HEADER LYASE 23-JAN-09 3FZ8
TITLE CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE 2 COLI: REDUCED SCHIFF BASE WITH PLP
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, REDUCED FORM, DECARBOXYLASE, LYASE,
KEYWDS 2 MEMBRANE, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
REVDAT 2 13-JUL-11 3FZ8 1 VERSN
REVDAT 1 03-FEB-09 3FZ8 0
JRNL AUTH V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA
JRNL TITL CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
JRNL TITL 2 ESCHERICHIA COLI: REDUCED SCHIFF BASE WITH PLP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 60684
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3072
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4273
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21835
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 90
REMARK 3 SOLVENT ATOMS : 60
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) : 12.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.455
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.327
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.481
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22489 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30497 ; 1.496 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2741 ; 6.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1092 ;35.170 ;23.974
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3718 ;19.143 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;17.463 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3185 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17470 ; 0.006 ; 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): 13669 ; 1.002 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21950 ; 4.235 ;20.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8820 ; 8.743 ;20.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8547 ; 3.288 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A -9999 A 9999 1
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 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3631 ; 0.290 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 B (A): 3631 ; 0.270 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 C (A): 3631 ; 0.290 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 D (A): 3631 ; 0.280 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 E (A): 3631 ; 0.400 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 F (A): 3631 ; 0.290 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 3631 ; 3.210 ;10.000
REMARK 3 TIGHT THERMAL 1 B (A**2): 3631 ; 2.960 ;10.000
REMARK 3 TIGHT THERMAL 1 C (A**2): 3631 ; 3.190 ;10.000
REMARK 3 TIGHT THERMAL 1 D (A**2): 3631 ; 3.050 ;10.000
REMARK 3 TIGHT THERMAL 1 E (A**2): 3631 ; 3.450 ;10.000
REMARK 3 TIGHT THERMAL 1 F (A**2): 3631 ; 2.940 ;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 : A 12 A 466
REMARK 3 RESIDUE RANGE : A 500 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5409 -17.9361 -5.6904
REMARK 3 T TENSOR
REMARK 3 T11: 0.0443 T22: 0.0331
REMARK 3 T33: 0.0554 T12: 0.0301
REMARK 3 T13: -0.0323 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 0.4650 L22: 0.8414
REMARK 3 L33: 0.5724 L12: -0.0296
REMARK 3 L13: -0.1297 L23: 0.1955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: 0.0117 S13: -0.0198
REMARK 3 S21: -0.0401 S22: 0.0714 S23: -0.1275
REMARK 3 S31: 0.0805 S32: 0.0995 S33: -0.0895
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 : B 4 B 466
REMARK 3 RESIDUE RANGE : B 500 B 500
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6378 -29.8846 12.7026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.0159
