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HEADER HYDROLASE 07-APR-09 3GZJ
TITLE CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE ESTERASE
TITLE 2 COMPLEXED WITH 16-EPI-VELLOSIMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYNEURIDINE-ALDEHYDE ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 EC: 3.1.1.78;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;
SOURCE 3 ORGANISM_COMMON: DEVILPEPPER;
SOURCE 4 ORGANISM_TAXID: 4060;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PREP4
KEYWDS HYDROLASE SUPERFAMILY, ALKALOID METABOLISM, HYDROLASE,
KEYWDS 2 SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.YANG,M.HILL,M.WANG,S.PANJIKAR,J.STOECKIGT
REVDAT 1 18-AUG-09 3GZJ 0
JRNL AUTH L.YANG,M.HILL,M.WANG,S.PANJIKAR,J.STOCKIGT
JRNL TITL STRUCTURAL BASIS AND ENZYMATIC MECHANISM OF THE
JRNL TITL 2 BIOSYNTHESIS OF C9- FROM C10-MONOTERPENOID INDOLE
JRNL TITL 3 ALKALOIDS
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 48 5211 2009
JRNL REFN ISSN 1433-7851
JRNL PMID 19496101
JRNL DOI 10.1002/ANIE.200900150
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 66881
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3407
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4198
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9985
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.05000
REMARK 3 B22 (A**2) : 3.26000
REMARK 3 B33 (A**2) : -0.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.321
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.201
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.041
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10343 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13968 ; 1.841 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1265 ; 6.814 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 430 ;35.778 ;24.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1845 ;18.159 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;16.221 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1486 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7734 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5227 ; 0.237 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6998 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 505 ; 0.177 ; 0.200
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): 145 ; 0.360 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.337 ; 0.200
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): 6542 ; 0.923 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10215 ; 1.427 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4378 ; 2.491 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3753 ; 3.613 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : E B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 114 E 136 1
REMARK 3 1 B 114 B 136 1
REMARK 3 2 E 146 E 153 1
