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3318 lines (3318 loc) · 260 KB
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HEADER OXIDOREDUCTASE 14-MAR-12 4E5N
TITLE THERMOSTABLE PHOSPHITE DEHYDROGENASE IN COMPLEX WITH NAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE PHOSPHITE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI;
SOURCE 3 ORGANISM_TAXID: 316;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS D-2-HYDROXYACID DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZOU,H.ZHANG,S.K.NAIR
REVDAT 2 13-JUN-12 4E5N 1 JRNL
REVDAT 1 30-MAY-12 4E5N 0
JRNL AUTH Y.ZOU,H.ZHANG,J.S.BRUNZELLE,T.W.JOHANNES,R.WOODYER,J.E.HUNG,
JRNL AUTH 2 N.NAIR,W.A.VAN DER DONK,H.ZHAO,S.K.NAIR
JRNL TITL CRYSTAL STRUCTURES OF PHOSPHITE DEHYDROGENASE PROVIDE
JRNL TITL 2 INSIGHTS INTO NICOTINAMIDE COFACTOR REGENERATION.
JRNL REF BIOCHEMISTRY V. 51 4263 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22564171
JRNL DOI 10.1021/BI2016926
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 256745
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13623
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13450
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 701
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20133
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 352
REMARK 3 SOLVENT ATOMS : 2458
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : -1.33000
REMARK 3 B33 (A**2) : 0.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.917
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20891 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 24 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28474 ; 1.159 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48 ; 0.252 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2622 ; 5.371 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 935 ;34.545 ;23.155
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3317 ;13.491 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 208 ;15.603 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3302 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15852 ; 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): 13076 ; 0.481 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20864 ; 0.918 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7815 ; 1.374 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7610 ; 2.293 ; 4.500
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 : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4E5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 270433
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: THERMOSTABLE PHOSPHITE DEHYDROGENASE E175A VARIANT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-30% PEG 3350, 100 MM KCL, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
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 56.77000
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, 4
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: 7870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -56.77000
REMARK 350 BIOMT3 2 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: 7850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
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: 7490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G
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: 4
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: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 90.71000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 56.77000
REMARK 350 BIOMT3 2 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 LYS A 330
REMARK 465 LYS B 330
REMARK 465 MET E 1
REMARK 465 LYS E 330
REMARK 465 MET F 1
REMARK 465 PRO F 329
REMARK 465 LYS F 330
REMARK 465 PRO G 329
REMARK 465 LYS G 330
REMARK 465 LYS H 330
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN D 135 CG CD OE1 NE2
REMARK 470 MET G 1 CG SD CE
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 NH1 ARG G 56 O HOH G 1263 2.05
REMARK 500 O HOH A 939 O HOH A 1239 2.07
REMARK 500 O ARG B 298 O HOH B 1264 2.10
REMARK 500 O HOH G 902 O HOH G 1264 2.11
REMARK 500 OE1 GLU D 196 O HOH D 1275 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH F 997 O HOH F 1270 2645 2.13
