HEADER OXIDOREDUCTASE 29-MAY-09 3HN2
TITLE CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM GEOBACTER
TITLE 2 METALLIREDUCENS GS-15
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-DEHYDROPANTOATE 2-REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.169;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACTER METALLIREDUCENS;
SOURCE 3 ORGANISM_TAXID: 269799;
SOURCE 4 STRAIN: GS-15;
SOURCE 5 ATCC: 53774;
SOURCE 6 GENE: GMET_2643;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON+RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS 2-DEHYDROPANTOATE 2-REDUCTASE, PSI-2, NYSGXRC, STRUCTURAL GENOMICS,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, NADP, OXIDOREDUCTASE, PANTOTHENATE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,S.CHANG,J.M.SAUDER,S.K.BURLEY,
AUTHOR 2 S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 (NYSGXRC)
REVDAT 6 21-FEB-24 3HN2 1 REMARK
REVDAT 5 10-FEB-21 3HN2 1 AUTHOR JRNL SEQADV
REVDAT 4 28-NOV-18 3HN2 1 REMARK
REVDAT 3 21-NOV-18 3HN2 1 AUTHOR
REVDAT 2 13-JUL-11 3HN2 1 VERSN
REVDAT 1 09-JUN-09 3HN2 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,S.CHANG,J.M.SAUDER,
JRNL AUTH 2 S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM
JRNL TITL 2 GEOBACTER METALLIREDUCENS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 42815
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1371
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2749
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.4310
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.4520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.97000
REMARK 3 B22 (A**2) : -4.35000
REMARK 3 B33 (A**2) : 8.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.800
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.346
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.353
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.145
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9466 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12798 ; 1.233 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1205 ; 7.137 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 438 ;33.283 ;23.219
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1621 ;20.150 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;15.157 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1436 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7210 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4079 ; 0.131 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6248 ; 0.302 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 387 ; 0.154 ; 0.500
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): 85 ; 0.105 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.109 ; 0.500
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): 6136 ; 3.973 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9465 ; 5.907 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3732 ; 8.789 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3332 ;11.922 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 303
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5300 22.5020 -7.7730
REMARK 3 T TENSOR
REMARK 3 T11: -0.0210 T22: -0.0268
REMARK 3 T33: -0.1380 T12: 0.0609
REMARK 3 T13: 0.0089 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.4573 L22: 0.4068
REMARK 3 L33: 0.3906 L12: -0.3505
REMARK 3 L13: 0.1128 L23: -0.3103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0522 S13: -0.2002
REMARK 3 S21: 0.0096 S22: -0.0929 S23: 0.1184
REMARK 3 S31: -0.0635 S32: 0.0209 S33: 0.0951
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 302
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8310 21.6050 -40.1980
REMARK 3 T TENSOR
REMARK 3 T11: -0.1043 T22: 0.0497
REMARK 3 T33: -0.0358 T12: 0.0894
REMARK 3 T13: -0.0784 T23: 0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 1.6536 L22: 0.8913
REMARK 3 L33: 1.2539 L12: -0.8023
