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HEADER HYDROLASE/HYDROLASE INHIBITOR 02-SEP-16 5GV5
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B WITH ACTIVE SER105
TITLE 2 MODIFIED WITH A PHOSPHONATE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 STRAIN: T-34;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5061
KEYWDS LIPASE, INHIBITOR, PHOSPHONATE, CAL-B, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.PARK,H.LEE
REVDAT 1 13-SEP-17 5GV5 0
JRNL AUTH H.LEE,S.S.PARK,S.Y.PARK
JRNL TITL STRUCTURAL AND EXPERIMENTAL EVIDENCES FOR ITS ENANTIOMERIC
JRNL TITL 2 RECOGNITION TOWARDS A BULKY SEC-ALCOHOL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.89 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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 70652
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3750
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4930
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 256
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18514
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 432
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.50000
REMARK 3 B22 (A**2) : 4.95000
REMARK 3 B33 (A**2) : -2.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.64000
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): 0.350
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.264
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19530 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 18222 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26860 ; 1.743 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 42012 ; 0.999 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2524 ; 6.671 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 664 ;36.798 ;25.060
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2708 ;16.337 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;18.123 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3168 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22176 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4072 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 10126 ; 2.027 ; 3.515
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 10125 ; 2.024 ; 3.514
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12640 ; 3.301 ; 5.264
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 12641 ; 3.301 ; 5.264
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9404 ; 2.348 ; 3.766
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9404 ; 2.348 ; 3.766
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 14221 ; 3.860 ; 5.588
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 21840 ; 6.068 ;28.833
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 21841 ; 6.068 ;28.837
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 5GV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74402
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.43200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM DIHYDROGEN PHOSPHATE,
REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 61.61100
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, 5, 6, 7, 8
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 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 LEU C 147
REMARK 465 GLY D 142
REMARK 465 PRO D 143
REMARK 465 LEU D 144
REMARK 465 ASP D 145
REMARK 465 ALA D 146
REMARK 465 LEU D 147
REMARK 465 ALA D 148
REMARK 465 VAL D 149
REMARK 465 ALA E 146
REMARK 465 LEU E 147
REMARK 465 ALA E 148
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 ND2 ASN B 74 O5 NAG B 402 1.77
REMARK 500 ND2 ASN D 74 O5 NAG D 402 2.02
REMARK 500 O ILE A 176 OG1 THR B 244 2.16
REMARK 500 OD2 ASP B 296 OG SER B 312 2.17
REMARK 500 OD2 ASP F 6 OG SER F 120 2.18
REMARK 500 O VAL C 139 O ALA C 141 2.18