REMARK 3 2 B 146 B 153 1
REMARK 3 3 E 189 E 207 1
REMARK 3 3 B 189 B 207 1
REMARK 3 4 E 221 E 235 1
REMARK 3 4 B 221 B 235 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 E (A): 524 ; 0.080 ; 0.050
REMARK 3 TIGHT THERMAL 1 E (A**2): 524 ; 0.310 ; 0.500
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 4
REMARK 4 3GZJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66881
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : 0.42500
REMARK 200 FOR SHELL : 2.200
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: 2WFL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 0.20M BIS-TRIS, 0.25M
REMARK 280 LIS2SO4, PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 85.60500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 85.60500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.30500
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
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 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 ALA A 7
REMARK 465 LYS A 8
REMARK 465 GLN A 9
REMARK 465 SER A 264
REMARK 465 ALA B 7
REMARK 465 LYS B 8
REMARK 465 GLN B 9
REMARK 465 SER B 264
REMARK 465 ALA C 7
REMARK 465 LYS C 8
REMARK 465 GLN C 9
REMARK 465 SER C 264
REMARK 465 ALA D 7
REMARK 465 LYS D 8
REMARK 465 GLN D 9
REMARK 465 SER D 264
REMARK 465 ALA E 7
REMARK 465 LYS E 8
REMARK 465 GLN E 9
REMARK 465 SER E 264
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 D 87 CAF EVS D 1000 1.42
REMARK 500 OG SER C 87 CAF EVS C 1000 1.45
REMARK 500 OG SER A 87 CAF EVS A 1000 1.46
REMARK 500 OG SER B 87 CAF EVS B 1000 1.48
REMARK 500 O HOH A 295 O HOH A 313 1.91
REMARK 500 CA GLY C 49 O HOH C 318 1.96
REMARK 500 OE2 GLU C 173 O HOH C 308 2.10
REMARK 500 O GLU A 79 NZ LYS A 103 2.16
REMARK 500 O HOH D 286 O HOH D 308 2.19
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 NZ LYS E 194 O GLU E 201 4555 1.71
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 B 196 CE LYS B 196 NZ 0.174
REMARK 500 TRP E 26 CE3 TRP E 26 CZ3 0.104
REMARK 500 LYS E 196 CE LYS E 196 NZ 0.163
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 44 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LYS E 127 CD - CE - NZ ANGL. DEV. = 21.2 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 LEU A 21 -156.53 -115.07
REMARK 500 ASP A 56 3.09 -67.17
REMARK 500 SER A 87 -132.99 48.44
REMARK 500 SER A 111 59.42 34.24
REMARK 500 LEU A 138 -121.89 61.34
REMARK 500 ARG A 202 -85.73 -109.92
REMARK 500 ASP A 243 -158.90 -96.76
REMARK 500 MET A 245 57.44 -103.44
REMARK 500 CYS B 20 14.18 57.61
REMARK 500 LEU B 21 -162.74 -121.74
REMARK 500 ALA B 73 -19.61 -48.24
REMARK 500 SER B 87 -124.21 39.13
REMARK 500 SER B 111 68.96 24.93
REMARK 500 LEU B 138 -119.34 57.71
REMARK 500 ASN B 150 66.55 -155.54
REMARK 500 ARG B 202 -72.69 -105.27
REMARK 500 LEU C 21 -168.48 -115.73
REMARK 500 ASP C 56 0.84 -66.17
