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HEADER HYDROLASE 13-FEB-14 4OYY
TITLE HUMICOLA INSOLENS CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMICOLA INSOLENS;
SOURCE 3 ORGANISM_TAXID: 34413;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.D.DAUTER,A.M.BRZOZOWSKI,J.P.TURKENBURG,K.S.WILSON
REVDAT 1 30-JUL-14 4OYY 0
JRNL AUTH D.KOLD,Z.DAUTER,A.K.LAUSTSEN,A.M.BRZOZOWSKI,J.P.TURKENBURG,
JRNL AUTH 2 A.D.NIELSEN,H.KOLDS,E.PETERSEN,B.SCHITT,L.DE MARIA,
JRNL AUTH 3 K.S.WILSON,A.SVENDSEN,R.WIMMER
JRNL TITL THERMODYNAMIC AND STRUCTURAL INVESTIGATION OF THE SPECIFIC
JRNL TITL 2 SDS BINDING OF HUMICOLA INSOLENS CUTINASE.
JRNL REF PROTEIN SCI. V. 23 1023 2014
JRNL REFN ESSN 1469-896X
JRNL PMID 24832484
JRNL DOI 10.1002/PRO.2489
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 42118
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3010
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16877
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : 2.39000
REMARK 3 B33 (A**2) : -1.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.378
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.276
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.789
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17189 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 16543 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23355 ; 1.445 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 37829 ; 1.539 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2289 ; 5.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 731 ;36.083 ;23.844
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2624 ;16.371 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 141 ;16.258 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2630 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20270 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3987 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9192 ; 1.757 ; 2.617
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9191 ; 1.756 ; 2.617
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11469 ; 2.917 ; 3.924
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11470 ; 2.918 ; 3.924
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7997 ; 2.312 ; 2.925
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7998 ; 2.312 ; 2.926
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11887 ; 3.869 ; 4.271
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 18530 ; 5.390 ;20.771
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 18531 ; 5.390 ;20.773
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 66
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 193 B 3 193 11229 0.07 0.05
REMARK 3 2 A 3 192 C 3 192 11032 0.07 0.05
REMARK 3 3 A 3 193 D 3 193 11457 0.05 0.05
REMARK 3 4 A 3 193 E 3 193 11074 0.07 0.05
REMARK 3 5 A 3 192 F 3 192 11069 0.07 0.05
REMARK 3 6 A 3 192 G 3 192 11234 0.06 0.05
REMARK 3 7 A 3 193 H 3 193 11337 0.06 0.05
REMARK 3 8 A 3 192 I 3 192 11051 0.06 0.05
REMARK 3 9 A 3 193 J 3 193 11380 0.06 0.05
REMARK 3 10 A 3 193 K 3 193 11244 0.06 0.05
REMARK 3 11 A 3 192 L 3 192 11035 0.08 0.05
REMARK 3 12 B 3 192 C 3 192 10906 0.08 0.05
REMARK 3 13 B 3 193 D 3 193 11228 0.07 0.05
REMARK 3 14 B 3 193 E 3 193 11103 0.08 0.05
REMARK 3 15 B 3 192 F 3 192 10953 0.08 0.05
REMARK 3 16 B 3 192 G 3 192 11015 0.08 0.05
REMARK 3 17 B 3 193 H 3 193 11358 0.06 0.05
REMARK 3 18 B 3 192 I 3 192 10892 0.07 0.05
REMARK 3 19 B 3 193 J 3 193 11144 0.08 0.05
REMARK 3 20 B 3 193 K 3 193 11276 0.06 0.05
REMARK 3 21 B 3 192 L 3 192 10938 0.09 0.05
REMARK 3 22 C 3 192 D 3 192 11018 0.07 0.05
REMARK 3 23 C 3 192 E 3 192 10864 0.08 0.05
REMARK 3 24 C 1 193 F 1 193 11392 0.06 0.05
REMARK 3 25 C 1 193 G 1 193 11237 0.07 0.05
REMARK 3 26 C 3 192 H 3 192 10955 0.08 0.05
REMARK 3 27 C 1 193 I 1 193 11180 0.07 0.05