REMARK 500 ND2 ASN C 74 O5 NAG C 402 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 296 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG C 249 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 LEU C 278 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG E 122 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LEU E 278 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG F 249 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU H 219 CB - CG - CD1 ANGL. DEV. = -10.2 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 ASP A 17 -34.79 -39.88
REMARK 500 ASN A 51 -87.64 -127.56
REMARK 500 ASP A 75 122.99 -34.32
REMARK 500 ASN A 96 48.98 39.82
REMARK 500 SER A 105 -127.08 55.88
REMARK 500 ASP A 134 74.26 -105.88
REMARK 500 ALA A 305 37.78 -147.12
REMARK 500 ASN B 51 -69.09 -131.05
REMARK 500 MET B 72 12.83 58.23
REMARK 500 SER B 105 -129.69 48.98
REMARK 500 ALA B 132 50.66 34.10
REMARK 500 ILE B 176 -53.58 -123.43
REMARK 500 SER B 312 4.00 -65.26
REMARK 500 PRO C 7 159.93 -49.01
REMARK 500 ASN C 51 -72.58 -138.38
REMARK 500 SER C 67 77.02 -118.12
REMARK 500 MET C 72 10.41 56.52
REMARK 500 ASN C 96 70.32 54.01
REMARK 500 SER C 105 -123.96 58.62
REMARK 500 PHE C 118 78.40 -118.13
REMARK 500 ASP C 134 60.57 -103.50
REMARK 500 ASN C 196 61.19 33.13
REMARK 500 ASN C 206 -8.35 78.68
REMARK 500 ALA C 305 32.26 -140.72
REMARK 500 THR C 310 -161.33 -117.78
REMARK 500 LYS D 32 59.80 30.91
REMARK 500 ASN D 51 -72.79 -136.17
REMARK 500 MET D 72 19.20 52.02
REMARK 500 ASN D 96 56.52 38.50
REMARK 500 SER D 105 -127.46 58.53
REMARK 500 ASP D 134 71.93 -103.67
REMARK 500 SER D 161 150.42 -44.44
REMARK 500 ASN D 206 -0.81 66.13
REMARK 500 ALA D 263 131.67 -31.75
REMARK 500 PRO D 299 -52.16 -28.26
REMARK 500 ASN E 51 -81.35 -131.27
REMARK 500 ASN E 96 71.50 47.71
REMARK 500 SER E 105 -126.80 51.92
REMARK 500 ARG E 127 163.68 173.95
REMARK 500 ASP E 134 69.80 -116.15
REMARK 500 ILE E 176 -51.87 -123.21
REMARK 500 PRO E 198 1.21 -69.67
REMARK 500 ALA E 263 123.75 -31.30
REMARK 500 PRO F 2 153.64 -45.54
REMARK 500 ASN F 51 -74.63 -137.26
REMARK 500 ASP F 75 123.37 -32.25
REMARK 500 ASN F 96 55.74 38.54
REMARK 500 SER F 105 -116.22 61.83
REMARK 500 ASP F 134 68.80 -113.82
REMARK 500 ALA F 146 -0.23 -58.05
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MSW A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 402 through NAG A 405 bound to ASN A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 402 through NAG B 403 bound to ASN B 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 402 through NAG C 405 bound to ASN C 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D
REMARK 800 402 through NAG D 403 bound to ASN D 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E
REMARK 800 402 through NAG E 403 bound to ASN E 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG F
REMARK 800 402 through NAG F 403 bound to ASN F 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G
REMARK 800 402 through NAG G 403 bound to ASN G 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG H
REMARK 800 402 through NAG H 403 bound to ASN H 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW B 401 and SER B
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW C 401 and SER C
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW D 401 and SER D
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW E 401 and SER E
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW F 401 and SER F
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW G 401 and SER G
REMARK 800 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MSW H 401 and SER H
REMARK 800 105
DBREF 5GV5 A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 B 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 C 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 D 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 E 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 F 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 G 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 5GV5 H 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 A 317 GLY ILE VAL THR PRO
