HEADER HYDROLASE/DNA 18-DEC-06 2E52
TITLE CRYSTAL STRUCTURAL ANALYSIS OF HINDIII RESTRICTION ENDONUCLEASE IN
TITLE 2 COMPLEX WITH COGNATE DNA AT 2.0 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE II RESTRICTION ENZYME HINDIII;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 SYNONYM: ENDONUCLEASE HINDIII, R.HINDIII;
COMPND 5 EC: 3.1.21.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*DGP*DCP*DCP*DAP*DAP*DGP*DCP*DTP*DTP*DGP*DGP*DC)-
COMPND 9 3');
COMPND 10 CHAIN: E, F, G, H, I, J;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 71421;
SOURCE 4 STRAIN: RD KW20;
SOURCE 5 GENE: HINDIIIR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS TYPE II RESTRICTION ENZYME HINDIII(E.C.3.1.21.4)/DNA, HYDROLASE-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.WATANABE,C.SATO,I.TANAKA
REVDAT 5 13-JUL-11 2E52 1 VERSN
REVDAT 4 20-OCT-09 2E52 1 JRNL
REVDAT 3 04-AUG-09 2E52 1 HELIX REMARK
REVDAT 2 24-FEB-09 2E52 1 VERSN
REVDAT 1 18-DEC-07 2E52 0
JRNL AUTH N.WATANABE,Y.TAKASAKI,C.SATO,S.ANDO,I.TANAKA
JRNL TITL CRYSTAL STRUCTURES OF RESTRICTION ENDONUCLEASE HINDIII
JRNL TITL 2 COMPLEX WITH ITS COGNATE DNA AND DIVALENT CATIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 119772
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6327
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 469
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9826
REMARK 3 NUCLEIC ACID ATOMS : 1458
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 968
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.59000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.872
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11655 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15971 ; 1.503 ; 2.133
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1190 ; 5.827 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 488 ;38.799 ;25.656
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2008 ;14.930 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;13.294 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1788 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8088 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5417 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8039 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1071 ; 0.140 ; 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): 57 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.123 ; 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): 6227 ; 0.952 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9666 ; 1.508 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6726 ; 2.227 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6305 ; 3.364 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2E52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB026234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126130
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.684
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : 0.15600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.08M AMMONIUM ACETATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 65.76600
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
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 0
REMARK 465 MET C 0
REMARK 465 MET B 0
REMARK 465 LYS B 1
REMARK 465 MET D 0
REMARK 465 LYS D 1
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 DT F 8 C6 DT F 8 N1 0.046
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 ARG C 116 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG C 116 NE - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 DA E 4 O4' - C1' - C2' ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC E 7 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DT E 9 O4' - C1' - N1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG E 10 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DG E 10 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG F 1 C5 - C6 - O6 ANGL. DEV. = -4.6 DEGREES
