HEADER LYASE 23-JAN-09 3FZ7
TITLE CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE 2 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: GAD-BETA;
COMPND 5 EC: 4.1.1.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: B1493, GADB, JW1488;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS GLUTAMATE DECARBOXYLASE, APO, DECARBOXYLASE, LYASE, MEMBRANE,
KEYWDS 2 PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
REVDAT 3 01-NOV-17 3FZ7 1 REMARK
REVDAT 2 13-JUL-11 3FZ7 1 VERSN
REVDAT 1 03-FEB-09 3FZ7 0
JRNL AUTH V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
JRNL TITL CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM
JRNL TITL 2 ESCHERICHIA COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 105257
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5253
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) : 7211
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 366
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21817
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 998
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) : 15.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.03000
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): 0.627
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.245
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22405 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30377 ; 1.694 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2739 ; 6.594 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1090 ;34.500 ;23.963
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3714 ;16.829 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;18.686 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3183 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17394 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 13659 ; 1.439 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21934 ; 4.780 ;20.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8746 ; 9.622 ;20.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8443 ; 5.243 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B C D E F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B -9999 B 9999 1
REMARK 3 1 C -9999 C 9999 1
REMARK 3 1 D -9999 D 9999 1
REMARK 3 1 E -9999 E 9999 1
REMARK 3 1 F -9999 F 9999 1
REMARK 3 1 G -9999 G 9999 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3607 ; 0.340 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 B (A): 3607 ; 0.300 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 C (A): 3607 ; 0.380 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 D (A): 3607 ; 0.320 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 E (A): 3607 ; 0.350 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 F (A): 3607 ; 0.340 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 3607 ; 3.630 ;10.000
REMARK 3 TIGHT THERMAL 1 B (A**2): 3607 ; 3.490 ;10.000
REMARK 3 TIGHT THERMAL 1 C (A**2): 3607 ; 3.670 ;10.000
REMARK 3 TIGHT THERMAL 1 D (A**2): 3607 ; 3.610 ;10.000
REMARK 3 TIGHT THERMAL 1 E (A**2): 3607 ; 4.310 ;10.000
REMARK 3 TIGHT THERMAL 1 F (A**2): 3607 ; 3.030 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 12 B 466
REMARK 3 RESIDUE RANGE : B 467 B 467
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2262 17.4531 -5.7648
REMARK 3 T TENSOR
REMARK 3 T11: 0.0060 T22: 0.0254
REMARK 3 T33: 0.0318 T12: -0.0029
REMARK 3 T13: 0.0106 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.3449 L22: 0.2748
REMARK 3 L33: 0.3463 L12: -0.0514
REMARK 3 L13: -0.1545 L23: 0.0399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: 0.0189 S13: 0.0563
REMARK 3 S21: -0.0208 S22: 0.0270 S23: -0.0219
REMARK 3 S31: -0.0290 S32: 0.0511 S33: -0.0675
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 466
REMARK 3 RESIDUE RANGE : C 467 C 467
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9117 -4.1016 12.3350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0195 T22: 0.0732
REMARK 3 T33: 0.0140 T12: 0.0244
REMARK 3 T13: -0.0157 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.2455 L22: 0.2310
REMARK 3 L33: 0.3139 L12: 0.1218
REMARK 3 L13: 0.1685 L23: 0.0412
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.0259 S13: -0.0130
