CC7 5 ILE A 165 GLY A 166 ASP A 167 GLN A 170
SITE 2 CC7 5 HOH A2189
SITE 1 CC8 4 ILE D 165 GLY D 166 ASP D 167 GLN D 170
SITE 1 CC9 4 ILE C 165 GLY C 166 ASP C 167 GLN C 170
SITE 1 DC1 4 GLU C 28 LYS C 290 ASN C 291 HOH C2248
SITE 1 DC2 6 HOH B2061 GLN C 170 TRP C 171 NAP C1340
SITE 2 DC2 6 HOH C2152 HOH C2274
SITE 1 DC3 6 GLN E 170 TRP E 171 NAP E1340 HOH E2126
SITE 2 DC3 6 HOH E2129 HOH E2216
CRYST1 101.310 153.590 108.010 90.00 109.85 90.00 P 1 21 1 12
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 0.009871 0.000000 0.003563 0.00000
SCALE2 0.000000 0.006511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009843 0.00000
MTRIX1 1 0.222400 -0.676100 -0.702400 70.85670 1
MTRIX2 1 -0.751400 -0.577900 0.318400 24.39160 1
MTRIX3 1 -0.621200 0.457000 -0.636600 63.42170 1
MTRIX1 2 -0.059300 -0.819800 0.569600 24.25470 1
MTRIX2 2 0.828600 -0.358600 -0.429900 -9.55710 1
MTRIX3 2 0.556700 0.446400 0.700600 -18.51880 1
MTRIX1 3 -0.199400 0.736600 -0.646200 58.40950 1
MTRIX2 3 0.660100 -0.588400 -0.467000 -2.96390 1
MTRIX3 3 -0.724300 -0.333400 -0.603600 66.63540 1
MTRIX1 4 -0.982500 0.186100 -0.011600 83.39430 1
MTRIX2 4 0.184200 0.958700 -0.216700 -2.63010 1
MTRIX3 4 -0.029200 -0.215000 -0.976200 47.09970 1
MTRIX1 5 -0.334800 0.543800 0.769600 16.62680 1
MTRIX2 5 -0.542300 -0.779100 0.314500 19.91380 1
MTRIX3 5 0.770600 -0.312100 0.555700 -21.50360 1
(ATOM LINES ARE NOT SHOWN.)
END