REMARK 500 SER C 87 -121.53 44.03
REMARK 500 LEU C 138 -118.52 57.57
REMARK 500 PRO C 148 22.13 -63.69
REMARK 500 ASN C 150 67.02 -161.94
REMARK 500 ARG C 202 -74.48 -98.26
REMARK 500 PHE C 219 72.81 -152.32
REMARK 500 ASP C 243 -152.70 -87.87
REMARK 500 MET C 245 61.06 -115.98
REMARK 500 LEU D 21 -161.80 -116.78
REMARK 500 SER D 87 -120.22 46.81
REMARK 500 LEU D 138 -116.66 47.18
REMARK 500 PRO D 148 5.06 -66.21
REMARK 500 GLU D 149 -84.79 -98.43
REMARK 500 ARG D 202 -79.89 -105.06
REMARK 500 ASP D 243 -155.13 -89.95
REMARK 500 MET D 245 55.01 -108.09
REMARK 500 LEU E 21 -157.08 -120.44
REMARK 500 PRO E 52 -8.87 -59.41
REMARK 500 ASP E 56 40.56 -67.80
REMARK 500 GLU E 57 -2.33 -168.68
REMARK 500 SER E 74 58.70 -108.47
REMARK 500 SER E 87 -136.44 51.67
REMARK 500 PHE E 88 -14.69 -46.86
REMARK 500 LEU E 138 -102.24 55.48
REMARK 500 ASN E 150 59.82 -153.13
REMARK 500 ARG E 202 -70.28 -101.52
REMARK 500 MET E 245 56.36 -114.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B 66 24.7 L L OUTSIDE RANGE
REMARK 500 ASP C 63 16.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 278 DISTANCE = 5.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVS A 1000
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVS B 1000
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVS C 1000
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVS D 1000
DBREF 3GZJ A 7 264 UNP Q9SE93 PNAE_RAUSE 7 264
DBREF 3GZJ B 7 264 UNP Q9SE93 PNAE_RAUSE 7 264
DBREF 3GZJ C 7 264 UNP Q9SE93 PNAE_RAUSE 7 264
DBREF 3GZJ D 7 264 UNP Q9SE93 PNAE_RAUSE 7 264
DBREF 3GZJ E 7 264 UNP Q9SE93 PNAE_RAUSE 7 264
SEQADV 3GZJ ALA A 244 UNP Q9SE93 HIS 244 ENGINEERED
SEQADV 3GZJ ALA B 244 UNP Q9SE93 HIS 244 ENGINEERED
SEQADV 3GZJ ALA C 244 UNP Q9SE93 HIS 244 ENGINEERED
SEQADV 3GZJ ALA D 244 UNP Q9SE93 HIS 244 ENGINEERED
SEQADV 3GZJ ALA E 244 UNP Q9SE93 HIS 244 ENGINEERED
SEQRES 1 A 258 ALA LYS GLN GLN LYS HIS PHE VAL LEU VAL HIS GLY GLY
SEQRES 2 A 258 CYS LEU GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 A 258 LEU GLU SER ALA GLY HIS LYS VAL THR ALA VAL ASP LEU
SEQRES 4 A 258 SER ALA ALA GLY ILE ASN PRO ARG ARG LEU ASP GLU ILE
SEQRES 5 A 258 HIS THR PHE ARG ASP TYR SER GLU PRO LEU MET GLU VAL
SEQRES 6 A 258 MET ALA SER ILE PRO PRO ASP GLU LYS VAL VAL LEU LEU
SEQRES 7 A 258 GLY HIS SER PHE GLY GLY MET SER LEU GLY LEU ALA MET
SEQRES 8 A 258 GLU THR TYR PRO GLU LYS ILE SER VAL ALA VAL PHE MET
SEQRES 9 A 258 SER ALA MET MET PRO ASP PRO ASN HIS SER LEU THR TYR
SEQRES 10 A 258 PRO PHE GLU LYS TYR ASN GLU LYS CYS PRO ALA ASP MET
SEQRES 11 A 258 MET LEU ASP SER GLN PHE SER THR TYR GLY ASN PRO GLU
SEQRES 12 A 258 ASN PRO GLY MET SER MET ILE LEU GLY PRO GLN PHE MET
SEQRES 13 A 258 ALA LEU LYS MET PHE GLN ASN CYS SER VAL GLU ASP LEU
SEQRES 14 A 258 GLU LEU ALA LYS MET LEU THR ARG PRO GLY SER LEU PHE
SEQRES 15 A 258 PHE GLN ASP LEU ALA LYS ALA LYS LYS PHE SER THR GLU