SEQRES 1 B 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 B 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 B 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 B 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 B 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 B 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 B 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 B 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 B 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 B 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 B 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 B 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 B 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 B 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 B 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 B 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 B 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 B 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 B 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 B 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 B 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 B 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 B 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 B 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 B 317 GLY ILE VAL THR PRO
SEQRES 1 C 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 C 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 C 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 C 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 C 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 C 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 C 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 C 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 C 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 C 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 C 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 C 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 C 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 C 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 C 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 C 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 C 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 C 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 C 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 C 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 C 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 C 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 C 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 C 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 C 317 GLY ILE VAL THR PRO
SEQRES 1 D 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 D 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 D 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 D 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 D 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 D 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 D 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 D 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 D 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 D 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 D 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 D 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 D 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 D 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 D 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 D 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 D 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 D 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 D 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 D 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 D 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 D 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 D 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 D 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 D 317 GLY ILE VAL THR PRO
SEQRES 1 E 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 E 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 E 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 E 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 E 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 E 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 E 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 E 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 E 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 E 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 E 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 E 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 E 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 E 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 E 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 E 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 E 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 E 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 E 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 E 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 E 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 E 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 E 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 E 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 E 317 GLY ILE VAL THR PRO
SEQRES 1 F 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 F 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 F 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 F 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 F 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 F 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 F 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 F 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 F 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 F 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 F 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 F 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 F 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 F 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 F 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 F 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 F 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 F 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 F 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 F 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 F 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 F 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 F 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 F 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 F 317 GLY ILE VAL THR PRO
SEQRES 1 G 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 G 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 G 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 G 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 G 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 G 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 G 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 G 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 G 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 G 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 G 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 G 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 G 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 G 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 G 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 G 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 G 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 G 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 G 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 G 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 G 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 G 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 G 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 G 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 G 317 GLY ILE VAL THR PRO
