HEADER OXIDOREDUCTASE 12-APR-11 3RHQ
TITLE CRYSTAL STRUCTURE OF THE C707A MUTANT OF C-TERMINAL DOMAIN OF
TITLE 2 10'FORMYLTETRAHYDROFOLATE DEHYDROGENASE IN COMPLEX WITH NADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE DEHYDROGENASE 1 FAMILY, MEMBER L1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 397-902;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ALDH1L1, FTHFD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FDH, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TSYBOVSKY
REVDAT 3 13-SEP-23 3RHQ 1 REMARK SEQADV
REVDAT 2 31-AUG-11 3RHQ 1 JRNL VERSN
REVDAT 1 04-MAY-11 3RHQ 0
JRNL AUTH Y.TSYBOVSKY,S.A.KRUPENKO
JRNL TITL CONSERVED CATALYTIC RESIDUES OF THE ALDH1L1 ALDEHYDE
JRNL TITL 2 DEHYDROGENASE DOMAIN CONTROL BINDING AND DISCHARGING OF THE
JRNL TITL 3 COENZYME.
JRNL REF J.BIOL.CHEM. V. 286 23357 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21540484
JRNL DOI 10.1074/JBC.M111.221069
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 239423
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
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 : 12640
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17133
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 912
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 356
REMARK 3 SOLVENT ATOMS : 1971
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.78000
REMARK 3 B23 (A**2) : 0.00000
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): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.752
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16270 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22060 ; 1.213 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2007 ; 6.273 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 720 ;34.840 ;24.694
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2818 ;13.471 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 87 ;23.689 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2440 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12111 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 9933 ; 0.453 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16037 ; 0.871 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6337 ; 1.511 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6012 ; 2.462 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : D*TREK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 252151
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.60500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2O2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.0, 1.7M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 1.000000 0.000000 0.000000 129.27950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 97.13400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 129.27950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 97.13400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -447.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C1998 LIES ON A SPECIAL POSITION.
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 386
REMARK 465 ARG A 387
REMARK 465 GLY A 388
REMARK 465 SER A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 HIS A 393
REMARK 465 HIS A 394
REMARK 465 THR A 395
REMARK 465 THR A 396
REMARK 465 GLY A 397
REMARK 465 GLU A 398
REMARK 465 ASP A 399
REMARK 465 ASP A 400
REMARK 465 GLU A 401
REMARK 465 SER A 402
REMARK 465 GLU A 403
REMARK 465 CYS A 404
REMARK 465 MET B 386
REMARK 465 ARG B 387
REMARK 465 GLY B 388
REMARK 465 SER B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
REMARK 465 HIS B 393
REMARK 465 HIS B 394
REMARK 465 THR B 395
REMARK 465 THR B 396
REMARK 465 GLY B 397
REMARK 465 GLU B 398
REMARK 465 ASP B 399
REMARK 465 ASP B 400
REMARK 465 GLU B 401
REMARK 465 SER B 402
REMARK 465 GLU B 403
REMARK 465 CYS B 404
REMARK 465 MET C 386
REMARK 465 ARG C 387
REMARK 465 GLY C 388
REMARK 465 SER C 389
REMARK 465 HIS C 390
REMARK 465 HIS C 391
REMARK 465 HIS C 392
REMARK 465 HIS C 393
REMARK 465 HIS C 394
REMARK 465 THR C 395
REMARK 465 THR C 396
REMARK 465 GLY C 397
REMARK 465 GLU C 398
REMARK 465 ASP C 399
REMARK 465 ASP C 400
REMARK 465 GLU C 401
REMARK 465 SER C 402
REMARK 465 GLU C 403
REMARK 465 CYS C 404
REMARK 465 MET D 386
REMARK 465 ARG D 387
