HEADER LYASE 23-JAN-09 3FZ6
TITLE CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE 2 COLI: COMPLEX WITH XENON
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, PMP FORM, XENON, 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 3FZ6 1 VERSN
REVDAT 1 03-FEB-09 3FZ6 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: COMPLEX WITH XENON
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.82 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) : 2.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 75035
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3768
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) : 2.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4696
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 261
REMARK 3 BIN FREE R VALUE : 0.3570
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 : 102
REMARK 3 SOLVENT ATOMS : 363
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) : 16.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
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): 0.328
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.219
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.017
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 22552 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 30590 ; 1.646 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2751 ; 6.167 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1097 ;34.944 ;23.956
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3723 ;18.873 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;19.254 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3190 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17551 ; 0.007 ; 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): 13687 ; 1.322 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21985 ; 5.347 ;20.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8865 ;10.736 ;20.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8601 ; 4.908 ; 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): 3613 ; 0.260 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 B (A): 3613 ; 0.240 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 C (A): 3613 ; 0.260 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 D (A): 3613 ; 0.250 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 E (A): 3613 ; 0.390 ; 5.000
REMARK 3 TIGHT POSITIONAL 1 F (A): 3613 ; 0.230 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 3613 ; 3.320 ;10.000
REMARK 3 TIGHT THERMAL 1 B (A**2): 3613 ; 3.290 ;10.000
REMARK 3 TIGHT THERMAL 1 C (A**2): 3613 ; 3.660 ;10.000
REMARK 3 TIGHT THERMAL 1 D (A**2): 3613 ; 3.510 ;10.000
REMARK 3 TIGHT THERMAL 1 E (A**2): 3613 ; 3.880 ;10.000
REMARK 3 TIGHT THERMAL 1 F (A**2): 3613 ; 3.110 ;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 501
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3926 -17.8234 -5.6146
REMARK 3 T TENSOR
REMARK 3 T11: 0.0270 T22: 0.0288
REMARK 3 T33: 0.0582 T12: 0.0200
REMARK 3 T13: -0.0209 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.3549 L22: 0.6745
REMARK 3 L33: 0.5172 L12: -0.0981
REMARK 3 L13: -0.1478 L23: 0.2346
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: 0.0123 S13: -0.0163
REMARK 3 S21: -0.0294 S22: 0.0717 S23: -0.1365
REMARK 3 S31: 0.0590 S32: 0.0924 S33: -0.0946
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 501
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5431 -29.7796 12.6742
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.0172
REMARK 3 T33: 0.0319 T12: 0.0186
REMARK 3 T13: -0.0495 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.5348 L22: 0.3001
REMARK 3 L33: 0.6637 L12: -0.0138
REMARK 3 L13: 0.1612 L23: -0.0890
REMARK 3 S TENSOR
REMARK 3 S11: 0.0570 S12: -0.0676 S13: -0.0945
REMARK 3 S21: 0.0889 S22: 0.0101 S23: -0.0414
REMARK 3 S31: 0.1663 S32: 0.0470 S33: -0.0670
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 501
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8134 -14.6972 -12.5202
REMARK 3 T TENSOR
REMARK 3 T11: 0.0060 T22: 0.0231
REMARK 3 T33: 0.0024 T12: -0.0083
REMARK 3 T13: 0.0023 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.2867 L22: 0.4932
REMARK 3 L33: 0.5692 L12: -0.0324
REMARK 3 L13: 0.0881 L23: 0.1936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: -0.0491 S13: -0.0063
REMARK 3 S21: 0.0398 S22: -0.0385 S23: 0.0339
REMARK 3 S31: 0.0259 S32: -0.1035 S33: 0.0126
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 501
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5347 4.5589 8.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.0156 T22: 0.0697
REMARK 3 T33: 0.0227 T12: -0.0185
REMARK 3 T13: 0.0183 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.6703 L22: 0.5323
REMARK 3 L33: 0.4363 L12: 0.2928
REMARK 3 L13: -0.2065 L23: 0.1481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0615 S12: -0.0253 S13: 0.0852
REMARK 3 S21: 0.0883 S22: -0.0763 S23: 0.1065
REMARK 3 S31: 0.0299 S32: -0.1470 S33: 0.0148
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 501
REMARK 3 RESIDUE RANGE : E 467 E 831
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3785 31.7658 -7.7922
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0027
REMARK 3 T33: 0.0006 T12: -0.0027
REMARK 3 T13: 0.0006 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.4961 L22: 0.4561
REMARK 3 L33: 0.4409 L12: 0.1848
REMARK 3 L13: 0.0481 L23: -0.0594
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.0325 S13: 0.0155
REMARK 3 S21: -0.0431 S22: 0.0149 S23: 0.0022
REMARK 3 S31: -0.0357 S32: 0.0175 S33: -0.0028
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 501
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8084 25.2567 14.6376
REMARK 3 T TENSOR
REMARK 3 T11: 0.0072 T22: 0.0182
REMARK 3 T33: 0.0165 T12: -0.0086
REMARK 3 T13: 0.0054 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.3799 L22: 0.5897
REMARK 3 L33: 0.5112 L12: -0.0642
REMARK 3 L13: 0.1442 L23: 0.1589
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: -0.0244 S13: 0.0018
REMARK 3 S21: -0.0162 S22: 0.0585 S23: -0.0951
REMARK 3 S31: -0.0520 S32: 0.0738 S33: -0.0443
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 3FZ6 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 RCSB051220.