REMARK 3 S21: 0.0571 S22: 0.0196 S23: -0.0373
REMARK 3 S31: 0.0310 S32: 0.0843 S33: -0.0391
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 13 D 466
REMARK 3 RESIDUE RANGE : D 467 D 467
REMARK 3 RESIDUE RANGE : D 468 D 1465
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2962 -28.8559 -12.4775
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0036
REMARK 3 T33: 0.0009 T12: -0.0058
REMARK 3 T13: -0.0012 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.2083 L22: 0.2567
REMARK 3 L33: 0.3607 L12: -0.0398
REMARK 3 L13: -0.0486 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.0158 S13: 0.0007
REMARK 3 S21: 0.0414 S22: -0.0071 S23: 0.0093
REMARK 3 S31: 0.0797 S32: -0.0225 S33: -0.0033
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 12 E 466
REMARK 3 RESIDUE RANGE : E 467 E 467
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1703 -24.0598 8.2757
REMARK 3 T TENSOR
REMARK 3 T11: 0.0613 T22: 0.0052
REMARK 3 T33: 0.0286 T12: -0.0145
REMARK 3 T13: 0.0308 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.1782 L22: 0.5002
REMARK 3 L33: 0.3177 L12: -0.0821
REMARK 3 L13: -0.1457 L23: -0.0611
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: -0.0029 S13: -0.0213
REMARK 3 S21: 0.0702 S22: 0.0046 S23: 0.0931
REMARK 3 S31: 0.1021 S32: -0.0254 S33: 0.0316
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 466
REMARK 3 RESIDUE RANGE : F 467 F 467
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8865 20.3910 -7.7364
REMARK 3 T TENSOR
REMARK 3 T11: 0.0108 T22: 0.0098
REMARK 3 T33: 0.0098 T12: 0.0093
REMARK 3 T13: -0.0055 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.2009 L22: 0.3745
REMARK 3 L33: 0.3127 L12: -0.0964
REMARK 3 L13: 0.0915 L23: 0.0331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: 0.0285 S13: -0.0358
REMARK 3 S21: -0.0255 S22: -0.0296 S23: 0.0209
REMARK 3 S31: -0.0224 S32: -0.0085 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 13 A 466
REMARK 3 RESIDUE RANGE : A 467 A 467
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6422 30.6387 14.7190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0201 T22: 0.0031
REMARK 3 T33: 0.0109 T12: 0.0063
REMARK 3 T13: 0.0070 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.3488 L22: 0.2018
REMARK 3 L33: 0.3008 L12: -0.1125
REMARK 3 L13: -0.0286 L23: 0.1245
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.0117 S13: 0.0334
REMARK 3 S21: -0.0198 S22: 0.0024 S23: -0.0398
REMARK 3 S31: -0.0702 S32: -0.0236 S33: -0.0254
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: RESIDUAL ONLY.
REMARK 4
REMARK 4 3FZ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051221.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106626
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 -HCL, PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.70733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.85367
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 46910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -217.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP A 2
REMARK 465 LYS A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 VAL A 6
REMARK 465 THR A 7
REMARK 465 ASP A 8
REMARK 465 LEU A 9
REMARK 465 ARG A 10
REMARK 465 SER A 11
REMARK 465 GLU A 12
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 3
REMARK 465 LYS B 4
REMARK 465 GLN B 5
REMARK 465 VAL B 6
REMARK 465 THR B 7
REMARK 465 ASP B 8
REMARK 465 LEU B 9
REMARK 465 ARG B 10
REMARK 465 SER B 11
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 LYS C 3
REMARK 465 MET D 1
REMARK 465 ASP D 2
REMARK 465 LYS D 3
REMARK 465 LYS D 4
REMARK 465 GLN D 5
REMARK 465 VAL D 6
REMARK 465 THR D 7
REMARK 465 ASP D 8
REMARK 465 LEU D 9
REMARK 465 ARG D 10
REMARK 465 SER D 11
REMARK 465 GLU D 12
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 LYS E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 VAL E 6
REMARK 465 THR E 7
REMARK 465 ASP E 8
REMARK 465 LEU E 9
REMARK 465 ARG E 10
REMARK 465 SER E 11
REMARK 465 MET F 1
REMARK 465 ASP F 2
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 OH TYR E 305 O HOH D 725 1.51
REMARK 500 OH TYR C 352 OE1 GLU C 435 1.96
REMARK 500 O GLU B 28 N LYS B 30 2.03
REMARK 500 OH TYR B 352 OE1 GLU B 435 2.06
REMARK 500 O ALA C 27 O HOH D 757 2.08