REMARK 3 28 C 3 192 J 3 192 11039 0.07 0.05
REMARK 3 29 C 3 192 K 3 192 11005 0.07 0.05
REMARK 3 30 C 2 192 L 2 192 11165 0.08 0.05
REMARK 3 31 D 3 193 E 3 193 11063 0.07 0.05
REMARK 3 32 D 3 192 F 3 192 11086 0.06 0.05
REMARK 3 33 D 3 192 G 3 192 11198 0.06 0.05
REMARK 3 34 D 3 193 H 3 193 11294 0.06 0.05
REMARK 3 35 D 3 192 I 3 192 11035 0.06 0.05
REMARK 3 36 D 3 193 J 3 193 11337 0.07 0.05
REMARK 3 37 D 3 193 K 3 193 11235 0.06 0.05
REMARK 3 38 D 3 192 L 3 192 11017 0.08 0.05
REMARK 3 39 E 3 192 F 3 192 10860 0.08 0.05
REMARK 3 40 E 3 192 G 3 192 10944 0.07 0.05
REMARK 3 41 E 3 193 H 3 193 11114 0.07 0.05
REMARK 3 42 E 3 192 I 3 192 10782 0.08 0.05
REMARK 3 43 E 3 193 J 3 193 11063 0.07 0.05
REMARK 3 44 E 3 193 K 3 193 11106 0.07 0.05
REMARK 3 45 E 3 192 L 3 192 10872 0.09 0.05
REMARK 3 46 F 1 193 G 1 193 11233 0.07 0.05
REMARK 3 47 F 3 192 H 3 192 11004 0.08 0.05
REMARK 3 48 F 1 193 I 1 193 11286 0.06 0.05
REMARK 3 49 F 3 192 J 3 192 11039 0.07 0.05
REMARK 3 50 F 3 192 K 3 192 11025 0.07 0.05
REMARK 3 51 F 2 192 L 2 192 11188 0.08 0.05
REMARK 3 52 G 3 192 H 3 192 11094 0.07 0.05
REMARK 3 53 G 1 193 I 1 193 11177 0.07 0.05
REMARK 3 54 G 3 192 J 3 192 11210 0.05 0.05
REMARK 3 55 G 3 192 K 3 192 11065 0.06 0.05
REMARK 3 56 G 2 192 L 2 192 11107 0.08 0.05
REMARK 3 57 H 3 192 I 3 192 10945 0.07 0.05
REMARK 3 58 H 3 193 J 3 193 11261 0.07 0.05
REMARK 3 59 H 3 193 K 3 193 11350 0.05 0.05
REMARK 3 60 H 3 192 L 3 192 10971 0.09 0.05
REMARK 3 61 I 3 192 J 3 192 10954 0.07 0.05
REMARK 3 62 I 3 192 K 3 192 11121 0.05 0.05
REMARK 3 63 I 2 192 L 2 192 11042 0.08 0.05
REMARK 3 64 J 3 193 K 3 193 11196 0.07 0.05
REMARK 3 65 J 3 192 L 3 192 11101 0.07 0.05
REMARK 3 66 K 3 192 L 3 192 11032 0.08 0.05
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4OYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-95
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43738
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HICUTINASE 30 MG ML-1, 0.1 M TRIS/HCL
REMARK 280 BUFFER PH 8.5, 50 MM LYSINE, 100 MG ML-1 (APP. 8.6%) ISOPROPANOL,
REMARK 280 50 MG ML-1 (APP. 4.3 %) DIOXANE, PEG 4K 22% V/V OF 50% W/V
REMARK 280 STOCK SOLUTIONS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 62.77400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.25250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.49950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.25250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.77400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.49950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 LEU A 2
REMARK 465 ALA A 194
REMARK 465 GLN B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 194
REMARK 465 ALA C 194
REMARK 465 GLN D 1
REMARK 465 LEU D 2
REMARK 465 ALA D 194
REMARK 465 GLN E 1
REMARK 465 LEU E 2
REMARK 465 ALA E 194
REMARK 465 ALA F 194
REMARK 465 ALA G 194
REMARK 465 GLN H 1
REMARK 465 LEU H 2
REMARK 465 ALA H 194
REMARK 465 ALA I 194
REMARK 465 GLN J 1
REMARK 465 LEU J 2
REMARK 465 ALA J 194
REMARK 465 GLN K 1
REMARK 465 LEU K 2
REMARK 465 ALA K 194
REMARK 465 GLN L 1
REMARK 465 ALA L 194
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 ARG B 141 CD NE CZ NH1 NH2
REMARK 470 ARG E 141 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 47 CD OE1 OE2
REMARK 470 ASN I 15 CG OD1 ND2
REMARK 470 ARG I 149 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 181 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 MET B 34 CG - SD - CE ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG C 51 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ALA E 4 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG F 51 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG G 51 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ILE G 192 CA - CB - CG1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU H 167 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG H 186 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG H 186 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG H 193 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG J 51 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG J 73 N - CA - CB ANGL. DEV. = -11.0 DEGREES