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) : 294
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-20
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
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 : 76681
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
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: XENON DERIVATIVE WAS PRODUCED BY APPLYING 9 BAR XENON GAS
REMARK 200 PRESSURE TO THE CRYSTAL MOUNTED IN THE QUARTZ X-RAY CAPILLARY.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
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 138.94867
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 69.47433
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: 47200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -241.0 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 B 352 OE1 GLU B 435 2.03
REMARK 500 ND1 HIS C 465 O HOH E 799 2.04
REMARK 500 NE ARG D 402 O HOH E 757 2.10
REMARK 500 ND1 HIS E 465 O HOH E 804 2.11
REMARK 500 O ASN A 59 NH2 ARG A 426 2.12
REMARK 500 OH TYR F 352 OE1 GLU F 435 2.14
REMARK 500 O THR B 368 NH2 ARG B 370 2.18
REMARK 500 OE2 GLU C 292 O HOH E 534 2.19
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. = 14.8 DEGREES
REMARK 500 ARG B 422 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP C 40 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU E 157 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 LEU E 436 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG F 290 NE - CZ - NH2 ANGL. DEV. = -3.3 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 GLU A 28 42.91 72.79
REMARK 500 ALA A 56 -4.07 67.13
REMARK 500 PRO A 161 78.71 -65.03
REMARK 500 LEU A 250 -63.17 -123.13
REMARK 500 ALA A 255 57.57 -154.89
REMARK 500 ASP A 261 -144.46 -106.16
REMARK 500 LYS A 276 -114.48 -96.75
REMARK 500 LEU A 279 -1.53 82.78
REMARK 500 PHE A 317 -97.75 -124.43
REMARK 500 GLN A 459 21.33 -146.32
REMARK 500 SER B 11 43.94 -101.53
REMARK 500 GLU B 28 14.47 92.93
REMARK 500 GLN B 186 85.78 -158.22
REMARK 500 ALA B 245 -50.78 -26.18
REMARK 500 ALA B 255 62.41 -152.17
REMARK 500 TRP B 260 -12.23 -140.13
REMARK 500 ASP B 261 -150.79 -111.54
REMARK 500 LYS B 276 -123.87 -102.35
REMARK 500 LEU B 282 135.95 -38.89
REMARK 500 PHE B 317 -98.59 -112.15
REMARK 500 THR B 416 -8.86 -55.18
REMARK 500 GLN B 459 28.66 -153.72
REMARK 500 PHE B 463 118.29 -34.54
REMARK 500 GLU C 28 46.95 -81.60
REMARK 500 TYR C 90 64.16 -111.17
REMARK 500 HIS C 109 34.63 72.36
REMARK 500 PRO C 161 69.46 -68.69
REMARK 500 GLN C 186 69.42 -155.44
REMARK 500 LEU C 250 -65.01 -102.35
REMARK 500 ALA C 255 57.53 -148.00
REMARK 500 ASP C 261 -149.26 -113.37
REMARK 500 LYS C 276 -108.77 -94.31
REMARK 500 PHE C 317 -109.64 -111.40
REMARK 500 ARG C 319 145.93 172.57
REMARK 500 PRO C 376 84.56 -67.54
REMARK 500 GLN C 459 23.65 -145.41
REMARK 500 ALA D 56 -7.42 69.32
REMARK 500 LYS D 154 56.95 -119.03
REMARK 500 ALA D 255 55.29 -151.43
REMARK 500 TRP D 260 -12.73 -151.37
REMARK 500 ASP D 261 -153.60 -104.89