REMARK 500 O HOH D 1230 O HOH E 987 1545 2.15
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 ALA A 74 58.24 -91.18
REMARK 500 PHE A 78 35.84 -94.89
REMARK 500 MET A 153 49.82 -146.23
REMARK 500 ALA A 207 47.50 -149.03
REMARK 500 CYS A 236 -85.54 -102.49
REMARK 500 ASN A 286 55.69 -94.52
REMARK 500 GLN B 29 40.98 -88.76
REMARK 500 PHE B 78 35.88 -99.07
REMARK 500 ASN B 145 -0.00 73.86
REMARK 500 MET B 153 48.49 -143.42
REMARK 500 ALA B 207 50.66 -147.15
REMARK 500 CYS B 236 -86.74 -101.78
REMARK 500 GLN C 29 33.65 -80.79
REMARK 500 ALA C 207 49.63 -146.93
REMARK 500 CYS C 236 -81.55 -104.33
REMARK 500 ASN C 286 55.13 -92.48
REMARK 500 GLN D 29 23.14 -79.10
REMARK 500 MET D 153 50.80 -140.76
REMARK 500 ALA D 207 46.44 -148.01
REMARK 500 CYS D 236 -83.35 -96.79
REMARK 500 ASN D 286 54.51 -91.44
REMARK 500 ASP E 31 49.54 -88.36
REMARK 500 PHE E 78 44.34 -102.09
REMARK 500 PRO E 136 -150.94 -71.26
REMARK 500 ARG E 137 -27.94 55.54
REMARK 500 ALA E 207 50.76 -150.74
REMARK 500 CYS E 236 -83.69 -100.01
REMARK 500 ASN E 286 56.64 -93.70
REMARK 500 PRO F 136 82.97 -67.72
REMARK 500 MET F 153 45.67 -142.16
REMARK 500 ALA F 207 56.98 -151.15
REMARK 500 CYS F 236 -85.09 -100.64
REMARK 500 ASN F 286 54.38 -96.56
REMARK 500 THR G 30 -31.05 -146.01
REMARK 500 ASP G 31 74.21 51.02
REMARK 500 THR G 33 95.73 53.85
REMARK 500 ASP G 82 91.29 -68.86
REMARK 500 ASN G 145 -0.06 67.29
REMARK 500 MET G 153 51.72 -141.75
REMARK 500 ALA G 207 49.18 -151.43
REMARK 500 CYS G 236 -85.33 -101.08
REMARK 500 ASN G 286 56.96 -92.47
REMARK 500 ARG G 298 -83.09 -39.74
REMARK 500 ALA H 74 58.74 -95.80
REMARK 500 PHE H 78 34.34 -92.75
REMARK 500 PRO H 136 78.08 -68.78
REMARK 500 MET H 153 46.38 -143.98
REMARK 500 ALA H 207 45.83 -147.20
REMARK 500 ASN H 211 -158.40 -157.64
REMARK 500 PRO H 228 93.24 -60.18
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1268 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH D1277 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH F1195 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH G1083 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH G1189 DISTANCE = 5.43 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E5M RELATED DB: PDB
REMARK 900 RELATED ID: 4E5K RELATED DB: PDB
REMARK 900 RELATED ID: 4E5P RELATED DB: PDB
DBREF 4E5N A 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N B 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N C 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N D 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N E 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N F 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N G 1 330 PDB 4E5N 4E5N 1 330
DBREF 4E5N H 1 330 PDB 4E5N 4E5N 1 330
SEQRES 1 A 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 A 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 A 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 A 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 A 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 A 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 A 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 A 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 A 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 A 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 A 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 A 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 A 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 A 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 A 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 A 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 A 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 A 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 A 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 A 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 A 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 A 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 A 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 A 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 A 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 A 330 ASN ARG LEU PRO LYS