SEQRES 1 H 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 H 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 H 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 H 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 H 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 H 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 H 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 H 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 H 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 H 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 H 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 H 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 H 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 H 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 H 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 H 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 H 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 H 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 H 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 H 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 H 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 H 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 H 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 H 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 H 317 GLY ILE VAL THR PRO
MODRES 5GV5 NAG A 402 NAG -D
MODRES 5GV5 NAG A 403 NAG -D
MODRES 5GV5 NAG A 404 NAG -D
MODRES 5GV5 NAG A 405 NAG -D
MODRES 5GV5 NAG B 402 NAG -D
MODRES 5GV5 NAG B 403 NAG -D
MODRES 5GV5 NAG C 402 NAG -D
MODRES 5GV5 NAG C 403 NAG -D
MODRES 5GV5 NAG C 404 NAG -D
MODRES 5GV5 NAG C 405 NAG -D
MODRES 5GV5 NAG D 402 NAG -D
MODRES 5GV5 NAG D 403 NAG -D
MODRES 5GV5 NAG E 402 NAG -D
MODRES 5GV5 NAG E 403 NAG -D
MODRES 5GV5 NAG F 402 NAG -D
MODRES 5GV5 NAG F 403 NAG -D
MODRES 5GV5 NAG G 402 NAG -D
MODRES 5GV5 NAG G 403 NAG -D
MODRES 5GV5 NAG H 402 NAG -D
MODRES 5GV5 NAG H 403 NAG -D
HET MSW A 401 19
HET NAG A 402 14
HET NAG A 403 14
HET NAG A 404 14
HET NAG A 405 14
HET MSW B 401 19
HET NAG B 402 14
HET NAG B 403 14
HET MSW C 401 19
HET NAG C 402 14
HET NAG C 403 14
HET NAG C 404 14
HET NAG C 405 14
HET MSW D 401 19
HET NAG D 402 14
HET NAG D 403 14
HET MSW E 401 19
HET NAG E 402 14
HET NAG E 403 14
HET MSW F 401 19
HET NAG F 402 14
HET NAG F 403 14
HET MSW G 401 19
HET NAG G 402 14
HET NAG G 403 14
HET MSW H 401 19
HET NAG H 402 14
HET NAG H 403 14
HETNAM MSW [(1S)-2-(METHOXYCARBONYLAMINO)-1-PHENYL-ETHOXY]-PROPYL-
HETNAM 2 MSW PHOSPHINIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 9 MSW 8(C13 H20 N O5 P)
FORMUL 10 NAG 20(C8 H15 N O6)
HELIX 1 AA1 PRO A 12 ALA A 18 1 7
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 SER A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 THR A 138 LEU A 140 5 3
HELIX 8 AA8 ALA A 141 LEU A 147 1 7
HELIX 9 AA9 ALA A 151 GLN A 157 1 7
HELIX 10 AB1 SER A 161 ALA A 170 1 10
HELIX 11 AB2 ALA A 212 GLY A 217 1 6
HELIX 12 AB3 ALA A 225 SER A 230 1 6
HELIX 13 AB4 SER A 230 SER A 243 1 14
HELIX 14 AB5 ARG A 249 TYR A 253 5 5
HELIX 15 AB6 GLY A 254 CYS A 258 5 5
HELIX 16 AB7 THR A 267 ALA A 276 1 10
HELIX 17 AB8 LEU A 278 ALA A 287 1 10
HELIX 18 AB9 MET A 298 ALA A 305 5 8
HELIX 19 AC1 PRO B 12 GLY B 19 1 8
HELIX 20 AC2 THR B 43 ASP B 49 1 7
HELIX 21 AC3 ASN B 51 LEU B 59 1 9
HELIX 22 AC4 ASP B 75 SER B 94 1 20
HELIX 23 AC5 SER B 105 PHE B 118 1 14
HELIX 24 AC6 PHE B 118 SER B 123 1 6
HELIX 25 AC7 ALA B 141 LEU B 147 1 7
HELIX 26 AC8 ALA B 151 GLN B 156 1 6
HELIX 27 AC9 SER B 161 ALA B 170 1 10
HELIX 28 AD1 ALA B 212 GLY B 217 1 6
HELIX 29 AD2 ALA B 225 SER B 230 1 6
HELIX 30 AD3 SER B 230 SER B 243 1 14
HELIX 31 AD4 ARG B 249 TYR B 253 5 5
HELIX 32 AD5 GLY B 254 CYS B 258 5 5
HELIX 33 AD6 THR B 267 ALA B 276 1 10
HELIX 34 AD7 LEU B 277 ALA B 287 1 11
HELIX 35 AD8 ALA B 301 VAL B 306 5 6
HELIX 36 AD9 PRO C 12 GLY C 19 1 8
HELIX 37 AE1 THR C 43 ASP C 49 1 7
HELIX 38 AE2 ASN C 51 LEU C 59 1 9
HELIX 39 AE3 ASP C 75 SER C 94 1 20
