HEADER LYASE 25-MAR-09 3A12
TITLE CRYSTAL STRUCTURE OF TYPE III RUBISCO COMPLEXED WITH 2-CABP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 SYNONYM: RUBISCO;
COMPND 5 EC: 4.1.1.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS KODAKARAENSIS;
SOURCE 3 ORGANISM_COMMON: THERMOCOCCUS KODAKARAENSIS;
SOURCE 4 ORGANISM_TAXID: 69014;
SOURCE 5 STRAIN: KOD1;
SOURCE 6 GENE: RBCL, TK2290;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS RIBULOSE-1, 5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, LYASE,
KEYWDS 2 CARBON DIOXIDE FIXATION, MAGNESIUM, METAL-BINDING, MONOOXYGENASE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI
REVDAT 2 02-FEB-11 3A12 1 JRNL
REVDAT 1 07-APR-10 3A12 0
JRNL AUTH Y.NISHITANI,S.YOSHIDA,M.FUJIHASHI,K.KITAGAWA,T.DOI,H.ATOMI,
JRNL AUTH 2 T.IMANAKA,K.MIKI
JRNL TITL STRUCTURE-BASED CATALYTIC OPTIMIZATION OF A TYPE III RUBISCO
JRNL TITL 2 FROM A HYPERTHERMOPHILE
JRNL REF J.BIOL.CHEM. V. 285 39339 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20926376
JRNL DOI 10.1074/JBC.M110.147587
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 257731
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13630
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 18587
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 975
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 34125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 2306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.52000
REMARK 3 B22 (A**2) : -2.27000
REMARK 3 B33 (A**2) : -2.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.268
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.948
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 35219 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47835 ; 0.995 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4354 ; 5.230 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1607 ;29.821 ;23.491
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5588 ;14.192 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 220 ;19.538 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5065 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27118 ; 0.004 ; 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): 21648 ; 0.421 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34454 ; 0.822 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13571 ; 1.274 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13381 ; 2.142 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3A12 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB028677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 271962
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1GEH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 0.1M CACL2, 5% PEG6000,
REMARK 280 10% MPD, PH6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 86.64350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 123.18850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 86.64350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 123.18850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -382.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 173.28700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -384.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H, I, J, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH G 592 LIES ON A SPECIAL POSITION.
REMARK 375 HOH I 652 LIES ON A SPECIAL POSITION.
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 VAL A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 ASP A 6
REMARK 465 THR A 7
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 GLU B 3
REMARK 465 LYS B 4
REMARK 465 PHE B 5
REMARK 465 ASP B 6
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 GLU C 3
REMARK 465 LYS C 4
REMARK 465 PHE C 5
REMARK 465 ASP C 6
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 GLU D 3
REMARK 465 LYS D 4
REMARK 465 PHE D 5
REMARK 465 ASP D 6
REMARK 465 THR D 7
REMARK 465 ILE D 8
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 GLU E 3
REMARK 465 LYS E 4
REMARK 465 PHE E 5
REMARK 465 ASP E 6
REMARK 465 LYS E 426
REMARK 465 THR E 427
REMARK 465 MET F 1
REMARK 465 VAL F 2
REMARK 465 GLU F 3
REMARK 465 LYS F 4
REMARK 465 PHE F 5
REMARK 465 ASP F 6
REMARK 465 THR F 7
REMARK 465 ILE F 8
REMARK 465 LEU F 58
REMARK 465 MET G 1
REMARK 465 VAL G 2
REMARK 465 GLU G 3
REMARK 465 LYS G 4
REMARK 465 PHE G 5
REMARK 465 ASP G 6
REMARK 465 THR G 7
REMARK 465 ILE G 8
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 GLU H 3
REMARK 465 LYS H 4
REMARK 465 PHE H 5
REMARK 465 ASP H 6
REMARK 465 THR H 7
REMARK 465 MET I 1
REMARK 465 VAL I 2
REMARK 465 GLU I 3
REMARK 465 LYS I 4
REMARK 465 PHE I 5
REMARK 465 ASP I 6
REMARK 465 THR I 7
REMARK 465 ILE I 8
REMARK 465 MET J 1
REMARK 465 VAL J 2
REMARK 465 GLU J 3
REMARK 465 LYS J 4
REMARK 465 PHE J 5
REMARK 465 ASP J 6
REMARK 465 THR J 7
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 8 CG1 CG2 CD1
REMARK 470 ASP A 10 CG OD1 OD2
REMARK 470 GLU A 18 CG CD OE1 OE2
REMARK 470 THR A 57 OG1 CG2
REMARK 470 LEU A 58 CG CD1 CD2
REMARK 470 TYR A 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 GLU A 346 CG CD OE1 OE2
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 THR B 7 OG1 CG2
REMARK 470 ILE B 8 CG1 CG2 CD1
REMARK 470 ASP B 10 CG OD1 OD2
REMARK 470 THR B 57 OG1 CG2
REMARK 470 LEU B 58 CG CD1 CD2
REMARK 470 GLU B 65 CG CD OE1 OE2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 GLU B 203 CG CD OE1 OE2
REMARK 470 GLU B 346 CG CD OE1 OE2
REMARK 470 GLU B 380 CG CD OE1 OE2
REMARK 470 THR C 7 OG1 CG2
REMARK 470 ASP C 10 CG OD1 OD2
REMARK 470 GLU C 35 CG CD OE1 OE2
REMARK 470 GLU C 65 CG CD OE1 OE2
REMARK 470 GLU C 144 CG CD OE1 OE2
REMARK 470 LYS C 153 CG CD CE NZ
REMARK 470 LYS C 211 CG CD CE NZ
REMARK 470 GLU C 346 CG CD OE1 OE2
REMARK 470 GLU C 380 CG CD OE1 OE2
REMARK 470 ASP C 422 CG OD1 OD2
REMARK 470 GLU C 423 CG CD OE1 OE2
REMARK 470 LYS C 429 CG CD CE NZ
REMARK 470 ASP D 10 CG OD1 OD2
REMARK 470 LEU D 58 CG CD1 CD2
REMARK 470 GLU D 65 CG CD OE1 OE2
REMARK 470 LYS D 211 CG CD CE NZ
REMARK 470 LYS D 343 CG CD CE NZ
REMARK 470 GLU D 346 CG CD OE1 OE2
REMARK 470 LYS D 429 CG CD CE NZ
REMARK 470 THR E 7 OG1 CG2
REMARK 470 ILE E 8 CG1 CG2 CD1
REMARK 470 GLU E 65 CG CD OE1 OE2
REMARK 470 GLU E 144 CG CD OE1 OE2
REMARK 470 LYS E 153 CG CD CE NZ
REMARK 470 LYS E 211 CG CD CE NZ
REMARK 470 GLU E 346 CG CD OE1 OE2
REMARK 470 GLU E 380 CG CD OE1 OE2
REMARK 470 GLU E 423 CG CD OE1 OE2
REMARK 470 LYS E 429 CG CD CE NZ
REMARK 470 GLU E 436 CG CD OE1 OE2
REMARK 470 VAL E 441 CG1 CG2
REMARK 470 ASP F 10 CG OD1 OD2
REMARK 470 TYR F 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU F 18 CG CD OE1 OE2
REMARK 470 LYS F 21 CG CD CE NZ
REMARK 470 GLU F 40 CG CD OE1 OE2
REMARK 470 THR F 57 OG1 CG2
REMARK 470 TYR F 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU F 65 CG CD OE1 OE2
REMARK 470 GLU F 144 CG CD OE1 OE2
REMARK 470 LYS F 148 CG CD CE NZ
REMARK 470 LYS F 153 CG CD CE NZ
REMARK 470 GLU F 203 CG CD OE1 OE2
REMARK 470 LYS F 343 CG CD CE NZ
REMARK 470 GLU F 346 CG CD OE1 OE2
REMARK 470 GLU F 380 CG CD OE1 OE2
REMARK 470 GLU F 423 CG CD OE1 OE2
REMARK 470 LYS F 426 CG CD CE NZ
REMARK 470 LYS F 429 CG CD CE NZ
REMARK 470 ASP G 10 CG OD1 OD2
REMARK 470 LEU G 58 CG CD1 CD2
REMARK 470 GLU G 65 CG CD OE1 OE2
REMARK 470 GLU G 144 CG CD OE1 OE2
REMARK 470 LYS G 175 CG CD CE NZ
REMARK 470 GLU G 203 CG CD OE1 OE2
REMARK 470 LYS G 211 CG CD CE NZ
REMARK 470 GLU G 346 CG CD OE1 OE2
REMARK 470 GLU G 380 CG CD OE1 OE2
REMARK 470 LYS G 429 CG CD CE NZ
REMARK 470 ILE H 8 CG1 CG2 CD1