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 29 -1.05 72.38
REMARK 500 THR A 37 -91.19 -110.89
REMARK 500 ARG A 73 -3.82 84.15
REMARK 500 SER A 105 -124.36 57.64
REMARK 500 THR B 29 -1.41 74.48
REMARK 500 THR B 37 -90.53 -110.47
REMARK 500 ARG B 73 -3.35 84.56
REMARK 500 SER B 105 -123.28 56.38
REMARK 500 ALA C 4 -11.85 -141.30
REMARK 500 THR C 29 -0.23 73.13
REMARK 500 THR C 37 -92.79 -110.37
REMARK 500 ARG C 73 -2.63 84.92
REMARK 500 SER C 105 -123.23 56.88
REMARK 500 THR D 37 -91.06 -110.64
REMARK 500 ARG D 73 -3.67 85.69
REMARK 500 SER D 105 -122.95 56.69
REMARK 500 ALA E 4 -31.23 148.78
REMARK 500 THR E 29 -0.43 72.14
REMARK 500 THR E 37 -91.47 -110.41
REMARK 500 ARG E 73 -3.23 84.07
REMARK 500 SER E 105 -123.25 57.61
REMARK 500 THR F 37 -92.25 -109.67
REMARK 500 ARG F 73 -2.84 84.52
REMARK 500 SER F 105 -122.64 56.23
REMARK 500 THR G 37 -91.44 -110.56
REMARK 500 ARG G 73 -3.55 84.17
REMARK 500 SER G 105 -124.04 57.69
REMARK 500 THR H 29 -1.89 73.91
REMARK 500 THR H 37 -91.44 -110.59
REMARK 500 ARG H 73 -3.87 84.64
REMARK 500 SER H 105 -122.82 57.79
REMARK 500 THR I 37 -92.63 -109.76
REMARK 500 ARG I 73 -2.47 85.21
REMARK 500 SER I 105 -123.83 57.08
REMARK 500 THR J 29 -7.44 78.12
REMARK 500 THR J 37 -91.02 -110.26
REMARK 500 SER J 105 -123.92 58.44
REMARK 500 THR K 29 -0.95 72.93
REMARK 500 THR K 37 -91.32 -110.56
REMARK 500 ARG K 73 -3.02 84.66
REMARK 500 SER K 105 -123.12 58.30
REMARK 500 THR L 29 -0.05 72.38
REMARK 500 THR L 37 -92.27 -110.39
REMARK 500 SER L 105 -123.19 56.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN C 1 LEU C 2 -144.00
REMARK 500 GLY C 3 ALA C 4 -43.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OYL RELATED DB: PDB
REMARK 900 CUTINASE COMPLEXED WITH MONOETHYLPHOSPHATE
DBREF 4OYY A 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY B 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY C 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY D 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY E 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY F 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY G 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY H 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY I 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY J 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY K 1 194 PDB PDB 4OYY 1 194
DBREF 4OYY L 1 194 PDB PDB 4OYY 1 194
SEQRES 1 A 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 A 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 A 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 A 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 A 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 A 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 A 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 A 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 A 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 A 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 A 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 A 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 A 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 A 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 A 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 B 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 B 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 B 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 B 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 B 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 