SEQRES 1 B 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 B 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 B 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 B 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 B 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 B 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 B 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 B 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 B 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 B 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 B 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 B 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 B 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 B 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 B 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 B 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 B 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 B 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 B 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 B 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 B 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 B 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 B 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 B 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 B 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 B 330 ASN ARG LEU PRO LYS
SEQRES 1 C 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 C 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 C 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 C 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 C 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 C 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 C 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 C 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 C 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 C 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 C 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 C 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 C 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 C 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 C 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 C 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 C 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 C 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 C 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 C 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 C 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 C 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 C 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 C 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 C 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 C 330 ASN ARG LEU PRO LYS
SEQRES 1 D 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 D 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 D 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 D 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 D 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 D 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 D 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 D 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 D 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 D 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 D 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 D 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 D 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 D 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 D 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 D 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 D 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 D 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 D 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 D 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 D 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 D 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 D 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 D 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 D 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 D 330 ASN ARG LEU PRO LYS
SEQRES 1 E 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 E 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 E 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 E 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 E 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 E 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 E 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 E 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 E 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 E 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 E 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 E 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 E 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 E 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 E 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 E 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 E 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 E 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 E 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 E 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 E 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 E 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 E 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 E 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 E 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 E 330 ASN ARG LEU PRO LYS
SEQRES 1 F 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 F 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 F 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 F 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 F 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 F 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 F 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 F 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 F 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 F 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 F 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 F 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 F 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 F 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 F 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 F 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 F 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 F 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 F 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 F 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 F 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 F 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 F 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 F 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 F 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 F 330 ASN ARG LEU PRO LYS
SEQRES 1 G 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 G 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 G 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 G 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 G 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 G 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 G 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 G 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 G 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 G 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 G 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 G 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 G 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 G 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 G 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 G 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 G 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 G 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 G 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 G 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 G 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 G 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 G 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 G 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 G 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 G 330 ASN ARG LEU PRO LYS
SEQRES 1 H 330 MET LEU PRO LYS LEU VAL ILE THR HIS ARG VAL HIS GLU