REMARK 465 GLY D 388
REMARK 465 SER D 389
REMARK 465 HIS D 390
REMARK 465 HIS D 391
REMARK 465 HIS D 392
REMARK 465 HIS D 393
REMARK 465 HIS D 394
REMARK 465 THR D 395
REMARK 465 THR D 396
REMARK 465 GLY D 397
REMARK 465 GLU D 398
REMARK 465 ASP D 399
REMARK 465 ASP D 400
REMARK 465 GLU D 401
REMARK 465 SER D 402
REMARK 465 GLU D 403
REMARK 465 CYS D 404
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 CG MET C 694 O HOH C 1850 2.04
REMARK 500 CG MET B 694 O HOH B 1165 2.10
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 THR A 521 -73.35 -106.65
REMARK 500 LEU A 632 -64.27 -102.51
REMARK 500 SER A 665 -84.28 -88.49
REMARK 500 LEU A 674 -154.42 -112.14
REMARK 500 ASN A 706 115.02 -161.66
REMARK 500 VAL A 820 -57.07 -135.38
REMARK 500 LYS A 876 -132.88 52.99
REMARK 500 LEU A 884 157.00 71.80
REMARK 500 SER B 436 28.60 49.56
REMARK 500 LEU B 632 -63.09 -105.96
REMARK 500 SER B 665 -83.21 -88.38
REMARK 500 VAL B 667 46.09 36.07
REMARK 500 LEU B 674 -154.70 -109.44
REMARK 500 ASP B 819 58.69 -94.92
REMARK 500 ASN B 864 17.55 58.35
REMARK 500 LYS B 876 -131.33 52.70
REMARK 500 LEU B 884 156.91 71.19
REMARK 500 THR C 521 -71.53 -113.68
REMARK 500 LEU C 632 -64.23 -100.08
REMARK 500 SER C 665 -86.93 -82.23
REMARK 500 LEU C 674 -152.78 -113.41
REMARK 500 ARG C 781 162.33 177.40
REMARK 500 VAL C 820 -55.61 -131.02
REMARK 500 SER C 836 169.06 179.91
REMARK 500 LYS C 876 -130.07 52.79
REMARK 500 LEU C 884 157.72 72.12
REMARK 500 THR D 521 -71.00 -109.36
REMARK 500 LEU D 632 -66.65 -104.74
REMARK 500 SER D 665 -85.00 -88.56
REMARK 500 VAL D 667 43.00 37.16
REMARK 500 LEU D 674 -152.57 -111.18
REMARK 500 VAL D 820 -58.14 -128.85
REMARK 500 LYS D 876 -132.66 50.73
REMARK 500 LEU D 884 157.95 71.62
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 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 15
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 18
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 24
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 29
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 19
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 25
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 23
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 26
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 28
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 16
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 20
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 27
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 32
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RHJ RELATED DB: PDB
REMARK 900 RELATED ID: 3RHL RELATED DB: PDB
REMARK 900 RELATED ID: 3RHM RELATED DB: PDB
REMARK 900 RELATED ID: 3RHO RELATED DB: PDB
REMARK 900 RELATED ID: 3RHP RELATED DB: PDB
REMARK 900 RELATED ID: 3RHR RELATED DB: PDB
DBREF 3RHQ A 397 902 UNP Q5HZB2 Q5HZB2_RAT 397 902
DBREF 3RHQ B 397 902 UNP Q5HZB2 Q5HZB2_RAT 397 902
DBREF 3RHQ C 397 902 UNP Q5HZB2 Q5HZB2_RAT 397 902
DBREF 3RHQ D 397 902 UNP Q5HZB2 Q5HZB2_RAT 397 902
SEQADV 3RHQ MET A 386 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ARG A 387 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ GLY A 388 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ SER A 389 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS A 390 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS A 391 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS A 392 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS A 393 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS A 394 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR A 395 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR A 396 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ALA A 707 UNP Q5HZB2 CYS 707 ENGINEERED MUTATION
SEQADV 3RHQ MET B 386 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ARG B 387 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ GLY B 388 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ SER B 389 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS B 390 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS B 391 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS B 392 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS B 393 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS B 394 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR B 395 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR B 396 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ALA B 707 UNP Q5HZB2 CYS 707 ENGINEERED MUTATION