REMARK 500 OD2 ASP A 239 O HOH D 1410 2.12
REMARK 500 OH TYR D 305 O HOH D 731 2.13
REMARK 500 OH TYR A 352 OE1 GLU A 435 2.15
REMARK 500 O ASN C 59 NH2 ARG C 426 2.16
REMARK 500 O HOH D 586 O HOH D 753 2.17
REMARK 500 O ASN B 59 NH2 ARG B 426 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 O HOH D 649 O HOH D 803 1455 1.88
REMARK 500 O HOH D 810 O HOH D 869 3555 2.10
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 LEU B 157 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG B 290 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 398 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 426 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 426 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 426 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LEU D 34 CB - CG - CD1 ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG D 193 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG D 193 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG D 290 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG D 290 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 LEU D 332 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG D 426 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 LEU E 157 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG F 398 NE - CZ - NH1 ANGL. DEV. = 3.4 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 ALA A 56 -2.16 58.30
REMARK 500 GLU A 200 -8.58 -59.36
REMARK 500 ALA A 255 69.51 -157.72
REMARK 500 ASP A 261 -149.21 -120.67
REMARK 500 LYS A 276 -115.88 -101.89
REMARK 500 LEU A 282 132.35 -35.75
REMARK 500 PHE A 317 -99.30 -132.51
REMARK 500 GLN A 459 23.66 -153.52
REMARK 500 GLU B 28 -85.70 72.55
REMARK 500 SER B 29 -14.24 28.22
REMARK 500 ALA B 56 -14.38 58.34
REMARK 500 PRO B 161 78.91 -69.15
REMARK 500 GLN B 186 79.94 -151.65
REMARK 500 LEU B 187 41.52 -93.55
REMARK 500 LEU B 250 -71.33 -119.51
REMARK 500 ASP B 261 -148.72 -110.28
REMARK 500 LYS B 276 -117.23 -97.62
REMARK 500 ASP B 291 -175.53 -175.07
REMARK 500 PHE B 317 -104.23 -138.96
REMARK 500 PRO B 376 77.03 -69.78
REMARK 500 GLU B 386 -5.03 -46.11
REMARK 500 ASP B 387 90.97 17.95
REMARK 500 GLN B 459 27.03 -148.81
REMARK 500 PHE B 463 121.94 -34.94
REMARK 500 SER C 11 35.32 -96.95
REMARK 500 LYS C 154 54.28 -117.32
REMARK 500 PRO C 161 70.96 -68.44
REMARK 500 THR C 214 -35.42 -130.75
REMARK 500 ALA C 245 -63.54 -26.65
REMARK 500 LEU C 250 -71.53 -114.03
REMARK 500 ALA C 255 59.95 -145.46
REMARK 500 ASP C 261 -150.90 -116.17
REMARK 500 PHE C 262 1.35 -64.43
REMARK 500 LYS C 276 -114.48 -103.59
REMARK 500 LEU C 279 -1.68 83.02
REMARK 500 PHE C 317 -94.31 -133.52
REMARK 500 LEU C 411 -177.98 -68.32
REMARK 500 GLN C 459 41.74 -152.73
REMARK 500 ALA D 27 -92.93 -49.76
REMARK 500 GLU D 28 33.10 -75.80
REMARK 500 ALA D 56 -4.83 71.16
REMARK 500 TYR D 90 67.55 -119.74
REMARK 500 GLN D 186 83.65 -157.82
REMARK 500 ALA D 245 -55.92 -28.29
REMARK 500 LEU D 250 -65.97 -108.73
REMARK 500 ALA D 255 55.99 -141.03
REMARK 500 ASP D 261 -141.51 -114.23
REMARK 500 LYS D 276 -107.53 -101.20
REMARK 500 LEU D 282 128.19 -34.18
REMARK 500 ASP D 291 -174.11 -170.16
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
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 SER F 11 GLU F 12 -131.46
REMARK 500 GLU F 12 LEU F 13 145.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 467
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
REMARK 900 COLI: COMPLEX WITH XENON
REMARK 900 RELATED ID: 3FZ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
REMARK 900 COLI: REDUCED SCHIFF BASE WITH PLP
DBREF 3FZ7 A 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ7 B 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ7 C 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ7 D 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ7 E 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ7 F 1 466 UNP P69910 DCEB_ECOLI 1 466