REMARK 500 DA F 5 O4' - C4' - C3' ANGL. DEV. = -3.1 DEGREES
REMARK 500 DG F 6 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC F 7 O4' - C4' - C3' ANGL. DEV. = -2.9 DEGREES
REMARK 500 DC F 7 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DT F 9 O4' - C1' - N1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 DG F 11 O4' - C1' - N9 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DC G 2 O4' - C1' - N1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 DC G 3 C1' - O4' - C4' ANGL. DEV. = -7.0 DEGREES
REMARK 500 DA G 4 O4' - C4' - C3' ANGL. DEV. = -2.8 DEGREES
REMARK 500 DA G 4 N9 - C1' - C2' ANGL. DEV. = 9.5 DEGREES
REMARK 500 DA G 5 O4' - C4' - C3' ANGL. DEV. = -2.6 DEGREES
REMARK 500 DT G 9 O4' - C1' - N1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 DG G 11 O4' - C1' - N9 ANGL. DEV. = -6.3 DEGREES
REMARK 500 DA H 5 O4' - C4' - C3' ANGL. DEV. = -3.9 DEGREES
REMARK 500 DC H 7 O4' - C4' - C3' ANGL. DEV. = -3.3 DEGREES
REMARK 500 DT H 8 N3 - C4 - O4 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT H 9 O4' - C1' - N1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 DC I 3 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG I 6 O4' - C1' - N9 ANGL. DEV. = 5.8 DEGREES
REMARK 500 DC I 7 O3' - P - O5' ANGL. DEV. = -22.4 DEGREES
REMARK 500 DC I 7 O3' - P - OP2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 DC I 7 O3' - P - OP1 ANGL. DEV. = -19.4 DEGREES
REMARK 500 DT I 8 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG I 10 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DC I 12 C1' - O4' - C4' ANGL. DEV. = -7.3 DEGREES
REMARK 500 DC I 12 O4' - C1' - N1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 DC J 3 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 DC J 3 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC J 3 C3' - O3' - P ANGL. DEV. = 9.5 DEGREES
REMARK 500 DA J 4 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 DA J 5 C3' - O3' - P ANGL. DEV. = 8.3 DEGREES
REMARK 500 DC J 7 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT J 9 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG J 10 O4' - C1' - N9 ANGL. DEV. = 1.9 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 ASN A 79 34.78 76.33
REMARK 500 ARG A 88 -70.41 -113.99
REMARK 500 PHE A 101 -169.13 -128.31
REMARK 500 THR A 117 -100.80 -84.68
REMARK 500 GLU A 134 -118.55 52.01
REMARK 500 THR A 151 -57.28 -127.29
REMARK 500 ASN C 79 36.90 73.68
REMARK 500 ARG C 88 -78.86 -100.92
REMARK 500 THR C 117 -99.62 -89.43
REMARK 500 GLU C 134 -116.29 51.70
REMARK 500 THR C 151 -52.96 -125.64
REMARK 500 SER C 153 146.95 -173.83
REMARK 500 PHE C 262 106.52 57.87
REMARK 500 ASN B 17 -1.92 78.03
REMARK 500 ASN B 79 36.06 72.93
REMARK 500 ARG B 88 -78.81 -108.71
REMARK 500 THR B 117 -108.82 -87.55
REMARK 500 GLU B 134 -116.89 49.84
REMARK 500 THR B 151 -50.71 -127.61
REMARK 500 SER B 153 144.72 -172.59
REMARK 500 ASN D 79 38.66 70.46
REMARK 500 ARG D 88 -76.73 -108.69
REMARK 500 PHE D 101 -168.08 -125.83
REMARK 500 THR D 117 -97.13 -87.40
REMARK 500 GLU D 134 -117.65 50.56
REMARK 500 THR D 151 -57.49 -131.05
REMARK 500 ARG D 264 -55.90 151.95
REMARK 500 GLU D 265 -98.57 109.92
REMARK 500 ASN D 276 37.28 70.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE D 262 THR D 263 146.81
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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 PHE C 262 18.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004
DBREF 2E52 A 0 299 UNP P43870 T2D3_HAEIN 1 300
DBREF 2E52 C 0 299 UNP P43870 T2D3_HAEIN 1 300
DBREF 2E52 B 0 299 UNP P43870 T2D3_HAEIN 1 300
DBREF 2E52 D 0 299 UNP P43870 T2D3_HAEIN 1 300
DBREF 2E52 E 1 12 PDB 2E52 2E52 1 12
DBREF 2E52 F 1 12 PDB 2E52 2E52 1 12
DBREF 2E52 G 1 12 PDB 2E52 2E52 1 12
DBREF 2E52 H 1 12 PDB 2E52 2E52 1 12
DBREF 2E52 I 1 12 PDB 2E52 2E52 1 12
DBREF 2E52 J 1 12 PDB 2E52 2E52 1 12