SEQADV 3RHQ MET C 386 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ARG C 387 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ GLY C 388 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ SER C 389 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS C 390 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS C 391 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS C 392 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS C 393 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS C 394 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR C 395 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR C 396 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ALA C 707 UNP Q5HZB2 CYS 707 ENGINEERED MUTATION
SEQADV 3RHQ MET D 386 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ARG D 387 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ GLY D 388 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ SER D 389 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS D 390 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS D 391 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS D 392 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS D 393 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ HIS D 394 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR D 395 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ THR D 396 UNP Q5HZB2 EXPRESSION TAG
SEQADV 3RHQ ALA D 707 UNP Q5HZB2 CYS 707 ENGINEERED MUTATION
SEQRES 1 A 517 MET ARG GLY SER HIS HIS HIS HIS HIS THR THR GLY GLU
SEQRES 2 A 517 ASP ASP GLU SER GLU CYS VAL ILE ASN TYR VAL GLU LYS
SEQRES 3 A 517 ALA VAL ASN LYS LEU THR LEU GLN MET PRO TYR GLN LEU
SEQRES 4 A 517 PHE ILE GLY GLY GLU PHE VAL ASP ALA GLU GLY SER LYS
SEQRES 5 A 517 THR TYR ASN THR ILE ASN PRO THR ASP GLY SER VAL ILE
SEQRES 6 A 517 CYS GLN VAL SER LEU ALA GLN VAL SER ASP VAL ASP LYS
SEQRES 7 A 517 ALA VAL ALA ALA ALA LYS GLU ALA PHE GLU ASN GLY LEU
SEQRES 8 A 517 TRP GLY LYS ILE ASN ALA ARG ASP ARG GLY ARG LEU LEU
SEQRES 9 A 517 TYR ARG LEU ALA ASP VAL MET GLU GLN HIS GLN GLU GLU
SEQRES 10 A 517 LEU ALA THR ILE GLU ALA LEU ASP ALA GLY ALA VAL TYR
SEQRES 11 A 517 THR LEU ALA LEU LYS THR HIS VAL GLY MET SER ILE GLN
SEQRES 12 A 517 THR PHE ARG TYR PHE ALA GLY TRP CYS ASP LYS ILE GLN
SEQRES 13 A 517 GLY ALA THR ILE PRO ILE ASN GLN ALA ARG PRO ASN ARG
SEQRES 14 A 517 ASN LEU THR LEU THR LYS LYS GLU PRO VAL GLY VAL CYS
SEQRES 15 A 517 GLY ILE VAL ILE PRO TRP ASN TYR PRO LEU MET MET LEU
SEQRES 16 A 517 SER TRP LYS THR ALA ALA CYS LEU ALA ALA GLY ASN THR
SEQRES 17 A 517 VAL VAL ILE LYS PRO ALA GLN VAL THR PRO LEU THR ALA
SEQRES 18 A 517 LEU LYS PHE ALA GLU LEU THR LEU LYS ALA GLY ILE PRO
SEQRES 19 A 517 LYS GLY VAL VAL ASN ILE LEU PRO GLY SER GLY SER LEU
SEQRES 20 A 517 VAL GLY GLN ARG LEU SER ASP HIS PRO ASP VAL ARG LYS
SEQRES 21 A 517 ILE GLY PHE THR GLY SER THR GLU VAL GLY LYS HIS ILE
SEQRES 22 A 517 MET LYS SER CYS ALA LEU SER ASN VAL LYS LYS VAL SER
SEQRES 23 A 517 LEU GLU LEU GLY GLY LYS SER PRO LEU ILE ILE PHE ALA
SEQRES 24 A 517 ASP CYS ASP LEU ASN LYS ALA VAL GLN MET GLY MET SER
SEQRES 25 A 517 SER VAL PHE PHE ASN LYS GLY GLU ASN ALA ILE ALA ALA
SEQRES 26 A 517 GLY ARG LEU PHE VAL GLU GLU SER ILE HIS ASN GLN PHE
SEQRES 27 A 517 VAL GLN LYS VAL VAL GLU GLU VAL GLU LYS MET LYS ILE
SEQRES 28 A 517 GLY ASN PRO LEU GLU ARG ASP THR ASN HIS GLY PRO GLN
SEQRES 29 A 517 ASN HIS GLU ALA HIS LEU ARG LYS LEU VAL GLU TYR CYS
SEQRES 30 A 517 GLN ARG GLY VAL LYS GLU GLY ALA THR LEU VAL CYS GLY
SEQRES 31 A 517 GLY ASN GLN VAL PRO ARG PRO GLY PHE PHE PHE GLN PRO
SEQRES 32 A 517 THR VAL PHE THR ASP VAL GLU ASP HIS MET TYR ILE ALA
SEQRES 33 A 517 LYS GLU GLU SER PHE GLY PRO ILE MET ILE ILE SER ARG
SEQRES 34 A 517 PHE ALA ASP GLY ASP VAL ASP ALA VAL LEU SER ARG ALA
SEQRES 35 A 517 ASN ALA THR GLU PHE GLY LEU ALA SER GLY VAL PHE THR
SEQRES 36 A 517 ARG ASP ILE ASN LYS ALA LEU TYR VAL SER ASP LYS LEU
SEQRES 37 A 517 GLN ALA GLY THR VAL PHE ILE ASN THR TYR ASN LYS THR
SEQRES 38 A 517 ASP VAL ALA ALA PRO PHE GLY GLY PHE LYS GLN SER GLY
