HEADER LYASE 23-OCT-09 3KDN
TITLE CRYSTAL STRUCTURE OF TYPE III RUBISCO SP4 MUTANT 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;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARAENSIS;
SOURCE 3 ORGANISM_TAXID: 69014;
SOURCE 4 STRAIN: KOD1;
SOURCE 5 GENE: RBCL, TK2290;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS RIBULOSE-1, 5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, CARBON
KEYWDS 2 DIOXIDE FIXATION, LYASE, MAGNESIUM, METAL-BINDING, MONOOXYGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI
REVDAT 5 22-NOV-23 3KDN 1 REMARK
REVDAT 4 01-NOV-23 3KDN 1 REMARK
REVDAT 3 10-NOV-21 3KDN 1 REMARK SEQADV LINK
REVDAT 2 02-FEB-11 3KDN 1 JRNL
REVDAT 1 06-OCT-10 3KDN 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. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 327701
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 17388
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) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17951
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 954
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 34127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 2652
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07000
REMARK 3 B22 (A**2) : -1.66000
REMARK 3 B33 (A**2) : -0.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.808
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 35203 ; 0.004 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47816 ; 0.768 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4361 ; 4.696 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1607 ;28.021 ;23.441
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5593 ;12.054 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 229 ;17.064 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5093 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27095 ; 0.003 ; 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): 21685 ; 0.294 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34534 ; 0.562 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13518 ; 0.786 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13282 ; 1.344 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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 : 1.20
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 3KDN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055860.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 345208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 (%): 60.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 80MM CACL2, 6% 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 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 123.12050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 125400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -386.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 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 THR B 7
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 THR C 7
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 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 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 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 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 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 TYR A 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 10 CG OD1 OD2
REMARK 470 TYR A 11 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 TYR A 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 18 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLU A 35 CG CD OE1 OE2
REMARK 470 LEU A 58 CG CD1 CD2
