| content |
HEADER HYDROLASE 02-JUL-15 5A71
TITLE OPEN AND CLOSED CONFORMATIONS AND PROTONATION STATES OF
TITLE 2 CANDIDA ANTARCTICA LIPASE B: ATOMIC RESOLUTION NATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 26-342;
COMPND 5 SYNONYM: CALB, CANDIDA ANTARCTICA LIPASE B;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE, LIPASE, CANDIDA ANTARCTICA, ATOMIC RESOLUTION, FREE FATTY
KEYWDS 2 ACIDS, LIPIDS, HYDROLASE FOLD, INTERFACIAL ACTIVATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.STAUCH,S.J.FISHER,M.CIANCI
REVDAT 1 21-OCT-15 5A71 0
JRNL AUTH B.STAUCH,S.J.FISHER,M.CIANCI
JRNL TITL OPEN AND CLOSED STATES OF CANDIDA ANTARCTICA LIPASE B:
JRNL TITL 2 PROTONATION AND THE MECHANISM OF INTERFACIAL ACTIVATION.
JRNL REF J.LIPID RES. 2015
JRNL REFN ESSN 0022-2275
JRNL PMID 26447231
JRNL DOI 10.1194/JLR.M063388
REMARK 2
REMARK 2 RESOLUTION. 0.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.48
REMARK 3 NUMBER OF REFLECTIONS : 326301
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) : 0.11255
REMARK 3 R VALUE (WORKING SET) : 0.11150
REMARK 3 FREE R VALUE : 0.13197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 17383
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) : 0.910
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 0.934
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.268
REMARK 3 BIN FREE R VALUE SET COUNT : 1080
REMARK 3 BIN FREE R VALUE : 0.277
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 1019
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.793
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04
REMARK 3 B22 (A**2) : 0.40
REMARK 3 B33 (A**2) : -0.29
REMARK 3 B12 (A**2) : -0.23
REMARK 3 B13 (A**2) : -0.10
REMARK 3 B23 (A**2) : 0.16
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.016
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.017
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.014
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.572
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.987
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.983
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5074 ; 0.026 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4781 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7009 ; 2.257 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11078 ; 1.454 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 687 ; 6.583 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 169 ;33.317 ;25.030
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 726 ;11.303 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;20.037 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 838 ; 0.159 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5839 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1062 ; 0.009 ; 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): 2643 ; 1.324 ; 0.914
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2642 ; 1.321 ; 0.913
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3325 ; 1.565 ; 1.379
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2431 ; 2.177 ; 1.073
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 9855 ; 6.779 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 123 ;35.794 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 10613 ;11.239 ;
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
REMARK 3 RIDING POSITIONS.
REMARK 3 U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5A71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-15.