SEQRES 39 A 517 PHE GLY LYS ASP LEU GLY GLU ALA ALA LEU ASN GLU TYR
SEQRES 40 A 517 LEU ARG ILE LYS THR VAL THR PHE GLU TYR
SEQRES 1 B 517 MET ARG GLY SER HIS HIS HIS HIS HIS THR THR GLY GLU
SEQRES 2 B 517 ASP ASP GLU SER GLU CYS VAL ILE ASN TYR VAL GLU LYS
SEQRES 3 B 517 ALA VAL ASN LYS LEU THR LEU GLN MET PRO TYR GLN LEU
SEQRES 4 B 517 PHE ILE GLY GLY GLU PHE VAL ASP ALA GLU GLY SER LYS
SEQRES 5 B 517 THR TYR ASN THR ILE ASN PRO THR ASP GLY SER VAL ILE
SEQRES 6 B 517 CYS GLN VAL SER LEU ALA GLN VAL SER ASP VAL ASP LYS
SEQRES 7 B 517 ALA VAL ALA ALA ALA LYS GLU ALA PHE GLU ASN GLY LEU
SEQRES 8 B 517 TRP GLY LYS ILE ASN ALA ARG ASP ARG GLY ARG LEU LEU
SEQRES 9 B 517 TYR ARG LEU ALA ASP VAL MET GLU GLN HIS GLN GLU GLU
SEQRES 10 B 517 LEU ALA THR ILE GLU ALA LEU ASP ALA GLY ALA VAL TYR
SEQRES 11 B 517 THR LEU ALA LEU LYS THR HIS VAL GLY MET SER ILE GLN
SEQRES 12 B 517 THR PHE ARG TYR PHE ALA GLY TRP CYS ASP LYS ILE GLN
SEQRES 13 B 517 GLY ALA THR ILE PRO ILE ASN GLN ALA ARG PRO ASN ARG
SEQRES 14 B 517 ASN LEU THR LEU THR LYS LYS GLU PRO VAL GLY VAL CYS
SEQRES 15 B 517 GLY ILE VAL ILE PRO TRP ASN TYR PRO LEU MET MET LEU
SEQRES 16 B 517 SER TRP LYS THR ALA ALA CYS LEU ALA ALA GLY ASN THR
SEQRES 17 B 517 VAL VAL ILE LYS PRO ALA GLN VAL THR PRO LEU THR ALA
SEQRES 18 B 517 LEU LYS PHE ALA GLU LEU THR LEU LYS ALA GLY ILE PRO
SEQRES 19 B 517 LYS GLY VAL VAL ASN ILE LEU PRO GLY SER GLY SER LEU
SEQRES 20 B 517 VAL GLY GLN ARG LEU SER ASP HIS PRO ASP VAL ARG LYS
SEQRES 21 B 517 ILE GLY PHE THR GLY SER THR GLU VAL GLY LYS HIS ILE
SEQRES 22 B 517 MET LYS SER CYS ALA LEU SER ASN VAL LYS LYS VAL SER
SEQRES 23 B 517 LEU GLU LEU GLY GLY LYS SER PRO LEU ILE ILE PHE ALA
SEQRES 24 B 517 ASP CYS ASP LEU ASN LYS ALA VAL GLN MET GLY MET SER
SEQRES 25 B 517 SER VAL PHE PHE ASN LYS GLY GLU ASN ALA ILE ALA ALA
SEQRES 26 B 517 GLY ARG LEU PHE VAL GLU GLU SER ILE HIS ASN GLN PHE
SEQRES 27 B 517 VAL GLN LYS VAL VAL GLU GLU VAL GLU LYS MET LYS ILE
SEQRES 28 B 517 GLY ASN PRO LEU GLU ARG ASP THR ASN HIS GLY PRO GLN
SEQRES 29 B 517 ASN HIS GLU ALA HIS LEU ARG LYS LEU VAL GLU TYR CYS
SEQRES 30 B 517 GLN ARG GLY VAL LYS GLU GLY ALA THR LEU VAL CYS GLY
SEQRES 31 B 517 GLY ASN GLN VAL PRO ARG PRO GLY PHE PHE PHE GLN PRO
SEQRES 32 B 517 THR VAL PHE THR ASP VAL GLU ASP HIS MET TYR ILE ALA
SEQRES 33 B 517 LYS GLU GLU SER PHE GLY PRO ILE MET ILE ILE SER ARG
SEQRES 34 B 517 PHE ALA ASP GLY ASP VAL ASP ALA VAL LEU SER ARG ALA
SEQRES 35 B 517 ASN ALA THR GLU PHE GLY LEU ALA SER GLY VAL PHE THR
SEQRES 36 B 517 ARG ASP ILE ASN LYS ALA LEU TYR VAL SER ASP LYS LEU
SEQRES 37 B 517 GLN ALA GLY THR VAL PHE ILE ASN THR TYR ASN LYS THR
SEQRES 38 B 517 ASP VAL ALA ALA PRO PHE GLY GLY PHE LYS GLN SER GLY
SEQRES 39 B 517 PHE GLY LYS ASP LEU GLY GLU ALA ALA LEU ASN GLU TYR
SEQRES 40 B 517 LEU ARG ILE LYS THR VAL THR PHE GLU TYR
SEQRES 1 C 517 MET ARG GLY SER HIS HIS HIS HIS HIS THR THR GLY GLU
SEQRES 2 C 517 ASP ASP GLU SER GLU CYS VAL ILE ASN TYR VAL GLU LYS
SEQRES 3 C 517 ALA VAL ASN LYS LEU THR LEU GLN MET PRO TYR GLN LEU
SEQRES 4 C 517 PHE ILE GLY GLY GLU PHE VAL ASP ALA GLU GLY SER LYS
SEQRES 5 C 517 THR TYR ASN THR ILE ASN PRO THR ASP GLY SER VAL ILE
SEQRES 6 C 517 CYS GLN VAL SER LEU ALA GLN VAL SER ASP VAL ASP LYS
SEQRES 7 C 517 ALA VAL ALA ALA ALA LYS GLU ALA PHE GLU ASN GLY LEU
SEQRES 8 C 517 TRP GLY LYS ILE ASN ALA ARG ASP ARG GLY ARG LEU LEU
SEQRES 9 C 517 TYR ARG LEU ALA ASP VAL MET GLU GLN HIS GLN GLU GLU
SEQRES 10 C 517 LEU ALA THR ILE GLU ALA LEU ASP ALA GLY ALA VAL TYR
SEQRES 11 C 517 THR LEU ALA LEU LYS THR HIS VAL GLY MET SER ILE GLN
SEQRES 12 C 517 THR PHE ARG TYR PHE ALA GLY TRP CYS ASP LYS ILE GLN
SEQRES 13 C 517 GLY ALA THR ILE PRO ILE ASN GLN ALA ARG PRO ASN ARG
SEQRES 14 C 517 ASN LEU THR LEU THR LYS LYS GLU PRO VAL GLY VAL CYS
SEQRES 15 C 517 GLY ILE VAL ILE PRO TRP ASN TYR PRO LEU MET MET LEU
SEQRES 16 C 517 SER TRP LYS THR ALA ALA CYS LEU ALA ALA GLY ASN THR
SEQRES 17 C 517 VAL VAL ILE LYS PRO ALA GLN VAL THR PRO LEU THR ALA
SEQRES 18 C 517 LEU LYS PHE ALA GLU LEU THR LEU LYS ALA GLY ILE PRO
SEQRES 19 C 517 LYS GLY VAL VAL ASN ILE LEU PRO GLY SER GLY SER LEU
SEQRES 20 C 517 VAL GLY GLN ARG LEU SER ASP HIS PRO ASP VAL ARG LYS
SEQRES 21 C 517 ILE GLY PHE THR GLY SER THR GLU VAL GLY LYS HIS ILE