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 ARG A 117 CG CD NE CZ NH1 NH2
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 LYS A 211 CG CD CE NZ
REMARK 470 ASP A 345 CG OD1 OD2
REMARK 470 GLU A 346 CG CD OE1 OE2
REMARK 470 GLN A 376 CG CD OE1 NE2
REMARK 470 LEU A 421 CG CD1 CD2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 LYS A 426 CG CD CE NZ
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 GLU A 436 CG CD OE1 OE2
REMARK 470 ILE B 8 CG1 CG2 CD1
REMARK 470 ASP B 10 CG OD1 OD2
REMARK 470 GLU B 18 CG CD OE1 OE2
REMARK 470 LEU B 58 CG CD1 CD2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 153 CG CD CE NZ
REMARK 470 GLU B 346 CG CD OE1 OE2
REMARK 470 GLU B 380 CG CD OE1 OE2
REMARK 470 ASP C 10 CG OD1 OD2
REMARK 470 GLU C 65 CG CD OE1 OE2
REMARK 470 LYS C 153 CG CD CE NZ
REMARK 470 LYS C 175 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 GLU C 436 CG CD OE1 OE2
REMARK 470 ILE D 8 CG1 CG2 CD1
REMARK 470 ASP D 10 CG OD1 OD2
REMARK 470 GLU D 18 CG CD OE1 OE2
REMARK 470 LYS D 21 CG CD CE NZ
REMARK 470 GLU D 65 CG CD OE1 OE2
REMARK 470 LYS D 153 CG CD CE NZ
REMARK 470 GLU D 203 CG CD OE1 OE2
REMARK 470 GLU D 346 CG CD OE1 OE2
REMARK 470 GLU D 423 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 LEU E 58 CG CD1 CD2
REMARK 470 GLU E 144 CG CD OE1 OE2
REMARK 470 LYS E 211 CG CD CE NZ
REMARK 470 GLU E 346 CG CD OE1 OE2
REMARK 470 GLN E 376 CG CD OE1 NE2
REMARK 470 GLU E 423 CG CD OE1 OE2
REMARK 470 LYS E 426 CG CD CE NZ
REMARK 470 LYS E 429 CG CD CE NZ
REMARK 470 VAL E 441 CG1 CG2
REMARK 470 ILE F 8 CG1 CG2 CD1
REMARK 470 ASP F 10 CG OD1 OD2
REMARK 470 GLU F 18 CG CD OE1 OE2
REMARK 470 LEU F 58 CG CD1 CD2
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 153 CG CD CE NZ
REMARK 470 GLU F 203 CG CD OE1 OE2
REMARK 470 ASN F 218 CG OD1 ND2
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 429 CG CD CE NZ
REMARK 470 ILE G 8 CG1 CG2 CD1
REMARK 470 ASP G 10 CG OD1 OD2
REMARK 470 GLU G 18 CG CD OE1 OE2
REMARK 470 GLU G 144 CG CD OE1 OE2
REMARK 470 GLU G 203 CG CD OE1 OE2
REMARK 470 GLU G 380 CG CD OE1 OE2
REMARK 470 LYS G 429 CG CD CE NZ
REMARK 470 THR H 7 OG1 CG2
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 ASN H 218 CG OD1 ND2
REMARK 470 GLU H 324 CG CD OE1 OE2
REMARK 470 GLU H 326 CG CD OE1 OE2
REMARK 470 ASP H 328 CG OD1 OD2
REMARK 470 GLU H 346 CG CD OE1 OE2
REMARK 470 GLU H 380 CG CD OE1 OE2
REMARK 470 GLN H 417 CG CD OE1 NE2
REMARK 470 LEU H 421 CG CD1 CD2
REMARK 470 ASP H 422 CG OD1 OD2
REMARK 470 GLU H 423 CG CD OE1 OE2
REMARK 470 LYS H 426 CG CD CE NZ
REMARK 470 LYS H 429 CG CD CE NZ
REMARK 470 GLU H 436 CG CD OE1 OE2
REMARK 470 VAL H 441 CG1 CG2
REMARK 470 ASP I 10 CG OD1 OD2
REMARK 470 LEU I 58 CG CD1 CD2
REMARK 470 GLU I 65 CG CD OE1 OE2
REMARK 470 GLU I 144 CG CD OE1 OE2
REMARK 470 LYS I 211 CG CD CE NZ
REMARK 470 GLU I 346 CG CD OE1 OE2
REMARK 470 GLU I 423 CG CD OE1 OE2
REMARK 470 LYS I 429 CG CD CE NZ
REMARK 470 ILE J 8 CG1 CG2 CD1
REMARK 470 GLU J 144 CG CD OE1 OE2
REMARK 470 LYS J 153 CG CD CE NZ
REMARK 470 GLU J 346 CG CD OE1 OE2
REMARK 470 GLU J 380 CG CD OE1 OE2
REMARK 470 GLU J 423 CG CD OE1 OE2
REMARK 470 LYS J 426 CG CD CE NZ
REMARK 470 LYS J 429 CG CD CE NZ
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 ASP A 14 82.72 -152.62
REMARK 500 ALA A 34 -173.26 -63.04
REMARK 500 SER A 51 -104.05 -150.05
REMARK 500 ASP A 82 16.66 -143.61
REMARK 500 ARG A 117 -9.52 -50.08
REMARK 500 ASP A 154 -56.11 -122.21
REMARK 500 THR A 195 -110.96 -111.13
REMARK 500 ASN A 200 87.08 -161.91
REMARK 500 ALA A 232 -170.22 -176.65
REMARK 500 ALA A 283 128.13 -32.40
REMARK 500 MET A 284 -18.27 94.66
REMARK 500 TYR A 357 -110.99 56.54