HELIX 40 AE4 SER C 105 PHE C 118 1 14
HELIX 41 AE5 PRO C 119 SER C 123 5 5
HELIX 42 AE6 ALA C 151 GLN C 157 1 7
HELIX 43 AE7 SER C 161 ALA C 170 1 10
HELIX 44 AE8 ALA C 212 GLY C 217 1 6
HELIX 45 AE9 ALA C 225 SER C 230 1 6
HELIX 46 AF1 SER C 230 SER C 243 1 14
HELIX 47 AF2 ARG C 249 TYR C 253 5 5
HELIX 48 AF3 GLY C 254 CYS C 258 5 5
HELIX 49 AF4 THR C 267 ALA C 276 1 10
HELIX 50 AF5 LEU C 278 GLY C 288 1 11
HELIX 51 AF6 ALA C 301 ALA C 305 5 5
HELIX 52 AF7 PRO D 12 ASP D 17 1 6
HELIX 53 AF8 THR D 43 ASP D 49 1 7
HELIX 54 AF9 ASN D 51 GLY D 60 1 10
HELIX 55 AG1 ASP D 75 SER D 94 1 20
HELIX 56 AG2 SER D 105 PHE D 118 1 14
HELIX 57 AG3 PRO D 119 ARG D 122 5 4
HELIX 58 AG4 ALA D 151 GLN D 157 1 7
HELIX 59 AG5 SER D 161 ALA D 170 1 10
HELIX 60 AG6 ALA D 212 GLY D 217 1 6
HELIX 61 AG7 ALA D 225 SER D 230 1 6
HELIX 62 AG8 SER D 230 SER D 243 1 14
HELIX 63 AG9 ARG D 249 TYR D 253 5 5
HELIX 64 AH1 GLY D 254 CYS D 258 5 5
HELIX 65 AH2 THR D 267 ALA D 276 1 10
HELIX 66 AH3 LEU D 278 GLY D 288 1 11
HELIX 67 AH4 ALA D 301 ALA D 305 5 5
HELIX 68 AH5 PRO E 12 GLY E 19 1 8
HELIX 69 AH6 THR E 43 ASP E 49 1 7
HELIX 70 AH7 ASN E 51 LEU E 59 1 9
HELIX 71 AH8 ASP E 75 SER E 94 1 20
HELIX 72 AH9 SER E 105 PHE E 118 1 14
HELIX 73 AI1 PRO E 119 SER E 123 5 5
HELIX 74 AI2 ALA E 151 GLN E 157 1 7
HELIX 75 AI3 SER E 161 ALA E 170 1 10
HELIX 76 AI4 ALA E 212 GLY E 217 1 6
HELIX 77 AI5 ALA E 225 SER E 230 1 6
HELIX 78 AI6 SER E 230 SER E 243 1 14
HELIX 79 AI7 ARG E 249 TYR E 253 5 5
HELIX 80 AI8 GLY E 254 CYS E 258 5 5
HELIX 81 AI9 THR E 267 ALA E 275 1 9
HELIX 82 AJ1 LEU E 278 GLY E 288 1 11
HELIX 83 AJ2 ALA E 301 VAL E 306 5 6
HELIX 84 AJ3 PRO F 12 GLY F 19 1 8
HELIX 85 AJ4 THR F 43 ASP F 49 1 7
HELIX 86 AJ5 ASN F 51 GLY F 60 1 10
HELIX 87 AJ6 ASP F 75 SER F 94 1 20
HELIX 88 AJ7 SER F 105 PHE F 118 1 14
HELIX 89 AJ8 PRO F 119 ARG F 122 5 4
HELIX 90 AJ9 LEU F 140 ALA F 146 1 7
HELIX 91 AK1 ALA F 151 GLN F 157 1 7
HELIX 92 AK2 SER F 161 ALA F 170 1 10
HELIX 93 AK3 ALA F 212 GLY F 217 1 6
HELIX 94 AK4 ASP F 223 SER F 230 1 8
HELIX 95 AK5 SER F 230 SER F 243 1 14
HELIX 96 AK6 ARG F 249 TYR F 253 5 5
HELIX 97 AK7 GLY F 254 CYS F 258 5 5
HELIX 98 AK8 THR F 267 ALA F 276 1 10
HELIX 99 AK9 LEU F 277 GLY F 288 1 12
HELIX 100 AL1 ALA F 301 VAL F 306 5 6
HELIX 101 AL2 PRO G 12 GLY G 19 1 8
HELIX 102 AL3 THR G 43 ASP G 49 1 7
HELIX 103 AL4 ASN G 51 LEU G 59 1 9
HELIX 104 AL5 ASP G 75 SER G 94 1 20
HELIX 105 AL6 SER G 105 PHE G 118 1 14
HELIX 106 AL7 PRO G 119 SER G 123 5 5
HELIX 107 AL8 ALA G 141 LEU G 147 1 7
HELIX 108 AL9 ALA G 151 GLN G 157 1 7
HELIX 109 AM1 SER G 161 ALA G 170 1 10
HELIX 110 AM2 ALA G 212 GLY G 217 1 6
HELIX 111 AM3 ASP G 223 SER G 230 1 8
HELIX 112 AM4 SER G 230 SER G 243 1 14
HELIX 113 AM5 ARG G 249 TYR G 253 5 5
HELIX 114 AM6 GLY G 254 CYS G 258 5 5
HELIX 115 AM7 THR G 267 ALA G 276 1 10
HELIX 116 AM8 LEU G 278 GLY G 288 1 11
HELIX 117 AM9 ALA G 301 VAL G 306 5 6
HELIX 118 AN1 PRO H 12 ALA H 18 1 7
HELIX 119 AN2 THR H 43 ASP H 49 1 7
HELIX 120 AN3 ASN H 51 LEU H 59 1 9
HELIX 121 AN4 ASP H 75 GLY H 93 1 19
HELIX 122 AN5 SER H 105 PHE H 118 1 14
HELIX 123 AN6 PRO H 119 SER H 123 5 5
HELIX 124 AN7 THR H 138 LEU H 140 5 3
HELIX 125 AN8 ALA H 141 LEU H 147 1 7
HELIX 126 AN9 ALA H 151 GLN H 157 1 7
HELIX 127 AO1 SER H 161 ALA H 170 1 10
HELIX 128 AO2 ALA H 212 GLY H 217 1 6
HELIX 129 AO3 ALA H 225 SER H 230 1 6
HELIX 130 AO4 SER H 230 SER H 243 1 14
HELIX 131 AO5 ARG H 249 TYR H 253 5 5
HELIX 132 AO6 GLY H 254 CYS H 258 5 5
HELIX 133 AO7 THR H 267 ALA H 276 1 10
HELIX 134 AO8 LEU H 277 ALA H 287 1 11
HELIX 135 AO9 ALA H 301 ALA H 305 5 5
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N ILE A 34 O CYS A 64
SHEET 4 AA1 7 LEU A 99 TRP A 104 1 O LEU A 102 N VAL A 37
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O PHE A 131 N THR A 103
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O LEU A 182 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N ILE B 34 O CYS B 64
SHEET 4 AA3 7 LEU B 99 TRP B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O ASP B 126 N LEU B 99