B 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 B 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 B 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 B 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 B 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 B 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 B 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 B 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 B 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 B 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 C 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 C 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 C 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 C 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 C 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 C 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 C 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 C 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 C 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 C 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 C 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 C 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 C 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 C 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 C 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 D 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 D 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 D 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 D 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 D 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 D 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 D 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 D 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 D 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 D 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 D 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 D 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 D 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 D 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 D 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 E 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 E 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 E 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 E 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 E 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 E 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 E 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 E 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 E 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 E 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 E 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 E 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 E 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 E 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 E 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 F 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 F 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 F 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 F 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 F 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 F 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 F 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 F 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 F 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 F 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 F 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 F 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 F 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 F 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 F 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 G 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 G 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 G 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 G 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 G 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 G 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 G 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 G 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 G 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 G 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 G 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 G 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 G 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 G 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 G 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 H 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 H 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 H 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 H 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 H 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 H 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 H 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 H 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 H 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 H 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 H 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 H 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 H 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 H 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 H 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 I 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 I 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 I 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 I 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 I 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 I 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 I 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 I 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 I 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 I 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 I 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 I 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 I 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 I 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 I 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 J 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 J 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 J 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 J 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 J 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 J 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 J 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 J 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 J 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 J 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 J 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 J 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 J 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 J 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 J 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 K 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 K 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 K 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 K 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 K 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 K 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 K 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 