REMARK 500 ILE A 359 108.25 -58.53
REMARK 500 ASN A 374 18.05 -149.57
REMARK 500 LYS A 426 10.94 -59.39
REMARK 500 THR A 427 -0.24 -146.42
REMARK 500 HIS A 440 27.52 -140.15
REMARK 500 SER B 51 -94.36 -135.36
REMARK 500 PRO B 60 93.67 -66.13
REMARK 500 ALA B 109 35.94 -144.77
REMARK 500 THR B 195 -107.21 -112.61
REMARK 500 SER B 196 57.90 -140.96
REMARK 500 ASN B 200 85.98 -164.54
REMARK 500 ALA B 232 -178.20 -175.91
REMARK 500 MET B 284 -16.35 96.18
REMARK 500 TYR B 357 -115.89 52.02
REMARK 500 SER C 51 -93.27 -134.04
REMARK 500 THR C 195 -111.41 -114.74
REMARK 500 ASN C 200 85.51 -160.03
REMARK 500 ALA C 232 -170.58 -178.51
REMARK 500 MET C 284 -17.74 95.81
REMARK 500 TYR C 357 -118.97 49.10
REMARK 500 SER D 51 -112.42 -135.10
REMARK 500 PRO D 60 81.49 -66.97
REMARK 500 ALA D 109 35.62 -144.92
REMARK 500 THR D 195 -113.35 -113.65
REMARK 500 ASN D 200 84.71 -159.97
REMARK 500 ALA D 232 -173.21 -172.52
REMARK 500 MET D 284 -19.77 95.85
REMARK 500 TYR D 357 -111.96 53.44
REMARK 500 SER E 51 -90.18 -134.43
REMARK 500 ALA E 109 37.27 -144.14
REMARK 500 ASP E 154 -56.63 -124.56
REMARK 500 THR E 195 -112.25 -114.04
REMARK 500 ASN E 200 80.14 -158.57
REMARK 500 ALA E 232 -171.99 -179.68
REMARK 500 MET E 284 -20.15 100.43
REMARK 500 TYR E 357 -113.17 51.06
REMARK 500 PRO E 420 134.68 -36.24
REMARK 500 ASP F 14 87.72 -150.25
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 189 OQ2
REMARK 620 2 ASP A 191 OD1 89.1
REMARK 620 3 GLU A 192 OE1 97.9 95.7
REMARK 620 4 CAP A 600 O3 86.7 173.2 90.2
REMARK 620 5 CAP A 600 O2 85.8 96.8 167.0 77.5
REMARK 620 6 CAP A 600 O7 157.9 99.1 101.6 83.0 72.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 189 OQ2
REMARK 620 2 ASP B 191 OD1 94.2
REMARK 620 3 GLU B 192 OE1 92.7 78.3
REMARK 620 4 CAP B 600 O3 80.7 171.2 94.6
REMARK 620 5 CAP B 600 O7 169.7 95.5 92.4 90.0
REMARK 620 6 CAP B 600 O2 97.9 111.2 165.0 76.9 75.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 189 OQ2
REMARK 620 2 ASP C 191 OD1 88.8
REMARK 620 3 GLU C 192 OE1 89.9 90.5
REMARK 620 4 CAP C 600 O2 93.2 105.9 163.3
REMARK 620 5 CAP C 600 O7 168.4 98.3 99.2 76.0
REMARK 620 6 CAP C 600 O3 83.0 171.7 89.6 74.5 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 189 OQ2
REMARK 620 2 ASP D 191 OD1 89.2
REMARK 620 3 GLU D 192 OE1 93.2 90.1
REMARK 620 4 CAP D 600 O3 86.1 175.3 89.9
REMARK 620 5 CAP D 600 O2 93.8 102.7 165.5 77.9
REMARK 620 6 CAP D 600 O7 168.8 97.3 95.9 87.3 75.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 189 OQ2
REMARK 620 2 ASP E 191 OD1 86.3
REMARK 620 3 GLU E 192 OE1 83.8 83.7
REMARK 620 4 CAP E 600 O3 89.4 171.1 88.1
REMARK 620 5 CAP E 600 O2 96.6 107.5 168.8 80.8
REMARK 620 6 CAP E 600 O7 176.9 95.2 99.0 89.5 80.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX F 189 OQ2
REMARK 620 2 ASP F 191 OD1 85.9
REMARK 620 3 GLU F 192 OE1 88.6 86.5
REMARK 620 4 CAP F 600 O3 86.7 171.6 89.2
REMARK 620 5 CAP F 600 O2 92.0 109.0 164.4 75.3
REMARK 620 6 CAP F 600 O7 166.3 100.1 104.0 88.0 74.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX G 189 OQ2
REMARK 620 2 ASP G 191 OD1 86.2
REMARK 620 3 GLU G 192 OE1 92.4 94.7
REMARK 620 4 CAP G 600 O3 88.2 173.9 83.1
REMARK 620 5 CAP G 600 O7 163.6 96.4 103.5 89.7
REMARK 620 6 CAP G 600 O2 86.3 104.0 161.1 78.0 77.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 189 OQ2
REMARK 620 2 ASP H 191 OD2 103.2
REMARK 620 3 GLU H 192 OE1 88.5 71.7
REMARK 620 4 CAP H 600 O2 101.6 116.0 164.8
REMARK 620 5 CAP H 600 O7 167.4 89.2 93.2 74.5
REMARK 620 6 CAP H 600 O3 87.4 158.7 90.3 79.0 80.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX I 189 OQ2
REMARK 620 2 ASP I 191 OD1 89.8