SEQRES 1 A 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 A 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 A 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 A 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 A 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 A 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 A 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 A 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 A 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 A 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 A 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 A 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 A 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 A 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 A 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 A 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 A 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 A 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 A 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 A 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 A 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 A 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 A 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 A 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 A 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 A 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 A 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 A 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 A 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 A 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 A 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 A 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 A 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 A 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 A 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 A 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 B 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 B 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 B 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 B 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 B 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 B 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 B 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 B 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 B 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 B 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 B 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 B 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 B 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 B 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 B 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 B 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 B 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 B 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 B 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 B 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 B 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 B 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 B 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 B 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 B 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 B 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 B 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 B 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 B 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 B 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 B 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 B 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 B 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 B 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 B 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 B 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 C 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 C 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 C 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 C 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 C 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 C 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 C 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 C 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 C 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 C 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 C 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 C 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 C 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 C 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 C 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 C 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 C 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 C 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 C 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 C 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 C 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 C 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 C 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 C 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 C 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 C 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 C 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 C 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 C 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 C 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 C 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 C 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 C 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 C 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 C 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 C 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 D 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 D 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 D 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 D 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 D 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 D 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 D 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 D 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 D 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 D 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 D 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 D 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 D 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 D 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 D 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 D 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 D 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 D 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 D 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 D 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 D 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 D 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 D 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 D 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 D 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 D 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 D 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 D 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 D 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 D 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 D 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 D 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 D 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 D 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 D 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 D 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 E 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 E 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 E 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 E 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 E 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 E 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 E 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 E 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 E 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 E 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 E 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 E 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 E 