SEQRES 2 H 330 GLU ILE LEU GLN LEU LEU ALA PRO HIS CYS GLU LEU ILE
SEQRES 3 H 330 THR ASN GLN THR ASP SER THR LEU THR ARG GLU GLU ILE
SEQRES 4 H 330 LEU ARG ARG CYS ARG ASP ALA GLN ALA MET MET ALA PHE
SEQRES 5 H 330 MET PRO ASP ARG VAL ASP ALA ASP PHE LEU GLN ALA CYS
SEQRES 6 H 330 PRO GLU LEU ARG VAL ILE GLY CYS ALA LEU LYS GLY PHE
SEQRES 7 H 330 ASP ASN PHE ASP VAL ASP ALA CYS THR ALA ARG GLY VAL
SEQRES 8 H 330 TRP LEU THR PHE VAL PRO ASP LEU LEU THR VAL PRO THR
SEQRES 9 H 330 ALA GLU LEU ALA ILE GLY LEU ALA VAL GLY LEU GLY ARG
SEQRES 10 H 330 HIS LEU ARG ALA ALA ASP ALA PHE VAL ARG SER GLY LYS
SEQRES 11 H 330 PHE ARG GLY TRP GLN PRO ARG PHE TYR GLY THR GLY LEU
SEQRES 12 H 330 ASP ASN ALA THR VAL GLY PHE LEU GLY MET GLY ALA ILE
SEQRES 13 H 330 GLY LEU ALA MET ALA ASP ARG LEU GLN GLY TRP GLY ALA
SEQRES 14 H 330 THR LEU GLN TYR HIS GLU ALA LYS ALA LEU ASP THR GLN
SEQRES 15 H 330 THR GLU GLN ARG LEU GLY LEU ARG GLN VAL ALA CYS SER
SEQRES 16 H 330 GLU LEU PHE ALA SER SER ASP PHE ILE LEU LEU ALA LEU
SEQRES 17 H 330 PRO LEU ASN ALA ASP THR LEU HIS LEU VAL ASN ALA GLU
SEQRES 18 H 330 LEU LEU ALA LEU VAL ARG PRO GLY ALA LEU LEU VAL ASN
SEQRES 19 H 330 PRO CYS ARG GLY SER VAL VAL ASP GLU ALA ALA VAL LEU
SEQRES 20 H 330 ALA ALA LEU GLU ARG GLY GLN LEU GLY GLY TYR ALA ALA
SEQRES 21 H 330 ASP VAL PHE GLU MET GLU ASP TRP ALA ARG ALA ASP ARG
SEQRES 22 H 330 PRO GLN GLN ILE ASP PRO ALA LEU LEU ALA HIS PRO ASN
SEQRES 23 H 330 THR LEU PHE THR PRO HIS ILE GLY SER ALA VAL ARG ALA
SEQRES 24 H 330 VAL ARG LEU GLU ILE GLU ARG CYS ALA ALA GLN ASN ILE
SEQRES 25 H 330 LEU GLN ALA LEU ALA GLY GLU ARG PRO ILE ASN ALA VAL
SEQRES 26 H 330 ASN ARG LEU PRO LYS
HET NAD A 800 44
HET NAD B 800 44
HET NAD C 800 44
HET NAD D 800 44
HET NAD E 800 44
HET NAD F 800 44
HET NAD G 800 44
HET NAD H 800 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 9 NAD 8(C21 H27 N7 O14 P2)
FORMUL 17 HOH *2458(H2 O)
HELIX 1 1 HIS A 12 ALA A 20 1 9
HELIX 2 2 THR A 35 ARG A 44 1 10
HELIX 3 3 ASP A 58 CYS A 65 1 8
HELIX 4 4 ASP A 82 ARG A 89 1 8
HELIX 5 5 LEU A 100 SER A 128 1 29
HELIX 6 6 GLY A 154 LEU A 164 1 11
HELIX 7 7 ASP A 180 GLY A 188 1 9
HELIX 8 8 ALA A 193 SER A 201 1 9
HELIX 9 9 ASN A 219 ALA A 224 1 6
HELIX 10 10 ARG A 237 ARG A 252 1 16
HELIX 11 11 PHE A 263 ASP A 267 1 5
HELIX 12 12 ASP A 278 ALA A 283 1 6
HELIX 13 13 VAL A 297 ALA A 317 1 21
SHEET 1 1 1 LYS A 4 ILE A 7 0
SHEET 2 2 1 GLU A 24 ILE A 26 0
SHEET 3 3 1 ALA A 48 ALA A 51 0
SHEET 4 4 1 VAL A 70 CYS A 73 0
SHEET 5 5 1 TRP A 92 THR A 94 0
SHEET 6 6 1 THR A 147 LEU A 151 0
SHEET 7 7 1 THR A 170 HIS A 174 0
SHEET 8 8 1 LEU A 189 GLN A 191 0
SHEET 9 9 1 PHE A 203 LEU A 206 0
SHEET 10 10 1 ALA A 230 ASN A 234 0
SHEET 11 11 1 LEU A 255 ALA A 260 0
SHEET 12 12 1 THR A 287 PHE A 289 0
SITE 1 AC1 30 LYS A 76 THR A 104 LEU A 151 GLY A 152
SITE 2 AC1 30 GLY A 154 ALA A 155 ILE A 156 HIS A 174
SITE 3 AC1 30 GLU A 175 ALA A 176 LEU A 208 PRO A 209
SITE 4 AC1 30 PRO A 235 CYS A 236 ARG A 237 ASP A 261
SITE 5 AC1 30 HIS A 292 GLY A 294 HOH A 905 HOH A 927
SITE 6 AC1 30 HOH A 937 HOH A 953 HOH A 954 HOH A 960
SITE 7 AC1 30 HOH A1008 HOH A1025 HOH A1055 HOH A1092
SITE 8 AC1 30 HOH A1151 HOH A1244
SITE 1 AC2 32 LYS B 76 GLY B 77 THR B 104 GLY B 152
SITE 2 AC2 32 GLY B 154 ALA B 155 ILE B 156 HIS B 174
SITE 3 AC2 32 GLU B 175 ALA B 176 ALA B 207 LEU B 208
SITE 4 AC2 32 PRO B 209 PRO B 235 CYS B 236 ARG B 237
SITE 5 AC2 32 ASP B 261 HIS B 292 GLY B 294 HOH B 902
SITE 6 AC2 32 HOH B 904 HOH B 910 HOH B 916 HOH B 958
SITE 7 AC2 32 HOH B 967 HOH B 979 HOH B 987 HOH B1006
SITE 8 AC2 32 HOH B1028 HOH B1039 HOH B1140 HOH B1220
SITE 1 AC3 28 LYS C 76 GLY C 77 THR C 104 GLY C 152
SITE 2 AC3 28 GLY C 154 ALA C 155 ILE C 156 HIS C 174
SITE 3 AC3 28 GLU C 175 ALA C 176 LYS C 177 ALA C 207
SITE 4 AC3 28 LEU C 208 PRO C 209 PRO C 235 CYS C 236
SITE 5 AC3 28 ARG C 237 ASP C 261 HIS C 292 GLY C 294
SITE 6 AC3 28 HOH C 911 HOH C 912 HOH C 919 HOH C 930
SITE 7 AC3 28 HOH C 971 HOH C1038 HOH C1066 HOH C1078
SITE 1 AC4 31 LYS D 76 GLY D 77 THR D 104 GLY D 152
SITE 2 AC4 31 GLY D 154 ALA D 155 ILE D 156 HIS D 174
SITE 3 AC4 31 GLU D 175 ALA D 176 ALA D 207 LEU D 208
SITE 4 AC4 31 PRO D 209 PRO D 235 CYS D 236 ARG D 237
SITE 5 AC4 31 ASP D 261 HIS D 292 GLY D 294 HOH D 904