REMARK 3 T33: 0.0326 T12: 0.0181
REMARK 3 T13: -0.0586 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.7300 L22: 0.4762
REMARK 3 L33: 0.6479 L12: -0.0595
REMARK 3 L13: 0.2061 L23: -0.1969
REMARK 3 S TENSOR
REMARK 3 S11: 0.0553 S12: -0.0632 S13: -0.0844
REMARK 3 S21: 0.1199 S22: -0.0029 S23: -0.0595
REMARK 3 S31: 0.1412 S32: 0.0585 S33: -0.0524
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 12 C 466
REMARK 3 RESIDUE RANGE : C 500 C 500
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8784 -14.7485 -12.6442
REMARK 3 T TENSOR
REMARK 3 T11: 0.0126 T22: 0.0240
REMARK 3 T33: 0.0035 T12: -0.0085
REMARK 3 T13: 0.0027 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.4416 L22: 0.6659
REMARK 3 L33: 0.7123 L12: -0.1313
REMARK 3 L13: 0.2872 L23: 0.1088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0583 S13: -0.0112
REMARK 3 S21: 0.0314 S22: 0.0186 S23: 0.0433
REMARK 3 S31: 0.0128 S32: -0.1064 S33: -0.0120
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 : D 12 D 466
REMARK 3 RESIDUE RANGE : D 500 D 500
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6473 4.4990 8.0410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0148 T22: 0.0592
REMARK 3 T33: 0.0238 T12: -0.0082
REMARK 3 T13: 0.0172 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.6531 L22: 0.5005
REMARK 3 L33: 0.5099 L12: 0.2601
REMARK 3 L13: -0.2893 L23: 0.1482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.0478 S13: 0.0776
REMARK 3 S21: 0.0781 S22: -0.0532 S23: 0.1060
REMARK 3 S31: 0.0280 S32: -0.1003 S33: 0.0094
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 466
REMARK 3 RESIDUE RANGE : E 500 E 500
REMARK 3 RESIDUE RANGE : E 467 E 527
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3713 31.9418 -7.8638
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: 0.0087
REMARK 3 T33: 0.0020 T12: -0.0054
REMARK 3 T13: -0.0039 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.5997 L22: 0.5036
REMARK 3 L33: 0.5092 L12: 0.1863
REMARK 3 L13: 0.0422 L23: -0.0262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: 0.0180 S13: 0.0100
REMARK 3 S21: -0.0231 S22: -0.0315 S23: 0.0278
REMARK 3 S31: -0.0723 S32: 0.0544 S33: 0.0012
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 : F 12 F 466
REMARK 3 RESIDUE RANGE : F 500 F 500
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8959 25.2825 14.6224
REMARK 3 T TENSOR
REMARK 3 T11: 0.0130 T22: 0.0114
REMARK 3 T33: 0.0132 T12: -0.0113
REMARK 3 T13: 0.0069 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.3234 L22: 0.7025
REMARK 3 L33: 0.6279 L12: -0.1150
REMARK 3 L13: 0.1493 L23: 0.1692
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.0071 S13: 0.0157
REMARK 3 S21: -0.0064 S22: 0.0370 S23: -0.0847
REMARK 3 S31: -0.0402 S32: 0.0520 S33: -0.0440
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 3FZ8 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 RCSB ID CODE IS RCSB051222.
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 : 63606
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
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 (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
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 -0.499991 -0.866040 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866011 -0.500009 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.05733
REMARK 290 SMTRY1 3 -0.500009 0.866040 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866011 -0.499991 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.52867
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: 47410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -217.3 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 MET B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 3