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 E 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 E 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 E 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 E 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 E 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 E 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 E 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 E 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 E 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 E 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 E 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 E 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 E 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 E 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 E 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 E 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 E 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 E 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 E 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 E 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 E 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 E 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 E 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 F 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 F 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 F 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 F 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 F 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 F 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 F 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 F 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 F 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 F 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 F 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 F 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 F 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 F 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 F 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 F 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 F 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 F 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 F 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 F 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 F 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 F 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 F 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 F 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 F 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 F 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 F 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 F 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 F 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 F 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 F 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 F 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 F 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 F 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 F 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 F 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
HET PO4 A 467 5
HET PO4 B 467 5
HET PO4 C 467 5
HET PO4 D 467 5
HET PO4 E 467 5
HET PO4 F 467 5
HETNAM PO4 PHOSPHATE ION
FORMUL 7 PO4 6(O4 P 3-)
FORMUL 13 HOH *998(H2 O)
HELIX 1 1 ARG A 38 TYR A 51 1 14
HELIX 2 2 ASP A 69 SER A 79 1 11
HELIX 3 3 TYR A 90 TRP A 108 1 19
HELIX 4 4 GLY A 125 ALA A 148 1 24
HELIX 5 5 GLN A 163 TRP A 173 1 11
HELIX 6 6 ASP A 190 CYS A 198 1 9
HELIX 7 7 PHE A 219 GLY A 235 1 17
HELIX 8 8 SER A 246 PHE A 249 5 4
HELIX 9 9 LEU A 250 ALA A 255 1 6
HELIX 10 10 ASP A 291 LEU A 295 5 5
HELIX 11 11 PRO A 296 VAL A 300 5 5
HELIX 12 12 ALA A 321 ALA A 358 1 38
HELIX 13 13 THR A 391 LEU A 401 1 11
HELIX 14 14 GLU A 430 HIS A 451 1 22
HELIX 15 15 PRO A 452 GLN A 455 5 4
HELIX 16 16 ARG B 38 TYR B 51 1 14
HELIX 17 17 ASP B 69 SER B 79 1 11
HELIX 18 18 TYR B 90 TRP B 108 1 19
HELIX 19 19 GLY B 125 ALA B 148 1 24
HELIX 20 20 GLN B 163 ASP B 174 1 12