SEQRES 22 C 517 MET LYS SER CYS ALA LEU SER ASN VAL LYS LYS VAL SER
SEQRES 23 C 517 LEU GLU LEU GLY GLY LYS SER PRO LEU ILE ILE PHE ALA
SEQRES 24 C 517 ASP CYS ASP LEU ASN LYS ALA VAL GLN MET GLY MET SER
SEQRES 25 C 517 SER VAL PHE PHE ASN LYS GLY GLU ASN ALA ILE ALA ALA
SEQRES 26 C 517 GLY ARG LEU PHE VAL GLU GLU SER ILE HIS ASN GLN PHE
SEQRES 27 C 517 VAL GLN LYS VAL VAL GLU GLU VAL GLU LYS MET LYS ILE
SEQRES 28 C 517 GLY ASN PRO LEU GLU ARG ASP THR ASN HIS GLY PRO GLN
SEQRES 29 C 517 ASN HIS GLU ALA HIS LEU ARG LYS LEU VAL GLU TYR CYS
SEQRES 30 C 517 GLN ARG GLY VAL LYS GLU GLY ALA THR LEU VAL CYS GLY
SEQRES 31 C 517 GLY ASN GLN VAL PRO ARG PRO GLY PHE PHE PHE GLN PRO
SEQRES 32 C 517 THR VAL PHE THR ASP VAL GLU ASP HIS MET TYR ILE ALA
SEQRES 33 C 517 LYS GLU GLU SER PHE GLY PRO ILE MET ILE ILE SER ARG
SEQRES 34 C 517 PHE ALA ASP GLY ASP VAL ASP ALA VAL LEU SER ARG ALA
SEQRES 35 C 517 ASN ALA THR GLU PHE GLY LEU ALA SER GLY VAL PHE THR
SEQRES 36 C 517 ARG ASP ILE ASN LYS ALA LEU TYR VAL SER ASP LYS LEU
SEQRES 37 C 517 GLN ALA GLY THR VAL PHE ILE ASN THR TYR ASN LYS THR
SEQRES 38 C 517 ASP VAL ALA ALA PRO PHE GLY GLY PHE LYS GLN SER GLY
SEQRES 39 C 517 PHE GLY LYS ASP LEU GLY GLU ALA ALA LEU ASN GLU TYR
SEQRES 40 C 517 LEU ARG ILE LYS THR VAL THR PHE GLU TYR
SEQRES 1 D 517 MET ARG GLY SER HIS HIS HIS HIS HIS THR THR GLY GLU
SEQRES 2 D 517 ASP ASP GLU SER GLU CYS VAL ILE ASN TYR VAL GLU LYS
SEQRES 3 D 517 ALA VAL ASN LYS LEU THR LEU GLN MET PRO TYR GLN LEU
SEQRES 4 D 517 PHE ILE GLY GLY GLU PHE VAL ASP ALA GLU GLY SER LYS
SEQRES 5 D 517 THR TYR ASN THR ILE ASN PRO THR ASP GLY SER VAL ILE
SEQRES 6 D 517 CYS GLN VAL SER LEU ALA GLN VAL SER ASP VAL ASP LYS
SEQRES 7 D 517 ALA VAL ALA ALA ALA LYS GLU ALA PHE GLU ASN GLY LEU
SEQRES 8 D 517 TRP GLY LYS ILE ASN ALA ARG ASP ARG GLY ARG LEU LEU
SEQRES 9 D 517 TYR ARG LEU ALA ASP VAL MET GLU GLN HIS GLN GLU GLU
SEQRES 10 D 517 LEU ALA THR ILE GLU ALA LEU ASP ALA GLY ALA VAL TYR
SEQRES 11 D 517 THR LEU ALA LEU LYS THR HIS VAL GLY MET SER ILE GLN
SEQRES 12 D 517 THR PHE ARG TYR PHE ALA GLY TRP CYS ASP LYS ILE GLN
SEQRES 13 D 517 GLY ALA THR ILE PRO ILE ASN GLN ALA ARG PRO ASN ARG
SEQRES 14 D 517 ASN LEU THR LEU THR LYS LYS GLU PRO VAL GLY VAL CYS
SEQRES 15 D 517 GLY ILE VAL ILE PRO TRP ASN TYR PRO LEU MET MET LEU
SEQRES 16 D 517 SER TRP LYS THR ALA ALA CYS LEU ALA ALA GLY ASN THR
SEQRES 17 D 517 VAL VAL ILE LYS PRO ALA GLN VAL THR PRO LEU THR ALA
SEQRES 18 D 517 LEU LYS PHE ALA GLU LEU THR LEU LYS ALA GLY ILE PRO
SEQRES 19 D 517 LYS GLY VAL VAL ASN ILE LEU PRO GLY SER GLY SER LEU
SEQRES 20 D 517 VAL GLY GLN ARG LEU SER ASP HIS PRO ASP VAL ARG LYS
SEQRES 21 D 517 ILE GLY PHE THR GLY SER THR GLU VAL GLY LYS HIS ILE
SEQRES 22 D 517 MET LYS SER CYS ALA LEU SER ASN VAL LYS LYS VAL SER
SEQRES 23 D 517 LEU GLU LEU GLY GLY LYS SER PRO LEU ILE ILE PHE ALA
SEQRES 24 D 517 ASP CYS ASP LEU ASN LYS ALA VAL GLN MET GLY MET SER
SEQRES 25 D 517 SER VAL PHE PHE ASN LYS GLY GLU ASN ALA ILE ALA ALA
SEQRES 26 D 517 GLY ARG LEU PHE VAL GLU GLU SER ILE HIS ASN GLN PHE
SEQRES 27 D 517 VAL GLN LYS VAL VAL GLU GLU VAL GLU LYS MET LYS ILE
SEQRES 28 D 517 GLY ASN PRO LEU GLU ARG ASP THR ASN HIS GLY PRO GLN
SEQRES 29 D 517 ASN HIS GLU ALA HIS LEU ARG LYS LEU VAL GLU TYR CYS
SEQRES 30 D 517 GLN ARG GLY VAL LYS GLU GLY ALA THR LEU VAL CYS GLY
SEQRES 31 D 517 GLY ASN GLN VAL PRO ARG PRO GLY PHE PHE PHE GLN PRO
SEQRES 32 D 517 THR VAL PHE THR ASP VAL GLU ASP HIS MET TYR ILE ALA
SEQRES 33 D 517 LYS GLU GLU SER PHE GLY PRO ILE MET ILE ILE SER ARG
SEQRES 34 D 517 PHE ALA ASP GLY ASP VAL ASP ALA VAL LEU SER ARG ALA
SEQRES 35 D 517 ASN ALA THR GLU PHE GLY LEU ALA SER GLY VAL PHE THR
SEQRES 36 D 517 ARG ASP ILE ASN LYS ALA LEU TYR VAL SER ASP LYS LEU
SEQRES 37 D 517 GLN ALA GLY THR VAL PHE ILE ASN THR TYR ASN LYS THR
SEQRES 38 D 517 ASP VAL ALA ALA PRO PHE GLY GLY PHE LYS GLN SER GLY
SEQRES 39 D 517 PHE GLY LYS ASP LEU GLY GLU ALA ALA LEU ASN GLU TYR
SEQRES 40 D 517 LEU ARG ILE LYS THR VAL THR PHE GLU TYR
HET NAP A 903 48
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 6 5
HET SO4 A 11 5
HET SO4 A 15 5
HET SO4 A 18 5
HET SO4 A 21 5
HET SO4 A 24 5
HET GOL A 29 6
HET NAP B 903 48
HET SO4 B 3 5
HET SO4 B 4 5
HET SO4 B 5 5
HET SO4 B 9 5
HET SO4 B 14 5
HET SO4 B 19 5
HET SO4 B 22 5
HET SO4 B 25 5