REMARK 470 ASP H 10 CG OD1 OD2
REMARK 470 GLU H 65 CG CD OE1 OE2
REMARK 470 LYS H 153 CG CD CE NZ
REMARK 470 LYS H 211 CG CD CE NZ
REMARK 470 GLU H 346 CG CD OE1 OE2
REMARK 470 GLU H 380 CG CD OE1 OE2
REMARK 470 ASP H 422 CG OD1 OD2
REMARK 470 GLU H 423 CG CD OE1 OE2
REMARK 470 LYS H 429 CG CD CE NZ
REMARK 470 ASP I 10 CG OD1 OD2
REMARK 470 TYR I 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU I 65 CG CD OE1 OE2
REMARK 470 LYS I 148 CG CD CE NZ
REMARK 470 LYS I 211 CG CD CE NZ
REMARK 470 GLU I 423 CG CD OE1 OE2
REMARK 470 ILE J 8 CG1 CG2 CD1
REMARK 470 GLU J 65 CG CD OE1 OE2
REMARK 470 GLU J 144 CG CD OE1 OE2
REMARK 470 LYS J 153 CG CD CE NZ
REMARK 470 SER J 358 OG
REMARK 470 GLN J 376 CG CD OE1 NE2
REMARK 470 GLU J 380 CG CD OE1 OE2
REMARK 470 GLN J 410 CG CD OE1 NE2
REMARK 470 GLU J 423 CG CD OE1 OE2
REMARK 470 LYS J 426 CG CD CE NZ
REMARK 470 THR J 427 OG1 CG2
REMARK 470 LYS J 429 CG CD CE NZ
REMARK 470 VAL J 441 CG1 CG2
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 SER A 51 -97.16 -142.26
REMARK 500 ALA A 109 40.54 -140.14
REMARK 500 THR A 195 -106.12 -122.75
REMARK 500 ASN A 200 79.40 -163.21
REMARK 500 ALA A 232 -177.74 -176.08
REMARK 500 MET A 284 -19.12 94.46
REMARK 500 TYR A 357 -116.60 51.48
REMARK 500 ASP B 14 87.07 -153.84
REMARK 500 SER B 51 -96.64 -135.39
REMARK 500 ALA B 109 37.24 -142.62
REMARK 500 THR B 195 -110.66 -117.69
REMARK 500 ASN B 200 83.68 -161.41
REMARK 500 MET B 284 -20.50 94.80
REMARK 500 TYR B 357 -113.90 48.66
REMARK 500 SER C 51 -93.20 -137.59
REMARK 500 ASP C 154 -44.49 -133.30
REMARK 500 THR C 195 -110.68 -114.49
REMARK 500 ASN C 200 84.01 -164.15
REMARK 500 ALA C 232 -175.10 -177.46
REMARK 500 MET C 284 -16.54 92.64
REMARK 500 ALA C 318 30.12 70.37
REMARK 500 TYR C 357 -114.06 52.82
REMARK 500 SER D 51 -111.15 -141.23
REMARK 500 THR D 56 -154.48 -114.45
REMARK 500 ALA D 109 35.19 -145.39
REMARK 500 ASP D 154 -40.53 -130.71
REMARK 500 THR D 195 -108.09 -118.67
REMARK 500 ASN D 200 81.83 -160.87
REMARK 500 ALA D 232 -178.73 -174.26
REMARK 500 MET D 284 -15.94 93.08
REMARK 500 TYR D 357 -114.45 62.27
REMARK 500 SER E 51 -107.85 -142.28
REMARK 500 ALA E 109 39.46 -140.61
REMARK 500 THR E 195 -104.08 -112.97
REMARK 500 SER E 196 58.09 -142.86
REMARK 500 ASN E 200 80.78 -157.40
REMARK 500 ALA E 232 -173.20 -179.35
REMARK 500 ALA E 283 128.72 -39.88
REMARK 500 MET E 284 -22.10 97.56
REMARK 500 TYR E 357 -116.70 46.67
REMARK 500 ASN E 374 26.63 -148.76
REMARK 500 SER F 51 -96.38 -142.89
REMARK 500 THR F 54 144.31 -172.10
REMARK 500 PRO F 60 100.26 -27.59
REMARK 500 HIS F 78 105.54 -177.57
REMARK 500 ALA F 109 38.40 -145.89
REMARK 500 THR F 195 -104.61 -121.32
REMARK 500 ASN F 200 80.14 -160.52
REMARK 500 ALA F 232 -178.88 -171.66
REMARK 500 MET F 284 -20.99 97.22
REMARK 500
REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 189 OQ2
REMARK 620 2 ASP A 191 OD1 88.7
REMARK 620 3 GLU A 192 OE1 85.3 95.0
REMARK 620 4 CAP A 446 O3 84.7 173.4 83.9
REMARK 620 5 CAP A 446 O2 86.0 104.6 158.3 75.4
REMARK 620 6 CAP A 446 O7 161.6 99.4 110.1 87.0 76.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 189 OQ2
REMARK 620 2 ASP B 191 OD1 83.0
REMARK 620 3 GLU B 192 OE1 88.2 85.9
REMARK 620 4 CAP B 446 O7 170.6 99.3 101.0
REMARK 620 5 CAP B 446 O2 94.0 110.1 163.9 76.6
REMARK 620 6 CAP B 446 O3 89.1 169.0 86.1 89.7 78.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 189 OQ2
REMARK 620 2 ASP C 191 OD1 87.2
REMARK 620 3 GLU C 192 OE1 84.9 85.5
REMARK 620 4 CAP C 446 O2 96.4 106.8 167.6
REMARK 620 5 CAP C 446 O7 174.3 98.1 97.6 80.0
REMARK 620 6 CAP C 446 O3 84.5 170.5 89.2 78.7 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 189 OQ2
REMARK 620 2 ASP D 191 OD1 91.2
REMARK 620 3 GLU D 192 OE1 87.9 87.8
REMARK 620 4 CAP D 446 O2 98.6 108.6 162.1
REMARK 620 5 CAP D 446 O3 85.2 173.4 86.5 77.5
REMARK 620 6 CAP D 446 O7 171.7 96.7 94.8 76.6 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 189 OQ2
REMARK 620 2 ASP E 191 OD2 92.9
REMARK 620 3 GLU E 192 OE1 78.7 76.5
REMARK 620 4 CAP E 446 O3 85.1 159.4 83.0
REMARK 620 5 CAP E 446 O2 94.4 117.6 164.9 83.0
REMARK 620 6 CAP E 446 O7 176.3 89.2 98.8 91.8 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 191 OD1
REMARK 620 2 GLU F 192 OE1 82.4
REMARK 620 3 CAP F 446 O3 168.4 88.9
REMARK 620 4 CAP F 446 O7 91.4 97.6 82.1
REMARK 620 5 CAP F 446 O2 111.5 162.3 75.7 72.0
REMARK 620 6 KCX F 189 OQ2 102.8 98.3 86.0 159.9 89.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX G 189 OQ2
REMARK 620 2 ASP G 191 OD2 100.4
REMARK 620 3 GLU G 192 OE1 92.0 73.9
REMARK 620 4 CAP G 446 O7 169.3 89.5 94.5
REMARK 620 5 CAP G 446 O2 94.8 125.2 157.9 76.1
REMARK 620 6 CAP G 446 O3 84.7 157.6 84.2 87.5 75.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 189 OQ2
REMARK 620 2 GLU H 192 OE1 77.2
REMARK 620 3 CAP H 446 O7 150.0 103.2
REMARK 620 4 CAP H 446 O2 86.0 151.2 80.0
REMARK 620 5 CAP H 446 O3 76.7 79.7 74.0 73.7
REMARK 620 6 ASP H 191 OD2 99.7 118.0 106.0 87.6 161.1
REMARK 620 7 ASP H 191 OD1 107.2 76.0 101.8 132.0 153.6 45.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX I 189 OQ2
REMARK 620 2 ASP I 191 OD1 94.9
REMARK 620 3 GLU I 192 OE1 88.7 89.8
REMARK 620 4 CAP I 446 O2 93.0 108.2 161.7
REMARK 620 5 CAP I 446 O3 83.0 176.5 87.3 74.8
REMARK 620 6 CAP I 446 O7 166.9 94.8 100.1 75.6 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX J 189 OQ2
REMARK 620 2 ASP J 191 OD1 92.3
REMARK 620 3 GLU J 192 OE1 82.4 84.1
REMARK 620 4 CAP J 446 O3 86.7 163.7 79.7
REMARK 620 5 CAP J 446 O2 85.2 115.8 157.0 80.3
REMARK 620 6 CAP J 446 O7 168.4 91.4 108.9 92.8 83.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 446
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 445
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 446
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GEH RELATED DB: PDB
REMARK 900 THE APO-FORM ABOUT THE SAME ENZYME
REMARK 900 RELATED ID: 3A13 RELATED DB: PDB
DBREF 3A12 A 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 B 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 C 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 D 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 E 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 F 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 G 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 H 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 I 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3A12 J 1 444 UNP O93627 RBL_PYRKO 1 444
SEQRES 1 A 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 A 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 A 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 A 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 A 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 A 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 A 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 A 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 A 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 A 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 A 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 A 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 A 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 A 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 A 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 A 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 A 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 A 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 A 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 A 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 A 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 A 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 A 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 A 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 A 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 A 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 A 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 A 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 A 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 A 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 A 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 A 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 A 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 A 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 A 444 PRO VAL