SEQRES 16 A 258 ARG TYR GLY SER VAL LYS ARG ALA TYR ILE PHE CYS ASN
SEQRES 17 A 258 GLU ASP LYS SER PHE PRO VAL GLU PHE GLN LYS TRP PHE
SEQRES 18 A 258 VAL GLU SER VAL GLY ALA ASP LYS VAL LYS GLU ILE LYS
SEQRES 19 A 258 GLU ALA ASP ALA MET GLY MET LEU SER GLN PRO ARG GLU
SEQRES 20 A 258 VAL CYS LYS CYS LEU LEU ASP ILE SER ASP SER
SEQRES 1 B 258 ALA LYS GLN GLN LYS HIS PHE VAL LEU VAL HIS GLY GLY
SEQRES 2 B 258 CYS LEU GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 B 258 LEU GLU SER ALA GLY HIS LYS VAL THR ALA VAL ASP LEU
SEQRES 4 B 258 SER ALA ALA GLY ILE ASN PRO ARG ARG LEU ASP GLU ILE
SEQRES 5 B 258 HIS THR PHE ARG ASP TYR SER GLU PRO LEU MET GLU VAL
SEQRES 6 B 258 MET ALA SER ILE PRO PRO ASP GLU LYS VAL VAL LEU LEU
SEQRES 7 B 258 GLY HIS SER PHE GLY GLY MET SER LEU GLY LEU ALA MET
SEQRES 8 B 258 GLU THR TYR PRO GLU LYS ILE SER VAL ALA VAL PHE MET
SEQRES 9 B 258 SER ALA MET MET PRO ASP PRO ASN HIS SER LEU THR TYR
SEQRES 10 B 258 PRO PHE GLU LYS TYR ASN GLU LYS CYS PRO ALA ASP MET
SEQRES 11 B 258 MET LEU ASP SER GLN PHE SER THR TYR GLY ASN PRO GLU
SEQRES 12 B 258 ASN PRO GLY MET SER MET ILE LEU GLY PRO GLN PHE MET
SEQRES 13 B 258 ALA LEU LYS MET PHE GLN ASN CYS SER VAL GLU ASP LEU
SEQRES 14 B 258 GLU LEU ALA LYS MET LEU THR ARG PRO GLY SER LEU PHE
SEQRES 15 B 258 PHE GLN ASP LEU ALA LYS ALA LYS LYS PHE SER THR GLU
SEQRES 16 B 258 ARG TYR GLY SER VAL LYS ARG ALA TYR ILE PHE CYS ASN
SEQRES 17 B 258 GLU ASP LYS SER PHE PRO VAL GLU PHE GLN LYS TRP PHE
SEQRES 18 B 258 VAL GLU SER VAL GLY ALA ASP LYS VAL LYS GLU ILE LYS
SEQRES 19 B 258 GLU ALA ASP ALA MET GLY MET LEU SER GLN PRO ARG GLU
SEQRES 20 B 258 VAL CYS LYS CYS LEU LEU ASP ILE SER ASP SER
SEQRES 1 C 258 ALA LYS GLN GLN LYS HIS PHE VAL LEU VAL HIS GLY GLY
SEQRES 2 C 258 CYS LEU GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 C 258 LEU GLU SER ALA GLY HIS LYS VAL THR ALA VAL ASP LEU
SEQRES 4 C 258 SER ALA ALA GLY ILE ASN PRO ARG ARG LEU ASP GLU ILE
SEQRES 5 C 258 HIS THR PHE ARG ASP TYR SER GLU PRO LEU MET GLU VAL
SEQRES 6 C 258 MET ALA SER ILE PRO PRO ASP GLU LYS VAL VAL LEU LEU
SEQRES 7 C 258 GLY HIS SER PHE GLY GLY MET SER LEU GLY LEU ALA MET
SEQRES 8 C 258 GLU THR TYR PRO GLU LYS ILE SER VAL ALA VAL PHE MET
SEQRES 9 C 258 SER ALA MET MET PRO ASP PRO ASN HIS SER LEU THR TYR
SEQRES 10 C 258 PRO PHE GLU LYS TYR ASN GLU LYS CYS PRO ALA ASP MET
SEQRES 11 C 258 MET LEU ASP SER GLN PHE SER THR TYR GLY ASN PRO GLU
SEQRES 12 C 258 ASN PRO GLY MET SER MET ILE LEU GLY PRO GLN PHE MET
SEQRES 13 C 258 ALA LEU LYS MET PHE GLN ASN CYS SER VAL GLU ASP LEU
SEQRES 14 C 258 GLU LEU ALA LYS MET LEU THR ARG PRO GLY SER LEU PHE
SEQRES 15 C 258 PHE GLN ASP LEU ALA LYS ALA LYS LYS PHE SER THR GLU
SEQRES 16 C 258 ARG TYR GLY SER VAL LYS ARG ALA TYR ILE PHE CYS ASN
SEQRES 17 C 258 GLU ASP LYS SER PHE PRO VAL GLU PHE GLN LYS TRP PHE