K 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 K 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 K 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 K 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 K 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 K 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 K 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 K 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 L 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 L 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 L 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 L 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 L 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 L 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 L 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 L 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 L 194 SER GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 L 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 L 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 L 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 L 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 L 194 THR PRO ALA HIS LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 L 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
FORMUL 13 HOH *98(H2 O)
HELIX 1 AA1 ASN A 7 GLY A 12 1 6
HELIX 2 AA2 SER A 13 CYS A 17 5 5
HELIX 3 AA3 THR A 37 SER A 48 1 12
HELIX 4 AA4 LEU A 66 LEU A 71 5 6
HELIX 5 AA5 SER A 76 CYS A 94 1 19
HELIX 6 AA6 SER A 105 GLU A 117 1 13
HELIX 7 AA7 SER A 119 GLN A 125 1 7
HELIX 8 AA8 PRO A 148 GLU A 150 5 3
HELIX 9 AA9 ASP A 160 GLY A 165 5 6
HELIX 10 AB1 THR A 170 SER A 175 5 6
HELIX 11 AB2 TYR A 176 GLY A 182 1 7
HELIX 12 AB3 GLY A 182 ARG A 193 1 12
HELIX 13 AB4 ASN B 7 GLY B 12 1 6
HELIX 14 AB5 SER B 13 CYS B 17 5 5
HELIX 15 AB6 THR B 37 SER B 48 1 12
HELIX 16 AB7 LEU B 66 LEU B 71 5 6
HELIX 17 AB8 SER B 76 CYS B 94 1 19
HELIX 18 AB9 SER B 105 GLU B 117 1 13
HELIX 19 AC1 SER B 119 GLN B 125 1 7
HELIX 20 AC2 PRO B 148 GLU B 150 5 3
HELIX 21 AC3 ASP B 160 GLY B 165 5 6
HELIX 22 AC4 THR B 170 SER B 175 5 6
HELIX 23 AC5 TYR B 176 GLY B 182 1 7
HELIX 24 AC6 GLY B 182 ARG B 193 1 12
HELIX 25 AC7 ASN C 7 GLY C 12 1 6
HELIX 26 AC8 THR C 37 SER C 48 1 12
HELIX 27 AC9 LEU C 66 LEU C 71 5 6
HELIX 28 AD1 SER C 76 CYS C 94 1 19
HELIX 29 AD2 SER C 105 GLU C 117 1 13
HELIX 30 AD3 SER C 119 GLN C 125 1 7
HELIX 31 AD4 PRO C 148 GLU C 150 5 3
HELIX 32 AD5 ASP C 160 GLY C 165 5 6
HELIX 33 AD6 THR C 170 SER C 175 5 6
HELIX 34 AD7 TYR C 176 GLY C 182 1 7
HELIX 35 AD8 GLY C 182 ILE C 192 1 11
HELIX 36 AD9 ASN D 7 GLY D 12 1 6
HELIX 37 AE1 SER D 13 CYS D 17 5 5
HELIX 38 AE2 THR D 37 SER D 48 1 12
HELIX 39 AE3 LEU D 66 LEU D 71 5 6
HELIX 40 AE4 SER D 76 CYS D 94 1 19
HELIX 41 AE5 SER D 105 GLU D 117 1 13
HELIX 42 AE6 SER D 119 GLN D 125 1 7
HELIX 43 AE7 PRO D 148 GLU D 150 5 3
HELIX 44 AE8 ASP D 160 GLY D 165 5 6
HELIX 45 AE9 THR D 170 SER D 175 5 6
HELIX 46 AF1 TYR D 176 GLY D 182 1 7
HELIX 47 AF2 GLY D 182 ARG D 193 1 12
HELIX 48 AF3 ASN E 7 GLY E 12 1 6
HELIX 49 AF4 SER E 13 CYS E 17 5 5
HELIX 50 AF5 THR E 37 SER E 48 1 12
HELIX 51 AF6 LEU E 66 LEU E 71 5 6
HELIX 52 AF7 SER E 76 CYS E 94 1 19
HELIX 53 AF8 SER E 105 GLU E 117 1 13
HELIX 54 AF9 SER E 119 GLN E 125 1 7
HELIX 55 AG1 PRO E 148 GLU E 150 5 3
HELIX 56 AG2 ASP E 160 GLY E 165 5 6
HELIX 57 AG3 THR E 170 SER E 175 5 6
HELIX 58 AG4 TYR E 176 GLY E 182 1 7
HELIX 59 AG5 GLY E 182 ARG E 193 1 12
HELIX 60 AG6 ASN F 7 GLY F 12 1 6
HELIX 61 AG7 THR F 37 SER F 48 1 12
HELIX 62 AG8 LEU F 66 LEU F 71 5 6
HELIX 63 AG9 SER F 76 CYS F 94 1 19
HELIX 64 AH1 SER F 105 GLU F 117 1 13
HELIX 65 AH2 SER F 119 GLN F 125 1 7
HELIX 66 AH3 PRO F 148 GLU F 150 5 3
HELIX 67 AH4 ASP F 160 GLY F 165 5 6
HELIX 68 AH5 THR F 170 SER F 175 5 6