SEQRES 1 B 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 B 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 B 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 B 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 B 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 B 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 B 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 B 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 B 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 B 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 B 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 B 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 B 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 B 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 B 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 B 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 B 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 B 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 B 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 B 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 B 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 B 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 B 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 B 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 B 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 B 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 B 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 B 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 B 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 B 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 B 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 B 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 B 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 B 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 B 444 PRO VAL
SEQRES 1 C 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 C 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 C 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 C 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 C 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 C 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 C 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 C 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 C 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 C 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 C 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 C 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 C 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 C 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 C 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 C 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 C 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 C 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 C 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 C 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 C 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 C 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 C 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 C 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 C 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 C 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 C 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 C 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 C 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 C 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 C 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 C 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 C 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 C 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 C 444 PRO VAL
SEQRES 1 D 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 D 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 D 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 D 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 D 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 D 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 D 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 D 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 D 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 D 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 D 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 D 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 D 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 D 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 D 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 D 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 D 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 D 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 D 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 D 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 D 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 D 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 D 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 D 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 D 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 D 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 D 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 D 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 D 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 D 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 D 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 D 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 D 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 D 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 D 444 PRO VAL
SEQRES 1 E 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 E 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 E 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 E 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 E 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 E 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 E 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 E 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 E 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 E 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 E 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 E 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 E 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 E 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 E 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 E 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 E 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 E 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 E 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 E 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 E 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 E 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 E 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 E 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 E 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 E 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 E 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 E 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 E 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 E 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 E 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 E 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 E 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 E 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 E 444 PRO VAL
SEQRES 1 F 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 F 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 F 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 F 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 F 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 F 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 F 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 F 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 F 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 F 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 F 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 F 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 F 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 F 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 F 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 F 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 F 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 F 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 F 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 F 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 F 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 F 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 F 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 F 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 F 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 F 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 F 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 F 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 F 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 F 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 F 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 F 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 F 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 F 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 F 444 PRO VAL
SEQRES 1 G 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 G 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 G 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 G 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 G 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 G 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 G 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 G 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 G 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 G 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 G 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 G 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 G 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 G 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 G 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 G 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 G 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 G 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 G 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 G 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 G 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 G 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 G 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 G 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 G 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 G 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 G 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 G 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 G 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 G 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 G 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 G 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 G 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 G 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 G 444 PRO VAL
SEQRES 1 H 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 H 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 H 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 H 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 H 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 H 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 H 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 H 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 H 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 H 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 H 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 H 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 H 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 H 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 H 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 H 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 H 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 H 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 H 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 H 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 H 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 H 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 H 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 H 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 H 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 H 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 H 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 H 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 H 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 H 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 H 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 H 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 H 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 H 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 H 444 PRO VAL