HET GOL B 30 6
HET NAP C 903 48
HET SO4 C 7 5
HET SO4 C 10 5
HET SO4 C 13 5
HET SO4 C 17 5
HET SO4 C 23 5
HET SO4 C 26 5
HET SO4 C 28 5
HET GOL C 31 6
HET NAP D 903 48
HET SO4 D 8 5
HET SO4 D 12 5
HET SO4 D 16 5
HET SO4 D 20 5
HET SO4 D 27 5
HET GOL D 32 6
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 6 SO4 28(O4 S 2-)
FORMUL 14 GOL 4(C3 H8 O3)
FORMUL 41 HOH *1971(H2 O)
HELIX 1 1 ALA A 433 SER A 436 5 4
HELIX 2 2 GLN A 457 ASN A 474 1 18
HELIX 3 3 GLY A 475 LYS A 479 5 5
HELIX 4 4 ASN A 481 HIS A 499 1 19
HELIX 5 5 HIS A 499 GLY A 512 1 14
HELIX 6 6 VAL A 514 THR A 521 1 8
HELIX 7 7 VAL A 523 CYS A 537 1 15
HELIX 8 8 ASP A 538 ILE A 540 5 3
HELIX 9 9 TYR A 575 ALA A 590 1 16
HELIX 10 10 PRO A 603 ALA A 616 1 14
HELIX 11 11 LEU A 632 HIS A 640 1 9
HELIX 12 12 SER A 651 SER A 665 1 15
HELIX 13 13 ASP A 687 PHE A 701 1 15
HELIX 14 14 ASN A 702 GLU A 705 5 4
HELIX 15 15 GLU A 717 LYS A 733 1 17
HELIX 16 16 HIS A 751 GLU A 768 1 18
HELIX 17 17 MET A 798 GLU A 803 1 6
HELIX 18 18 VAL A 820 ALA A 829 1 10
HELIX 19 19 ASP A 842 LEU A 853 1 12
HELIX 20 20 PHE A 875 GLN A 877 5 3
HELIX 21 21 LEU A 884 ASN A 890 1 7
HELIX 22 22 ALA B 433 SER B 436 5 4
HELIX 23 23 GLN B 457 ASN B 474 1 18
HELIX 24 24 GLY B 475 LYS B 479 5 5
HELIX 25 25 ASN B 481 HIS B 499 1 19
HELIX 26 26 HIS B 499 GLY B 512 1 14
HELIX 27 27 VAL B 514 THR B 521 1 8
HELIX 28 28 VAL B 523 CYS B 537 1 15
HELIX 29 29 ASP B 538 ILE B 540 5 3
HELIX 30 30 TYR B 575 ALA B 590 1 16
HELIX 31 31 PRO B 603 ALA B 616 1 14
HELIX 32 32 LEU B 632 HIS B 640 1 9
HELIX 33 33 SER B 651 SER B 665 1 15
HELIX 34 34 ASP B 687 PHE B 701 1 15
HELIX 35 35 ASN B 702 GLU B 705 5 4
HELIX 36 36 GLU B 717 GLU B 732 1 16
HELIX 37 37 HIS B 751 GLU B 768 1 18
HELIX 38 38 MET B 798 GLU B 803 1 6
HELIX 39 39 ASP B 819 ALA B 829 1 11
HELIX 40 40 ASP B 842 LEU B 853 1 12
HELIX 41 41 PHE B 875 GLN B 877 5 3
HELIX 42 42 LEU B 884 ASN B 890 1 7
HELIX 43 43 ALA C 433 SER C 436 5 4
HELIX 44 44 GLN C 457 ASN C 474 1 18
HELIX 45 45 GLY C 475 LYS C 479 5 5
HELIX 46 46 ASN C 481 HIS C 499 1 19
HELIX 47 47 HIS C 499 GLY C 512 1 14
HELIX 48 48 VAL C 514 THR C 521 1 8
HELIX 49 49 VAL C 523 CYS C 537 1 15
HELIX 50 50 ASP C 538 ILE C 540 5 3
HELIX 51 51 TYR C 575 ALA C 590 1 16
HELIX 52 52 PRO C 603 ALA C 616 1 14
HELIX 53 53 LEU C 632 HIS C 640 1 9
HELIX 54 54 SER C 651 SER C 665 1 15
HELIX 55 55 ASP C 687 PHE C 701 1 15
HELIX 56 56 ASN C 702 GLU C 705 5 4
HELIX 57 57 GLU C 717 LYS C 733 1 17
HELIX 58 58 HIS C 751 GLU C 768 1 18
HELIX 59 59 MET C 798 GLU C 803 1 6
HELIX 60 60 VAL C 820 ALA C 829 1 10
HELIX 61 61 ASP C 842 LEU C 853 1 12
HELIX 62 62 PHE C 875 GLN C 877 5 3
HELIX 63 63 GLY C 885 GLU C 891 5 7
HELIX 64 64 ALA D 433 SER D 436 5 4
HELIX 65 65 GLN D 457 ASN D 474 1 18
HELIX 66 66 GLY D 475 LYS D 479 5 5
HELIX 67 67 ASN D 481 HIS D 499 1 19
HELIX 68 68 HIS D 499 GLY D 512 1 14
HELIX 69 69 VAL D 514 THR D 521 1 8
HELIX 70 70 VAL D 523 GLY D 535 1 13
HELIX 71 71 TRP D 536 ILE D 540 5 5
HELIX 72 72 TYR D 575 ALA D 590 1 16
HELIX 73 73 PRO D 603 ALA D 616 1 14
HELIX 74 74 LEU D 632 HIS D 640 1 9
HELIX 75 75 SER D 651 SER D 665 1 15
HELIX 76 76 ASP D 687 PHE D 701 1 15
HELIX 77 77 ASN D 702 GLU D 705 5 4
HELIX 78 78 GLU D 717 LYS D 733 1 17
HELIX 79 79 HIS D 751 GLU D 768 1 18
HELIX 80 80 MET D 798 GLU D 803 1 6
HELIX 81 81 VAL D 820 ALA D 829 1 10
HELIX 82 82 ASP D 842 LEU D 853 1 12
HELIX 83 83 PHE D 875 GLN D 877 5 3
HELIX 84 84 LEU D 884 ASN D 890 1 7
SHEET 1 A 2 VAL A 409 VAL A 413 0
SHEET 2 A 2 LEU A 416 MET A 420 -1 O LEU A 418 N LYS A 411
SHEET 1 B 2 LEU A 424 ILE A 426 0
SHEET 2 B 2 GLU A 429 VAL A 431 -1 O GLU A 429 N ILE A 426
SHEET 1 C 2 THR A 438 ILE A 442 0
SHEET 2 C 2 VAL A 449 SER A 454 -1 O ILE A 450 N THR A 441
SHEET 1 D20 THR B 771 CYS B 774 0
SHEET 2 D20 THR B 789 THR B 792 -1 O THR B 792 N THR B 771
SHEET 3 D20 ILE B 809 PHE B 815 1 O MET B 810 N PHE B 791
SHEET 4 D20 ALA B 710 GLU B 716 1 N LEU B 713 O SER B 813
SHEET 5 D20 SER B 678 ILE B 682 1 N ILE B 682 O PHE B 714
SHEET 6 D20 GLY B 837 PHE B 839 1 O PHE B 839 N ILE B 681
SHEET 7 D20 THR B 857 ILE B 860 1 O PHE B 859 N VAL B 838
SHEET 8 D20 LEU A 893 TYR A 902 1 N THR A 899 O ILE B 860
SHEET 9 D20 ARG A 554 PRO A 563 -1 N LEU A 558 O VAL A 898
SHEET 10 D20 GLY A 542 ILE A 545 -1 N ILE A 545 O THR A 557