SEQRES 18 C 258 VAL GLU SER VAL GLY ALA ASP LYS VAL LYS GLU ILE LYS
SEQRES 19 C 258 GLU ALA ASP ALA MET GLY MET LEU SER GLN PRO ARG GLU
SEQRES 20 C 258 VAL CYS LYS CYS LEU LEU ASP ILE SER ASP SER
SEQRES 1 D 258 ALA LYS GLN GLN LYS HIS PHE VAL LEU VAL HIS GLY GLY
SEQRES 2 D 258 CYS LEU GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 D 258 LEU GLU SER ALA GLY HIS LYS VAL THR ALA VAL ASP LEU
SEQRES 4 D 258 SER ALA ALA GLY ILE ASN PRO ARG ARG LEU ASP GLU ILE
SEQRES 5 D 258 HIS THR PHE ARG ASP TYR SER GLU PRO LEU MET GLU VAL
SEQRES 6 D 258 MET ALA SER ILE PRO PRO ASP GLU LYS VAL VAL LEU LEU
SEQRES 7 D 258 GLY HIS SER PHE GLY GLY MET SER LEU GLY LEU ALA MET
SEQRES 8 D 258 GLU THR TYR PRO GLU LYS ILE SER VAL ALA VAL PHE MET
SEQRES 9 D 258 SER ALA MET MET PRO ASP PRO ASN HIS SER LEU THR TYR
SEQRES 10 D 258 PRO PHE GLU LYS TYR ASN GLU LYS CYS PRO ALA ASP MET
SEQRES 11 D 258 MET LEU ASP SER GLN PHE SER THR TYR GLY ASN PRO GLU
SEQRES 12 D 258 ASN PRO GLY MET SER MET ILE LEU GLY PRO GLN PHE MET
SEQRES 13 D 258 ALA LEU LYS MET PHE GLN ASN CYS SER VAL GLU ASP LEU
SEQRES 14 D 258 GLU LEU ALA LYS MET LEU THR ARG PRO GLY SER LEU PHE
SEQRES 15 D 258 PHE GLN ASP LEU ALA LYS ALA LYS LYS PHE SER THR GLU
SEQRES 16 D 258 ARG TYR GLY SER VAL LYS ARG ALA TYR ILE PHE CYS ASN
SEQRES 17 D 258 GLU ASP LYS SER PHE PRO VAL GLU PHE GLN LYS TRP PHE
SEQRES 18 D 258 VAL GLU SER VAL GLY ALA ASP LYS VAL LYS GLU ILE LYS
SEQRES 19 D 258 GLU ALA ASP ALA MET GLY MET LEU SER GLN PRO ARG GLU
SEQRES 20 D 258 VAL CYS LYS CYS LEU LEU ASP ILE SER ASP SER
SEQRES 1 E 258 ALA LYS GLN GLN LYS HIS PHE VAL LEU VAL HIS GLY GLY
SEQRES 2 E 258 CYS LEU GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 E 258 LEU GLU SER ALA GLY HIS LYS VAL THR ALA VAL ASP LEU
SEQRES 4 E 258 SER ALA ALA GLY ILE ASN PRO ARG ARG LEU ASP GLU ILE
SEQRES 5 E 258 HIS THR PHE ARG ASP TYR SER GLU PRO LEU MET GLU VAL
SEQRES 6 E 258 MET ALA SER ILE PRO PRO ASP GLU LYS VAL VAL LEU LEU
SEQRES 7 E 258 GLY HIS SER PHE GLY GLY MET SER LEU GLY LEU ALA MET
SEQRES 8 E 258 GLU THR TYR PRO GLU LYS ILE SER VAL ALA VAL PHE MET
SEQRES 9 E 258 SER ALA MET MET PRO ASP PRO ASN HIS SER LEU THR TYR
SEQRES 10 E 258 PRO PHE GLU LYS TYR ASN GLU LYS CYS PRO ALA ASP MET
SEQRES 11 E 258 MET LEU ASP SER GLN PHE SER THR TYR GLY ASN PRO GLU
SEQRES 12 E 258 ASN PRO GLY MET SER MET ILE LEU GLY PRO GLN PHE MET
SEQRES 13 E 258 ALA LEU LYS MET PHE GLN ASN CYS SER VAL GLU ASP LEU
SEQRES 14 E 258 GLU LEU ALA LYS MET LEU THR ARG PRO GLY SER LEU PHE
SEQRES 15 E 258 PHE GLN ASP LEU ALA LYS ALA LYS LYS PHE SER THR GLU
SEQRES 16 E 258 ARG TYR GLY SER VAL LYS ARG ALA TYR ILE PHE CYS ASN
SEQRES 17 E 258 GLU ASP LYS SER PHE PRO VAL GLU PHE GLN LYS TRP PHE
SEQRES 18 E 258 VAL GLU SER VAL GLY ALA ASP LYS VAL LYS GLU ILE LYS
SEQRES 19 E 258 GLU ALA ASP ALA MET GLY MET LEU SER GLN PRO ARG GLU
SEQRES 20 E 258 VAL CYS LYS CYS LEU LEU ASP ILE SER ASP SER