SEQRES 1 I 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 I 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 I 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 I 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 I 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 I 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 I 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 I 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 I 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 I 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 I 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 I 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 I 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 I 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 I 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 I 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 I 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 I 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 I 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 I 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 I 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 I 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 I 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 I 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 I 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 I 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 I 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 I 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 I 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 I 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 I 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 I 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 I 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 I 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 I 444 PRO VAL
SEQRES 1 J 444 MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL
SEQRES 2 J 444 ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE
SEQRES 3 J 444 ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE
SEQRES 4 J 444 GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR
SEQRES 5 J 444 GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU
SEQRES 6 J 444 ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS
SEQRES 7 J 444 ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR
SEQRES 8 J 444 PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU
SEQRES 9 J 444 LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG
SEQRES 10 J 444 VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU
SEQRES 11 J 444 LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE
SEQRES 12 J 444 GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO
SEQRES 13 J 444 ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER
SEQRES 14 J 444 PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER
SEQRES 15 J 444 ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR
SEQRES 16 J 444 SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE
SEQRES 17 J 444 MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY
SEQRES 18 J 444 GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU
SEQRES 19 J 444 LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU
SEQRES 20 J 444 GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY
SEQRES 21 J 444 TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP
SEQRES 22 J 444 TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA
SEQRES 23 J 444 ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE
SEQRES 24 J 444 VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN
SEQRES 25 J 444 LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY
SEQRES 26 J 444 GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE LEU ARG
SEQRES 27 J 444 GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS
SEQRES 28 J 444 LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO
SEQRES 29 J 444 THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO
SEQRES 30 J 444 VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU
SEQRES 31 J 444 GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA
SEQRES 32 J 444 GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET
SEQRES 33 J 444 GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS
SEQRES 34 J 444 GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR
SEQRES 35 J 444 PRO VAL
MODRES 3A12 KCX A 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX B 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX C 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX D 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX E 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX F 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX G 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX H 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX I 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3A12 KCX J 189 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 189 12
HET KCX B 189 12
HET KCX C 189 12
HET KCX D 189 12
HET KCX E 189 12
HET KCX F 189 12
HET KCX G 189 12
HET KCX H 189 12
HET KCX I 189 12
HET KCX J 189 12
HET MG A 445 1
HET CAP A 446 21
HET MG B 445 1
HET CAP B 446 21
HET MG C 445 1
HET CAP C 446 21
HET MG D 445 1
HET CAP D 446 21
HET MG E 445 1
HET CAP E 446 21
HET MG F 445 1
HET CAP F 446 21
HET MG G 445 1
HET CAP G 446 21
HET MG H 445 1
HET CAP H 446 21
HET MG I 445 1
HET CAP I 446 21
HET MG J 445 1
HET CAP J 446 21
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM MG MAGNESIUM ION
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL 1 KCX 10(C7 H14 N2 O4)
FORMUL 11 MG 10(MG 2+)
FORMUL 12 CAP 10(C6 H14 O13 P2)
FORMUL 31 HOH *2306(H2 O)
HELIX 1 1 TYR A 9 VAL A 13 5 5
HELIX 2 2 THR A 38 SER A 50 1 13
HELIX 3 3 GLU A 63 LEU A 70 1 8
HELIX 4 4 HIS A 94 PHE A 96 5 3
HELIX 5 5 ASN A 100 ALA A 109 1 10
HELIX 6 6 GLY A 110 MET A 115 5 6
HELIX 7 7 PRO A 129 ARG A 134 1 6
HELIX 8 8 PHE A 141 GLU A 151 1 11
HELIX 9 9 SER A 169 ASN A 183 1 15
HELIX 10 10 ARG A 201 GLY A 221 1 21
HELIX 11 11 ASP A 233 LEU A 247 1 15
HELIX 12 12 VAL A 256 GLY A 260 1 5
HELIX 13 13 GLY A 260 GLY A 275 1 16
HELIX 14 14 HIS A 285 ARG A 290 1 6
HELIX 15 15 SER A 297 GLY A 309 1 13
HELIX 16 16 GLY A 326 GLU A 339 1 14
HELIX 17 17 HIS A 371 ASN A 374 5 4
HELIX 18 18 ILE A 375 GLY A 383 1 9
HELIX 19 19 GLY A 391 GLY A 396 1 6
HELIX 20 20 GLY A 400 GLY A 418 1 19
HELIX 21 21 PRO A 420 LYS A 426 1 7
HELIX 22 22 HIS A 428 GLY A 439 1 12
HELIX 23 23 THR B 7 VAL B 13 5 7
HELIX 24 24 THR B 38 SER B 51 1 14
HELIX 25 25 GLU B 63 SER B 71 1 9
HELIX 26 26 HIS B 94 PHE B 96 5 3
HELIX 27 27 ASN B 100 ALA B 109 1 10
HELIX 28 28 GLY B 110 MET B 115 5 6
HELIX 29 29 PRO B 129 ARG B 134 1 6
HELIX 30 30 PHE B 141 GLU B 151 1 11
HELIX 31 31 SER B 169 ASN B 183 1 15
HELIX 32 32 ARG B 201 GLY B 221 1 21
HELIX 33 33 ASP B 233 LEU B 247 1 15
HELIX 34 34 VAL B 256 GLY B 260 1 5
HELIX 35 35 GLY B 260 TYR B 274 1 15
HELIX 36 36 HIS B 285 ARG B 290 1 6
HELIX 37 37 SER B 297 GLY B 309 1 13
HELIX 38 38 GLY B 326 GLU B 339 1 14
HELIX 39 39 HIS B 371 ASN B 374 5 4
HELIX 40 40 ILE B 375 GLY B 383 1 9
HELIX 41 41 GLY B 391 GLY B 396 1 6
HELIX 42 42 GLY B 400 GLY B 418 1 19
HELIX 43 43 PRO B 420 ALA B 425 1 6
HELIX 44 44 HIS B 428 GLY B 439 1 12
HELIX 45 45 ILE C 8 VAL C 13 5 6
HELIX 46 46 THR C 38 SER C 50 1 13
HELIX 47 47 GLU C 63 SER C 71 1 9
HELIX 48 48 HIS C 94 PHE C 96 5 3
HELIX 49 49 ASN C 100 ALA C 109 1 10
HELIX 50 50 GLY C 110 MET C 115 5 6
HELIX 51 51 PRO C 129 ARG C 134 1 6
HELIX 52 52 PHE C 141 GLU C 151 1 11
HELIX 53 53 SER C 169 ASN C 183 1 15
HELIX 54 54 ARG C 201 GLY C 221 1 21
HELIX 55 55 ASP C 233 GLY C 248 1 16
HELIX 56 56 VAL C 256 GLY C 260 1 5
HELIX 57 57 GLY C 260 TYR C 274 1 15
HELIX 58 58 HIS C 285 ARG C 290 1 6
HELIX 59 59 SER C 297 GLY C 309 1 13
HELIX 60 60 GLY C 326 GLU C 339 1 14
HELIX 61 61 HIS C 371 ASN C 374 5 4
HELIX 62 62 ILE C 375 GLY C 383 1 9
HELIX 63 63 GLY C 391 GLY C 396 1 6
HELIX 64 64 GLY C 400 GLN C 417 1 18
HELIX 65 65 PRO C 420 ALA C 425 1 6
HELIX 66 66 HIS C 428 GLY C 439 1 12
HELIX 67 67 TYR D 9 VAL D 13 5 5
HELIX 68 68 THR D 38 SER D 50 1 13
HELIX 69 69 GLU D 63 SER D 71 1 9
HELIX 70 70 HIS D 94 PHE D 96 5 3
HELIX 71 71 ASN D 100 ALA D 109 1 10
HELIX 72 72 GLY D 110 MET D 115 5 6