REMARK 100 THE PDBE ID CODE IS EBI-64247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.826
REMARK 200 MONOCHROMATOR : SI(III)
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 343684
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.91
REMARK 200 RESOLUTION RANGE LOW (A) : 71.04
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 17.2
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.65
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.5
REMARK 200 R MERGE FOR SHELL (I) : 0.57
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.59
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1TCA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CANDIDA ANTARCTICA LIPASE B
REMARK 280 (CALB) WAS PURCHASED BY HAMPTON RESEARCH AND CRYSTALLIZED
REMARK 280 WITHOUT FURTHER PURIFICATION. CRYSTALLIZATION TRIALS WERE
REMARK 280 PERFORMED AT 293 K USING THE HANGING-DROP METHOD USING A
REMARK 280 QUIAGEN EASYXTAL 15-WELL PLATE. 1 UL OF A 15 MG/ML CALB
REMARK 280 SOLUTION IN 20MM NA(CH3COO) PH = 4.8 WAS DILUTED WITH 1 UL
REMARK 280 OF THE PRECIPITANT SOLUTION, MADE OF 200MM NA(CH3COO) PH =
REMARK 280 4.8, 20% (W/V) PEG4000, AND 10-13% (V/V) 2-PROPANOL. THE
REMARK 280 DROP WAS EQUILIBRATED BY VAPOR DIFFUSION AGAINST 500 ML OF
REMARK 280 THE PRECIPITANT SOLUTION. PROTEIN CRYSTALS OF NATIVE CALB
REMARK 280 APPEARED WITHIN ONE WEEK AND GREW TO A SIZE OF 0.2 X 0.4 X
REMARK 280 0.5 MM3 IN THREE WEEKS.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 PRO A 317
REMARK 465 PRO B 317
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 OG SER A 28 O HOH A 2097 2.04
REMARK 500 OD1B ASN A 74 O HOH A 2189 2.14
REMARK 500 O GLY A 95 O HOH A 2243 2.10
REMARK 500 OG1A THR A 159 O HOH A 2332 2.15
REMARK 500 OD1B ASN B 97 O HOH B 2212 2.03
REMARK 500 OG B SER B 105 O HOH B 2111 2.06
REMARK 500 O PRO B 218 O HOH B 2344 2.13
REMARK 500 NH2 ARG B 309 O HOH B 2465 1.87
REMARK 500 O HOH A 2107 O HOH A 2166 2.10
REMARK 500 O HOH A 2148 O HOH A 2161 2.00
REMARK 500 O HOH A 2167 O HOH A 2174 1.80
REMARK 500 O HOH A 2198 O HOH A 2373 2.15
REMARK 500 O HOH A 2213 O HOH A 2214 2.10
REMARK 500 O HOH A 2301 O HOH A 2302 2.04
REMARK 500 O HOH A 2322 O HOH A 2324 1.94
REMARK 500 O HOH B 2036 O HOH B 2083 2.04
REMARK 500 O HOH B 2062 O HOH B 2119 1.87
REMARK 500 O HOH B 2062 O HOH B 2481 2.20
REMARK 500 O HOH B 2215 O HOH B 2404 1.88
REMARK 500 O HOH B 2225 O HOH B 2413 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG B 309 O HOH B 2390 2665 1.94
REMARK 500 NA NA B 1325 O HOH A 2462 2665 1.85
REMARK 500 NA NA B 1325 O HOH A 2419 2665 1.81
REMARK 500 O HOH A 2055 O HOH A 2434 2655 2.15
REMARK 500 O HOH A 2065 O HOH A 2444 2655 1.79
REMARK 500 O HOH A 2071 O HOH A 2442 2655 1.92
REMARK 500 O HOH A 2072 O HOH A 2393 2655 2.19
REMARK 500 O HOH A 2305 O HOH B 2372 2554 2.13
REMARK 500 O HOH B 2022 O HOH B 2385 2565 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 32 CD LYS A 32 CE 0.157
REMARK 500 GLY A 95 N GLY A 95 CA 0.114
REMARK 500 ASN A 96 CA ASN A 96 C -0.162
REMARK 500 LYS A 124 CE LYS A 124 NZ -0.163
REMARK 500 GLY B 4 N GLY B 4 CA 0.103
REMARK 500 SER B 28 CA SER B 28 CB 0.110
REMARK 500 SER B 123 CA SER B 123 CB 0.102
REMARK 500 SER B 123 CB SER B 123 OG 0.095
REMARK 500 SER B 150 CB SER B 150 OG -0.081
REMARK 500 ARG B 238 CZ ARG B 238 NH2 -0.100
REMARK 500 ARG B 242 CZ A ARG B 242 NH1A -0.106
REMARK 500 ARG B 242 CZ A ARG B 242 NH2A -0.129