SHEET 11 D20 GLY D 542 ILE D 545 -1 O THR D 544 N GLY A 542
SHEET 12 D20 ARG D 554 PRO D 563 -1 O THR D 557 N ILE D 545
SHEET 13 D20 LEU D 893 TYR D 902 -1 O PHE D 900 N LEU D 556
SHEET 14 D20 THR C 857 ILE C 860 1 N ILE C 860 O THR D 899
SHEET 15 D20 GLY C 837 PHE C 839 1 N VAL C 838 O PHE C 859
SHEET 16 D20 SER C 678 ILE C 682 1 N ILE C 681 O PHE C 839
SHEET 17 D20 ALA C 710 GLU C 716 1 O PHE C 714 N ILE C 682
SHEET 18 D20 ILE C 809 PHE C 815 1 O ILE C 811 N LEU C 713
SHEET 19 D20 THR C 789 THR C 792 1 N PHE C 791 O MET C 810
SHEET 20 D20 THR C 771 CYS C 774 -1 N VAL C 773 O VAL C 790
SHEET 1 E 6 VAL A 623 ILE A 625 0
SHEET 2 E 6 THR A 593 LYS A 597 1 N ILE A 596 O ASN A 624
SHEET 3 E 6 VAL A 566 VAL A 570 1 N ILE A 569 O LYS A 597
SHEET 4 E 6 LYS A 645 THR A 649 1 O GLY A 647 N GLY A 568
SHEET 5 E 6 LYS A 669 GLU A 673 1 O LYS A 669 N ILE A 646
SHEET 6 E 6 GLY A 879 PHE A 880 -1 O PHE A 880 N LEU A 672
SHEET 1 F20 THR A 771 CYS A 774 0
SHEET 2 F20 THR A 789 THR A 792 -1 O VAL A 790 N VAL A 773
SHEET 3 F20 ILE A 809 PHE A 815 1 O MET A 810 N PHE A 791
SHEET 4 F20 ALA A 710 GLU A 716 1 N LEU A 713 O ILE A 811
SHEET 5 F20 SER A 678 ILE A 682 1 N ILE A 682 O PHE A 714
SHEET 6 F20 ALA A 835 PHE A 839 1 O GLY A 837 N ILE A 681
SHEET 7 F20 THR A 857 ILE A 860 1 O PHE A 859 N SER A 836
SHEET 8 F20 LEU B 893 TYR B 902 1 O THR B 897 N VAL A 858
SHEET 9 F20 ARG B 554 PRO B 563 -1 N ARG B 554 O TYR B 902
SHEET 10 F20 GLY B 542 ILE B 545 -1 N ILE B 545 O THR B 557
SHEET 11 F20 GLY C 542 ILE C 545 -1 O THR C 544 N GLY B 542
SHEET 12 F20 ARG C 554 PRO C 563 -1 O THR C 557 N ILE C 545
SHEET 13 F20 LEU C 893 TYR C 902 -1 O PHE C 900 N LEU C 556
SHEET 14 F20 THR D 857 ILE D 860 1 O ILE D 860 N THR C 899
SHEET 15 F20 GLY D 837 PHE D 839 1 N VAL D 838 O PHE D 859
SHEET 16 F20 SER D 678 ILE D 682 1 N ILE D 681 O GLY D 837
SHEET 17 F20 ALA D 710 GLU D 716 1 O PHE D 714 N ILE D 682
SHEET 18 F20 ILE D 809 PHE D 815 1 O SER D 813 N LEU D 713
SHEET 19 F20 THR D 789 THR D 792 1 N PHE D 791 O MET D 810
SHEET 20 F20 THR D 771 CYS D 774 -1 N THR D 771 O THR D 792
SHEET 1 G 2 VAL B 409 VAL B 413 0
SHEET 2 G 2 LEU B 416 MET B 420 -1 O LEU B 418 N LYS B 411
SHEET 1 H 2 LEU B 424 ILE B 426 0
SHEET 2 H 2 GLU B 429 VAL B 431 -1 O VAL B 431 N LEU B 424
SHEET 1 I 2 THR B 438 ILE B 442 0
SHEET 2 I 2 VAL B 449 SER B 454 -1 O ILE B 450 N THR B 441
SHEET 1 J 6 VAL B 623 ILE B 625 0
SHEET 2 J 6 THR B 593 LYS B 597 1 N ILE B 596 O ASN B 624
SHEET 3 J 6 VAL B 566 VAL B 570 1 N ILE B 569 O LYS B 597
SHEET 4 J 6 LYS B 645 THR B 649 1 O GLY B 647 N GLY B 568
SHEET 5 J 6 LYS B 669 GLU B 673 1 O LYS B 669 N ILE B 646
SHEET 6 J 6 GLY B 879 PHE B 880 -1 O PHE B 880 N LEU B 672
SHEET 1 K 2 VAL C 409 VAL C 413 0
SHEET 2 K 2 LEU C 416 MET C 420 -1 O MET C 420 N VAL C 409
SHEET 1 L 2 LEU C 424 ILE C 426 0
SHEET 2 L 2 GLU C 429 VAL C 431 -1 O GLU C 429 N ILE C 426
SHEET 1 M 2 THR C 438 ILE C 442 0
SHEET 2 M 2 VAL C 449 SER C 454 -1 O ILE C 450 N THR C 441
SHEET 1 N 6 VAL C 623 ILE C 625 0
SHEET 2 N 6 THR C 593 LYS C 597 1 N ILE C 596 O ASN C 624
SHEET 3 N 6 VAL C 566 VAL C 570 1 N ILE C 569 O LYS C 597
SHEET 4 N 6 LYS C 645 THR C 649 1 O LYS C 645 N GLY C 568
SHEET 5 N 6 LYS C 669 GLU C 673 1 O LYS C 669 N ILE C 646
SHEET 6 N 6 GLY C 879 PHE C 880 -1 O PHE C 880 N LEU C 672
SHEET 1 O 2 VAL D 409 VAL D 413 0
SHEET 2 O 2 LEU D 416 MET D 420 -1 O LEU D 418 N LYS D 411
SHEET 1 P 2 LEU D 424 ILE D 426 0
SHEET 2 P 2 GLU D 429 VAL D 431 -1 O GLU D 429 N ILE D 426
SHEET 1 Q 2 THR D 438 ILE D 442 0
SHEET 2 Q 2 VAL D 449 SER D 454 -1 O ILE D 450 N THR D 441
SHEET 1 R 6 VAL D 623 ILE D 625 0
SHEET 2 R 6 THR D 593 LYS D 597 1 N ILE D 596 O ASN D 624
SHEET 3 R 6 VAL D 566 VAL D 570 1 N ILE D 569 O LYS D 597
SHEET 4 R 6 LYS D 645 THR D 649 1 O LYS D 645 N GLY D 568
SHEET 5 R 6 LYS D 669 GLU D 673 1 O LYS D 669 N ILE D 646
SHEET 6 R 6 GLY D 879 PHE D 880 -1 O PHE D 880 N LEU D 672
CISPEP 1 ARG A 551 PRO A 552 0 5.98
CISPEP 2 ARG B 551 PRO B 552 0 4.32
CISPEP 3 ARG C 551 PRO C 552 0 3.98
CISPEP 4 ARG D 551 PRO D 552 0 4.44
SITE 1 AC1 37 VAL A 570 ILE A 571 PRO A 572 TRP A 573
SITE 2 AC1 37 ASN A 574 LYS A 597 ALA A 599 GLN A 600
SITE 3 AC1 37 SER A 629 GLY A 630 GLY A 634 GLN A 635
SITE 4 AC1 37 PHE A 648 THR A 649 GLY A 650 SER A 651