SITE 6 AC4 31 HOH D 908 HOH D 929 HOH D 967 HOH D 977
SITE 7 AC4 31 HOH D 981 HOH D1164 HOH D1197 HOH D1237
SITE 8 AC4 31 HOH D1241 HOH D1285 HOH D1286
SITE 1 AC5 31 LYS E 76 GLY E 77 THR E 104 GLY E 152
SITE 2 AC5 31 GLY E 154 ALA E 155 ILE E 156 HIS E 174
SITE 3 AC5 31 GLU E 175 ALA E 176 ALA E 207 LEU E 208
SITE 4 AC5 31 PRO E 209 PRO E 235 CYS E 236 ARG E 237
SITE 5 AC5 31 ASP E 261 HIS E 292 GLY E 294 HOH E 906
SITE 6 AC5 31 HOH E 908 HOH E 916 HOH E 929 HOH E 939
SITE 7 AC5 31 HOH E1005 HOH E1014 HOH E1056 HOH E1067
SITE 8 AC5 31 HOH E1078 HOH E1105 HOH E1125
SITE 1 AC6 36 LYS F 76 GLY F 77 THR F 104 LEU F 151
SITE 2 AC6 36 GLY F 152 GLY F 154 ALA F 155 ILE F 156
SITE 3 AC6 36 HIS F 174 GLU F 175 ALA F 176 LYS F 177
SITE 4 AC6 36 ALA F 207 LEU F 208 PRO F 209 LEU F 217
SITE 5 AC6 36 PRO F 235 CYS F 236 ARG F 237 ASP F 261
SITE 6 AC6 36 HIS F 292 GLY F 294 HOH F 902 HOH F 904
SITE 7 AC6 36 HOH F 919 HOH F 940 HOH F 947 HOH F 972
SITE 8 AC6 36 HOH F1014 HOH F1092 HOH F1101 HOH F1143
SITE 9 AC6 36 HOH F1148 HOH F1237 HOH F1238 HOH F1242
SITE 1 AC7 33 LYS G 76 GLY G 77 THR G 104 LEU G 151
SITE 2 AC7 33 GLY G 152 GLY G 154 ALA G 155 ILE G 156
SITE 3 AC7 33 HIS G 174 GLU G 175 ALA G 176 LYS G 177
SITE 4 AC7 33 ALA G 207 LEU G 208 PRO G 209 PRO G 235
SITE 5 AC7 33 CYS G 236 ARG G 237 ASP G 261 HIS G 292
SITE 6 AC7 33 GLY G 294 HOH G 908 HOH G 915 HOH G 917
SITE 7 AC7 33 HOH G 934 HOH G 939 HOH G 972 HOH G1036
SITE 8 AC7 33 HOH G1044 HOH G1082 HOH G1106 HOH G1226
SITE 9 AC7 33 HOH G1239
SITE 1 AC8 23 LYS H 76 GLY H 77 LEU H 100 THR H 104
SITE 2 AC8 23 GLY H 154 ALA H 155 ILE H 156 HIS H 174
SITE 3 AC8 23 GLU H 175 ALA H 176 ALA H 207 LEU H 208
SITE 4 AC8 23 PRO H 209 PRO H 235 CYS H 236 ARG H 237
SITE 5 AC8 23 ASP H 261 HIS H 292 GLY H 294 HOH H 910
SITE 6 AC8 23 HOH H 942 HOH H 954 HOH H1023
CRYST1 90.710 113.540 130.190 90.00 100.16 90.00 P 1 21 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 0.011024 0.000000 0.001976 0.00000
SCALE2 0.000000 0.008807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007803 0.00000
ATOM 1 N MET A 1 0.071 41.550 19.059 1.00 36.71 N
ATOM 2 CA MET A 1 -0.198 40.478 18.057 1.00 36.49 C
ATOM 3 C MET A 1 1.074 39.709 17.681 1.00 35.42 C
ATOM 4 O MET A 1 1.901 40.186 16.895 1.00 35.82 O
ATOM 5 CB MET A 1 -0.866 41.060 16.800 1.00 37.28 C
ATOM 6 CG MET A 1 -2.346 41.435 16.970 1.00 39.86 C
ATOM 7 SD MET A 1 -3.039 42.250 15.503 1.00 45.46 S
ATOM 8 CE MET A 1 -4.730 42.526 16.032 1.00 44.37 C
ATOM 9 N LEU A 2 1.226 38.522 18.258 1.00 33.43 N
ATOM 10 CA LEU A 2 2.295 37.602 17.877 1.00 31.42 C
ATOM 11 C LEU A 2 1.921 36.909 16.566 1.00 29.94 C
ATOM 12 O LEU A 2 0.743 36.881 16.211 1.00 29.74 O
ATOM 13 CB LEU A 2 2.489 36.554 18.971 1.00 31.31 C
ATOM 14 CG LEU A 2 2.923 37.054 20.352 1.00 31.20 C
ATOM 15 CD1 LEU A 2 2.645 35.984 21.399 1.00 30.74 C
ATOM 16 CD2 LEU A 2 4.390 37.451 20.350 1.00 31.29 C
ATOM 17 N PRO A 3 2.915 36.351 15.843 1.00 28.64 N
ATOM 18 CA PRO A 3 2.571 35.559 14.655 1.00 27.67 C
ATOM 19 C PRO A 3 1.686 34.367 15.020 1.00 26.50 C
ATOM 20 O PRO A 3 1.899 33.722 16.046 1.00 25.89 O
ATOM 21 CB PRO A 3 3.932 35.084 14.127 1.00 27.35 C
ATOM 22 CG PRO A 3 4.899 35.303 15.261 1.00 28.26 C
ATOM 23 CD PRO A 3 4.374 36.495 15.997 1.00 28.66 C
ATOM 24 N LYS A 4 0.690 34.103 14.183 1.00 25.44 N
ATOM 25 CA LYS A 4 -0.276 33.044 14.432 1.00 24.62 C
ATOM 26 C LYS A 4 0.237 31.713 13.883 1.00 23.30 C
ATOM 27 O LYS A 4 0.614 31.620 12.714 1.00 22.85 O
ATOM 28 CB LYS A 4 -1.611 33.418 13.794 1.00 25.27 C
ATOM 29 CG LYS A 4 -2.702 32.401 13.972 1.00 27.41 C
ATOM 30 CD LYS A 4 -4.053 33.031 13.689 1.00 30.65 C
ATOM 31 CE LYS A 4 -5.003 31.996 13.133 1.00 32.64 C
ATOM 32 NZ LYS A 4 -4.377 31.335 11.974 1.00 33.97 N
ATOM 33 N LEU A 5 0.260 30.692 14.738 1.00 21.38 N
ATOM 34 CA LEU A 5 0.719 29.357 14.340 1.00 19.61 C
ATOM 35 C LEU A 5 -0.407 28.347 14.539 1.00 19.17 C
ATOM 36 O LEU A 5 -0.948 28.223 15.642 1.00 18.83 O
ATOM 37 CB LEU A 5 1.950 28.942 15.163 1.00 19.61 C
ATOM 38 CG LEU A 5 2.322 27.453 15.195 1.00 19.25 C
ATOM 39 CD1 LEU A 5 2.689 26.924 13.812 1.00 18.79 C
ATOM 40 CD2 LEU A 5 3.469 27.223 16.173 1.00 17.83 C
ATOM 41 N VAL A 6 -0.743 27.632 13.466 1.00 18.23 N
ATOM 42 CA VAL A 6 -1.767 26.602 13.495 1.00 17.92 C