REMARK 500 GLU B 269 CD GLU B 269 OE1 0.077
REMARK 500 GLU B 269 CD GLU B 269 OE2 0.093
REMARK 500 GLU B 269 CG GLU B 269 CD 0.102
REMARK 500 LEU B 277 CB LEU B 277 CG -0.183
REMARK 500 GLU B 294 CD GLU B 294 OE1 -0.070
REMARK 500 ARG B 309 CZ ARG B 309 NH2 0.088
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 MET A 83 CG - SD - CE ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP A 134 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 134 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 VAL A 139 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP A 145 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 145 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 168 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 168 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 LEU A 278 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU B 1 CA - CB - CG ANGL. DEV. = 19.2 DEGREES
REMARK 500 ASP B 134 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP B 134 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG B 238 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 242 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 242 NH1 - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU B 277 CB - CG - CD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG B 302 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 CYS B 311 CB - CA - C ANGL. DEV. = -7.3 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 SER A 3 20.77 -146.03
REMARK 500 SER A 29 87.07 -156.88
REMARK 500 ASN A 51 -96.65 -149.77
REMARK 500 ASP A 75 118.98 -32.43
REMARK 500 SER A 105 -133.68 59.74
REMARK 500 ASP A 134 66.15 -113.53
REMARK 500 ALA A 305 38.19 -142.84
REMARK 500 SER B 29 82.84 -156.37
REMARK 500 ASN B 51 -96.77 -149.21
REMARK 500 ASP B 75 120.17 -30.64
REMARK 500 SER B 105 -130.71 59.60
REMARK 500 ASP B 134 65.66 -111.69
REMARK 500 ASN B 206 -0.76 71.38
REMARK 500 ALA B 305 33.79 -140.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 285 10.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1320 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2298 O
REMARK 620 2 HOH A2230 O 128.4
REMARK 620 3 ASP A 252 OD1 126.0 105.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1321 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 29 OG
REMARK 620 2 ASN B 96 OD1 107.1
REMARK 620 3 HOH A2099 O 129.3 98.9
REMARK 620 4 HOH A2100 O 50.4 64.7 109.9
REMARK 620 5 HOH A2106 O 88.1 108.8 123.6 126.2
REMARK 620 6 SER A 29 O 59.6 153.6 77.9 91.4 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1321 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2376 O
REMARK 620 2 ASN B 206 O 113.1
REMARK 620 3 HOH B2298 O 134.0 59.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1322 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 20 O
REMARK 620 2 HOH A2062 O 93.1
REMARK 620 3 ASP A 17 O 74.3 67.3
REMARK 620 4 HOH A2061 O 136.2 96.9 70.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1323 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 220 O
REMARK 620 2 HOH A2404 O 142.4
REMARK 620 3 HOH A2405 O 117.2 94.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1323 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 294 OE1
REMARK 620 2 HOH B2284 O 109.5
REMARK 620 3 ARG B 309 O 107.9 101.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1324 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 46 OE1
REMARK 620 2 GLY B 41 O 98.8