REMARK 500 LYS D 276 -122.36 -100.55
REMARK 500 LEU D 282 129.79 -39.79
REMARK 500 ASP D 291 172.86 179.24
REMARK 500 PHE D 317 -98.67 -106.36
REMARK 500 ALA D 415 34.70 -98.58
REMARK 500 GLN D 459 32.36 -147.16
REMARK 500 LYS E 4 23.97 -74.81
REMARK 500 ALA E 56 -0.23 71.01
REMARK 500 ASP E 261 -148.57 -115.05
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 PMP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP F 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI
REMARK 900 RELATED ID: 3FZ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM
REMARK 900 ESCHERICHIA COLI: REDUCED SCHIFF BASE WITH PLP
DBREF 3FZ6 A 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ6 B 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ6 C 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ6 D 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ6 E 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 3FZ6 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 PMP A 500 16
HET XE A 501 1
HET PMP B 500 16
HET XE B 501 1
HET PMP C 500 16
HET XE C 501 1
HET PMP D 500 16
HET XE D 501 1
HET PMP E 500 16
HET XE E 501 1
HET PMP F 500 16
HET XE F 501 1
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETNAM XE XENON
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL 7 PMP 6(C8 H13 N2 O5 P)
FORMUL 8 XE 6(XE)
FORMUL 19 HOH *363(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 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 TYR B 51 1 14
HELIX 17 17 ASP B 69 ILE B 80 1 12
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 ARG B 402 1 12
HELIX 30 30 GLY B 412 THR B 416 5 5
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 ILE C 26 LYS C 30 5 5
HELIX 34 34 ARG C 38 TYR C 51 1 14
HELIX 35 35 ASP C 69 SER C 79 1 11
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 CYS C 198 1 9
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 GLY C 412 ASP C 417 5 6
HELIX 48 48 GLU C 430 HIS C 451 1 22
HELIX 49 49 PRO C 452 GLN C 455 5 4
HELIX 50 50 ARG D 38 LEU D 50 1 13
HELIX 51 51 TYR D 51 ASP D 53 5 3
HELIX 52 52 ASP D 69 SER D 79 1 11
HELIX 53 53 TYR D 90 TRP D 108 1 19
HELIX 54 54 GLY D 125 ALA D 148 1 24
HELIX 55 55 ILE D 164 TRP D 173 1 10
HELIX 56 56 ASP D 190 ALA D 197 1 8
HELIX 57 57 PHE D 219 GLY D 235 1 17
HELIX 58 58 SER D 246 PHE D 249 5 4
HELIX 59 59 LEU D 250 ALA D 255 1 6
HELIX 60 60 PRO D 296 VAL D 300 5 5
HELIX 61 61 ALA D 321 LYS D 359 1 39
HELIX 62 62 THR D 391 ARG D 402 1 12
HELIX 63 63 GLY D 412 THR D 416 5 5
HELIX 64 64 GLU D 430 HIS D 451 1 22
HELIX 65 65 PRO D 452 GLN D 455 5 4
HELIX 66 66 VAL E 6 ARG E 10 5 5
HELIX 67 67 ILE E 26 LYS E 30 5 5
HELIX 68 68 ARG E 38 LEU E 50 1 13
HELIX 69 69 TYR E 51 ASP E 53 5 3
HELIX 70 70 ASP E 69 SER E 79 1 11
HELIX 71 71 TYR E 90 TRP E 108 1 19
HELIX 72 72 GLY E 125 ALA E 148 1 24
HELIX 73 73 GLN E 163 TRP E 173 1 11
HELIX 74 74 ASP E 190 CYS E 198 1 9
HELIX 75 75 PHE E 219 GLY E 235 1 17
HELIX 76 76 SER E 246 PHE E 249 5 4
HELIX 77 77 LEU E 250 ALA E 255 1 6
HELIX 78 78 ASP E 291 LEU E 295 5 5