HELIX 21 21 ASP B 190 CYS B 198 1 9
HELIX 22 22 PHE B 219 GLY B 235 1 17
HELIX 23 23 SER B 246 PHE B 249 5 4
HELIX 24 24 LEU B 250 ALA B 255 1 6
HELIX 25 25 ASP B 291 LEU B 295 5 5
HELIX 26 26 PRO B 296 VAL B 300 5 5
HELIX 27 27 ALA B 321 LYS B 359 1 39
HELIX 28 28 THR B 391 LEU B 401 1 11
HELIX 29 29 GLU B 430 HIS B 451 1 22
HELIX 30 30 PRO B 452 GLN B 455 5 4
HELIX 31 31 ARG C 38 TYR C 51 1 14
HELIX 32 32 ASP C 69 SER C 79 1 11
HELIX 33 33 TYR C 90 TRP C 108 1 19
HELIX 34 34 GLY C 125 ALA C 148 1 24
HELIX 35 35 GLN C 163 TRP C 173 1 11
HELIX 36 36 ASP C 190 CYS C 198 1 9
HELIX 37 37 PHE C 219 GLY C 235 1 17
HELIX 38 38 SER C 246 PHE C 249 5 4
HELIX 39 39 LEU C 250 ALA C 255 1 6
HELIX 40 40 ASP C 291 LEU C 295 5 5
HELIX 41 41 PRO C 296 VAL C 300 5 5
HELIX 42 42 ALA C 321 LYS C 359 1 39
HELIX 43 43 THR C 391 ARG C 402 1 12
HELIX 44 44 GLY C 412 THR C 416 5 5
HELIX 45 45 GLU C 430 HIS C 451 1 22
HELIX 46 46 PRO C 452 GLN C 455 5 4
HELIX 47 47 ARG D 38 TYR D 51 1 14
HELIX 48 48 ASP D 69 SER D 79 1 11
HELIX 49 49 TYR D 90 TRP D 108 1 19
HELIX 50 50 GLY D 125 ALA D 147 1 23
HELIX 51 51 GLN D 163 TRP D 173 1 11
HELIX 52 52 ASP D 190 ALA D 197 1 8
HELIX 53 53 PHE D 219 GLY D 235 1 17
HELIX 54 54 SER D 246 PHE D 249 5 4
HELIX 55 55 LEU D 250 ALA D 255 1 6
HELIX 56 56 ASP D 291 LEU D 295 5 5
HELIX 57 57 PRO D 296 VAL D 300 5 5
HELIX 58 58 ALA D 321 LYS D 359 1 39
HELIX 59 59 THR D 391 LEU D 401 1 11
HELIX 60 60 GLU D 430 HIS D 451 1 22
HELIX 61 61 PRO D 452 GLN D 455 5 4
HELIX 62 62 ARG E 38 TYR E 51 1 14
HELIX 63 63 ASP E 69 SER E 79 1 11
HELIX 64 64 TYR E 90 TRP E 108 1 19
HELIX 65 65 GLY E 125 ALA E 148 1 24
HELIX 66 66 GLN E 163 TRP E 173 1 11
HELIX 67 67 ASP E 190 CYS E 198 1 9
HELIX 68 68 PHE E 219 GLY E 235 1 17
HELIX 69 69 SER E 246 PHE E 249 5 4
HELIX 70 70 LEU E 250 ALA E 255 1 6
HELIX 71 71 ASP E 291 LEU E 295 5 5
HELIX 72 72 PRO E 296 VAL E 300 5 5
HELIX 73 73 ALA E 321 ALA E 358 1 38
HELIX 74 74 THR E 391 ARG E 402 1 12
HELIX 75 75 GLY E 412 THR E 416 5 5
HELIX 76 76 GLU E 430 HIS E 451 1 22
HELIX 77 77 PRO E 452 GLN E 455 5 4
HELIX 78 78 VAL F 6 ARG F 10 5 5
HELIX 79 79 ARG F 38 LEU F 50 1 13
HELIX 80 80 TYR F 51 ASP F 53 5 3
HELIX 81 81 ASP F 69 SER F 79 1 11
HELIX 82 82 TYR F 90 TRP F 108 1 19
HELIX 83 83 GLY F 125 GLY F 149 1 25
HELIX 84 84 GLN F 163 TRP F 173 1 11
HELIX 85 85 ASP F 190 ALA F 197 1 8
HELIX 86 86 PHE F 219 GLY F 235 1 17
HELIX 87 87 SER F 246 PHE F 249 5 4
HELIX 88 88 LEU F 250 ALA F 255 1 6
HELIX 89 89 ASP F 291 LEU F 295 5 5
HELIX 90 90 PRO F 296 VAL F 300 5 5
HELIX 91 91 ALA F 321 LYS F 359 1 39
HELIX 92 92 THR F 391 ARG F 402 1 12
HELIX 93 93 GLY F 412 THR F 416 5 5
HELIX 94 94 GLU F 430 HIS F 451 1 22
HELIX 95 95 PRO F 452 GLN F 455 5 4
SHEET 1 A 2 LEU A 14 ASP A 15 0
SHEET 2 A 2 ALA A 20 LYS A 21 -1 O ALA A 20 N ASP A 15
SHEET 1 B 4 VAL A 119 THR A 123 0
SHEET 2 B 4 GLY A 285 TRP A 289 -1 O GLY A 285 N THR A 123
SHEET 3 B 4 VAL A 267 SER A 273 -1 N ALA A 272 O TRP A 286
SHEET 4 B 4 MET A 240 ASP A 243 1 N MET A 240 O LYS A 268
SHEET 1 C 3 GLU A 176 GLU A 179 0
SHEET 2 C 3 ASN A 156 CYS A 159 1 N LEU A 157 O ARG A 178
SHEET 3 C 3 THR A 202 VAL A 206 1 O ILE A 203 N ASN A 156
SHEET 1 D 2 PHE A 301 TYR A 305 0
SHEET 2 D 2 GLY A 308 THR A 312 -1 O THR A 312 N PHE A 301
SHEET 1 E 4 TYR A 363 THR A 368 0
SHEET 2 E 4 ALA A 377 LEU A 382 -1 O LYS A 381 N GLU A 364
SHEET 3 E 4 VAL A 419 MET A 424 -1 O MET A 421 N PHE A 380
SHEET 4 E 4 ALA A 408 THR A 410 -1 N PHE A 409 O VAL A 420
SHEET 1 F 2 LEU B 14 ASP B 15 0
SHEET 2 F 2 ALA B 20 LYS B 21 -1 O ALA B 20 N ASP B 15
SHEET 1 G 4 VAL B 119 THR B 123 0
SHEET 2 G 4 GLY B 285 TRP B 289 -1 O GLY B 285 N THR B 123
SHEET 3 G 4 VAL B 267 SER B 273 -1 N ILE B 270 O ILE B 288
SHEET 4 G 4 MET B 240 ASP B 243 1 N MET B 240 O LYS B 268
SHEET 1 H 3 GLU B 176 GLU B 179 0
SHEET 2 H 3 ASN B 156 CYS B 159 1 N LEU B 157 O ARG B 178
SHEET 3 H 3 THR B 202 VAL B 206 1 O ILE B 203 N ASN B 156
SHEET 1 I 2 PHE B 301 TYR B 305 0
SHEET 2 I 2 GLY B 308 THR B 312 -1 O THR B 312 N PHE B 301
SHEET 1 J 4 TYR B 363 THR B 368 0
SHEET 2 J 4 ALA B 377 LEU B 382 -1 O LYS B 381 N GLU B 364
SHEET 3 J 4 VAL B 419 MET B 424 -1 O ILE B 423 N VAL B 378
SHEET 4 J 4 ALA B 408 THR B 410 -1 N PHE B 409 O VAL B 420