REMARK 3 L13: 0.9063 L23: 0.1769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: 0.4352 S13: 0.3377
REMARK 3 S21: 0.0254 S22: -0.2513 S23: 0.0576
REMARK 3 S31: -0.1024 S32: 0.2499 S33: 0.3176
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 302
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2660 57.1050 14.0500
REMARK 3 T TENSOR
REMARK 3 T11: -0.0382 T22: -0.0566
REMARK 3 T33: -0.0677 T12: -0.1117
REMARK 3 T13: 0.0147 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 0.9516 L22: 1.5522
REMARK 3 L33: 0.3592 L12: 0.3658
REMARK 3 L13: -0.0464 L23: -0.0936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: -0.1432 S13: 0.3217
REMARK 3 S21: -0.1864 S22: -0.1014 S23: 0.0801
REMARK 3 S31: -0.0010 S32: 0.0820 S33: 0.0826
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 301
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4150 68.8350 36.8590
REMARK 3 T TENSOR
REMARK 3 T11: -0.0325 T22: 0.0114
REMARK 3 T33: 0.0035 T12: -0.1581
REMARK 3 T13: 0.0398 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.9619 L22: 1.4244
REMARK 3 L33: 0.9482 L12: 1.6448
REMARK 3 L13: -0.8796 L23: -0.5789
REMARK 3 S TENSOR
REMARK 3 S11: 0.1270 S12: -0.3462 S13: -0.1607
REMARK 3 S21: 0.1219 S22: -0.2252 S23: 0.0269
REMARK 3 S31: 0.0446 S32: 0.0118 S33: 0.0982
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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 3HN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45333
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXDE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, PH 6.0, 20% PEG8000, 200MM
REMARK 280 CALCIUM ACETATE, 10% GLYCEROL, TEMPERATURE 294K, VAPOR DIFFUSION,
REMARK 280 SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.65900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.64550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.08950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.64550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.65900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.08950
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
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 -1
REMARK 465 SER A 0
REMARK 465 LEU A 1
REMARK 465 GLY A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 MET B -1
REMARK 465 SER B 0
REMARK 465 GLU B 303
REMARK 465 GLY B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLU C 303
REMARK 465 GLY C 304
REMARK 465 HIS C 305
REMARK 465 HIS C 306
REMARK 465 HIS C 307
REMARK 465 HIS C 308
REMARK 465 HIS C 309
REMARK 465 HIS C 310
REMARK 465 MET D -1
REMARK 465 SER D 0
REMARK 465 GLY D 302
REMARK 465 GLU D 303
REMARK 465 GLY D 304
REMARK 465 HIS D 305
REMARK 465 HIS D 306
REMARK 465 HIS D 307
REMARK 465 HIS D 308
REMARK 465 HIS D 309
REMARK 465 HIS D 310
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 PRO B 133 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO C 133 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO D 133 C - N - CA ANGL. DEV. = 11.3 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 ARG A 31 -75.48 -130.77
REMARK 500 ASN A 48 35.30 -92.86
REMARK 500 GLU A 93 108.31 -58.35
REMARK 500 PRO A 133 94.95 -11.10
REMARK 500 ALA A 141 -143.17 53.68
REMARK 500 PRO A 151 46.23 -80.14
REMARK 500 ASP A 153 175.19 116.41
REMARK 500 THR A 301 56.46 -115.40
REMARK 500 ALA B 8 -139.16 55.43
REMARK 500 ASP B 33 59.92 -113.95
REMARK 500 ASN B 48 37.15 -95.62
REMARK 500 ALA B 79 42.94 -104.06
REMARK 500 PHE B 114 -37.88 -135.19
REMARK 500 PRO B 133 93.08 -10.81
REMARK 500 ALA B 141 -139.82 48.91
REMARK 500 ASP B 153 149.19 179.80
REMARK 500 ALA B 228 66.95 -113.65
REMARK 500 GLU B 252 54.58 -93.48
REMARK 500 ALA C 8 59.65 -95.09
REMARK 500 ARG C 31 -70.22 -116.75
REMARK 500 ASN C 48 38.21 -90.73
REMARK 500 GLU C 93 95.72 -53.62
REMARK 500 PRO C 133 84.36 -21.74
REMARK 500 ALA C 141 -139.44 50.77
REMARK 500 PRO C 151 36.47 -91.04
REMARK 500 ASP C 153 -90.66 -95.16
REMARK 500 THR C 154 -81.99 -127.46