SITE 5 AC1 37 VAL A 654 HIS A 657 ILE A 658 GLU A 673
SITE 6 AC1 37 LEU A 674 GLY A 675 ALA A 707 GLU A 804
SITE 7 AC1 37 PHE A 806 LEU A 834 PHE A 872 HOH A 918
SITE 8 AC1 37 HOH A 935 HOH A 950 HOH A 992 HOH A1123
SITE 9 AC1 37 HOH A1139 HOH A1182 HOH A1394 HOH A1444
SITE 10 AC1 37 HOH A1588
SITE 1 AC2 3 ASP A 851 LYS A 852 ARG C 554
SITE 1 AC3 3 HOH A 287 ARG A 554 LYS C 852
SITE 1 AC4 4 ARG A 636 PRO A 641 HOH A1483 HOH A1521
SITE 1 AC5 3 ARG A 764 TYR A 799 HOH A1966
SITE 1 AC6 10 HOH A 57 LYS A 669 LEU A 893 ARG A 894
SITE 2 AC6 10 ILE A 895 HOH A 970 HOH A1235 HOH A1867
SITE 3 AC6 10 GLY B 881 LYS B 882
SITE 1 AC7 4 ARG A 551 ARG A 554 HOH A1835 TYR C 848
SITE 1 AC8 4 ASN A 548 HOH A1035 HOH A1271 GLN B 528
SITE 1 AC9 7 THR A 445 ASN A 738 GLU A 741 ARG A 781
SITE 2 AC9 7 HOH A 994 HOH A1533 HOH C1087
SITE 1 BC1 5 TYR A 575 ASN A 706 THR A 866 HOH A1922
SITE 2 BC1 5 HOH A2000
SITE 1 BC2 38 HOH B 255 HOH B 328 VAL B 570 ILE B 571
SITE 2 BC2 38 PRO B 572 TRP B 573 ASN B 574 LYS B 597
SITE 3 BC2 38 ALA B 599 GLN B 600 SER B 629 GLY B 630
SITE 4 BC2 38 GLY B 634 GLN B 635 PHE B 648 THR B 649
SITE 5 BC2 38 GLY B 650 SER B 651 VAL B 654 HIS B 657
SITE 6 BC2 38 ILE B 658 GLU B 673 LEU B 674 GLY B 675
SITE 7 BC2 38 ALA B 707 GLU B 804 PHE B 806 LEU B 834
SITE 8 BC2 38 PHE B 872 HOH B 977 HOH B 984 HOH B1010
SITE 9 BC2 38 HOH B1186 HOH B1202 HOH B1297 HOH B1443
SITE 10 BC2 38 HOH B1684 HOH B1707
SITE 1 BC3 5 ARG B 554 HOH B1739 ASP D 851 LYS D 852
SITE 2 BC3 5 HOH D 991
SITE 1 BC4 4 LYS B 852 HOH B 957 HOH B1726 ARG D 554
SITE 1 BC5 2 ARG B 636 PRO B 641
SITE 1 BC6 2 ARG B 764 HOH B1920
SITE 1 BC7 8 HOH A 39 GLY A 881 LYS A 882 HOH B 254
SITE 2 BC7 8 LYS B 669 ARG B 894 ILE B 895 HOH B1389
SITE 1 BC8 5 ARG B 551 ARG B 554 HOH B1423 HOH B1747
SITE 2 BC8 5 TYR D 848
SITE 1 BC9 5 GLN A 528 ASN B 548 HOH B 936 HOH B 979
SITE 2 BC9 5 HOH B1097
SITE 1 CC1 6 THR B 445 ASN B 738 GLU B 741 ARG B 781
SITE 2 CC1 6 HOH B 973 HOH B1708
SITE 1 CC2 4 TYR B 575 ASN B 706 THR B 866 HOH B2001
SITE 1 CC3 39 HOH C 200 HOH C 244 HOH C 311 HOH C 332
SITE 2 CC3 39 VAL C 570 ILE C 571 PRO C 572 TRP C 573
SITE 3 CC3 39 ASN C 574 LYS C 597 ALA C 599 GLN C 600
SITE 4 CC3 39 SER C 629 GLY C 630 GLY C 634 GLN C 635
SITE 5 CC3 39 PHE C 648 THR C 649 GLY C 650 SER C 651
SITE 6 CC3 39 VAL C 654 HIS C 657 ILE C 658 GLU C 673
SITE 7 CC3 39 LEU C 674 GLY C 675 ALA C 707 GLU C 804
SITE 8 CC3 39 PHE C 806 LEU C 834 PHE C 872 HOH C 936
SITE 9 CC3 39 HOH C 946 HOH C1020 HOH C1114 HOH C1408
SITE 10 CC3 39 HOH C1505 HOH C1589 HOH C1953
SITE 1 CC4 4 ARG C 636 PRO C 641 HOH C1499 HOH C1810
SITE 1 CC5 2 ARG C 764 HOH C1913
SITE 1 CC6 9 HOH C 45 HOH C 280 LYS C 669 ARG C 894
SITE 2 CC6 9 ILE C 895 HOH C 942 HOH C1066 GLY D 881
SITE 3 CC6 9 LYS D 882
SITE 1 CC7 3 ARG C 551 ARG C 554 HOH C1813
SITE 1 CC8 7 ASN C 548 HOH C1043 HOH C1049 HOH C1085
SITE 2 CC8 7 HOH C1842 LYS D 520 GLN D 528
SITE 1 CC9 3 HOH C 130 ASN C 738 ARG C 781
SITE 1 DC1 5 LEU A 416 THR A 417 LYS C 415 ARG C 742
SITE 2 DC1 5 HOH C1968
SITE 1 DC2 4 TYR C 575 ASN C 706 THR C 866 HOH C2002
SITE 1 DC3 37 HOH D 161 HOH D 228 HOH D 369 VAL D 570
SITE 2 DC3 37 ILE D 571 PRO D 572 TRP D 573 ASN D 574
SITE 3 DC3 37 LYS D 597 ALA D 599 GLN D 600 SER D 629
SITE 4 DC3 37 GLY D 630 GLY D 634 GLN D 635 PHE D 648
SITE 5 DC3 37 THR D 649 GLY D 650 SER D 651 VAL D 654
SITE 6 DC3 37 HIS D 657 ILE D 658 GLU D 673 LEU D 674
SITE 7 DC3 37 GLY D 675 ALA D 707 GLU D 804 PHE D 806
SITE 8 DC3 37 LEU D 834 PHE D 872 HOH D 948 HOH D1007
SITE 9 DC3 37 HOH D1213 HOH D1216 HOH D1322 HOH D1345
SITE 10 DC3 37 HOH D1662
SITE 1 DC4 3 ARG D 636 PRO D 641 HOH D1959
SITE 1 DC5 1 ARG D 764
SITE 1 DC6 11 GLY C 881 LYS C 882 HOH C1851 HOH D 53
SITE 2 DC6 11 LYS D 669 LEU D 893 ARG D 894 ILE D 895
SITE 3 DC6 11 HOH D 905 HOH D1037 HOH D1198
SITE 1 DC7 3 TYR B 848 ARG D 551 ARG D 554
SITE 1 DC8 6 THR D 445 ASN D 738 GLU D 741 ARG D 781
SITE 2 DC8 6 HOH D 983 HOH D1575
SITE 1 DC9 7 TYR D 575 MET D 578 TRP D 582 ASN D 706
SITE 2 DC9 7 THR D 866 HOH D1352 HOH D2003
CRYST1 258.559 194.268 97.177 90.00 108.80 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003868 0.000000 0.001317 0.00000
SCALE2 0.000000 0.005148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010870 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