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O LEU B 182 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SHEET 1 AA5 7 LEU C 20 CYS C 22 0
SHEET 2 AA5 7 THR C 62 ILE C 66 -1 O TRP C 65 N THR C 21
SHEET 3 AA5 7 PRO C 33 VAL C 37 1 N LEU C 36 O CYS C 64
SHEET 4 AA5 7 LEU C 99 TRP C 104 1 O LEU C 102 N LEU C 35
SHEET 5 AA5 7 VAL C 125 PHE C 131 1 O ARG C 127 N VAL C 101
SHEET 6 AA5 7 THR C 179 TYR C 183 1 O THR C 180 N ALA C 130
SHEET 7 AA5 7 LYS C 208 GLN C 211 1 O VAL C 210 N ASN C 181
SHEET 1 AA6 7 LEU D 20 CYS D 22 0
SHEET 2 AA6 7 THR D 62 ILE D 66 -1 O TRP D 65 N THR D 21
SHEET 3 AA6 7 PRO D 33 VAL D 37 1 N ILE D 34 O CYS D 64
SHEET 4 AA6 7 LEU D 99 TRP D 104 1 O LEU D 102 N LEU D 35
SHEET 5 AA6 7 VAL D 125 PHE D 131 1 O MET D 129 N VAL D 101
SHEET 6 AA6 7 THR D 179 TYR D 183 1 O THR D 180 N ALA D 130
SHEET 7 AA6 7 LYS D 208 GLN D 211 1 O VAL D 210 N ASN D 181
SHEET 1 AA7 2 ARG D 309 THR D 310 0
SHEET 2 AA7 2 GLY D 313 ILE D 314 -1 O GLY D 313 N THR D 310
SHEET 1 AA8 7 LEU E 20 CYS E 22 0
SHEET 2 AA8 7 THR E 62 ILE E 66 -1 O TRP E 65 N THR E 21
SHEET 3 AA8 7 PRO E 33 VAL E 37 1 N LEU E 36 O CYS E 64
SHEET 4 AA8 7 LEU E 99 TRP E 104 1 O LEU E 102 N LEU E 35
SHEET 5 AA8 7 VAL E 125 PHE E 131 1 O PHE E 131 N THR E 103
SHEET 6 AA8 7 THR E 179 TYR E 183 1 O THR E 180 N ALA E 130
SHEET 7 AA8 7 LYS E 208 GLN E 211 1 O VAL E 210 N ASN E 181
SHEET 1 AA9 7 LEU F 20 CYS F 22 0
SHEET 2 AA9 7 THR F 62 ILE F 66 -1 O TRP F 65 N THR F 21
SHEET 3 AA9 7 PRO F 33 VAL F 37 1 N LEU F 36 O CYS F 64
SHEET 4 AA9 7 LEU F 99 TRP F 104 1 O LEU F 102 N VAL F 37
SHEET 5 AA9 7 VAL F 125 PHE F 131 1 O ASP F 126 N LEU F 99
SHEET 6 AA9 7 THR F 179 TYR F 183 1 O LEU F 182 N ALA F 130
SHEET 7 AA9 7 LYS F 208 GLN F 211 1 O VAL F 210 N ASN F 181
SHEET 1 AB1 7 LEU G 20 CYS G 22 0
SHEET 2 AB1 7 THR G 62 ILE G 66 -1 O TRP G 65 N THR G 21
SHEET 3 AB1 7 PRO G 33 VAL G 37 1 N LEU G 36 O CYS G 64
SHEET 4 AB1 7 LEU G 99 TRP G 104 1 O LEU G 102 N VAL G 37
SHEET 5 AB1 7 VAL G 125 PHE G 131 1 O MET G 129 N VAL G 101
SHEET 6 AB1 7 THR G 179 TYR G 183 1 O THR G 180 N ALA G 130
SHEET 7 AB1 7 LYS G 208 GLN G 211 1 O VAL G 210 N ASN G 181
SHEET 1 AB2 2 ARG G 309 THR G 310 0
SHEET 2 AB2 2 GLY G 313 ILE G 314 -1 O GLY G 313 N THR G 310
SHEET 1 AB3 7 LEU H 20 CYS H 22 0
SHEET 2 AB3 7 THR H 62 ILE H 66 -1 O TRP H 65 N THR H 21
SHEET 3 AB3 7 PRO H 33 VAL H 37 1 N ILE H 34 O CYS H 64
SHEET 4 AB3 7 LEU H 99 TRP H 104 1 O LEU H 102 N LEU H 35
SHEET 5 AB3 7 VAL H 125 PHE H 131 1 O ASP H 126 N LEU H 99
SHEET 6 AB3 7 THR H 179 TYR H 183 1 O THR H 180 N ALA H 130
SHEET 7 AB3 7 LYS H 208 GLN H 211 1 O VAL H 210 N ASN H 181
SHEET 1 AB4 2 ARG H 309 THR H 310 0
SHEET 2 AB4 2 GLY H 313 ILE H 314 -1 O GLY H 313 N THR H 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.13
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.05
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.06
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.09
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.04
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.09
SSBOND 7 CYS C 22 CYS C 64 1555 1555 2.11
SSBOND 8 CYS C 216 CYS C 258 1555 1555 2.00
SSBOND 9 CYS C 293 CYS C 311 1555 1555 2.07
SSBOND 10 CYS D 22 CYS D 64 1555 1555 2.11
SSBOND 11 CYS D 216 CYS D 258 1555 1555 2.03
SSBOND 12 CYS D 293 CYS D 311 1555 1555 2.07
SSBOND 13 CYS E 22 CYS E 64 1555 1555 2.15
SSBOND 14 CYS E 216 CYS E 258 1555 1555 2.03
SSBOND 15 CYS E 293 CYS E 311 1555 1555 2.07
SSBOND 16 CYS F 22 CYS F 64 1555 1555 2.09
SSBOND 17 CYS F 216 CYS F 258 1555 1555 2.04
SSBOND 18 CYS F 293 CYS F 311 1555 1555 2.08
SSBOND 19 CYS G 22 CYS G 64 1555 1555 2.10
SSBOND 20 CYS G 216 CYS G 258 1555 1555 2.06
SSBOND 21 CYS G 293 CYS G 311 1555 1555 2.07
SSBOND 22 CYS H 22 CYS H 64 1555 1555 2.08
SSBOND 23 CYS H 216 CYS H 258 1555 1555 2.04
SSBOND 24 CYS H 293 CYS H 311 1555 1555 2.04
LINK ND2 ASN A 74 C1 NAG A 402 1555 1555 1.46
LINK OG SER A 105 PAY MSW A 401 1555 1555 1.62
LINK ND2 ASN B 74 C1 NAG B 402 1555 1555 1.26
LINK OG SER B 105 PAY MSW B 401 1555 1555 1.60