REMARK 500 ASP C 170 98.37 -67.99
REMARK 500 GLN C 199 63.21 35.60
REMARK 500 GLU C 268 49.17 -85.15
REMARK 500 MET C 287 67.79 -119.37
REMARK 500 ALA D 8 -128.77 53.38
REMARK 500 ARG D 31 -32.31 -140.91
REMARK 500 PHE D 45 76.63 -104.18
REMARK 500 GLU D 93 96.45 -57.92
REMARK 500 PHE D 114 -67.10 -127.60
REMARK 500 PRO D 133 73.40 -17.37
REMARK 500 THR D 154 -64.35 -97.71
REMARK 500 GLU D 252 54.87 -96.96
REMARK 500 GLU D 268 48.02 -97.91
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 ARG B 130 GLY B 131 144.17
REMARK 500 GLY B 131 GLU B 132 138.24
REMARK 500 LEU B 150 PRO B 151 -149.10
REMARK 500 ARG B 152 ASP B 153 130.75
REMARK 500 LEU C 150 PRO C 151 -144.58
REMARK 500 ARG C 152 ASP C 153 -48.92
REMARK 500 ASP C 153 THR C 154 -143.11
REMARK 500 LEU D 150 PRO D 151 -147.49
REMARK 500 ARG D 152 ASP D 153 -133.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11135A RELATED DB: TARGETDB
DBREF 3HN2 A 2 302 UNP Q39SB2 Q39SB2_GEOMG 2 302
DBREF 3HN2 B 2 302 UNP Q39SB2 Q39SB2_GEOMG 2 302
DBREF 3HN2 C 2 302 UNP Q39SB2 Q39SB2_GEOMG 2 302
DBREF 3HN2 D 2 302 UNP Q39SB2 Q39SB2_GEOMG 2 302
SEQADV 3HN2 MET A -1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 SER A 0 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 LEU A 1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLU A 303 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLY A 304 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 305 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 306 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 307 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 308 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 309 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS A 310 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 MET B -1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 SER B 0 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 LEU B 1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLU B 303 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLY B 304 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 305 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 306 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 307 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 308 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 309 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS B 310 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 MET C -1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 SER C 0 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 LEU C 1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLU C 303 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLY C 304 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 305 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 306 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 307 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 308 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 309 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS C 310 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 MET D -1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 SER D 0 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 LEU D 1 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLU D 303 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 GLY D 304 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 305 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 306 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 307 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 308 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 309 UNP Q39SB2 EXPRESSION TAG
SEQADV 3HN2 HIS D 310 UNP Q39SB2 EXPRESSION TAG
SEQRES 1 A 312 MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU
SEQRES 2 A 312 GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU
SEQRES 3 A 312 ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE
SEQRES 4 A 312 ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP
SEQRES 5 A 312 PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU
SEQRES 6 A 312 GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS
SEQRES 7 A 312 THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO
SEQRES 8 A 312 LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN
SEQRES 9 A 312 GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY
SEQRES 10 A 312 ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER
SEQRES 11 A 312 ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA
SEQRES 12 A 312 GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR
SEQRES 13 A 312 GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA
SEQRES 14 A 312 GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA
SEQRES 15 A 312 ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY
SEQRES 16 A 312 LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU
SEQRES 17 A 312 ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET
SEQRES 18 A 312 LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA
SEQRES 19 A 312 THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU
SEQRES 20 A 312 PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU
SEQRES 21 A 312 ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA
SEQRES 22 A 312 ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY
SEQRES 23 A 312 ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU
SEQRES 24 A 312 GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 312 MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU
SEQRES 2 B 312 GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU
SEQRES 3 B 312 ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE
SEQRES 4 B 312 ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP
SEQRES 5 B 312 PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU
SEQRES 6 B 312 GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS
SEQRES 7 B 312 THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO
SEQRES 8 B 312 LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN
SEQRES 9 B 312 GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY
SEQRES 10 B 312 ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER
SEQRES 11 B 312 ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA
SEQRES 12 B 312 GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR
SEQRES 13 B 312 GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA
SEQRES 14 B 312 GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA
SEQRES 15 B 312 ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY
SEQRES 16 B 312 LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU
SEQRES 17 B 312 ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET
SEQRES 18 B 312 LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA
SEQRES 19 B 312 THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU
SEQRES 20 B 312 PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU
SEQRES 21 B 312 ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA
SEQRES 22 B 312 ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY
SEQRES 23 B 312 ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU
SEQRES 24 B 312 GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 312 MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU
SEQRES 2 C 312 GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU
SEQRES 3 C 312 ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE
SEQRES 4 C 312 ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP
SEQRES 5 C 312 PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU
SEQRES 6 C 312 GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS
SEQRES 7 C 312 THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO
SEQRES 8 C 312 LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN
SEQRES 9 C 312 GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY
SEQRES 10 C 312 ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER
SEQRES 11 C 312 ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA
SEQRES 12 C 312 GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR
SEQRES 13 C 312 GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA
SEQRES 14 C 312 GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA
SEQRES 15 C 312 ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY
SEQRES 16 C 312 LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU
SEQRES 17 C 312 ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET
SEQRES 18 C 312 LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA
SEQRES 19 C 312 THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU
SEQRES 20 C 312 PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU
SEQRES 21 C 312 ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA
SEQRES 22 C 312 ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY
SEQRES 23 C 312 ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU
SEQRES 24 C 312 GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 312 MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU
SEQRES 2 D 312 GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU
SEQRES 3 D 312 ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE
SEQRES 4 D 312 ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP
SEQRES 5 D 312 PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU
SEQRES 6 D 312 GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS
SEQRES 7 D 312 THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO
SEQRES 8 D 312 LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN
SEQRES 9 D 312 GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY
SEQRES 10 D 312 ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER
SEQRES 11 D 312 ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA
SEQRES 12 D 312 GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR
SEQRES 13 D 312 GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA
SEQRES 14 D 312 GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA
SEQRES 15 D 312 ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY
SEQRES 16 D 312 LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU
SEQRES 17 D 312 ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET
SEQRES 18 D 312 LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA
SEQRES 19 D 312 THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU
SEQRES 20 D 312 PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU
SEQRES 21 D 312 ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA
SEQRES 22 D 312 ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY
SEQRES 23 D 312 ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU
SEQRES 24 D 312 GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *7(H2 O)
HELIX 1 1 LEU A 11 SER A 22 1 12
HELIX 2 2 ASP A 33 ASN A 40 1 8
HELIX 3 3 ALA A 61 GLY A 66 1 6
HELIX 4 4 LYS A 76 SER A 81 5 6
HELIX 5 5 ARG A 82 ARG A 88 1 7
HELIX 6 6 PRO A 89 VAL A 91 5 3
HELIX 7 7 GLY A 105 PHE A 114 1 10
HELIX 8 8 GLY A 115 GLU A 117 5 3
HELIX 9 9 THR A 154 ALA A 167 1 14
HELIX 10 10 ASP A 176 GLN A 199 1 24
HELIX 11 11 PRO A 201 LEU A 206 1 6
HELIX 12 12 ARG A 208 ALA A 228 1 21
HELIX 13 13 GLY A 238 ASP A 248 1 11
HELIX 14 14 PRO A 255 GLU A 263 1 9
HELIX 15 15 GLU A 268 PHE A 273 1 6
HELIX 16 16 PHE A 273 GLU A 283 1 11
HELIX 17 17 MET A 287 THR A 301 1 15
HELIX 18 18 ALA B 8 SER B 22 1 15
HELIX 19 19 TYR B 34 GLY B 39 1 6
HELIX 20 20 ALA B 61 GLY B 66 1 6
HELIX 21 21 LYS B 76 ASN B 80 5 5
HELIX 22 22 ARG B 82 ARG B 88 1 7
HELIX 23 23 PRO B 89 VAL B 91 5 3
HELIX 24 24 GLY B 105 PHE B 114 1 10
HELIX 25 25 GLY B 115 GLU B 117 5 3
HELIX 26 26 ASP B 153 ALA B 167 1 15
HELIX 27 27 ASP B 176 GLN B 199 1 24
HELIX 28 28 PRO B 201 LEU B 206 1 6
HELIX 29 29 ARG B 208 ALA B 228 1 21
HELIX 30 30 GLY B 238 ASP B 248 1 11
HELIX 31 31 PRO B 255 GLY B 264 1 10
HELIX 32 32 GLU B 268 PHE B 273 1 6
HELIX 33 33 PHE B 273 GLU B 283 1 11
HELIX 34 34 MET B 287 GLY B 302 1 16
HELIX 35 35 LEU C 11 SER C 22 1 12
HELIX 36 36 ASP C 33 ALA C 38 1 6