HET EVS A1000 22
HET EVS B1000 22
HET EVS C1000 22
HET EVS D1000 22
HETNAM EVS 16-EPI-VELLOSIMINE
FORMUL 6 EVS 4(C19 H20 N2 O)
FORMUL 10 HOH *245(H2 O)
HELIX 1 1 GLY A 22 TYR A 27 5 6
HELIX 2 2 LYS A 28 ALA A 36 1 9
HELIX 3 3 ARG A 54 ILE A 58 5 5
HELIX 4 4 THR A 60 SER A 74 1 15
HELIX 5 5 PHE A 88 TYR A 100 1 13
HELIX 6 6 THR A 122 CYS A 132 1 11
HELIX 7 7 GLY A 158 MET A 166 1 9
HELIX 8 8 SER A 171 THR A 182 1 12
HELIX 9 9 PHE A 188 ALA A 193 1 6
HELIX 10 10 ARG A 202 VAL A 206 5 5
HELIX 11 11 PRO A 220 GLY A 232 1 13
HELIX 12 12 MET A 245 GLN A 250 1 6
HELIX 13 13 GLN A 250 ASP A 263 1 14
HELIX 14 14 GLY B 22 TYR B 27 5 6
HELIX 15 15 LEU B 29 ALA B 36 1 8
HELIX 16 16 ARG B 54 ILE B 58 5 5
HELIX 17 17 THR B 60 SER B 74 1 15
HELIX 18 18 PHE B 88 TYR B 100 1 13
HELIX 19 19 THR B 122 PRO B 124 5 3
HELIX 20 20 PHE B 125 CYS B 132 1 8
HELIX 21 21 GLY B 158 MET B 166 1 9
HELIX 22 22 SER B 171 THR B 182 1 12
HELIX 23 23 PHE B 188 LYS B 194 1 7
HELIX 24 24 ARG B 202 VAL B 206 5 5
HELIX 25 25 PRO B 220 VAL B 231 1 12
HELIX 26 26 MET B 245 GLN B 250 1 6
HELIX 27 27 GLN B 250 ASP B 263 1 14
HELIX 28 28 GLY C 22 TYR C 27 5 6
HELIX 29 29 LYS C 28 ALA C 36 1 9
HELIX 30 30 ARG C 54 ILE C 58 5 5
HELIX 31 31 THR C 60 ILE C 75 1 16
HELIX 32 32 PHE C 88 TYR C 100 1 13
HELIX 33 33 THR C 122 PRO C 124 5 3
HELIX 34 34 PHE C 125 CYS C 132 1 8
HELIX 35 35 GLY C 158 MET C 166 1 9
HELIX 36 36 SER C 171 MET C 180 1 10
HELIX 37 37 PHE C 188 ALA C 195 1 8
HELIX 38 38 ARG C 202 VAL C 206 5 5
HELIX 39 39 PRO C 220 VAL C 231 1 12
HELIX 40 40 MET C 245 GLN C 250 1 6
HELIX 41 41 GLN C 250 ASP C 263 1 14
HELIX 42 42 GLY D 22 TYR D 27 5 6
HELIX 43 43 LYS D 28 ALA D 36 1 9
HELIX 44 44 ARG D 54 ILE D 58 5 5
HELIX 45 45 THR D 60 SER D 74 1 15
HELIX 46 46 PHE D 88 TYR D 100 1 13
HELIX 47 47 THR D 122 CYS D 132 1 11
HELIX 48 48 GLY D 158 MET D 166 1 9
HELIX 49 49 SER D 171 THR D 182 1 12
HELIX 50 50 PHE D 188 ALA D 195 1 8
HELIX 51 51 ARG D 202 VAL D 206 5 5
HELIX 52 52 PRO D 220 GLY D 232 1 13
HELIX 53 53 MET D 245 GLN D 250 1 6
HELIX 54 54 GLN D 250 ASP D 263 1 14
HELIX 55 55 GLY E 22 TYR E 27 5 6
HELIX 56 56 LYS E 28 ALA E 36 1 9
HELIX 57 57 THR E 60 SER E 65 1 6
HELIX 58 58 SER E 65 SER E 74 1 10
HELIX 59 59 PHE E 88 TYR E 100 1 13
HELIX 60 60 THR E 122 PRO E 124 5 3
HELIX 61 61 PHE E 125 CYS E 132 1 8
HELIX 62 62 PRO E 133 LEU E 138 5 6
HELIX 63 63 GLY E 158 MET E 166 1 9
HELIX 64 64 SER E 171 THR E 182 1 12
HELIX 65 65 PHE E 188 LYS E 194 1 7
HELIX 66 66 ARG E 202 VAL E 206 5 5
HELIX 67 67 PRO E 220 VAL E 231 1 12
HELIX 68 68 MET E 245 GLN E 250 1 6
HELIX 69 69 GLN E 250 SER E 262 1 13
SHEET 1 A 6 LYS A 39 ALA A 42 0
SHEET 2 A 6 HIS A 12 VAL A 16 1 N LEU A 15 O THR A 41
SHEET 3 A 6 VAL A 81 SER A 87 1 O VAL A 82 N VAL A 14
SHEET 4 A 6 ILE A 104 ALA A 112 1 O VAL A 108 N LEU A 83
SHEET 5 A 6 ARG A 208 CYS A 213 1 O ALA A 209 N ALA A 107