SEQRES 1 A 300 MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE
SEQRES 2 A 300 GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN
SEQRES 3 A 300 SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU
SEQRES 4 A 300 VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU
SEQRES 5 A 300 ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER
SEQRES 6 A 300 LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU
SEQRES 7 A 300 LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN
SEQRES 8 A 300 ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR
SEQRES 9 A 300 GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG
SEQRES 10 A 300 THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU
SEQRES 11 A 300 SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR
SEQRES 12 A 300 ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE
SEQRES 13 A 300 PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER
SEQRES 14 A 300 TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU
SEQRES 15 A 300 GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE
SEQRES 16 A 300 PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA
SEQRES 17 A 300 GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET
SEQRES 18 A 300 ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU
SEQRES 19 A 300 LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU
SEQRES 20 A 300 ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE
SEQRES 21 A 300 LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU
SEQRES 22 A 300 LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP
SEQRES 23 A 300 SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR
SEQRES 24 A 300 LEU
SEQRES 1 C 300 MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE
SEQRES 2 C 300 GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN
SEQRES 3 C 300 SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU
SEQRES 4 C 300 VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU
SEQRES 5 C 300 ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER
SEQRES 6 C 300 LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU
SEQRES 7 C 300 LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN
SEQRES 8 C 300 ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR
SEQRES 9 C 300 GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG
SEQRES 10 C 300 THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU
SEQRES 11 C 300 SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR
SEQRES 12 C 300 ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE
SEQRES 13 C 300 PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER
SEQRES 14 C 300 TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU
SEQRES 15 C 300 GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE
SEQRES 16 C 300 PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA
SEQRES 17 C 300 GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET
SEQRES 18 C 300 ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU
SEQRES 19 C 300 LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU
SEQRES 20 C 300 ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE
SEQRES 21 C 300 LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU
SEQRES 22 C 300 LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP
SEQRES 23 C 300 SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR
SEQRES 24 C 300 LEU
SEQRES 1 B 300 MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE
SEQRES 2 B 300 GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN
SEQRES 3 B 300 SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU
SEQRES 4 B 300 VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU
SEQRES 5 B 300 ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER
SEQRES 6 B 300 LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU
SEQRES 7 B 300 LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN
SEQRES 8 B 300 ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR
SEQRES 9 B 300 GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG
SEQRES 10 B 300 THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU
SEQRES 11 B 300 SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR
SEQRES 12 B 300 ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE
SEQRES 13 B 300 PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER
SEQRES 14 B 300 TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU
SEQRES 15 B 300 GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE
SEQRES 16 B 300 PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA
SEQRES 17 B 300 GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET
SEQRES 18 B 300 ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU
SEQRES 19 B 300 LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU
SEQRES 20 B 300 ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE
SEQRES 21 B 300 LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU
SEQRES 22 B 300 LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP
SEQRES 23 B 300 SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR
SEQRES 24 B 300 LEU
SEQRES 1 D 300 MET LYS LYS SER ALA LEU GLU LYS LEU LEU SER LEU ILE
SEQRES 2 D 300 GLU ASN LEU THR ASN GLN GLU PHE LYS GLN ALA THR ASN
SEQRES 3 D 300 SER LEU ILE SER PHE ILE TYR LYS LEU ASN ARG ASN GLU
SEQRES 4 D 300 VAL ILE GLU LEU VAL ARG SER ILE GLY ILE LEU PRO GLU
SEQRES 5 D 300 ALA ILE LYS PRO SER SER THR GLN GLU LYS LEU PHE SER
SEQRES 6 D 300 LYS ALA GLY ASP ILE VAL LEU ALA LYS ALA PHE GLN LEU
SEQRES 7 D 300 LEU ASN LEU ASN SER LYS PRO LEU GLU GLN ARG GLY ASN
SEQRES 8 D 300 ALA GLY ASP VAL ILE ALA LEU SER LYS GLU PHE ASN TYR
SEQRES 9 D 300 GLY LEU VAL ALA ASP ALA LYS SER PHE ARG LEU SER ARG
SEQRES 10 D 300 THR ALA LYS ASN GLN LYS ASP PHE LYS VAL LYS ALA LEU
SEQRES 11 D 300 SER GLU TRP ARG GLU ASP LYS ASP TYR ALA VAL LEU THR
SEQRES 12 D 300 ALA PRO PHE PHE GLN TYR PRO THR THR LYS SER GLN ILE
SEQRES 13 D 300 PHE LYS GLN SER LEU ASP GLU ASN VAL LEU LEU PHE SER
SEQRES 14 D 300 TRP GLU HIS LEU ALA ILE LEU LEU GLN LEU ASP LEU GLU
SEQRES 15 D 300 GLU THR ASN ILE PHE SER PHE GLU GLN LEU TRP ASN PHE
SEQRES 16 D 300 PRO LYS LYS GLN SER LYS LYS THR SER VAL SER ASP ALA
SEQRES 17 D 300 GLU ASN ASN PHE MET ARG ASP PHE ASN LYS TYR PHE MET
SEQRES 18 D 300 ASP LEU PHE LYS ILE ASP LYS ASP THR LEU ASN GLN LEU
SEQRES 19 D 300 LEU GLN LYS GLU ILE ASN PHE ILE GLU GLU ARG SER LEU
SEQRES 20 D 300 ILE GLU LYS GLU TYR TRP LYS LYS GLN ILE ASN ILE ILE
SEQRES 21 D 300 LYS ASN PHE THR ARG GLU GLU ALA ILE GLU ALA LEU LEU
SEQRES 22 D 300 LYS ASP ILE ASN MET SER SER LYS ILE GLU THR ILE ASP
SEQRES 23 D 300 SER PHE ILE LYS GLY ILE LYS SER ASN ASP ARG LEU TYR
SEQRES 24 D 300 LEU
SEQRES 1 E 12 DG DC DC DA DA DG DC DT DT DG DG DC
SEQRES 1 F 12 DG DC DC DA DA DG DC DT DT DG DG DC
SEQRES 1 G 12 DG DC DC DA DA DG DC DT DT DG DG DC
SEQRES 1 H 12 DG DC DC DA DA DG DC DT DT DG DG DC
SEQRES 1 I 12 DG DC DC DA DA DG DC DT DT DG DG DC
SEQRES 1 J 12 DG DC DC DA DA DG DC DT DT DG DG DC
HET GOL E1001 6
HET GOL A1004 6
HET ACT C2001 4
HET ACT C2003 4
HET GOL C1002 6
HET GOL C1003 6
HET ACT B2002 4
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 11 GOL 4(C3 H8 O3)
FORMUL 13 ACT 3(C2 H3 O2 1-)
FORMUL 18 HOH *968(H2 O)
HELIX 1 1 ALA A 4 ASN A 14 1 11
HELIX 2 2 PHE A 20 TYR A 32 1 13
HELIX 3 3 ARG A 36 ILE A 46 1 11
HELIX 4 4 THR A 58 LEU A 77 1 20
HELIX 5 5 GLN A 121 PHE A 124 1 4
HELIX 6 6 VAL A 126 TRP A 132 1 7
HELIX 7 7 PHE A 145 TYR A 148 5 4
HELIX 8 8 GLN A 154 GLU A 162 1 9
HELIX 9 9 TRP A 169 GLN A 177 1 9
HELIX 10 10 GLU A 189 SER A 199 1 11
HELIX 11 11 VAL A 204 ASP A 206 5 3
HELIX 12 12 MET A 212 PHE A 223 1 12
HELIX 13 13 LYS A 227 LYS A 260 1 34
HELIX 14 14 ARG A 264 ASP A 274 1 11
HELIX 15 15 MET A 277 LYS A 292 1 16
HELIX 16 16 ASN A 294 LEU A 297 5 4
HELIX 17 17 ALA C 4 ASN C 14 1 11
HELIX 18 18 PHE C 20 TYR C 32 1 13
HELIX 19 19 ARG C 36 ILE C 46 1 11