HELIX 37 37 ALA C 61 ILE C 65 5 5
HELIX 38 38 LYS C 76 SER C 81 5 6
HELIX 39 39 ARG C 82 ARG C 88 1 7
HELIX 40 40 PRO C 89 VAL C 91 5 3
HELIX 41 41 GLY C 105 GLY C 115 1 11
HELIX 42 42 THR C 154 GLN C 166 1 13
HELIX 43 43 ASP C 176 ILE C 189 1 14
HELIX 44 44 ILE C 189 GLN C 199 1 11
HELIX 45 45 PRO C 201 LEU C 206 1 6
HELIX 46 46 ARG C 208 ASN C 227 1 20
HELIX 47 47 GLY C 238 ALA C 249 1 12
HELIX 48 48 PRO C 255 GLY C 264 1 10
HELIX 49 49 GLU C 268 PHE C 273 1 6
HELIX 50 50 PHE C 273 ARG C 282 1 10
HELIX 51 51 MET C 287 THR C 301 1 15
HELIX 52 52 ALA D 8 SER D 22 1 15
HELIX 53 53 TYR D 34 GLY D 39 1 6
HELIX 54 54 ALA D 61 GLY D 66 1 6
HELIX 55 55 LYS D 76 SER D 81 5 6
HELIX 56 56 ARG D 82 ARG D 88 1 7
HELIX 57 57 PRO D 89 VAL D 91 5 3
HELIX 58 58 GLY D 105 PHE D 114 1 10
HELIX 59 59 THR D 154 ALA D 167 1 14
HELIX 60 60 ASP D 176 ASN D 192 1 17
HELIX 61 61 GLY D 193 GLN D 199 1 7
HELIX 62 62 PRO D 201 LEU D 206 1 6
HELIX 63 63 ARG D 208 ALA D 228 1 21
HELIX 64 64 GLY D 238 MET D 250 1 13
HELIX 65 65 PRO D 255 GLU D 263 1 9
HELIX 66 66 GLU D 268 PHE D 273 1 6
HELIX 67 67 PHE D 273 GLU D 283 1 11
HELIX 68 68 MET D 287 THR D 301 1 15
SHEET 1 A 8 GLY A 58 TYR A 59 0
SHEET 2 A 8 VAL A 26 LEU A 29 1 N PHE A 28 O TYR A 59
SHEET 3 A 8 ILE A 3 VAL A 6 1 N ILE A 5 O HIS A 27
SHEET 4 A 8 LEU A 70 VAL A 73 1 O LEU A 72 N VAL A 6
SHEET 5 A 8 GLN A 96 THR A 99 1 O LEU A 98 N VAL A 73
SHEET 6 A 8 ILE A 119 CYS A 127 1 O ILE A 120 N ILE A 97
SHEET 7 A 8 GLY A 140 GLU A 148 -1 O GLY A 147 N GLY A 121
SHEET 8 A 8 CYS A 171 THR A 173 1 O ARG A 172 N ILE A 144
SHEET 1 B 3 PHE A 51 LEU A 53 0
SHEET 2 B 3 LEU A 42 SER A 46 -1 N VAL A 44 O PHE A 51
SHEET 3 B 3 GLU A 135 HIS A 138 1 O VAL A 136 N PHE A 45
SHEET 1 C 9 PHE B 51 LEU B 53 0
SHEET 2 C 9 LEU B 42 PHE B 45 -1 N VAL B 44 O PHE B 51
SHEET 3 C 9 GLU B 135 GLU B 148 1 O VAL B 136 N PHE B 45
SHEET 4 C 9 ILE B 119 ARG B 130 -1 N GLY B 121 O GLY B 147
SHEET 5 C 9 GLN B 96 THR B 99 1 N ILE B 97 O ILE B 120
SHEET 6 C 9 LEU B 70 VAL B 73 1 N VAL B 73 O LEU B 98
SHEET 7 C 9 ARG B 2 VAL B 6 1 N ALA B 4 O LEU B 72
SHEET 8 C 9 ASP B 25 LEU B 29 1 O HIS B 27 N ILE B 3
SHEET 9 C 9 GLY B 58 TYR B 59 1 O TYR B 59 N PHE B 28
SHEET 1 D 4 PHE B 51 LEU B 53 0
SHEET 2 D 4 LEU B 42 PHE B 45 -1 N VAL B 44 O PHE B 51
SHEET 3 D 4 GLU B 135 GLU B 148 1 O VAL B 136 N PHE B 45
SHEET 4 D 4 CYS B 171 THR B 173 1 O ARG B 172 N LEU B 146
SHEET 1 E 9 PHE C 51 LEU C 53 0
SHEET 2 E 9 LEU C 42 PHE C 45 -1 N VAL C 44 O PHE C 51
SHEET 3 E 9 GLU C 135 GLU C 148 1 O VAL C 136 N PHE C 45
SHEET 4 E 9 ILE C 119 GLU C 132 -1 N GLY C 121 O GLY C 147
SHEET 5 E 9 GLN C 96 THR C 99 1 N ILE C 97 O ILE C 120
SHEET 6 E 9 LEU C 70 VAL C 73 1 N VAL C 71 O LEU C 98
SHEET 7 E 9 ARG C 2 VAL C 6 1 N ALA C 4 O LEU C 72
SHEET 8 E 9 ASP C 25 LEU C 29 1 O ASP C 25 N ILE C 3
SHEET 9 E 9 GLY C 58 TYR C 59 1 O TYR C 59 N PHE C 28
SHEET 1 F 4 PHE C 51 LEU C 53 0
SHEET 2 F 4 LEU C 42 PHE C 45 -1 N VAL C 44 O PHE C 51
SHEET 3 F 4 GLU C 135 GLU C 148 1 O VAL C 136 N PHE C 45
SHEET 4 F 4 CYS C 171 THR C 173 1 O ARG C 172 N LEU C 146
SHEET 1 G 9 ASP D 50 LEU D 53 0
SHEET 2 G 9 LEU D 42 PHE D 45 -1 N VAL D 44 O PHE D 51
SHEET 3 G 9 GLU D 135 GLU D 148 1 O VAL D 136 N PHE D 45
SHEET 4 G 9 ILE D 119 ARG D 130 -1 N CYS D 127 O LEU D 139
SHEET 5 G 9 GLN D 96 THR D 99 1 N ILE D 97 O ILE D 120
SHEET 6 G 9 LEU D 70 VAL D 73 1 N VAL D 73 O LEU D 98
SHEET 7 G 9 ARG D 2 VAL D 6 1 N ALA D 4 O LEU D 72
SHEET 8 G 9 ASP D 25 LEU D 29 1 O HIS D 27 N ILE D 3
SHEET 9 G 9 LYS D 57 TYR D 59 1 O LYS D 57 N PHE D 28
SHEET 1 H 4 ASP D 50 LEU D 53 0
SHEET 2 H 4 LEU D 42 PHE D 45 -1 N VAL D 44 O PHE D 51
SHEET 3 H 4 GLU D 135 GLU D 148 1 O VAL D 136 N PHE D 45
SHEET 4 H 4 CYS D 171 THR D 173 1 O ARG D 172 N LEU D 146
CRYST1 77.318 82.179 201.291 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012934 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004968 0.00000
(ATOM LINES ARE NOT SHOWN.)
END