HELIX 73 73 PRO D 129 ARG D 134 1 6
HELIX 74 74 PHE D 141 GLU D 151 1 11
HELIX 75 75 SER D 169 ASN D 183 1 15
HELIX 76 76 ARG D 201 GLY D 221 1 21
HELIX 77 77 ASP D 233 LEU D 247 1 15
HELIX 78 78 VAL D 256 GLY D 260 1 5
HELIX 79 79 GLY D 260 TYR D 274 1 15
HELIX 80 80 HIS D 285 ARG D 290 1 6
HELIX 81 81 SER D 297 GLY D 309 1 13
HELIX 82 82 GLY D 326 GLU D 339 1 14
HELIX 83 83 HIS D 371 ASN D 374 5 4
HELIX 84 84 ILE D 375 GLY D 383 1 9
HELIX 85 85 GLY D 391 GLY D 396 1 6
HELIX 86 86 GLY D 400 GLY D 418 1 19
HELIX 87 87 PRO D 420 LYS D 426 1 7
HELIX 88 88 HIS D 428 GLY D 439 1 12
HELIX 89 89 ILE E 8 VAL E 13 5 6
HELIX 90 90 THR E 38 SER E 50 1 13
HELIX 91 91 GLU E 63 SER E 71 1 9
HELIX 92 92 HIS E 94 PHE E 96 5 3
HELIX 93 93 ASN E 100 ALA E 109 1 10
HELIX 94 94 GLY E 110 MET E 115 5 6
HELIX 95 95 PRO E 129 ARG E 134 1 6
HELIX 96 96 PHE E 141 GLU E 151 1 11
HELIX 97 97 SER E 169 ASN E 183 1 15
HELIX 98 98 ARG E 201 GLY E 221 1 21
HELIX 99 99 ASP E 233 GLY E 248 1 16
HELIX 100 100 VAL E 256 GLY E 260 1 5
HELIX 101 101 GLY E 260 TYR E 274 1 15
HELIX 102 102 HIS E 285 ARG E 290 1 6
HELIX 103 103 SER E 297 GLY E 309 1 13
HELIX 104 104 GLY E 326 GLU E 339 1 14
HELIX 105 105 ILE E 375 GLY E 383 1 9
HELIX 106 106 GLY E 391 GLY E 396 1 6
HELIX 107 107 GLY E 400 GLN E 417 1 18
HELIX 108 108 PRO E 420 ALA E 425 1 6
HELIX 109 109 HIS E 428 GLY E 439 1 12
HELIX 110 110 TYR F 9 VAL F 13 5 5
HELIX 111 111 THR F 38 SER F 50 1 13
HELIX 112 112 GLU F 63 SER F 71 1 9
HELIX 113 113 HIS F 94 PHE F 96 5 3
HELIX 114 114 ASN F 100 ALA F 109 1 10
HELIX 115 115 GLY F 110 MET F 115 5 6
HELIX 116 116 PRO F 129 ARG F 134 1 6
HELIX 117 117 PHE F 141 GLU F 151 1 11
HELIX 118 118 SER F 169 ASN F 183 1 15
HELIX 119 119 ARG F 201 GLY F 221 1 21
HELIX 120 120 ASP F 233 GLY F 248 1 16
HELIX 121 121 VAL F 256 GLY F 260 1 5
HELIX 122 122 GLY F 260 GLY F 275 1 16
HELIX 123 123 HIS F 285 ARG F 290 1 6
HELIX 124 124 SER F 297 GLY F 309 1 13
HELIX 125 125 GLY F 326 GLU F 339 1 14
HELIX 126 126 HIS F 371 GLY F 383 1 13
HELIX 127 127 GLY F 391 GLY F 396 1 6
HELIX 128 128 GLY F 400 GLN F 417 1 18
HELIX 129 129 PRO F 420 ALA F 425 1 6
HELIX 130 130 HIS F 428 GLY F 439 1 12
HELIX 131 131 TYR G 9 VAL G 13 5 5
HELIX 132 132 THR G 38 SER G 50 1 13
HELIX 133 133 GLU G 63 SER G 71 1 9
HELIX 134 134 HIS G 94 PHE G 96 5 3
HELIX 135 135 ASN G 100 ALA G 109 1 10
HELIX 136 136 GLY G 110 MET G 115 5 6
HELIX 137 137 PRO G 129 ARG G 134 1 6
HELIX 138 138 PHE G 141 GLU G 151 1 11
HELIX 139 139 SER G 169 ASN G 183 1 15
HELIX 140 140 ARG G 201 GLY G 221 1 21
HELIX 141 141 ASP G 233 LEU G 247 1 15
HELIX 142 142 VAL G 256 GLY G 260 1 5
HELIX 143 143 GLY G 260 TYR G 274 1 15
HELIX 144 144 HIS G 285 ARG G 290 1 6
HELIX 145 145 SER G 297 GLY G 309 1 13
HELIX 146 146 GLY G 326 GLU G 339 1 14
HELIX 147 147 HIS G 371 ASN G 374 5 4
HELIX 148 148 ILE G 375 GLY G 383 1 9
HELIX 149 149 GLY G 391 GLY G 396 1 6
HELIX 150 150 GLY G 400 GLY G 418 1 19
HELIX 151 151 PRO G 420 ALA G 425 1 6
HELIX 152 152 HIS G 428 GLY G 439 1 12
HELIX 153 153 TYR H 9 VAL H 13 5 5
HELIX 154 154 THR H 38 SER H 50 1 13
HELIX 155 155 GLU H 63 SER H 71 1 9
HELIX 156 156 HIS H 94 PHE H 96 5 3
HELIX 157 157 ASN H 100 ALA H 109 1 10
HELIX 158 158 GLY H 110 MET H 115 5 6
HELIX 159 159 PRO H 129 ARG H 134 1 6
HELIX 160 160 PHE H 141 GLU H 151 1 11
HELIX 161 161 SER H 169 ASN H 183 1 15
HELIX 162 162 ARG H 201 GLY H 221 1 21
HELIX 163 163 ASP H 233 LEU H 247 1 15
HELIX 164 164 VAL H 256 GLY H 260 1 5
HELIX 165 165 GLY H 260 TYR H 274 1 15
HELIX 166 166 HIS H 285 ARG H 290 1 6
HELIX 167 167 SER H 297 GLY H 309 1 13
HELIX 168 168 GLY H 326 GLU H 339 1 14
HELIX 169 169 HIS H 371 ASN H 374 5 4
HELIX 170 170 ILE H 375 GLY H 383 1 9
HELIX 171 171 GLY H 391 GLY H 396 1 6
HELIX 172 172 GLY H 400 GLN H 417 1 18
HELIX 173 173 PRO H 420 THR H 427 1 8
HELIX 174 174 HIS H 428 GLY H 439 1 12
HELIX 175 175 TYR I 9 VAL I 13 5 5
HELIX 176 176 THR I 38 SER I 50 1 13
HELIX 177 177 GLU I 63 SER I 71 1 9
HELIX 178 178 HIS I 94 PHE I 96 5 3
HELIX 179 179 ASN I 100 ALA I 109 1 10
HELIX 180 180 GLY I 110 MET I 115 5 6
HELIX 181 181 PRO I 129 ARG I 134 1 6
HELIX 182 182 PHE I 141 GLU I 151 1 11
HELIX 183 183 SER I 169 ASN I 183 1 15
HELIX 184 184 ARG I 201 GLY I 221 1 21
HELIX 185 185 ASP I 233 GLY I 248 1 16
HELIX 186 186 VAL I 256 GLY I 260 1 5
HELIX 187 187 GLY I 260 TYR I 274 1 15
HELIX 188 188 HIS I 285 ARG I 290 1 6
HELIX 189 189 SER I 297 GLY I 309 1 13
HELIX 190 190 GLY I 326 GLU I 339 1 14
HELIX 191 191 HIS I 371 ASN I 374 5 4
HELIX 192 192 ILE I 375 GLY I 383 1 9
HELIX 193 193 GLY I 391 GLY I 396 1 6
HELIX 194 194 GLY I 400 GLY I 418 1 19
HELIX 195 195 PRO I 420 LYS I 426 1 7
HELIX 196 196 HIS I 428 GLY I 439 1 12
HELIX 197 197 ILE J 8 VAL J 13 5 6
HELIX 198 198 THR J 38 SER J 50 1 13
HELIX 199 199 GLU J 63 SER J 71 1 9
HELIX 200 200 HIS J 94 PHE J 96 5 3
HELIX 201 201 ASN J 100 ALA J 109 1 10
HELIX 202 202 GLY J 110 MET J 115 5 6
HELIX 203 203 PRO J 129 ARG J 134 1 6
HELIX 204 204 PHE J 141 GLU J 151 1 11
HELIX 205 205 SER J 169 ASN J 183 1 15
HELIX 206 206 ARG J 201 GLY J 221 1 21
HELIX 207 207 ASP J 233 LEU J 247 1 15
HELIX 208 208 VAL J 256 GLY J 260 1 5
HELIX 209 209 GLY J 260 TYR J 274 1 15
HELIX 210 210 HIS J 285 ARG J 290 1 6
HELIX 211 211 SER J 297 GLY J 309 1 13
HELIX 212 212 GLY J 326 GLU J 339 1 14
HELIX 213 213 ILE J 375 GLY J 383 1 9
HELIX 214 214 GLY J 391 GLY J 396 1 6
HELIX 215 215 GLY J 400 GLY J 418 1 19
HELIX 216 216 PRO J 420 ALA J 425 1 6
HELIX 217 217 HIS J 428 GLY J 439 1 12
SHEET 1 A 5 LYS A 73 ASP A 79 0
SHEET 2 A 5 TRP A 85 PRO A 92 -1 O ALA A 90 N LYS A 73
SHEET 3 A 5 ASP A 24 PRO A 33 -1 N PHE A 29 O VAL A 87
SHEET 4 A 5 VAL A 118 TYR A 127 -1 O LYS A 119 N THR A 32
SHEET 5 A 5 GLY A 295 ILE A 296 1 O GLY A 295 N LEU A 121
SHEET 1 B 9 ILE A 157 VAL A 160 0
SHEET 2 B 9 TYR A 187 KCX A 189 1 O KCX A 189 N VAL A 160
SHEET 3 B 9 THR A 225 ASN A 229 1 O PHE A 227 N MET A 188
SHEET 4 B 9 HIS A 251 ASP A 255 1 O MET A 253 N ALA A 228
SHEET 5 B 9 ALA A 277 HIS A 281 1 O HIS A 281 N VAL A 254
SHEET 6 B 9 GLN A 312 HIS A 314 1 O GLN A 312 N GLY A 280
SHEET 7 B 9 PHE A 363 SER A 367 1 O THR A 365 N LEU A 313
SHEET 8 B 9 VAL A 387 GLN A 389 1 O VAL A 387 N SER A 366
SHEET 9 B 9 ILE A 157 VAL A 160 1 N ILE A 157 O LEU A 388
SHEET 1 C 2 HIS A 341 TYR A 342 0
SHEET 2 C 2 GLN A 354 LYS A 355 -1 O GLN A 354 N TYR A 342
SHEET 1 D 5 LYS B 73 ASP B 79 0
SHEET 2 D 5 TRP B 85 PRO B 92 -1 O ILE B 86 N HIS B 78
SHEET 3 D 5 ASP B 24 PRO B 33 -1 N ILE B 25 O TYR B 91
SHEET 4 D 5 VAL B 118 TYR B 127 -1 O LYS B 119 N THR B 32
SHEET 5 D 5 GLY B 295 ILE B 296 1 O GLY B 295 N LEU B 123
SHEET 1 E 9 ILE B 157 VAL B 160 0
SHEET 2 E 9 TYR B 187 KCX B 189 1 O KCX B 189 N VAL B 160
SHEET 3 E 9 THR B 225 ASN B 229 1 O PHE B 227 N MET B 188
SHEET 4 E 9 HIS B 251 ASP B 255 1 O MET B 253 N ALA B 228
SHEET 5 E 9 ALA B 277 HIS B 281 1 O HIS B 279 N ALA B 252
SHEET 6 E 9 GLN B 312 HIS B 314 1 O GLN B 312 N GLY B 280
SHEET 7 E 9 PHE B 363 SER B 367 1 O THR B 365 N LEU B 313
SHEET 8 E 9 VAL B 387 GLN B 389 1 O VAL B 387 N SER B 366
SHEET 9 E 9 ILE B 157 VAL B 160 1 N ILE B 157 O LEU B 388
SHEET 1 F 2 HIS B 341 TYR B 342 0
SHEET 2 F 2 GLN B 354 LYS B 355 -1 O GLN B 354 N TYR B 342
SHEET 1 G 5 LYS C 73 ASP C 79 0
SHEET 2 G 5 TRP C 85 PRO C 92 -1 O ALA C 90 N LYS C 73
SHEET 3 G 5 ASP C 24 PRO C 33 -1 N VAL C 31 O TRP C 85
SHEET 4 G 5 VAL C 118 TYR C 127 -1 O LYS C 119 N THR C 32
SHEET 5 G 5 GLY C 295 ILE C 296 1 O GLY C 295 N LEU C 121
SHEET 1 H 9 ILE C 157 VAL C 160 0
SHEET 2 H 9 TYR C 187 KCX C 189 1 O KCX C 189 N VAL C 160