REMARK 620 3 GLU I 192 OE1 92.3 88.4
REMARK 620 4 CAP I 600 O2 97.6 104.6 163.6
REMARK 620 5 CAP I 600 O3 91.2 175.8 87.5 79.3
REMARK 620 6 CAP I 600 O7 171.3 95.6 94.7 74.4 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX J 189 OQ2
REMARK 620 2 ASP J 191 OD2 85.8
REMARK 620 3 GLU J 192 OE1 85.0 86.2
REMARK 620 4 CAP J 600 O3 83.3 166.6 85.1
REMARK 620 5 CAP J 600 O2 90.2 110.7 162.1 77.3
REMARK 620 6 CAP J 600 O7 169.1 101.3 103.6 90.6 79.6
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 600
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: 3KBO RELATED DB: PDB
REMARK 900 RELATED ID: 3A12 RELATED DB: PDB
REMARK 900 RELATED ID: 3A13 RELATED DB: PDB
DBREF 3KDN A 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN B 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN C 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN D 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN E 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN F 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN G 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN H 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN I 1 444 UNP O93627 RBL_PYRKO 1 444
DBREF 3KDN J 1 444 UNP O93627 RBL_PYRKO 1 444
SEQADV 3KDN GLU A 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG A 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP A 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE A 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR A 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU B 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG B 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP B 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE B 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR B 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU C 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG C 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP C 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE C 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR C 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU D 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG D 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP D 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE D 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR D 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU E 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG E 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP E 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE E 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR E 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU F 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG F 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP F 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE F 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR F 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU G 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG G 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP G 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE G 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR G 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU H 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG H 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP H 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE H 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR H 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU I 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG I 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP I 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE I 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR I 330 UNP O93627 VAL 330 ENGINEERED MUTATION