HELIX 69 AH6 TYR F 176 GLY F 182 1 7
HELIX 70 AH7 GLY F 182 ILE F 192 1 11
HELIX 71 AH8 ASN G 7 GLY G 12 1 6
HELIX 72 AH9 THR G 37 SER G 48 1 12
HELIX 73 AI1 LEU G 66 LEU G 71 5 6
HELIX 74 AI2 SER G 76 CYS G 94 1 19
HELIX 75 AI3 SER G 105 GLU G 117 1 13
HELIX 76 AI4 SER G 119 GLN G 125 1 7
HELIX 77 AI5 PRO G 148 GLU G 150 5 3
HELIX 78 AI6 ASP G 160 GLY G 165 5 6
HELIX 79 AI7 THR G 170 SER G 175 5 6
HELIX 80 AI8 TYR G 176 GLY G 182 1 7
HELIX 81 AI9 GLY G 182 ARG G 193 1 12
HELIX 82 AJ1 ASN H 7 GLY H 12 1 6
HELIX 83 AJ2 SER H 13 CYS H 17 5 5
HELIX 84 AJ3 THR H 37 SER H 48 1 12
HELIX 85 AJ4 LEU H 66 LEU H 71 5 6
HELIX 86 AJ5 SER H 76 CYS H 94 1 19
HELIX 87 AJ6 SER H 105 GLU H 117 1 13
HELIX 88 AJ7 SER H 119 GLN H 125 1 7
HELIX 89 AJ8 PRO H 148 GLU H 150 5 3
HELIX 90 AJ9 ASP H 160 GLY H 165 5 6
HELIX 91 AK1 THR H 170 SER H 175 5 6
HELIX 92 AK2 TYR H 176 GLY H 182 1 7
HELIX 93 AK3 GLY H 182 ARG H 193 1 12
HELIX 94 AK4 ASN I 7 GLY I 12 1 6
HELIX 95 AK5 SER I 13 CYS I 17 5 5
HELIX 96 AK6 THR I 37 SER I 48 1 12
HELIX 97 AK7 LEU I 66 LEU I 71 5 6
HELIX 98 AK8 SER I 76 CYS I 94 1 19
HELIX 99 AK9 SER I 105 GLU I 117 1 13
HELIX 100 AL1 SER I 119 GLN I 125 1 7
HELIX 101 AL2 PRO I 148 GLU I 150 5 3
HELIX 102 AL3 ASP I 160 GLY I 165 5 6
HELIX 103 AL4 THR I 170 SER I 175 5 6
HELIX 104 AL5 TYR I 176 GLY I 182 1 7
HELIX 105 AL6 GLY I 182 ILE I 192 1 11
HELIX 106 AL7 ASN J 7 GLY J 12 1 6
HELIX 107 AL8 THR J 37 SER J 48 1 12
HELIX 108 AL9 LEU J 66 LEU J 71 5 6
HELIX 109 AM1 SER J 76 CYS J 94 1 19
HELIX 110 AM2 SER J 105 GLU J 117 1 13
HELIX 111 AM3 SER J 119 GLN J 125 1 7
HELIX 112 AM4 PRO J 148 GLU J 150 5 3
HELIX 113 AM5 ASP J 160 GLY J 165 5 6
HELIX 114 AM6 THR J 170 SER J 175 5 6
HELIX 115 AM7 TYR J 176 GLY J 182 1 7
HELIX 116 AM8 GLY J 182 ARG J 193 1 12
HELIX 117 AM9 ASN K 7 GLY K 12 1 6
HELIX 118 AN1 SER K 13 CYS K 17 5 5
HELIX 119 AN2 THR K 37 SER K 48 1 12
HELIX 120 AN3 LEU K 66 LEU K 71 5 6
HELIX 121 AN4 SER K 76 CYS K 94 1 19
HELIX 122 AN5 SER K 105 GLU K 117 1 13
HELIX 123 AN6 SER K 119 GLN K 125 1 7
HELIX 124 AN7 PRO K 148 GLU K 150 5 3
HELIX 125 AN8 ASP K 160 GLY K 165 5 6
HELIX 126 AN9 THR K 170 SER K 175 5 6
HELIX 127 AO1 TYR K 176 GLY K 182 1 7
HELIX 128 AO2 GLY K 182 ARG K 193 1 12
HELIX 129 AO3 ASN L 7 GLY L 12 1 6
HELIX 130 AO4 SER L 13 CYS L 17 5 5
HELIX 131 AO5 THR L 37 SER L 48 1 12
HELIX 132 AO6 LEU L 66 LEU L 71 5 6
HELIX 133 AO7 SER L 76 CYS L 94 1 19
HELIX 134 AO8 SER L 105 GLU L 117 1 13
HELIX 135 AO9 SER L 119 GLN L 125 1 7
HELIX 136 AP1 PRO L 148 GLU L 150 5 3
HELIX 137 AP2 ASP L 160 GLY L 165 5 6
HELIX 138 AP3 THR L 170 SER L 175 5 6
HELIX 139 AP4 TYR L 176 GLY L 182 1 7
HELIX 140 AP5 GLY L 182 ILE L 192 1 11
SHEET 1 AA1 5 ILE A 53 GLY A 57 0
SHEET 2 AA1 5 ALA A 20 ALA A 25 1 N LEU A 22 O TRP A 54
SHEET 3 AA1 5 VAL A 99 TYR A 104 1 O VAL A 100 N ILE A 21
SHEET 4 AA1 5 VAL A 126 PHE A 132 1 O ALA A 130 N ALA A 101
SHEET 5 AA1 5 THR A 152 PHE A 155 1 O PHE A 155 N LEU A 131
SHEET 1 AA2 5 ILE B 53 GLY B 57 0
SHEET 2 AA2 5 ALA B 20 ALA B 25 1 N LEU B 22 O TRP B 54
SHEET 3 AA2 5 VAL B 99 TYR B 104 1 O VAL B 100 N ILE B 21
SHEET 4 AA2 5 VAL B 126 PHE B 132 1 O ALA B 130 N ALA B 101
SHEET 5 AA2 5 THR B 152 PHE B 155 1 O PHE B 155 N LEU B 131
SHEET 1 AA3 5 ILE C 53 GLY C 57 0
SHEET 2 AA3 5 ALA C 20 ALA C 25 1 N LEU C 22 O TRP C 54
SHEET 3 AA3 5 VAL C 99 TYR C 104 1 O VAL C 100 N ILE C 21
SHEET 4 AA3 5 VAL C 126 PHE C 132 1 O ALA C 130 N ALA C 101
SHEET 5 AA3 5 THR C 152 PHE C 155 1 O PHE C 155 N LEU C 131
SHEET 1 AA4 5 ILE D 53 GLY D 57 0
SHEET 2 AA4 5 ALA D 20 ALA D 25 1 N LEU D 22 O TRP D 54
SHEET 3 AA4 5 VAL D 99 TYR D 104 1 O VAL D 100 N ILE D 21
SHEET 4 AA4 5 VAL D 126 PHE D 132 1 O ALA D 130 N ALA D 101
SHEET 5 AA4 5 THR D 152 PHE D 155 1 O PHE D 155 N LEU D 131
SHEET 1 AA5 5 ILE E 53 GLY E 57 0
SHEET 2 AA5 5 ALA E 20 ALA E 25 1 N LEU E 22 O TRP E 54