SHEET 3 H 9 THR C 225 ASN C 229 1 O PHE C 227 N MET C 188
SHEET 4 H 9 HIS C 251 ASP C 255 1 O MET C 253 N ALA C 228
SHEET 5 H 9 ALA C 277 HIS C 281 1 O HIS C 279 N VAL C 254
SHEET 6 H 9 GLN C 312 HIS C 314 1 O GLN C 312 N GLY C 280
SHEET 7 H 9 PHE C 363 SER C 367 1 O THR C 365 N LEU C 313
SHEET 8 H 9 VAL C 387 GLN C 389 1 O VAL C 387 N SER C 366
SHEET 9 H 9 ILE C 157 VAL C 160 1 N ILE C 157 O LEU C 388
SHEET 1 I 2 HIS C 341 TYR C 342 0
SHEET 2 I 2 GLN C 354 LYS C 355 -1 O GLN C 354 N TYR C 342
SHEET 1 J 5 LYS D 73 ASP D 79 0
SHEET 2 J 5 TRP D 85 PRO D 92 -1 O ILE D 86 N HIS D 78
SHEET 3 J 5 ASP D 24 PRO D 33 -1 N ILE D 25 O TYR D 91
SHEET 4 J 5 VAL D 118 TYR D 127 -1 O LYS D 119 N THR D 32
SHEET 5 J 5 GLY D 295 ILE D 296 1 O GLY D 295 N LEU D 123
SHEET 1 K 9 ILE D 157 VAL D 160 0
SHEET 2 K 9 TYR D 187 KCX D 189 1 O KCX D 189 N VAL D 160
SHEET 3 K 9 THR D 225 ASN D 229 1 O PHE D 227 N MET D 188
SHEET 4 K 9 HIS D 251 ASP D 255 1 O MET D 253 N ALA D 228
SHEET 5 K 9 ALA D 277 HIS D 281 1 O ALA D 277 N ALA D 252
SHEET 6 K 9 GLN D 312 HIS D 314 1 O GLN D 312 N GLY D 280
SHEET 7 K 9 PHE D 363 SER D 367 1 O THR D 365 N LEU D 313
SHEET 8 K 9 VAL D 387 GLN D 389 1 O VAL D 387 N SER D 366
SHEET 9 K 9 ILE D 157 VAL D 160 1 N ILE D 157 O LEU D 388
SHEET 1 L 2 HIS D 341 TYR D 342 0
SHEET 2 L 2 GLN D 354 LYS D 355 -1 O GLN D 354 N TYR D 342
SHEET 1 M 5 LYS E 73 ASP E 79 0
SHEET 2 M 5 TRP E 85 PRO E 92 -1 O ILE E 86 N HIS E 78
SHEET 3 M 5 ASP E 24 PRO E 33 -1 N ILE E 25 O TYR E 91
SHEET 4 M 5 VAL E 118 TYR E 127 -1 O TYR E 127 N ILE E 26
SHEET 5 M 5 GLY E 295 ILE E 296 1 O GLY E 295 N LEU E 121
SHEET 1 N 9 ILE E 157 VAL E 160 0
SHEET 2 N 9 TYR E 187 KCX E 189 1 O KCX E 189 N VAL E 160
SHEET 3 N 9 THR E 225 ASN E 229 1 O PHE E 227 N MET E 188
SHEET 4 N 9 HIS E 251 ASP E 255 1 O MET E 253 N ALA E 228
SHEET 5 N 9 ALA E 277 HIS E 281 1 O ALA E 277 N ALA E 252
SHEET 6 N 9 GLN E 312 HIS E 314 1 O GLN E 312 N GLY E 280
SHEET 7 N 9 PHE E 363 SER E 367 1 O PHE E 363 N LEU E 313
SHEET 8 N 9 VAL E 387 GLN E 389 1 O VAL E 387 N SER E 366
SHEET 9 N 9 ILE E 157 VAL E 160 1 N ILE E 157 O LEU E 388
SHEET 1 O 2 HIS E 341 TYR E 342 0
SHEET 2 O 2 GLN E 354 LYS E 355 -1 O GLN E 354 N TYR E 342
SHEET 1 P 5 LYS F 73 ASP F 76 0
SHEET 2 P 5 TRP F 85 PRO F 92 -1 O ALA F 90 N LYS F 73
SHEET 3 P 5 ASP F 24 PRO F 33 -1 N ILE F 25 O TYR F 91
SHEET 4 P 5 VAL F 118 TYR F 127 -1 O TYR F 127 N ILE F 26
SHEET 5 P 5 GLY F 295 ILE F 296 1 O GLY F 295 N LEU F 123
SHEET 1 Q 8 THR F 225 PHE F 227 0
SHEET 2 Q 8 TYR F 187 KCX F 189 1 N MET F 188 O PHE F 227
SHEET 3 Q 8 ILE F 157 VAL F 160 1 N VAL F 160 O KCX F 189
SHEET 4 Q 8 VAL F 387 GLN F 389 1 O LEU F 388 N ILE F 157
SHEET 5 Q 8 PHE F 363 SER F 367 1 N SER F 366 O VAL F 387
SHEET 6 Q 8 GLN F 312 HIS F 314 1 N LEU F 313 O THR F 365
SHEET 7 Q 8 ALA F 277 HIS F 281 1 N GLY F 280 O GLN F 312
SHEET 8 Q 8 HIS F 251 ASP F 255 1 N VAL F 254 O HIS F 281
SHEET 1 R 2 HIS F 341 TYR F 342 0
SHEET 2 R 2 GLN F 354 LYS F 355 -1 O GLN F 354 N TYR F 342
SHEET 1 S 5 LYS G 73 ASP G 79 0
SHEET 2 S 5 TRP G 85 PRO G 92 -1 O ILE G 86 N HIS G 78
SHEET 3 S 5 ASP G 24 PRO G 33 -1 N ILE G 25 O TYR G 91
SHEET 4 S 5 VAL G 118 TYR G 127 -1 O LYS G 119 N THR G 32
SHEET 5 S 5 GLY G 295 ILE G 296 1 O GLY G 295 N LEU G 121
SHEET 1 T 9 ILE G 157 VAL G 160 0
SHEET 2 T 9 TYR G 187 KCX G 189 1 O KCX G 189 N VAL G 160
SHEET 3 T 9 THR G 225 ASN G 229 1 O PHE G 227 N MET G 188
SHEET 4 T 9 HIS G 251 ASP G 255 1 O MET G 253 N ALA G 228
SHEET 5 T 9 ALA G 277 HIS G 281 1 O HIS G 279 N ALA G 252
SHEET 6 T 9 GLN G 312 HIS G 314 1 O GLN G 312 N GLY G 280
SHEET 7 T 9 PHE G 363 SER G 367 1 O THR G 365 N LEU G 313
SHEET 8 T 9 VAL G 387 GLN G 389 1 O VAL G 387 N SER G 366
SHEET 9 T 9 ILE G 157 VAL G 160 1 N ILE G 157 O LEU G 388
SHEET 1 U 2 HIS G 341 TYR G 342 0
SHEET 2 U 2 GLN G 354 LYS G 355 -1 O GLN G 354 N TYR G 342
SHEET 1 V 5 LYS H 73 ASP H 79 0
SHEET 2 V 5 TRP H 85 PRO H 92 -1 O ILE H 86 N HIS H 78
SHEET 3 V 5 ASP H 24 PRO H 33 -1 N PHE H 29 O VAL H 87
SHEET 4 V 5 VAL H 118 TYR H 127 -1 O LYS H 119 N THR H 32
SHEET 5 V 5 GLY H 295 ILE H 296 1 O GLY H 295 N LEU H 123
SHEET 1 W 8 THR H 225 PHE H 227 0
SHEET 2 W 8 TYR H 187 KCX H 189 1 N MET H 188 O PHE H 227
SHEET 3 W 8 ILE H 157 VAL H 160 1 N VAL H 160 O KCX H 189
SHEET 4 W 8 VAL H 387 GLN H 389 1 O LEU H 388 N ILE H 157
SHEET 5 W 8 PHE H 363 SER H 367 1 N PRO H 364 O VAL H 387
SHEET 6 W 8 GLN H 312 HIS H 314 1 N LEU H 313 O PHE H 363
SHEET 7 W 8 ALA H 277 HIS H 281 1 N GLY H 280 O GLN H 312
SHEET 8 W 8 HIS H 251 ASP H 255 1 N VAL H 254 O HIS H 281
SHEET 1 X 2 HIS H 341 TYR H 342 0
SHEET 2 X 2 GLN H 354 LYS H 355 -1 O GLN H 354 N TYR H 342
SHEET 1 Y 5 LYS I 73 ASP I 79 0
SHEET 2 Y 5 TRP I 85 PRO I 92 -1 O ILE I 86 N HIS I 78
SHEET 3 Y 5 ASP I 24 PRO I 33 -1 N VAL I 31 O TRP I 85
SHEET 4 Y 5 VAL I 118 TYR I 127 -1 O LYS I 119 N THR I 32
SHEET 5 Y 5 GLY I 295 ILE I 296 1 O GLY I 295 N LEU I 123
SHEET 1 Z 9 ILE I 157 VAL I 160 0
SHEET 2 Z 9 TYR I 187 KCX I 189 1 O KCX I 189 N VAL I 160
SHEET 3 Z 9 THR I 225 ASN I 229 1 O PHE I 227 N MET I 188
SHEET 4 Z 9 HIS I 251 ASP I 255 1 O MET I 253 N ALA I 228
SHEET 5 Z 9 ALA I 277 HIS I 281 1 O ALA I 277 N ALA I 252
SHEET 6 Z 9 GLN I 312 HIS I 314 1 O GLN I 312 N GLY I 280
SHEET 7 Z 9 PHE I 363 SER I 367 1 O THR I 365 N LEU I 313
SHEET 8 Z 9 VAL I 387 GLN I 389 1 O VAL I 387 N SER I 366
SHEET 9 Z 9 ILE I 157 VAL I 160 1 N ILE I 157 O LEU I 388
SHEET 1 AA 2 HIS I 341 TYR I 342 0
SHEET 2 AA 2 GLN I 354 LYS I 355 -1 O GLN I 354 N TYR I 342
SHEET 1 AB 5 LYS J 73 ASP J 79 0
SHEET 2 AB 5 TRP J 85 PRO J 92 -1 O ILE J 86 N HIS J 78
SHEET 3 AB 5 ASP J 24 PRO J 33 -1 N ILE J 25 O TYR J 91
SHEET 4 AB 5 VAL J 118 TYR J 127 -1 O GLU J 124 N VAL J 28
SHEET 5 AB 5 GLY J 295 ILE J 296 1 O GLY J 295 N LEU J 121
SHEET 1 AC 8 THR J 225 PHE J 227 0
SHEET 2 AC 8 TYR J 187 KCX J 189 1 N MET J 188 O PHE J 227
SHEET 3 AC 8 ILE J 157 VAL J 160 1 N VAL J 160 O KCX J 189
SHEET 4 AC 8 VAL J 387 GLN J 389 1 O LEU J 388 N ILE J 157
SHEET 5 AC 8 PHE J 363 SER J 367 1 N PRO J 364 O VAL J 387
SHEET 6 AC 8 GLN J 312 HIS J 314 1 N LEU J 313 O PHE J 363
SHEET 7 AC 8 ALA J 277 HIS J 281 1 N GLY J 280 O GLN J 312
SHEET 8 AC 8 HIS J 251 ASP J 255 1 N VAL J 254 O HIS J 281
SHEET 1 AD 2 HIS J 341 TYR J 342 0
SHEET 2 AD 2 GLN J 354 LYS J 355 -1 O GLN J 354 N TYR J 342
LINK C MET A 188 N KCX A 189 1555 1555 1.33
LINK C KCX A 189 N ASP A 190 1555 1555 1.33
LINK C MET B 188 N KCX B 189 1555 1555 1.32
LINK C KCX B 189 N ASP B 190 1555 1555 1.33
LINK C MET C 188 N KCX C 189 1555 1555 1.33
LINK C KCX C 189 N ASP C 190 1555 1555 1.33
LINK C MET D 188 N KCX D 189 1555 1555 1.33
LINK C KCX D 189 N ASP D 190 1555 1555 1.33
LINK C MET E 188 N KCX E 189 1555 1555 1.33
LINK C KCX E 189 N ASP E 190 1555 1555 1.33
LINK C MET F 188 N KCX F 189 1555 1555 1.33
LINK C KCX F 189 N ASP F 190 1555 1555 1.33
LINK C MET G 188 N KCX G 189 1555 1555 1.32
LINK C KCX G 189 N ASP G 190 1555 1555 1.33
LINK C MET H 188 N KCX H 189 1555 1555 1.33
LINK C KCX H 189 N ASP H 190 1555 1555 1.33
LINK C MET I 188 N KCX I 189 1555 1555 1.33
LINK C KCX I 189 N ASP I 190 1555 1555 1.33
LINK C MET J 188 N KCX J 189 1555 1555 1.33
LINK C KCX J 189 N ASP J 190 1555 1555 1.33
LINK OQ2 KCX A 189 MG MG A 445 1555 1555 2.00
LINK OD1 ASP A 191 MG MG A 445 1555 1555 2.01
LINK OE1 GLU A 192 MG MG A 445 1555 1555 1.97
LINK OQ2 KCX B 189 MG MG B 445 1555 1555 2.01
LINK OD1 ASP B 191 MG MG B 445 1555 1555 1.97
LINK OE1 GLU B 192 MG MG B 445 1555 1555 2.02
LINK OQ2 KCX C 189 MG MG C 445 1555 1555 1.94
LINK OD1 ASP C 191 MG MG C 445 1555 1555 1.94