SHEET 6 A 6 LYS A 235 ILE A 239 1 O LYS A 237 N PHE A 212
SHEET 1 B 2 GLN A 141 TYR A 145 0
SHEET 2 B 2 GLY A 152 ILE A 156 -1 O GLY A 152 N TYR A 145
SHEET 1 C 6 LYS B 39 ALA B 42 0
SHEET 2 C 6 HIS B 12 VAL B 16 1 N LEU B 15 O THR B 41
SHEET 3 C 6 VAL B 81 SER B 87 1 O VAL B 82 N VAL B 14
SHEET 4 C 6 ILE B 104 ALA B 112 1 O VAL B 108 N LEU B 83
SHEET 5 C 6 LYS B 207 CYS B 213 1 O ALA B 209 N ALA B 107
SHEET 6 C 6 LYS B 235 ILE B 239 1 O LYS B 237 N PHE B 212
SHEET 1 D 2 GLN B 141 GLY B 146 0
SHEET 2 D 2 PRO B 151 ILE B 156 -1 O SER B 154 N SER B 143
SHEET 1 E 6 LYS C 39 ALA C 42 0
SHEET 2 E 6 HIS C 12 VAL C 16 1 N LEU C 15 O THR C 41
SHEET 3 E 6 VAL C 81 SER C 87 1 O VAL C 82 N HIS C 12
SHEET 4 E 6 ILE C 104 ALA C 112 1 O VAL C 108 N LEU C 83
SHEET 5 E 6 LYS C 207 CYS C 213 1 O LYS C 207 N ALA C 107
SHEET 6 E 6 LYS C 235 ILE C 239 1 O LYS C 237 N PHE C 212
SHEET 1 F 2 GLN C 141 TYR C 145 0
SHEET 2 F 2 GLY C 152 ILE C 156 -1 O GLY C 152 N TYR C 145
SHEET 1 G 6 LYS D 39 VAL D 43 0
SHEET 2 G 6 HIS D 12 VAL D 16 1 N PHE D 13 O LYS D 39
SHEET 3 G 6 VAL D 81 SER D 87 1 O LEU D 84 N VAL D 16
SHEET 4 G 6 ILE D 104 ALA D 112 1 O MET D 110 N GLY D 85
SHEET 5 G 6 LYS D 207 CYS D 213 1 O ILE D 211 N PHE D 109
SHEET 6 G 6 LYS D 235 ILE D 239 1 O ILE D 239 N PHE D 212
SHEET 1 H 2 GLN D 141 TYR D 145 0
SHEET 2 H 2 GLY D 152 ILE D 156 -1 O SER D 154 N SER D 143
SHEET 1 I 6 LYS E 39 VAL E 43 0
SHEET 2 I 6 HIS E 12 VAL E 16 1 N PHE E 13 O THR E 41
SHEET 3 I 6 VAL E 81 SER E 87 1 O VAL E 82 N VAL E 14
SHEET 4 I 6 ILE E 104 ALA E 112 1 O MET E 110 N GLY E 85
SHEET 5 I 6 ARG E 208 CYS E 213 1 O ALA E 209 N PHE E 109
SHEET 6 I 6 LYS E 235 ILE E 239 1 O ILE E 239 N PHE E 212
SHEET 1 J 3 GLN E 141 SER E 143 0
SHEET 2 J 3 SER E 154 ILE E 156 -1 O SER E 154 N SER E 143
SHEET 3 J 3 GLY E 185 SER E 186 -1 O GLY E 185 N MET E 155
SITE 1 AC1 10 HOH A 3 GLY A 19 SER A 87 PHE A 88
SITE 2 AC1 10 MET A 113 PRO A 124 TYR A 128 MET A 155
SITE 3 AC1 10 LEU A 187 HOH A 270
SITE 1 AC2 10 GLY B 19 SER B 87 PHE B 88 MET B 113
SITE 2 AC2 10 PRO B 124 PHE B 125 TYR B 128 MET B 137
SITE 3 AC2 10 LEU B 187 HOH B 290
SITE 1 AC3 12 GLY C 19 SER C 87 PHE C 88 MET C 113
SITE 2 AC3 12 PHE C 125 TYR C 128 MET C 155 LEU C 157
SITE 3 AC3 12 LEU C 187 HOH C 270 HOH C 289 HOH D 301
SITE 1 AC4 11 GLY D 19 SER D 87 PHE D 88 MET D 113
SITE 2 AC4 11 PRO D 124 PHE D 125 TYR D 128 MET D 137
SITE 3 AC4 11 LEU D 157 HOH D 270 HOH D 282
CRYST1 171.210 44.610 180.410 90.00 104.44 90.00 C 1 2 1 20
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 0.005841 0.000000 0.001504 0.00000
SCALE2 0.000000 0.022416 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005724 0.00000
TER 1998 ASP A 263
TER 3996 ASP B 263
TER 5994 ASP C 263
TER 7992 ASP D 263
TER 9990 ASP E 263
MASTER 485 0 4 69 41 0 12 610318 5 88 100
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