SHEET 1 K 2 LEU C 14 ASP C 15 0
SHEET 2 K 2 ALA C 20 LYS C 21 -1 O ALA C 20 N ASP C 15
SHEET 1 L 4 GLY C 120 THR C 123 0
SHEET 2 L 4 GLY C 285 TRP C 289 -1 O GLY C 285 N THR C 123
SHEET 3 L 4 VAL C 267 SER C 273 -1 N ILE C 270 O ILE C 288
SHEET 4 L 4 MET C 240 ASP C 243 1 N ILE C 242 O SER C 271
SHEET 1 M 3 GLU C 176 GLU C 179 0
SHEET 2 M 3 ASN C 156 CYS C 159 1 N LEU C 157 O ARG C 178
SHEET 3 M 3 THR C 202 VAL C 206 1 O ILE C 203 N ASN C 156
SHEET 1 N 2 PHE C 301 TYR C 305 0
SHEET 2 N 2 GLY C 308 THR C 312 -1 O THR C 312 N PHE C 301
SHEET 1 O 4 TYR C 363 THR C 368 0
SHEET 2 O 4 ALA C 377 LEU C 382 -1 O CYS C 379 N ILE C 366
SHEET 3 O 4 VAL C 419 MET C 424 -1 O MET C 421 N PHE C 380
SHEET 4 O 4 ALA C 408 THR C 410 -1 N PHE C 409 O VAL C 420
SHEET 1 P 2 LEU D 14 ASP D 15 0
SHEET 2 P 2 ALA D 20 LYS D 21 -1 O ALA D 20 N ASP D 15
SHEET 1 Q 4 VAL D 119 THR D 123 0
SHEET 2 Q 4 GLY D 285 TRP D 289 -1 O GLY D 285 N THR D 123
SHEET 3 Q 4 VAL D 267 SER D 273 -1 N ALA D 272 O TRP D 286
SHEET 4 Q 4 MET D 240 ASP D 243 1 N MET D 240 O LYS D 268
SHEET 1 R 3 GLU D 176 GLU D 179 0
SHEET 2 R 3 ASN D 156 CYS D 159 1 N LEU D 157 O ARG D 178
SHEET 3 R 3 THR D 202 VAL D 206 1 O ILE D 203 N ASN D 156
SHEET 1 S 2 PHE D 301 TYR D 305 0
SHEET 2 S 2 GLY D 308 THR D 312 -1 O GLY D 308 N TYR D 305
SHEET 1 T 4 TYR D 363 THR D 368 0
SHEET 2 T 4 ALA D 377 LEU D 382 -1 O LYS D 381 N GLU D 364
SHEET 3 T 4 VAL D 419 MET D 424 -1 O ILE D 423 N VAL D 378
SHEET 4 T 4 ALA D 408 THR D 410 -1 N PHE D 409 O VAL D 420
SHEET 1 U 2 LEU E 14 ASP E 15 0
SHEET 2 U 2 ALA E 20 LYS E 21 -1 O ALA E 20 N ASP E 15
SHEET 1 V 4 GLY E 120 THR E 123 0
SHEET 2 V 4 GLY E 285 TRP E 289 -1 O GLY E 285 N THR E 123
SHEET 3 V 4 VAL E 267 SER E 273 -1 N ILE E 270 O ILE E 288
SHEET 4 V 4 MET E 240 ASP E 243 1 N MET E 240 O LYS E 268
SHEET 1 W 3 GLU E 176 GLU E 179 0
SHEET 2 W 3 ASN E 156 CYS E 159 1 N LEU E 157 O ARG E 178
SHEET 3 W 3 THR E 202 VAL E 206 1 O ILE E 203 N ASN E 156
SHEET 1 X 2 PHE E 301 TYR E 305 0
SHEET 2 X 2 GLY E 308 THR E 312 -1 O THR E 312 N PHE E 301
SHEET 1 Y 4 TYR E 363 THR E 368 0
SHEET 2 Y 4 ALA E 377 LEU E 382 -1 O LYS E 381 N GLU E 364
SHEET 3 Y 4 VAL E 419 MET E 424 -1 O MET E 421 N PHE E 380
SHEET 4 Y 4 ALA E 408 THR E 410 -1 N PHE E 409 O VAL E 420
SHEET 1 Z 2 LEU F 14 ASP F 15 0
SHEET 2 Z 2 ALA F 20 LYS F 21 -1 O ALA F 20 N ASP F 15
SHEET 1 AA 4 GLY F 120 THR F 123 0
SHEET 2 AA 4 GLY F 285 TRP F 289 -1 O GLY F 285 N THR F 123
SHEET 3 AA 4 VAL F 267 SER F 273 -1 N ALA F 272 O TRP F 286
SHEET 4 AA 4 MET F 240 ASP F 243 1 N MET F 240 O LYS F 268
SHEET 1 AB 3 GLU F 176 GLU F 179 0
SHEET 2 AB 3 ASN F 156 CYS F 159 1 N LEU F 157 O ARG F 178
SHEET 3 AB 3 THR F 202 VAL F 206 1 O ILE F 203 N ASN F 156
SHEET 1 AC 2 PHE F 301 TYR F 305 0
SHEET 2 AC 2 GLY F 308 THR F 312 -1 O THR F 312 N PHE F 301
SHEET 1 AD 4 TYR F 363 THR F 368 0
SHEET 2 AD 4 ALA F 377 LEU F 382 -1 O CYS F 379 N ILE F 366
SHEET 3 AD 4 VAL F 419 MET F 424 -1 O ILE F 423 N VAL F 378
SHEET 4 AD 4 ALA F 408 THR F 410 -1 N PHE F 409 O VAL F 420
SSBOND 1 CYS A 130 CYS A 165 1555 1555 2.86
SSBOND 2 CYS B 130 CYS B 165 1555 1555 3.00
SSBOND 3 CYS E 130 CYS E 165 1555 1555 2.79
SITE 1 AC1 10 GLY A 125 SER A 126 SER A 127 SER A 273
SITE 2 AC1 10 HIS A 275 LYS A 276 HOH D1316 HOH D1437
SITE 3 AC1 10 PHE F 317 SER F 318
SITE 1 AC2 11 PHE A 317 SER A 318 HOH D 813 HOH D1058
SITE 2 AC2 11 HOH D1193 HOH D1288 SER F 126 SER F 127
SITE 3 AC2 11 SER F 273 HIS F 275 LYS F 276
SITE 1 AC3 10 GLY D 125 SER D 126 SER D 127 SER D 273
SITE 2 AC3 10 HIS D 275 LYS D 276 HOH D1352 HOH D1396
SITE 3 AC3 10 PHE E 317 SER E 318
SITE 1 AC4 9 SER B 126 SER B 127 SER B 273 HIS B 275
SITE 2 AC4 9 LYS B 276 PHE C 317 SER C 318 HOH D1002
SITE 3 AC4 9 HOH D1098
SITE 1 AC5 9 PHE D 317 SER D 318 HOH D1256 GLY E 125
SITE 2 AC5 9 SER E 126 SER E 127 SER E 273 HIS E 275
SITE 3 AC5 9 LYS E 276
SITE 1 AC6 9 PHE B 317 SER B 318 GLY C 125 SER C 126
SITE 2 AC6 9 SER C 127 SER C 273 HIS C 275 LYS C 276
SITE 3 AC6 9 HOH D1169
CRYST1 115.564 115.564 206.561 90.00 90.00 120.00 P 32 18
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 0.008653 0.004996 0.000000 0.00000
SCALE2 0.000000 0.009992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END