HELIX 20 20 THR C 58 LEU C 77 1 20
HELIX 21 21 GLN C 121 PHE C 124 1 4
HELIX 22 22 VAL C 126 TRP C 132 1 7
HELIX 23 23 PHE C 145 GLN C 147 5 3
HELIX 24 24 GLN C 154 GLU C 162 1 9
HELIX 25 25 TRP C 169 GLN C 177 1 9
HELIX 26 26 GLU C 189 SER C 199 1 11
HELIX 27 27 VAL C 204 ASP C 206 5 3
HELIX 28 28 MET C 212 PHE C 223 1 12
HELIX 29 29 LYS C 227 LYS C 260 1 34
HELIX 30 30 ARG C 264 ILE C 275 1 12
HELIX 31 31 MET C 277 ILE C 291 1 15
HELIX 32 32 ASN C 294 LEU C 297 5 4
HELIX 33 33 ALA B 4 GLU B 13 1 10
HELIX 34 34 PHE B 20 LYS B 33 1 14
HELIX 35 35 ARG B 36 SER B 45 1 10
HELIX 36 36 THR B 58 LEU B 77 1 20
HELIX 37 37 GLN B 121 PHE B 124 1 4
HELIX 38 38 VAL B 126 TRP B 132 1 7
HELIX 39 39 PHE B 145 GLN B 147 5 3
HELIX 40 40 GLN B 154 GLU B 162 1 9
HELIX 41 41 TRP B 169 GLN B 177 1 9
HELIX 42 42 GLU B 189 LYS B 200 1 12
HELIX 43 43 MET B 212 PHE B 223 1 12
HELIX 44 44 LYS B 227 LYS B 260 1 34
HELIX 45 45 ARG B 264 ILE B 275 1 12
HELIX 46 46 MET B 277 ILE B 291 1 15
HELIX 47 47 ASN B 294 LEU B 297 5 4
HELIX 48 48 ALA D 4 ASN D 14 1 11
HELIX 49 49 PHE D 20 TYR D 32 1 13
HELIX 50 50 ARG D 36 SER D 45 1 10
HELIX 51 51 THR D 58 LEU D 77 1 20
HELIX 52 52 GLN D 121 PHE D 124 1 4
HELIX 53 53 VAL D 126 TRP D 132 1 7
HELIX 54 54 PHE D 145 GLN D 147 5 3
HELIX 55 55 GLN D 154 GLU D 162 1 9
HELIX 56 56 TRP D 169 GLN D 177 1 9
HELIX 57 57 GLU D 189 SER D 199 1 11
HELIX 58 58 VAL D 204 ASP D 206 5 3
HELIX 59 59 MET D 212 PHE D 223 1 12
HELIX 60 60 LYS D 227 LYS D 260 1 34
HELIX 61 61 GLU D 266 ILE D 275 1 10
HELIX 62 62 MET D 277 ILE D 291 1 15
HELIX 63 63 ASN D 294 LEU D 297 5 4
SHEET 1 A 2 ILE A 48 LEU A 49 0
SHEET 2 A 2 PHE A 112 ARG A 113 1 O PHE A 112 N LEU A 49
SHEET 1 B 5 LEU A 80 PRO A 84 0
SHEET 2 B 5 VAL A 94 SER A 98 -1 O LEU A 97 N ASN A 81
SHEET 3 B 5 GLY A 104 ALA A 109 -1 O ALA A 107 N VAL A 94
SHEET 4 B 5 TYR A 138 ALA A 143 1 O THR A 142 N ASP A 108
SHEET 5 B 5 VAL A 164 SER A 168 1 O LEU A 165 N LEU A 141
SHEET 1 C 2 ILE C 48 LEU C 49 0
SHEET 2 C 2 PHE C 112 ARG C 113 1 O PHE C 112 N LEU C 49
SHEET 1 D 5 LEU C 80 PRO C 84 0
SHEET 2 D 5 VAL C 94 SER C 98 -1 O LEU C 97 N ASN C 81
SHEET 3 D 5 GLY C 104 ALA C 109 -1 O ALA C 107 N VAL C 94
SHEET 4 D 5 TYR C 138 ALA C 143 1 O THR C 142 N ASP C 108
SHEET 5 D 5 VAL C 164 SER C 168 1 O LEU C 165 N LEU C 141
SHEET 1 E 2 ILE B 48 LEU B 49 0
SHEET 2 E 2 PHE B 112 ARG B 113 1 O PHE B 112 N LEU B 49
SHEET 1 F 5 LEU B 80 PRO B 84 0
SHEET 2 F 5 VAL B 94 SER B 98 -1 O LEU B 97 N ASN B 81
SHEET 3 F 5 GLY B 104 ALA B 109 -1 O ALA B 107 N VAL B 94
SHEET 4 F 5 TYR B 138 ALA B 143 1 O THR B 142 N ASP B 108
SHEET 5 F 5 LEU B 165 SER B 168 1 O LEU B 165 N LEU B 141
SHEET 1 G 2 ILE D 48 LEU D 49 0
SHEET 2 G 2 PHE D 112 ARG D 113 1 O PHE D 112 N LEU D 49
SHEET 1 H 5 LEU D 80 PRO D 84 0
SHEET 2 H 5 VAL D 94 SER D 98 -1 O LEU D 97 N ASN D 81
SHEET 3 H 5 GLY D 104 ALA D 109 -1 O ALA D 107 N VAL D 94
SHEET 4 H 5 TYR D 138 ALA D 143 1 O THR D 142 N ASP D 108
SHEET 5 H 5 LEU D 165 SER D 168 1 O LEU D 165 N LEU D 141
CISPEP 1 ASN C 261 PHE C 262 0 -2.30
CISPEP 2 THR D 263 ARG D 264 0 21.38
CISPEP 3 ARG D 264 GLU D 265 0 -12.26
SITE 1 AC1 3 ASN C 209 ASP C 214 HOH C2016
SITE 1 AC2 4 ASP B 161 SER B 199 THR B 202 ALA B 207
SITE 1 AC3 5 PHE C 186 LEU C 222 PHE C 223 LYS C 224
SITE 2 AC3 5 HOH C2145
SITE 1 AC4 7 GLY A 89 LYS B 152 DC E 2 DC E 3
SITE 2 AC4 7 HOH E1007 HOH E1010 DG G 11
SITE 1 AC5 8 ARG C 296 TYR C 298 PHE D 145 PHE D 146
SITE 2 AC5 8 TYR D 148 PRO D 149 ASN D 210 MET D 212
SITE 1 AC6 8 PHE C 145 PHE C 146 TYR C 148 PRO C 149
SITE 2 AC6 8 ASN C 210 MET C 212 ARG D 296 TYR D 298
SITE 1 AC7 8 PHE A 145 PHE A 146 TYR A 148 PRO A 149
SITE 2 AC7 8 ASN A 210 MET A 212 ARG B 296 TYR B 298
CRYST1 83.125 131.532 93.718 90.00 111.20 90.00 P 1 21 1 12
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 0.012030 0.000000 0.004666 0.00000
SCALE2 0.000000 0.007603 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