REMARK 620 3 HOH B2120 O 81.0 103.1
REMARK 620 4 HOH B2432 O 125.8 122.9 58.6
REMARK 620 5 HOH B2481 O 117.8 130.9 113.4 60.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1325 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2494 O
REMARK 620 2 HOH A2420 O 89.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG A1317 THROUGH NAG A1318 BOUND TO ASN A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE
REMARK 800 RESIDUES NAG B1317 THROUGH NAG B1318 BOUND TO ASN B 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A6V RELATED DB: PDB
REMARK 900 OPEN AND CLOSED CONFORMATIONS AND PROTONATION STATES OF
REMARK 900 CANDIDA ANTARCTICA LIPASE B: XENON COMPLEX
DBREF 5A71 A 1 317 UNP P41365 LIPB_CANAR 26 342
DBREF 5A71 B 1 317 UNP P41365 LIPB_CANAR 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
HET NAG A1317 28
HET NAG A1318 28
HET IPA A1319 4
HET NAG B1317 14
HET NAG B1318 14
HET IPA B1319 4
HET IPA B1320 4
HET K A1320 1
HET K A1321 1
HET K A1322 1
HET K B1321 1
HET NA B1322 1
HET NA B1323 1
HET NA B1324 1
HET NA A1323 1
HET NA B1325 1
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM K POTASSIUM ION
HETNAM NA SODIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN IPA 2-PROPANOL
FORMUL 3 IPA 3(C3 H8 O)
FORMUL 4 NA 5(NA 1+)
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 6 K 4(K 1+)
FORMUL 7 HOH *1019(H2 O)
HELIX 1 1 PRO A 12 GLY A 19 1 8
HELIX 2 2 THR A 43 ASP A 49 1 7
HELIX 3 3 ASN A 51 LEU A 59 1 9
HELIX 4 4 ASP A 75 SER A 94 1 20
HELIX 5 5 SER A 105 PHE A 118 1 14
HELIX 6 6 PRO A 119 ARG A 122 5 4
HELIX 7 7 ALA A 141 LEU A 147 1 7
HELIX 8 8 ALA A 151 GLN A 157 1 7
HELIX 9 9 SER A 161 ALA A 170 1 10
HELIX 10 10 ALA A 212 GLY A 217 1 6
HELIX 11 11 ALA A 225 SER A 230 1 6
HELIX 12 12 SER A 230 SER A 243 1 14
HELIX 13 13 ARG A 249 TYR A 253 5 5
HELIX 14 14 GLY A 254 CYS A 258 5 5
HELIX 15 15 THR A 267 ALA A 276 1 10
HELIX 16 16 LEU A 277 GLY A 288 1 12
HELIX 17 17 ALA A 301 ALA A 305 5 5
HELIX 18 18 PRO B 12 GLY B 19 1 8
HELIX 19 19 THR B 43 ASP B 49 1 7
HELIX 20 20 ASN B 51 LEU B 59 1 9
HELIX 21 21 ASP B 75 SER B 94 1 20
HELIX 22 22 SER B 105 PHE B 118 1 14
HELIX 23 23 PRO B 119 SER B 123 5 5
HELIX 24 24 ALA B 151 GLN B 157 1 7
HELIX 25 25 SER B 161 ALA B 170 1 10
HELIX 26 26 ALA B 212 GLY B 217 1 6
HELIX 27 27 ALA B 225 SER B 230 1 6
HELIX 28 28 SER B 230 SER B 243 1 14
HELIX 29 29 ARG B 249 TYR B 253 5 5
HELIX 30 30 GLY B 254 CYS B 258 5 5
HELIX 31 31 THR B 267 ALA B 276 1 10
HELIX 32 32 LEU B 277 GLY B 288 1 12
HELIX 33 33 ALA B 301 ALA B 305 5 5
SHEET 1 AA 7 LEU A 20 CYS A 22 0
SHEET 2 AA 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA 7 PRO A 33 VAL A 37 1 O ILE A 34 N CYS A 64
SHEET 4 AA 7 LEU A 99 TRP A 104 1 O PRO A 100 N LEU A 35
SHEET 5 AA 7 VAL A 125 PHE A 131 1 N ASP A 126 O LEU A 99
SHEET 6 AA 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA 7 LYS A 208 GLN A 211 1 O LYS A 208 N ASN A 181
SHEET 1 AB 2 ARG A 309 THR A 310 0
SHEET 2 AB 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 BA 7 LEU B 20 CYS B 22 0
SHEET 2 BA 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 BA 7 PRO B 33 VAL B 37 1 O ILE B 34 N CYS B 64
SHEET 4 BA 7 LEU B 99 TRP B 104 1 O PRO B 100 N LEU B 35
SHEET 5 BA 7 VAL B 125 PHE B 131 1 N ASP B 126 O LEU B 99
SHEET 6 BA 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 BA 7 LYS B 208 GLN B 211 1 O LYS B 208 N ASN B 181
SHEET 1 BB 2 ARG B 309 THR B 310 0