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 LYS C 3
REMARK 465 LYS C 4
REMARK 465 GLN C 5
REMARK 465 VAL C 6
REMARK 465 THR C 7
REMARK 465 ASP C 8
REMARK 465 LEU C 9
REMARK 465 ARG C 10
REMARK 465 SER C 11
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 MET E 1
REMARK 465 ASP E 2
REMARK 465 MET F 1
REMARK 465 ASP F 2
REMARK 465 LYS F 3
REMARK 465 LYS F 4
REMARK 465 GLN F 5
REMARK 465 VAL F 6
REMARK 465 THR F 7
REMARK 465 ASP F 8
REMARK 465 LEU F 9
REMARK 465 ARG F 10
REMARK 465 SER F 11
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 D 352 OE1 GLU D 435 2.14
REMARK 500 O ALA A 27 N SER A 29 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS C 276 CE LYS C 276 NZ -0.175
REMARK 500 CYS E 367 CB CYS E 367 SG -0.101
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 LYS C 276 CD - CE - NZ ANGL. DEV. = 19.9 DEGREES
REMARK 500 LEU E 157 CA - CB - CG ANGL. DEV. = 19.0 DEGREES
REMARK 500 LEU E 436 CA - CB - CG ANGL. DEV. = 15.3 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 ALA A 27 -113.69 -73.66
REMARK 500 GLU A 28 66.29 -46.12
REMARK 500 SER A 29 37.49 -150.19
REMARK 500 ALA A 56 -13.71 74.53
REMARK 500 PRO A 161 75.17 -58.73
REMARK 500 ARG A 178 72.26 -107.47
REMARK 500 GLN A 186 87.68 -156.23
REMARK 500 MET A 194 -71.11 -51.83
REMARK 500 ASP A 199 -168.38 -164.18
REMARK 500 LEU A 250 -59.12 -126.58
REMARK 500 ALA A 255 72.30 -161.67
REMARK 500 ASP A 261 -152.49 -108.21
REMARK 500 PHE A 262 -8.42 -59.09
REMARK 500 LYS A 276 -113.57 -98.84
REMARK 500 PHE A 317 -96.44 -113.64
REMARK 500 PRO A 376 76.63 -69.40
REMARK 500 GLN A 459 35.79 -157.72
REMARK 500 SER B 11 50.17 -101.59
REMARK 500 GLU B 28 65.61 20.71
REMARK 500 ALA B 56 -9.23 72.78
REMARK 500 TYR B 90 69.35 -116.57
REMARK 500 ALA B 112 125.36 -38.42
REMARK 500 PRO B 161 83.12 -65.15
REMARK 500 GLN B 186 66.63 -178.92
REMARK 500 ALA B 244 37.40 -87.89
REMARK 500 LEU B 250 -72.07 -109.80
REMARK 500 TRP B 260 -18.22 -148.55
REMARK 500 ASP B 261 -146.96 -97.67
REMARK 500 SER B 269 141.89 -174.51
REMARK 500 LYS B 276 -111.90 -114.30
REMARK 500 LEU B 282 135.75 -36.94
REMARK 500 PHE B 317 -95.30 -117.28
REMARK 500 ARG B 319 161.86 175.46
REMARK 500 ALA B 434 -51.14 -29.34
REMARK 500 GLN B 459 23.29 -151.10
REMARK 500 GLU C 28 36.04 39.94
REMARK 500 ALA C 56 -4.35 73.92
REMARK 500 TYR C 90 67.08 -114.19
REMARK 500 ALA C 112 124.61 -38.82
REMARK 500 PRO C 161 66.54 -68.30
REMARK 500 ALA C 244 37.00 -94.56
REMARK 500 LEU C 250 -68.46 -123.06
REMARK 500 ASP C 261 -150.23 -109.13
REMARK 500 PHE C 262 6.01 -65.92
REMARK 500 LYS C 276 -114.71 -92.62
REMARK 500 LEU C 282 128.62 -37.98
REMARK 500 PHE C 317 -99.39 -119.55
REMARK 500 GLN C 459 25.56 -145.57
REMARK 500 ALA D 27 -173.39 -69.03
REMARK 500 GLU D 28 46.27 22.14
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
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 GLU A 49 23.1 L L OUTSIDE RANGE
REMARK 500 GLU C 49 23.2 L L OUTSIDE RANGE
REMARK 500 ASP C 257 22.6 L L OUTSIDE RANGE
REMARK 500 GLU D 49 24.9 L L OUTSIDE RANGE
REMARK 500 GLU F 28 23.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 486 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH E 519 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH E 525 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH E 526 DISTANCE = 6.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLR F 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI: COMPLEX WITH XENON
REMARK 900 RELATED ID: 3FZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI
DBREF 3FZ8 A 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ8 B 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ8 C 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ8 D 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ8 E 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ8 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 PLR A 500 15
HET PLR B 500 15
HET PLR C 500 15
HET PLR D 500 15
HET PLR E 500 15
HET PLR F 500 15
HETNAM PLR (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN
HETNAM 2 PLR PHOSPHATE
HETSYN PLR 4'-DEOXYPYRIDOXINE PHOSPHATE
FORMUL 7 PLR 6(C8 H12 N O5 P)
FORMUL 13 HOH *60(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 ALA A 197 1 8
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 LYS A 359 1 39
HELIX 13 13 THR A 391 ARG A 402 1 12
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 GLU B 49 1 12
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 TRP B 173 1 11
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 ALA B 358 1 38
HELIX 28 28 LYS B 359 GLY B 361 5 3
HELIX 29 29 THR B 391 LEU B 401 1 11
HELIX 30 30 GLU B 414 ASP B 417 5 4
HELIX 31 31 GLU B 430 HIS B 451 1 22
HELIX 32 32 PRO B 452 GLN B 455 5 4
HELIX 33 33 ARG C 38 TYR C 51 1 14
HELIX 34 34 ASP C 69 SER C 79 1 11
HELIX 35 35 ILE C 80 LYS C 82 5 3
HELIX 36 36 TYR C 90 TRP C 108 1 19
HELIX 37 37 GLY C 125 ALA C 148 1 24
HELIX 38 38 ILE C 164 TRP C 173 1 10
HELIX 39 39 ASP C 190 ALA C 197 1 8
HELIX 40 40 PHE C 219 GLY C 235 1 17
HELIX 41 41 SER C 246 PHE C 249 5 4
HELIX 42 42 LEU C 250 ALA C 255 1 6
HELIX 43 43 ASP C 291 LEU C 295 5 5
HELIX 44 44 PRO C 296 VAL C 300 5 5
HELIX 45 45 ALA C 321 ALA C 358 1 38
HELIX 46 46 THR C 391 LEU C 401 1 11
HELIX 47 47 GLU C 430 HIS C 451 1 22
HELIX 48 48 PRO C 452 GLN C 455 5 4
HELIX 49 49 ARG D 38 TYR D 51 1 14
HELIX 50 50 ASP D 69 SER D 79 1 11
HELIX 51 51 TYR D 90 TRP D 108 1 19
HELIX 52 52 GLY D 125 GLY D 149 1 25
HELIX 53 53 ILE D 164 ASP D 174 1 11
HELIX 54 54 ASP D 190 ALA D 197 1 8
HELIX 55 55 PHE D 219 GLY D 235 1 17
HELIX 56 56 SER D 246 PHE D 249 5 4
HELIX 57 57 LEU D 250 ALA D 255 1 6
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 LEU E 50 1 13
HELIX 63 63 TYR E 51 ASP E 53 5 3
HELIX 64 64 ASP E 69 ILE E 80 1 12
HELIX 65 65 TYR E 90 TRP E 108 1 19
HELIX 66 66 GLY E 125 ALA E 148 1 24
HELIX 67 67 GLN E 163 TRP E 173 1 11
HELIX 68 68 ASP E 190 ALA E 197 1 8
HELIX 69 69 PHE E 219 GLY E 235 1 17
HELIX 70 70 SER E 246 PHE E 249 5 4
HELIX 71 71 LEU E 250 ALA E 255 1 6
HELIX 72 72 ASP E 291 LEU E 295 5 5
HELIX 73 73 PRO E 296 VAL E 300 5 5
HELIX 74 74 ALA E 321 ALA E 358 1 38
HELIX 75 75 THR E 391 ARG E 402 1 12
HELIX 76 76 GLY E 412 THR E 416 5 5
HELIX 77 77 GLU E 430 HIS E 451 1 22
HELIX 78 78 PRO E 452 GLN E 455 5 4
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 CYS F 198 1 9
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 LEU F 401 1 11
HELIX 93 93 GLU F 430 HIS F 451 1 22
HELIX 94 94 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 GLY A 120 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 CYS A 379 N ILE A 366
SHEET 3 E 4 VAL A 419 MET A 424 -1 O ILE A 423 N VAL A 378
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 TRP B 289 N VAL B 119
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 ILE B 242 O SER B 271
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 VAL C 119 THR C 123 0
SHEET 2 L 4 GLY C 285 TRP C 289 -1 O TRP C 289 N VAL C 119
SHEET 3 L 4 VAL C 267 SER C 273 -1 N ALA C 272 O TRP C 286
SHEET 4 L 4 MET C 240 ASP C 243 1 N MET C 240 O LYS C 268
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 LYS C 381 N GLU C 364
SHEET 3 O 4 VAL C 419 MET C 424 -1 O ILE C 423 N VAL C 378