LINK OE1 GLU C 192 MG MG C 445 1555 1555 2.08
LINK OQ2 KCX D 189 MG MG D 445 1555 1555 1.91
LINK OD1 ASP D 191 MG MG D 445 1555 1555 1.90
LINK OE1 GLU D 192 MG MG D 445 1555 1555 2.14
LINK OQ2 KCX E 189 MG MG E 445 1555 1555 2.06
LINK OD2 ASP E 191 MG MG E 445 1555 1555 2.25
LINK OE1 GLU E 192 MG MG E 445 1555 1555 2.17
LINK OD1 ASP F 191 MG MG F 445 1555 1555 2.01
LINK OE1 GLU F 192 MG MG F 445 1555 1555 1.99
LINK OQ2 KCX G 189 MG MG G 445 1555 1555 2.07
LINK OD2 ASP G 191 MG MG G 445 1555 1555 2.43
LINK OE1 GLU G 192 MG MG G 445 1555 1555 2.06
LINK OQ2 KCX H 189 MG MG H 445 1555 1555 2.22
LINK OE1 GLU H 192 MG MG H 445 1555 1555 2.07
LINK OQ2 KCX I 189 MG MG I 445 1555 1555 1.94
LINK OD1 ASP I 191 MG MG I 445 1555 1555 1.96
LINK OE1 GLU I 192 MG MG I 445 1555 1555 2.00
LINK OQ2 KCX J 189 MG MG J 445 1555 1555 2.08
LINK OD1 ASP J 191 MG MG J 445 1555 1555 2.18
LINK OE1 GLU J 192 MG MG J 445 1555 1555 2.00
LINK MG MG A 445 O3 CAP A 446 1555 1555 2.14
LINK MG MG A 445 O2 CAP A 446 1555 1555 2.38
LINK MG MG A 445 O7 CAP A 446 1555 1555 1.92
LINK MG MG B 445 O7 CAP B 446 1555 1555 2.02
LINK MG MG B 445 O2 CAP B 446 1555 1555 2.19
LINK MG MG B 445 O3 CAP B 446 1555 1555 2.11
LINK MG MG C 445 O2 CAP C 446 1555 1555 2.38
LINK MG MG C 445 O7 CAP C 446 1555 1555 1.84
LINK MG MG C 445 O3 CAP C 446 1555 1555 2.14
LINK MG MG D 445 O2 CAP D 446 1555 1555 2.29
LINK MG MG D 445 O3 CAP D 446 1555 1555 2.11
LINK MG MG D 445 O7 CAP D 446 1555 1555 2.18
LINK MG MG E 445 O3 CAP E 446 1555 1555 2.04
LINK MG MG E 445 O2 CAP E 446 1555 1555 2.20
LINK MG MG E 445 O7 CAP E 446 1555 1555 1.79
LINK MG MG F 445 O3 CAP F 446 1555 1555 2.21
LINK MG MG F 445 O7 CAP F 446 1555 1555 2.19
LINK MG MG F 445 O2 CAP F 446 1555 1555 2.36
LINK MG MG G 445 O7 CAP G 446 1555 1555 2.09
LINK MG MG G 445 O2 CAP G 446 1555 1555 2.32
LINK MG MG G 445 O3 CAP G 446 1555 1555 2.19
LINK MG MG H 445 O7 CAP H 446 1555 1555 1.98
LINK MG MG H 445 O2 CAP H 446 1555 1555 2.36
LINK MG MG H 445 O3 CAP H 446 1555 1555 2.30
LINK MG MG I 445 O2 CAP I 446 1555 1555 2.28
LINK MG MG I 445 O3 CAP I 446 1555 1555 2.13
LINK MG MG I 445 O7 CAP I 446 1555 1555 2.09
LINK MG MG J 445 O3 CAP J 446 1555 1555 2.08
LINK MG MG J 445 O2 CAP J 446 1555 1555 2.32
LINK OQ2 KCX F 189 MG MG F 445 1555 1555 1.71
LINK MG MG J 445 O7 CAP J 446 1555 1555 1.72
LINK OD2 ASP H 191 MG MG H 445 1555 1555 2.73
LINK OD1 ASP H 191 MG MG H 445 1555 1555 2.94
CISPEP 1 LYS A 163 PRO A 164 0 6.12
CISPEP 2 LYS B 163 PRO B 164 0 5.42
CISPEP 3 LYS C 163 PRO C 164 0 5.75
CISPEP 4 LYS D 163 PRO D 164 0 8.10
CISPEP 5 LYS E 163 PRO E 164 0 3.07
CISPEP 6 LYS F 163 PRO F 164 0 8.05
CISPEP 7 LYS G 163 PRO G 164 0 4.80
CISPEP 8 LYS H 163 PRO H 164 0 4.80
CISPEP 9 LYS I 163 PRO I 164 0 5.67
CISPEP 10 LYS J 163 PRO J 164 0 5.36
SITE 1 AC1 5 KCX A 189 ASP A 191 GLU A 192 CAP A 446
SITE 2 AC1 5 ASN C 111
SITE 1 AC2 30 VAL A 161 LYS A 163 LYS A 165 KCX A 189
SITE 2 AC2 30 ASP A 191 GLU A 192 HIS A 281 ARG A 282
SITE 3 AC2 30 HIS A 314 LYS A 322 LEU A 323 SER A 367
SITE 4 AC2 30 GLY A 368 GLY A 369 GLN A 389 GLY A 391
SITE 5 AC2 30 GLY A 392 MG A 445 HOH A 521 HOH A 523
SITE 6 AC2 30 HOH A 528 HOH A 574 HOH A 579 HOH A 615
SITE 7 AC2 30 HOH A 626 HOH A 684 GLU C 49 THR C 54
SITE 8 AC2 30 TRP C 55 ASN C 111
SITE 1 AC3 5 ASN B 111 KCX B 189 ASP B 191 GLU B 192
SITE 2 AC3 5 CAP B 446
SITE 1 AC4 29 GLU B 49 TRP B 55 ASN B 111 LYS B 163
SITE 2 AC4 29 LYS B 165 KCX B 189 ASP B 191 GLU B 192
SITE 3 AC4 29 HIS B 281 ARG B 282 HIS B 314 LYS B 322
SITE 4 AC4 29 LEU B 323 SER B 367 GLY B 368 GLY B 369
SITE 5 AC4 29 GLN B 389 GLY B 391 GLY B 392 MG B 445
SITE 6 AC4 29 HOH B 519 HOH B 521 HOH B 542 HOH B 551
SITE 7 AC4 29 HOH B 556 HOH B 559 HOH B 692 HOH B 712
SITE 8 AC4 29 HOH B 713
SITE 1 AC5 4 KCX C 189 ASP C 191 GLU C 192 CAP C 446
SITE 1 AC6 28 GLU A 49 TRP A 55 ASN A 111 HOH A 611
SITE 2 AC6 28 LYS C 163 LYS C 165 KCX C 189 ASP C 191
SITE 3 AC6 28 GLU C 192 HIS C 281 ARG C 282 HIS C 314
SITE 4 AC6 28 LYS C 322 LEU C 323 SER C 367 GLY C 368
SITE 5 AC6 28 GLY C 369 GLN C 389 GLY C 391 GLY C 392
SITE 6 AC6 28 MG C 445 HOH C 524 HOH C 528 HOH C 557
SITE 7 AC6 28 HOH C 562 HOH C 591 HOH C 658 HOH C 740
SITE 1 AC7 4 KCX D 189 ASP D 191 GLU D 192 CAP D 446
SITE 1 AC8 28 LYS D 163 LYS D 165 KCX D 189 ASP D 191
SITE 2 AC8 28 GLU D 192 HIS D 281 ARG D 282 HIS D 314
SITE 3 AC8 28 LYS D 322 LEU D 323 SER D 367 GLY D 368
SITE 4 AC8 28 GLY D 369 GLN D 389 GLY D 391 GLY D 392
SITE 5 AC8 28 MG D 445 HOH D 515 HOH D 519 HOH D 524
SITE 6 AC8 28 HOH D 537 HOH D 538 HOH D 539 HOH D 665
SITE 7 AC8 28 HOH D 716 GLU E 49 TRP E 55 ASN E 111
SITE 1 AC9 4 KCX E 189 ASP E 191 GLU E 192 CAP E 446
SITE 1 BC1 28 GLU D 49 TRP D 55 ASN D 111 HOH D 682
SITE 2 BC1 28 LYS E 163 LYS E 165 KCX E 189 ASP E 191
SITE 3 BC1 28 GLU E 192 HIS E 281 ARG E 282 HIS E 314
SITE 4 BC1 28 LYS E 322 LEU E 323 SER E 367 GLY E 368
SITE 5 BC1 28 GLY E 369 GLN E 389 GLY E 391 GLY E 392
SITE 6 BC1 28 MG E 445 HOH E 525 HOH E 532 HOH E 543
SITE 7 BC1 28 HOH E 570 HOH E 574 HOH E 580 HOH E 608
SITE 1 BC2 4 KCX F 189 ASP F 191 GLU F 192 CAP F 446
SITE 1 BC3 27 LYS F 163 LYS F 165 KCX F 189 ASP F 191
SITE 2 BC3 27 GLU F 192 HIS F 281 ARG F 282 HIS F 314
SITE 3 BC3 27 LYS F 322 LEU F 323 SER F 367 GLY F 368
SITE 4 BC3 27 GLY F 369 GLN F 389 GLY F 391 GLY F 392
SITE 5 BC3 27 MG F 445 HOH F 519 HOH F 525 HOH F 536
SITE 6 BC3 27 HOH F 537 HOH F 556 GLU H 49 THR H 54
SITE 7 BC3 27 TRP H 55 ASN H 111 HOH H 513
SITE 1 BC4 4 KCX G 189 ASP G 191 GLU G 192 CAP G 446
SITE 1 BC5 29 GLU G 49 TRP G 55 ASN G 111 LYS G 163
SITE 2 BC5 29 LYS G 165 KCX G 189 ASP G 191 GLU G 192
SITE 3 BC5 29 HIS G 281 ARG G 282 HIS G 314 LYS G 322
SITE 4 BC5 29 LEU G 323 SER G 367 GLY G 368 GLY G 369
SITE 5 BC5 29 GLN G 389 GLY G 391 GLY G 392 MG G 445
SITE 6 BC5 29 HOH G 507 HOH G 524 HOH G 529 HOH G 536
SITE 7 BC5 29 HOH G 540 HOH G 561 HOH G 574 HOH G 602
SITE 8 BC5 29 HOH G 607
SITE 1 BC6 7 ASN F 111 LYS H 163 LYS H 165 KCX H 189
SITE 2 BC6 7 ASP H 191 GLU H 192 CAP H 446
SITE 1 BC7 28 GLU F 49 TRP F 55 ASN F 111 LYS H 163
SITE 2 BC7 28 LYS H 165 KCX H 189 ASP H 191 GLU H 192
SITE 3 BC7 28 HIS H 281 ARG H 282 HIS H 314 LYS H 322
SITE 4 BC7 28 LEU H 323 SER H 367 GLY H 368 GLY H 369
SITE 5 BC7 28 GLN H 389 GLY H 391 GLY H 392 MG H 445
SITE 6 BC7 28 HOH H 520 HOH H 547 HOH H 571 HOH H 584
SITE 7 BC7 28 HOH H 595 HOH H 601 HOH H 604 HOH H 613
SITE 1 BC8 4 KCX I 189 ASP I 191 GLU I 192 CAP I 446
SITE 1 BC9 28 LYS I 163 LYS I 165 KCX I 189 ASP I 191
SITE 2 BC9 28 GLU I 192 HIS I 281 ARG I 282 HIS I 314
SITE 3 BC9 28 LYS I 322 LEU I 323 SER I 367 GLY I 368
SITE 4 BC9 28 GLY I 369 GLN I 389 GLY I 391 GLY I 392
SITE 5 BC9 28 MG I 445 HOH I 515 HOH I 518 HOH I 521
SITE 6 BC9 28 HOH I 525 HOH I 531 HOH I 616 HOH I 662
SITE 7 BC9 28 HOH I 744 GLU J 49 TRP J 55 ASN J 111
SITE 1 CC1 6 ASN I 111 LYS J 163 KCX J 189 ASP J 191
SITE 2 CC1 6 GLU J 192 CAP J 446
SITE 1 CC2 28 GLU I 49 TRP I 55 ASN I 111 HOH I 603
SITE 2 CC2 28 LYS J 163 LYS J 165 KCX J 189 ASP J 191
SITE 3 CC2 28 GLU J 192 HIS J 281 ARG J 282 HIS J 314
SITE 4 CC2 28 LYS J 322 LEU J 323 SER J 367 GLY J 368
SITE 5 CC2 28 GLY J 369 GLN J 389 GLY J 391 GLY J 392
SITE 6 CC2 28 MG J 445 HOH J 502 HOH J 546 HOH J 566
SITE 7 CC2 28 HOH J 580 HOH J 586 HOH J 587 HOH J 633
CRYST1 173.287 246.377 144.589 90.00 90.00 90.00 P 21 21 2 40
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 0.005771 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004059 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006916 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