HELIX 79 79 PRO E 296 VAL E 300 5 5
HELIX 80 80 ALA E 321 ALA E 358 1 38
HELIX 81 81 THR E 391 ARG E 402 1 12
HELIX 82 82 GLY E 412 THR E 416 5 5
HELIX 83 83 GLU E 430 HIS E 451 1 22
HELIX 84 84 PRO E 452 GLN E 455 5 4
HELIX 85 85 ARG F 38 TYR F 51 1 14
HELIX 86 86 ASP F 69 SER F 79 1 11
HELIX 87 87 TYR F 90 TRP F 108 1 19
HELIX 88 88 GLY F 125 ALA F 148 1 24
HELIX 89 89 GLN F 163 ASP F 174 1 12
HELIX 90 90 ASP F 190 ALA F 197 1 8
HELIX 91 91 PHE F 219 GLY F 235 1 17
HELIX 92 92 SER F 246 PHE F 249 5 4
HELIX 93 93 LEU F 250 ALA F 255 1 6
HELIX 94 94 ASP F 291 LEU F 295 5 5
HELIX 95 95 PRO F 296 VAL F 300 5 5
HELIX 96 96 ALA F 321 LYS F 359 1 39
HELIX 97 97 THR F 391 ARG F 402 1 12
HELIX 98 98 GLY F 412 THR F 416 5 5
HELIX 99 99 GLU F 430 HIS F 451 1 22
HELIX 100 100 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 LYS A 381 N GLU A 364
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 ILE C 270 O ILE C 288
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 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 VAL D 303 0
SHEET 2 S 2 ILE D 310 THR D 312 -1 O ILE D 310 N VAL D 303
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 13 ASP E 15 0
SHEET 2 U 2 ALA E 20 SER E 22 -1 O SER E 22 N LEU E 13
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 ALA E 272 O TRP E 286
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 ILE E 423 N VAL E 378
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
SITE 1 AC1 15 SER A 126 SER A 127 GLN A 163 GLY A 210
SITE 2 AC1 15 THR A 212 ASP A 243 ALA A 245 SER A 273
SITE 3 AC1 15 HIS A 275 LYS A 276 HIS A 465 THR A 466
SITE 4 AC1 15 PHE B 317 SER B 318 HOH E 519
SITE 1 AC2 1 GLY A 120
SITE 1 AC3 14 PHE A 317 SER A 318 SER B 126 SER B 127
SITE 2 AC3 14 GLN B 163 THR B 208 THR B 212 ASP B 243
SITE 3 AC3 14 ALA B 245 SER B 273 HIS B 275 LYS B 276
SITE 4 AC3 14 HIS B 465 THR B 466
SITE 1 AC4 17 GLY C 125 SER C 126 SER C 127 GLN C 163
SITE 2 AC4 17 CYS C 165 THR C 208 THR C 212 ASP C 243
SITE 3 AC4 17 ALA C 245 SER C 273 HIS C 275 LYS C 276
SITE 4 AC4 17 HIS C 465 THR C 466 PHE D 317 SER D 318
SITE 5 AC4 17 HOH E 515
SITE 1 AC5 14 PHE C 317 SER C 318 SER D 126 SER D 127
SITE 2 AC5 14 GLN D 163 THR D 208 THR D 212 ASP D 243
SITE 3 AC5 14 ALA D 245 SER D 273 HIS D 275 LYS D 276
SITE 4 AC5 14 HIS D 465 THR D 466
SITE 1 AC6 1 GLY D 120
SITE 1 AC7 14 SER E 126 SER E 127 GLN E 163 THR E 208
SITE 2 AC7 14 THR E 212 ASP E 243 ALA E 245 SER E 273
SITE 3 AC7 14 HIS E 275 LYS E 276 HIS E 465 THR E 466
SITE 4 AC7 14 PHE F 317 SER F 318
SITE 1 AC8 15 PHE E 317 SER E 318 HOH E 467 GLY F 125
SITE 2 AC8 15 SER F 126 SER F 127 GLN F 163 THR F 212
SITE 3 AC8 15 ASP F 243 ALA F 245 SER F 273 HIS F 275
SITE 4 AC8 15 LYS F 276 HIS F 465 THR F 466
CRYST1 116.729 116.729 208.423 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 0.008567 0.004946 0.000000 0.00000
SCALE2 0.000000 0.009892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004798 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