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 GLY D 120 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 ILE D 270 O ILE D 288
SHEET 4 Q 4 MET D 240 ASP D 243 1 N ILE D 242 O SER D 269
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 VAL D 206 N VAL D 158
SHEET 1 S 2 PHE D 301 TYR D 305 0
SHEET 2 S 2 GLY D 308 THR D 312 -1 O THR D 312 N PHE D 301
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 4 VAL E 119 THR E 123 0
SHEET 2 U 4 GLY E 285 TRP E 289 -1 O GLY E 285 N THR E 123
SHEET 3 U 4 VAL E 267 SER E 273 -1 N ALA E 272 O TRP E 286
SHEET 4 U 4 MET E 240 ASP E 243 1 N MET E 240 O LYS E 268
SHEET 1 V 3 GLU E 176 GLU E 179 0
SHEET 2 V 3 ASN E 156 CYS E 159 1 N LEU E 157 O ARG E 178
SHEET 3 V 3 THR E 202 VAL E 206 1 O ILE E 203 N ASN E 156
SHEET 1 W 2 PHE E 301 TYR E 305 0
SHEET 2 W 2 GLY E 308 THR E 312 -1 O THR E 312 N PHE E 301
SHEET 1 X 4 TYR E 363 THR E 368 0
SHEET 2 X 4 ALA E 377 LEU E 382 -1 O LYS E 381 N GLU E 364
SHEET 3 X 4 VAL E 419 MET E 424 -1 O ILE E 423 N VAL E 378
SHEET 4 X 4 ALA E 408 THR E 410 -1 N PHE E 409 O VAL E 420
SHEET 1 Y 2 LEU F 14 ASP F 15 0
SHEET 2 Y 2 ALA F 20 LYS F 21 -1 O ALA F 20 N ASP F 15
SHEET 1 Z 4 GLY F 120 THR F 123 0
SHEET 2 Z 4 GLY F 285 TRP F 289 -1 O GLY F 285 N THR F 123
SHEET 3 Z 4 VAL F 267 SER F 273 -1 N ILE F 270 O ILE F 288
SHEET 4 Z 4 MET F 240 ASP F 243 1 N MET F 240 O LYS F 268
SHEET 1 AA 3 GLU F 176 GLU F 179 0
SHEET 2 AA 3 ASN F 156 CYS F 159 1 N LEU F 157 O ARG F 178
SHEET 3 AA 3 THR F 202 VAL F 206 1 O ILE F 203 N ASN F 156
SHEET 1 AB 2 PHE F 301 TYR F 305 0
SHEET 2 AB 2 GLY F 308 THR F 312 -1 O THR F 312 N PHE F 301
SHEET 1 AC 4 TYR F 363 CYS F 367 0
SHEET 2 AC 4 ALA F 377 LEU F 382 -1 O CYS F 379 N CYS F 367
SHEET 3 AC 4 VAL F 419 MET F 424 -1 O ILE F 423 N VAL F 378
SHEET 4 AC 4 ALA F 408 THR F 410 -1 N PHE F 409 O VAL F 420
LINK NZ LYS A 276 C4A PLR A 500 1555 1555 1.60
LINK NZ LYS B 276 C4A PLR B 500 1555 1555 1.50
LINK NZ LYS C 276 C4A PLR C 500 1555 1555 1.50
LINK NZ LYS D 276 C4A PLR D 500 1555 1555 1.54
LINK NZ LYS E 276 C4A PLR E 500 1555 1555 1.51
LINK NZ LYS F 276 C4A PLR F 500 1555 1555 1.54
SITE 1 AC1 15 SER A 126 SER A 127 GLN A 163 THR A 208
SITE 2 AC1 15 GLY A 210 THR A 212 ASP A 243 ALA A 245
SITE 3 AC1 15 SER A 273 HIS A 275 LYS A 276 HIS A 465
SITE 4 AC1 15 THR A 466 PHE B 317 SER B 318
SITE 1 AC2 14 PHE A 317 SER A 318 GLY B 125 SER B 126
SITE 2 AC2 14 SER B 127 GLN B 163 THR B 208 THR B 212
SITE 3 AC2 14 ASP B 243 ALA B 245 SER B 273 HIS B 275
SITE 4 AC2 14 LYS B 276 THR B 466
SITE 1 AC3 15 SER C 126 SER C 127 GLN C 163 THR C 208
SITE 2 AC3 15 GLY C 210 THR C 212 ASP C 243 ALA C 245
SITE 3 AC3 15 SER C 273 HIS C 275 LYS C 276 HIS C 465
SITE 4 AC3 15 THR C 466 PHE D 317 SER D 318
SITE 1 AC4 15 PHE C 317 SER C 318 GLY D 125 SER D 126
SITE 2 AC4 15 SER D 127 GLN D 163 THR D 208 THR D 212
SITE 3 AC4 15 ASP D 243 ALA D 245 SER D 273 HIS D 275
SITE 4 AC4 15 LYS D 276 HIS D 465 THR D 466
SITE 1 AC5 15 GLY E 125 SER E 126 SER E 127 GLN E 163
SITE 2 AC5 15 THR E 208 GLY E 210 THR E 212 ASP E 243
SITE 3 AC5 15 ALA E 245 SER E 273 HIS E 275 LYS E 276
SITE 4 AC5 15 THR E 466 PHE F 317 SER F 318
SITE 1 AC6 14 PHE E 317 SER E 318 GLY F 125 SER F 126
SITE 2 AC6 14 SER F 127 GLN F 163 GLY F 210 THR F 212
SITE 3 AC6 14 ASP F 243 ALA F 245 SER F 273 HIS F 275
SITE 4 AC6 14 LYS F 276 THR F 466
CRYST1 116.896 116.894 208.586 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 0.008555 0.004939 0.000000 0.00000
SCALE2 0.000000 0.009878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004794 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