LINK ND2 ASN C 74 C1 NAG C 402 1555 1555 1.41
LINK OG SER C 105 PAY MSW C 401 1555 1555 1.59
LINK ND2 ASN D 74 C1 NAG D 402 1555 1555 1.26
LINK OG SER D 105 PAY MSW D 401 1555 1555 1.60
LINK ND2 ASN E 74 C1 NAG E 402 1555 1555 1.45
LINK OG SER E 105 PAY MSW E 401 1555 1555 1.54
LINK ND2 ASN F 74 C1 NAG F 402 1555 1555 1.46
LINK OG SER F 105 PAY MSW F 401 1555 1555 1.59
LINK ND2 ASN G 74 C1 NAG G 402 1555 1555 1.45
LINK OG SER G 105 PAY MSW G 401 1555 1555 1.59
LINK ND2 ASN H 74 C1 NAG H 402 1555 1555 1.46
LINK OG SER H 105 PAY MSW H 401 1555 1555 1.63
LINK O4 NAG A 402 C1 NAG A 403 1555 1555 1.45
LINK O4 NAG A 403 C1 NAG A 404 1555 1555 1.44
LINK O4 NAG A 404 C1 NAG A 405 1555 1555 1.44
LINK O4 NAG B 402 C1 NAG B 403 1555 1555 1.45
LINK O4 NAG C 402 C1 NAG C 403 1555 1555 1.45
LINK O4 NAG C 403 C1 NAG C 404 1555 1555 1.46
LINK O4 NAG C 404 C1 NAG C 405 1555 1555 1.46
LINK O4 NAG D 402 C1 NAG D 403 1555 1555 1.44
LINK O4 NAG E 402 C1 NAG E 403 1555 1555 1.47
LINK O4 NAG F 402 C1 NAG F 403 1555 1555 1.45
LINK O4 NAG G 402 C1 NAG G 403 1555 1555 1.46
LINK O4 NAG H 402 C1 NAG H 403 1555 1555 1.45
CISPEP 1 PRO A 69 PRO A 70 0 -1.87
CISPEP 2 GLN A 191 PRO A 192 0 7.94
CISPEP 3 PRO B 69 PRO B 70 0 -9.07
CISPEP 4 GLN B 191 PRO B 192 0 10.33
CISPEP 5 PRO C 69 PRO C 70 0 -10.51
CISPEP 6 GLN C 191 PRO C 192 0 -5.11
CISPEP 7 PRO D 69 PRO D 70 0 -11.99
CISPEP 8 GLN D 191 PRO D 192 0 4.04
CISPEP 9 PRO E 69 PRO E 70 0 -7.52
CISPEP 10 GLN E 191 PRO E 192 0 -5.16
CISPEP 11 PRO F 69 PRO F 70 0 -11.29
CISPEP 12 GLN F 191 PRO F 192 0 7.95
CISPEP 13 PRO G 69 PRO G 70 0 -6.47
CISPEP 14 GLN G 191 PRO G 192 0 4.14
CISPEP 15 PRO H 69 PRO H 70 0 -9.20
CISPEP 16 GLN H 191 PRO H 192 0 4.85
SITE 1 AC1 12 GLY A 39 THR A 40 TRP A 104 SER A 105
SITE 2 AC1 12 GLN A 106 ASP A 134 GLN A 157 ILE A 189
SITE 3 AC1 12 HIS A 224 LEU A 278 ALA A 281 ILE A 285
SITE 1 AC2 6 SER A 10 GLN A 11 PRO A 69 ASN A 74
SITE 2 AC2 6 ASP A 75 VAL A 78
SITE 1 AC3 2 PRO B 69 ASN B 74
SITE 1 AC4 6 PHE C 9 SER C 10 GLN C 11 ASN C 74
SITE 2 AC4 6 ASP C 75 VAL C 78
SITE 1 AC5 1 ASN D 74
SITE 1 AC6 1 ASN E 74
SITE 1 AC7 1 ASN F 74
SITE 1 AC8 7 SER G 10 GLN G 11 PRO G 69 ASN G 74
SITE 2 AC8 7 ASP G 75 VAL G 78 MET G 298
SITE 1 AC9 1 ASN H 74
SITE 1 AD1 14 THR B 40 TRP B 104 GLN B 106 GLY B 107
SITE 2 AD1 14 GLY B 108 PHE B 131 ALA B 132 PRO B 133
SITE 3 AD1 14 GLN B 157 ILE B 189 HIS B 224 LEU B 278
SITE 4 AD1 14 ALA B 281 ILE B 285
SITE 1 AD2 13 THR C 40 TRP C 104 GLN C 106 GLY C 107
SITE 2 AD2 13 GLY C 108 PHE C 131 ALA C 132 PRO C 133
SITE 3 AD2 13 ASP C 134 GLN C 157 HIS C 224 LEU C 278
SITE 4 AD2 13 ILE C 285
SITE 1 AD3 12 THR D 40 TRP D 104 GLN D 106 GLY D 107
SITE 2 AD3 12 GLY D 108 PHE D 131 ALA D 132 ASP D 134
SITE 3 AD3 12 GLN D 157 HIS D 224 LEU D 278 ILE D 285
SITE 1 AD4 13 THR E 40 TRP E 104 GLN E 106 GLY E 107
SITE 2 AD4 13 GLY E 108 PHE E 131 ALA E 132 ASP E 134
SITE 3 AD4 13 GLN E 157 HIS E 224 LEU E 278 ALA E 281
SITE 4 AD4 13 ILE E 285
SITE 1 AD5 15 GLY F 39 THR F 40 TRP F 104 GLN F 106
SITE 2 AD5 15 GLY F 107 GLY F 108 PHE F 131 ALA F 132
SITE 3 AD5 15 PRO F 133 ASP F 134 GLN F 157 ILE F 189
SITE 4 AD5 15 HIS F 224 LEU F 278 ILE F 285
SITE 1 AD6 15 GLY G 39 THR G 40 TRP G 104 GLN G 106
SITE 2 AD6 15 GLY G 107 GLY G 108 PHE G 131 ALA G 132
SITE 3 AD6 15 ASP G 134 GLN G 157 ILE G 189 HIS G 224
SITE 4 AD6 15 LEU G 278 ALA G 281 ILE G 285
SITE 1 AD7 16 THR H 40 GLY H 41 TRP H 104 GLN H 106
SITE 2 AD7 16 GLY H 107 GLY H 108 PHE H 131 ALA H 132
SITE 3 AD7 16 ASP H 134 GLN H 157 ILE H 189 HIS H 224
SITE 4 AD7 16 LEU H 278 ALA H 281 ALA H 282 ILE H 285
CRYST1 92.462 123.222 150.316 90.00 96.20 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 0.010815 0.000000 0.001174 0.00000
SCALE2 0.000000 0.008115 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006692 0.00000
TER 2325 PRO A 317
TER 4650 PRO B 317
TER 6967 PRO C 317
TER 9240 PRO D 317
TER 11547 PRO E 317
TER 13872 PRO F 317
TER 16197 PRO G 317
TER 18522 PRO H 317
MASTER 483 0 28 135 66 0 41 618946 8 496 200
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