SHEET 3 AA5 5 VAL E 99 TYR E 104 1 O VAL E 100 N ILE E 21
SHEET 4 AA5 5 VAL E 126 PHE E 132 1 O ALA E 130 N ALA E 101
SHEET 5 AA5 5 THR E 152 PHE E 155 1 O PHE E 155 N LEU E 131
SHEET 1 AA6 5 ILE F 53 GLY F 57 0
SHEET 2 AA6 5 ALA F 20 ALA F 25 1 N LEU F 22 O TRP F 54
SHEET 3 AA6 5 VAL F 99 TYR F 104 1 O VAL F 100 N ILE F 21
SHEET 4 AA6 5 VAL F 126 PHE F 132 1 O ALA F 130 N ALA F 101
SHEET 5 AA6 5 THR F 152 PHE F 155 1 O PHE F 155 N LEU F 131
SHEET 1 AA7 5 ILE G 53 GLY G 57 0
SHEET 2 AA7 5 ALA G 20 ALA G 25 1 N LEU G 22 O TRP G 54
SHEET 3 AA7 5 VAL G 99 TYR G 104 1 O VAL G 100 N ILE G 21
SHEET 4 AA7 5 VAL G 126 PHE G 132 1 O ALA G 130 N ALA G 101
SHEET 5 AA7 5 THR G 152 PHE G 155 1 O PHE G 155 N LEU G 131
SHEET 1 AA8 5 ILE H 53 GLY H 57 0
SHEET 2 AA8 5 ALA H 20 ALA H 25 1 N PHE H 24 O GLN H 56
SHEET 3 AA8 5 VAL H 99 TYR H 104 1 O VAL H 100 N ILE H 21
SHEET 4 AA8 5 VAL H 126 PHE H 132 1 O ALA H 130 N ALA H 101
SHEET 5 AA8 5 THR H 152 PHE H 155 1 O PHE H 155 N LEU H 131
SHEET 1 AA9 5 ILE I 53 GLY I 57 0
SHEET 2 AA9 5 ALA I 20 ALA I 25 1 N LEU I 22 O TRP I 54
SHEET 3 AA9 5 VAL I 99 TYR I 104 1 O VAL I 100 N ILE I 21
SHEET 4 AA9 5 VAL I 126 PHE I 132 1 O ALA I 130 N ALA I 101
SHEET 5 AA9 5 THR I 152 PHE I 155 1 O PHE I 155 N LEU I 131
SHEET 1 AB1 5 ILE J 53 GLY J 57 0
SHEET 2 AB1 5 ALA J 20 ALA J 25 1 N LEU J 22 O TRP J 54
SHEET 3 AB1 5 VAL J 99 TYR J 104 1 O VAL J 100 N ILE J 21
SHEET 4 AB1 5 VAL J 126 PHE J 132 1 O ALA J 130 N ALA J 101
SHEET 5 AB1 5 THR J 152 PHE J 155 1 O PHE J 155 N LEU J 131
SHEET 1 AB2 5 ILE K 53 GLY K 57 0
SHEET 2 AB2 5 ALA K 20 ALA K 25 1 N LEU K 22 O TRP K 54
SHEET 3 AB2 5 VAL K 99 TYR K 104 1 O VAL K 100 N ILE K 21
SHEET 4 AB2 5 VAL K 126 PHE K 132 1 O ALA K 130 N ALA K 101
SHEET 5 AB2 5 THR K 152 PHE K 155 1 O PHE K 155 N LEU K 131
SHEET 1 AB3 5 ILE L 53 GLY L 57 0
SHEET 2 AB3 5 ALA L 20 ALA L 25 1 N LEU L 22 O TRP L 54
SHEET 3 AB3 5 VAL L 99 TYR L 104 1 O VAL L 100 N ILE L 21
SHEET 4 AB3 5 VAL L 126 PHE L 132 1 O ALA L 130 N ALA L 101
SHEET 5 AB3 5 THR L 152 PHE L 155 1 O PHE L 155 N LEU L 131
SSBOND 1 CYS A 17 CYS A 94 1555 1555 2.04
SSBOND 2 CYS A 156 CYS A 163 1555 1555 2.03
SSBOND 3 CYS B 17 CYS B 94 1555 1555 2.02
SSBOND 4 CYS B 156 CYS B 163 1555 1555 2.02
SSBOND 5 CYS C 17 CYS C 94 1555 1555 2.02
SSBOND 6 CYS C 156 CYS C 163 1555 1555 1.99
SSBOND 7 CYS D 17 CYS D 94 1555 1555 2.02
SSBOND 8 CYS D 156 CYS D 163 1555 1555 2.03
SSBOND 9 CYS E 17 CYS E 94 1555 1555 2.03
SSBOND 10 CYS E 156 CYS E 163 1555 1555 2.01
SSBOND 11 CYS F 17 CYS F 94 1555 1555 2.01
SSBOND 12 CYS F 156 CYS F 163 1555 1555 2.00
SSBOND 13 CYS G 17 CYS G 94 1555 1555 2.02
SSBOND 14 CYS G 156 CYS G 163 1555 1555 2.02
SSBOND 15 CYS H 17 CYS H 94 1555 1555 2.02
SSBOND 16 CYS H 156 CYS H 163 1555 1555 2.01
SSBOND 17 CYS I 17 CYS I 94 1555 1555 2.03
SSBOND 18 CYS I 156 CYS I 163 1555 1555 2.00
SSBOND 19 CYS J 17 CYS J 94 1555 1555 2.02
SSBOND 20 CYS J 156 CYS J 163 1555 1555 2.01
SSBOND 21 CYS K 17 CYS K 94 1555 1555 2.02
SSBOND 22 CYS K 156 CYS K 163 1555 1555 2.00
SSBOND 23 CYS L 17 CYS L 94 1555 1555 2.02
SSBOND 24 CYS L 156 CYS L 163 1555 1555 2.01
CISPEP 1 GLY A 3 ALA A 4 0 1.47
CISPEP 2 GLY B 3 ALA B 4 0 2.80
CISPEP 3 GLY D 3 ALA D 4 0 1.54
CISPEP 4 GLY E 3 ALA E 4 0 12.96
CISPEP 5 GLY H 3 ALA H 4 0 1.99
CISPEP 6 GLY J 3 ALA J 4 0 1.64
CISPEP 7 GLY K 3 ALA K 4 0 2.62
CRYST1 125.548 126.999 134.505 90.00 90.00 90.00 P 21 21 21 48
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 0.007965 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007435 0.00000
TER 1403 ARG A 193
TER 2801 ARG B 193
TER 4221 ARG C 193
TER 5624 ARG D 193
TER 7021 ARG E 193
TER 8441 ARG F 193
TER 9858 ARG G 193
TER 11261 ARG H 193
TER 12672 ARG I 193
TER 14075 ARG J 193
TER 15478 ARG K 193
TER 16889 ARG L 193
MASTER 536 0 0 140 60 0 0 616975 12 48 180
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