ATOM 43 C VAL A 6 -1.055 25.255 13.591 1.00 18.08 C
ATOM 44 O VAL A 6 -0.177 24.938 12.788 1.00 17.94 O
ATOM 45 CB VAL A 6 -2.685 26.664 12.237 1.00 17.90 C
ATOM 46 CG1 VAL A 6 -3.542 25.404 12.102 1.00 17.69 C
ATOM 47 CG2 VAL A 6 -3.576 27.902 12.273 1.00 17.73 C
ATOM 48 N ILE A 7 -1.404 24.493 14.621 1.00 17.58 N
ATOM 49 CA ILE A 7 -0.846 23.163 14.809 1.00 17.60 C
ATOM 50 C ILE A 7 -1.987 22.196 14.565 1.00 17.63 C
ATOM 51 O ILE A 7 -2.967 22.172 15.327 1.00 17.46 O
ATOM 52 CB ILE A 7 -0.263 22.989 16.223 1.00 17.40 C
ATOM 53 CG1 ILE A 7 0.687 24.152 16.541 1.00 18.24 C
ATOM 54 CG2 ILE A 7 0.465 21.642 16.338 1.00 17.13 C
ATOM 55 CD1 ILE A 7 1.297 24.132 17.937 1.00 20.05 C
ATOM 56 N THR A 8 -1.873 21.405 13.501 1.00 17.49 N
ATOM 57 CA THR A 8 -3.031 20.674 12.986 1.00 17.70 C
ATOM 58 C THR A 8 -3.395 19.429 13.787 1.00 17.49 C
ATOM 59 O THR A 8 -4.521 18.953 13.686 1.00 17.48 O
ATOM 60 CB THR A 8 -2.861 20.272 11.497 1.00 18.15 C
ATOM 61 OG1 THR A 8 -1.791 19.331 11.383 1.00 18.65 O
ATOM 62 CG2 THR A 8 -2.553 21.488 10.634 1.00 18.79 C
ATOM 63 N HIS A 9 -2.441 18.919 14.564 1.00 17.21 N
ATOM 64 CA HIS A 9 -2.627 17.724 15.385 1.00 17.46 C
ATOM 65 C HIS A 9 -2.052 17.908 16.792 1.00 17.42 C
ATOM 66 O HIS A 9 -1.294 18.846 17.046 1.00 16.99 O
ATOM 67 CB HIS A 9 -2.008 16.496 14.697 1.00 17.17 C
ATOM 68 CG HIS A 9 -2.779 16.040 13.503 1.00 18.09 C
ATOM 69 ND1 HIS A 9 -2.728 16.697 12.293 1.00 17.61 N
ATOM 70 CD2 HIS A 9 -3.654 15.018 13.343 1.00 18.26 C
ATOM 71 CE1 HIS A 9 -3.529 16.091 11.436 1.00 19.45 C
ATOM 72 NE2 HIS A 9 -4.105 15.071 12.049 1.00 20.04 N
ATOM 73 N ARG A 10 -2.423 16.994 17.691 1.00 18.02 N
ATOM 74 CA ARG A 10 -2.031 17.037 19.090 1.00 19.13 C
ATOM 75 C ARG A 10 -0.525 16.950 19.284 1.00 19.34 C
ATOM 76 O ARG A 10 0.138 16.088 18.697 1.00 19.81 O
ATOM 77 CB ARG A 10 -2.685 15.874 19.837 1.00 19.42 C
ATOM 78 CG ARG A 10 -2.540 15.936 21.335 1.00 22.75 C
ATOM 79 CD ARG A 10 -3.103 14.671 21.937 1.00 27.49 C
ATOM 80 NE ARG A 10 -3.825 14.970 23.165 1.00 32.02 N
ATOM 81 CZ ARG A 10 -4.734 14.172 23.716 1.00 35.09 C
ATOM 82 NH1 ARG A 10 -5.043 13.008 23.150 1.00 36.24 N
ATOM 83 NH2 ARG A 10 -5.339 14.542 24.838 1.00 36.21 N
ATOM 84 N VAL A 11 0.001 17.834 20.127 1.00 18.97 N
ATOM 85 CA VAL A 11 1.415 17.809 20.495 1.00 19.29 C
ATOM 86 C VAL A 11 1.535 17.799 22.011 1.00 19.97 C
ATOM 87 O VAL A 11 0.552 18.043 22.702 1.00 20.24 O
ATOM 88 CB VAL A 11 2.182 19.015 19.917 1.00 19.37 C
ATOM 89 CG1 VAL A 11 2.185 18.957 18.375 1.00 19.27 C
ATOM 90 CG2 VAL A 11 1.590 20.336 20.418 1.00 17.53 C
ATOM 91 N HIS A 12 2.731 17.508 22.516 1.00 20.80 N
ATOM 92 CA HIS A 12 3.008 17.576 23.954 1.00 21.71 C
ATOM 93 C HIS A 12 2.816 18.997 24.477 1.00 22.37 C
ATOM 94 O HIS A 12 3.180 19.966 23.806 1.00 22.35 O
ATOM 95 CB HIS A 12 4.432 17.102 24.240 1.00 21.72 C
ATOM 96 CG HIS A 12 4.624 15.629 24.066 1.00 23.40 C
ATOM 97 ND1 HIS A 12 4.682 15.025 22.829 1.00 24.47 N
ATOM 98 CD2 HIS A 12 4.783 14.637 24.976 1.00 25.99 C
ATOM 99 CE1 HIS A 12 4.860 13.724 22.982 1.00 26.09 C
ATOM 100 NE2 HIS A 12 4.926 13.463 24.276 1.00 26.00 N
ATOM 101 N GLU A 13 2.238 19.122 25.672 1.00 23.31 N
ATOM 102 CA GLU A 13 1.975 20.446 26.252 1.00 23.95 C
ATOM 103 C GLU A 13 3.226 21.309 26.436 1.00 24.19 C
ATOM 104 O GLU A 13 3.147 22.534 26.383 1.00 24.60 O
ATOM 105 CB GLU A 13 1.190 20.330 27.561 1.00 24.43 C
ATOM 106 CG GLU A 13 -0.234 19.861 27.339 1.00 25.76 C
ATOM 107 CD GLU A 13 -0.984 19.567 28.622 1.00 28.24 C
ATOM 108 OE1 GLU A 13 -0.346 19.315 29.670 1.00 29.50 O
ATOM 109 OE2 GLU A 13 -2.228 19.568 28.561 1.00 29.47 O
ATOM 110 N GLU A 14 4.381 20.680 26.629 1.00 24.37 N
ATOM 111 CA GLU A 14 5.610 21.447 26.779 1.00 25.02 C
ATOM 112 C GLU A 14 6.090 22.059 25.463 1.00 24.60 C
ATOM 113 O GLU A 14 6.812 23.050 25.475 1.00 24.32 O
ATOM 114 CB GLU A 14 6.708 20.633 27.462 1.00 25.79 C
ATOM 115 CG GLU A 14 7.335 19.538 26.634 1.00 28.38 C
ATOM 116 CD GLU A 14 8.614 19.033 27.270 1.00 32.59 C
ATOM 117 OE1 GLU A 14 8.596 17.925 27.844 1.00 34.45 O
ATOM 118 OE2 GLU A 14 9.634 19.758 27.218 1.00 35.67 O
ATOM 119 N ILE A 15 5.674 21.473 24.337 1.00 23.68 N
ATOM 120 CA ILE A 15 5.951 22.057 23.023 1.00 23.09 C
ATOM 121 C ILE A 15 5.101 23.314 22.838 1.00 23.00 C
ATOM 122 O ILE A 15 5.567 24.318 22.293 1.00 22.18 O