SHEET 2 BB 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.07
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.05
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.07
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.05
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.04
LINK ND2AASN A 74 C1 ANAG A1317 1555 1555 1.46
LINK ND2BASN A 74 C1 BNAG A1317 1555 1555 1.47
LINK O PRO A 218 NA NA A1323 1555 1555 1.77
LINK O4 ANAG A1317 C1 ANAG A1318 1555 1555 1.38
LINK O4 BNAG A1317 C1 BNAG A1318 1555 1555 1.39
LINK K K A1320 O HOH A2230 1555 1555 3.07
LINK K K A1320 OD1 ASP A 252 1555 1555 2.79
LINK K K A1320 O HOH A2298 1555 1445 2.45
LINK K K A1321 O SER A 29 1555 1555 3.18
LINK K K A1321 O HOH A2100 1555 1555 2.55
LINK K K A1321 O HOH A2106 1555 1555 2.63
LINK K K A1321 OG SER A 29 1555 1555 3.34
LINK K K A1321 O HOH A2099 1555 1555 2.37
LINK K K A1321 OD1 ASN B 96 1555 1544 3.04
LINK K K A1322 O ASP A 17 1555 1555 2.92
LINK K K A1322 O HOH A2061 1555 1555 3.04
LINK K K A1322 O LEU A 20 1555 1555 2.75
LINK K K A1322 O HOH A2062 1555 1555 2.55
LINK NA NA A1323 O HOH A2405 1555 1555 2.62
LINK NA NA A1323 O HOH A2404 1555 1555 2.49
LINK NA NA A1323 O PHE A 220 1555 1555 2.82
LINK ND2 ASN B 74 C1 NAG B1317 1555 1555 1.52
LINK O4 NAG B1317 C1 NAG B1318 1555 1555 1.38
LINK K K B1321 O ASN B 206 1555 1555 2.97
LINK K K B1321 O HOH B2376 1555 1555 2.52
LINK K K B1321 O HOH B2298 1555 1555 2.70
LINK NA NA B1322 O HOH B2418 1555 1555 2.75
LINK NA NA B1323 O ARG B 309 1555 1555 2.34
LINK NA NA B1323 O HOH B2284 1555 1555 2.49
LINK NA NA B1323 OE1 GLU B 294 1555 1555 2.58
LINK NA NA B1324 O HOH B2481 1555 1555 3.10
LINK NA NA B1324 O HOH B2432 1555 1555 2.27
LINK NA NA B1324 O HOH B2120 1555 1555 2.96
LINK NA NA B1324 O GLY B 41 1555 1555 2.78
LINK NA NA B1324 OE1 GLN B 46 1555 1555 2.69
LINK NA NA B1325 O HOH A2420 1555 1665 2.75
LINK NA NA B1325 O HOH A2494 1555 1555 2.77
CISPEP 1 PRO A 69 PRO A 70 0 -14.76
CISPEP 2 GLN A 191 PRO A 192 0 8.71
CISPEP 3 PRO B 69 PRO B 70 0 -10.53
CISPEP 4 GLN B 191 PRO B 192 0 -0.23
SITE 1 AC1 6 THR A 40 SER A 105 ASP A 134 GLN A 157
SITE 2 AC1 6 ILE A 189 HOH A2281
SITE 1 AC2 5 THR B 40 ALA B 282 ILE B 285 IPA B1320
SITE 2 AC2 5 HOH B2111
SITE 1 AC3 5 THR B 40 GLN B 157 IPA B1319 HOH B2276
SITE 2 AC3 5 HOH B2480
SITE 1 AC4 4 ASP A 252 THR A 316 HOH A2230 HOH A2298
SITE 1 AC5 5 SER A 29 HOH A2099 HOH A2100 HOH A2106
SITE 2 AC5 5 ASN B 96
SITE 1 AC6 4 ASP A 17 LEU A 20 HOH A2061 HOH A2062
SITE 1 AC7 4 ASN B 206 GLN B 247 HOH B2298 HOH B2376
SITE 1 AC8 2 THR B 267 HOH B2418
SITE 1 AC9 3 GLU B 294 ARG B 309 HOH B2284
SITE 1 BC1 7 GLY B 41 GLN B 46 PHE B 71 ALA B 284
SITE 2 BC1 7 HOH B2120 HOH B2432 HOH B2481
SITE 1 BC2 6 GLN A 213 PRO A 218 LEU A 219 PHE A 220
SITE 2 BC2 6 HOH A2404 HOH A2405
SITE 1 BC3 6 ASP A 265 ASN A 292 HOH A2419 HOH A2420
SITE 2 BC3 6 HOH A2462 HOH A2494
SITE 1 BC4 12 SER A 10 GLN A 11 ASN A 74 ASP A 75
SITE 2 BC4 12 VAL A 78 HOH A2039 HOH A2040 HOH A2046
SITE 3 BC4 12 HOH A2047 HOH A2179 HOH A2530 HOH A2531
SITE 1 BC5 10 SER B 10 GLN B 11 ASN B 74 ASP B 75
SITE 2 BC5 10 VAL B 78 HOH B2038 HOH B2164 HOH B2184
SITE 3 BC5 10 HOH B2473 HOH B2474
CRYST1 39.670 48.940 71.610 88.74 97.15 108.44 P 1 2
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 0.025208 0.008405 0.003318 0.00000
SCALE2 0.000000 0.021539 0.000398 0.00000
SCALE3 0.000000 0.000000 0.014076 0.00000
TER 2418 THR A 316
TER 4826 THR B 316
MASTER 555 0 16 33 18 0 25 6 5948 2 151 50
END |