ATOM 123 CB ILE A 15 5.691 21.052 21.864 1.00 23.09 C
ATOM 124 CG1 ILE A 15 6.580 19.808 22.009 1.00 22.23 C
ATOM 125 CG2 ILE A 15 5.883 21.736 20.494 1.00 22.75 C
ATOM 126 CD1 ILE A 15 8.088 20.080 21.988 1.00 23.89 C
ATOM 127 N LEU A 16 3.856 23.259 23.307 1.00 23.14 N
ATOM 128 CA LEU A 16 3.012 24.450 23.317 1.00 23.80 C
ATOM 129 C LEU A 16 3.633 25.552 24.183 1.00 24.21 C
ATOM 130 O LEU A 16 3.601 26.720 23.811 1.00 23.92 O
ATOM 131 CB LEU A 16 1.588 24.120 23.785 1.00 23.63 C
ATOM 132 CG LEU A 16 0.763 23.100 22.986 1.00 23.72 C
ATOM 133 CD1 LEU A 16 -0.635 22.964 23.561 1.00 24.02 C
ATOM 134 CD2 LEU A 16 0.692 23.471 21.516 1.00 24.33 C
ATOM 135 N GLN A 17 4.209 25.162 25.322 1.00 25.46 N
ATOM 136 CA GLN A 17 4.899 26.092 26.226 1.00 26.93 C
ATOM 137 C GLN A 17 6.113 26.745 25.580 1.00 26.70 C
ATOM 138 O GLN A 17 6.370 27.934 25.795 1.00 27.15 O
ATOM 139 CB GLN A 17 5.333 25.390 27.514 1.00 27.51 C
ATOM 140 CG GLN A 17 4.242 25.258 28.553 1.00 31.40 C
ATOM 141 CD GLN A 17 4.702 24.505 29.801 1.00 35.49 C
ATOM 142 OE1 GLN A 17 5.375 23.472 29.712 1.00 38.40 O
ATOM 143 NE2 GLN A 17 4.320 25.009 30.968 1.00 37.12 N
ATOM 144 N LEU A 18 6.863 25.956 24.815 1.00 26.30 N
ATOM 145 CA LEU A 18 8.003 26.454 24.051 1.00 26.31 C
ATOM 146 C LEU A 18 7.569 27.485 23.000 1.00 26.11 C
ATOM 147 O LEU A 18 8.235 28.499 22.799 1.00 26.19 O
ATOM 148 CB LEU A 18 8.729 25.282 23.376 1.00 26.32 C
ATOM 149 CG LEU A 18 9.902 25.554 22.426 1.00 27.27 C
ATOM 150 CD1 LEU A 18 11.098 26.130 23.181 1.00 28.58 C
ATOM 151 CD2 LEU A 18 10.299 24.279 21.705 1.00 28.59 C
ATOM 152 N LEU A 19 6.443 27.228 22.343 1.00 25.79 N
ATOM 153 CA LEU A 19 5.981 28.089 21.254 1.00 25.55 C
ATOM 154 C LEU A 19 5.243 29.346 21.732 1.00 26.02 C
ATOM 155 O LEU A 19 5.382 30.413 21.135 1.00 26.14 O
ATOM 156 CB LEU A 19 5.105 27.285 20.279 1.00 25.22 C
ATOM 157 CG LEU A 19 5.831 26.223 19.440 1.00 24.62 C
ATOM 158 CD1 LEU A 19 4.847 25.220 18.840 1.00 25.00 C
ATOM 159 CD2 LEU A 19 6.674 26.878 18.357 1.00 23.40 C
ATOM 160 N ALA A 20 4.475 29.217 22.814 1.00 26.44 N
ATOM 161 CA ALA A 20 3.552 30.276 23.264 1.00 27.12 C
ATOM 162 C ALA A 20 4.118 31.708 23.412 1.00 27.54 C
ATOM 163 O ALA A 20 3.411 32.675 23.092 1.00 28.00 O
ATOM 164 CB ALA A 20 2.811 29.849 24.532 1.00 27.25 C
ATOM 165 N PRO A 21 5.375 31.862 23.889 1.00 28.01 N
ATOM 166 CA PRO A 21 5.897 33.234 23.998 1.00 28.43 C
ATOM 167 C PRO A 21 6.089 33.926 22.650 1.00 28.57 C
ATOM 168 O PRO A 21 6.047 35.158 22.579 1.00 28.80 O
ATOM 169 CB PRO A 21 7.262 33.040 24.672 1.00 28.38 C
ATOM 170 CG PRO A 21 7.149 31.772 25.401 1.00 28.70 C
ATOM 171 CD PRO A 21 6.282 30.897 24.537 1.00 28.13 C
ATOM 172 N HIS A 22 6.291 33.134 21.599 1.00 28.37 N
ATOM 173 CA HIS A 22 6.603 33.661 20.280 1.00 28.32 C
ATOM 174 C HIS A 22 5.396 33.658 19.345 1.00 27.77 C
ATOM 175 O HIS A 22 5.371 34.387 18.358 1.00 27.80 O
ATOM 176 CB HIS A 22 7.724 32.842 19.635 1.00 28.72 C
ATOM 177 CG HIS A 22 8.903 32.594 20.529 1.00 30.71 C
ATOM 178 ND1 HIS A 22 9.980 33.452 20.597 1.00 33.03 N
ATOM 179 CD2 HIS A 22 9.187 31.567 21.366 1.00 32.04 C
ATOM 180 CE1 HIS A 22 10.871 32.972 21.447 1.00 33.06 C
ATOM 181 NE2 HIS A 22 10.415 31.829 21.928 1.00 34.00 N
ATOM 182 N CYS A 23 4.408 32.821 19.641 1.00 27.14 N
ATOM 183 CA CYS A 23 3.340 32.547 18.699 1.00 26.69 C
ATOM 184 C CYS A 23 1.990 32.563 19.376 1.00 26.17 C
ATOM 185 O CYS A 23 1.858 32.109 20.508 1.00 26.34 O
ATOM 186 CB CYS A 23 3.556 31.171 18.050 1.00 26.26 C
ATOM 187 SG CYS A 23 5.098 31.009 17.129 1.00 29.08 S
ATOM 188 N GLU A 24 0.995 33.094 18.673 1.00 25.94 N
ATOM 189 CA GLU A 24 -0.398 32.919 19.042 1.00 26.07 C
ATOM 190 C GLU A 24 -0.810 31.547 18.516 1.00 25.38 C
ATOM 191 O GLU A 24 -0.753 31.294 17.308 1.00 25.25 O
ATOM 192 CB GLU A 24 -1.259 34.044 18.449 1.00 26.57 C
ATOM 193 CG GLU A 24 -2.762 33.745 18.430 1.00 30.00 C
ATOM 194 CD GLU A 24 -3.649 34.969 18.584 1.00 34.43 C
ATOM 195 OE1 GLU A 24 -3.153 36.113 18.479 1.00 37.22 O
ATOM 196 OE2 GLU A 24 -4.866 34.779 18.822 1.00 37.45 O
ATOM 197 N LEU A 25 -1.210 30.664 19.428 1.00 24.38 N
ATOM 198 CA LEU A 25 -1.438 29.255 19.093 1.00 23.68 C
ATOM 199 C LEU A 25 -2.888 28.928 18.772 1.00 23.28 C
ATOM 200 O LEU A 25 -3.801 29.280 19.521 1.00 23.34 O
ATOM 201 CB LEU A 25 -0.935 28.341 20.217 1.00 23.84 C