SEQADV 3KDN GLU J 326 UNP O93627 GLY 326 ENGINEERED MUTATION
SEQADV 3KDN ARG J 327 UNP O93627 LYS 327 ENGINEERED MUTATION
SEQADV 3KDN ASP J 328 UNP O93627 TRP 328 ENGINEERED MUTATION
SEQADV 3KDN ILE J 329 UNP O93627 ASP 329 ENGINEERED MUTATION
SEQADV 3KDN THR J 330 UNP O93627 VAL 330 ENGINEERED MUTATION
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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 GLU ARG ASP ILE THR 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 3KDN KCX A 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX B 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX C 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX D 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX E 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX F 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX G 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX H 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN KCX I 189 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3KDN 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 500 1
HET CAP A 600 21
HET MG B 500 1
HET CAP B 600 21
HET MG C 500 1
HET CAP C 600 21
HET MG D 500 1
HET CAP D 600 21
HET MG E 500 1
HET CAP E 600 21
HET MG F 500 1
HET CAP F 600 21
HET MG G 500 1
HET CAP G 600 21
HET MG H 500 1
HET CAP H 600 21
HET MG I 500 1
HET CAP I 600 21
HET MG J 500 1
HET CAP J 600 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 *2652(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 SER A 71 1 9
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 GLY A 248 1 16
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 GLU A 326 GLU A 339 1 14
HELIX 17 17 ILE A 375 GLY A 383 1 9
HELIX 18 18 GLY A 391 GLY A 396 1 6
HELIX 19 19 GLY A 400 MET A 416 1 17
HELIX 20 20 PRO A 420 LYS A 426 1 7
HELIX 21 21 HIS A 428 GLY A 439 1 12
HELIX 22 22 ILE B 8 VAL B 13 5 6
HELIX 23 23 THR B 38 SER B 50 1 13
HELIX 24 24 GLU B 63 SER B 71 1 9
HELIX 25 25 HIS B 94 PHE B 96 5 3
HELIX 26 26 ASN B 100 ALA B 109 1 10
HELIX 27 27 GLY B 110 MET B 115 5 6
HELIX 28 28 PRO B 129 ARG B 134 1 6
HELIX 29 29 PHE B 141 GLU B 151 1 11
HELIX 30 30 SER B 169 ASN B 183 1 15
HELIX 31 31 ARG B 201 GLY B 221 1 21
HELIX 32 32 ASP B 233 LEU B 247 1 15
HELIX 33 33 VAL B 256 GLY B 260 1 5
HELIX 34 34 GLY B 260 TYR B 274 1 15
HELIX 35 35 HIS B 285 ARG B 290 1 6
HELIX 36 36 SER B 297 GLY B 309 1 13
HELIX 37 37 GLU B 326 GLU B 339 1 14
HELIX 38 38 ILE B 375 GLY B 383 1 9
HELIX 39 39 GLY B 391 GLY B 396 1 6
HELIX 40 40 GLY B 400 GLY B 418 1 19
HELIX 41 41 PRO B 420 ALA B 425 1 6
HELIX 42 42 HIS B 428 GLY B 439 1 12
HELIX 43 43 ILE C 8 VAL C 13 5 6
HELIX 44 44 THR C 38 SER C 50 1 13
HELIX 45 45 GLU C 63 LEU C 70 1 8
HELIX 46 46 HIS C 94 PHE C 96 5 3
HELIX 47 47 ASN C 100 ALA C 109 1 10
HELIX 48 48 GLY C 110 MET C 115 5 6
HELIX 49 49 PRO C 129 ARG C 134 1 6
HELIX 50 50 PHE C 141 GLU C 151 1 11
HELIX 51 51 SER C 169 ASN C 183 1 15
HELIX 52 52 ARG C 201 GLY C 221 1 21
HELIX 53 53 ASP C 233 GLY C 248 1 16
HELIX 54 54 VAL C 256 GLY C 260 1 5
HELIX 55 55 GLY C 260 TYR C 274 1 15
HELIX 56 56 HIS C 285 ARG C 290 1 6
HELIX 57 57 SER C 297 GLY C 309 1 13
HELIX 58 58 GLU C 326 GLU C 339 1 14
HELIX 59 59 HIS C 371 ASN C 374 5 4
HELIX 60 60 ILE C 375 GLY C 383 1 9
HELIX 61 61 GLY C 391 GLY C 396 1 6
HELIX 62 62 GLY C 400 GLN C 417 1 18
HELIX 63 63 PRO C 420 LYS C 426 1 7
HELIX 64 64 HIS C 428 GLY C 439 1 12
HELIX 65 65 TYR D 9 VAL D 13 5 5
HELIX 66 66 THR D 38 SER D 50 1 13
HELIX 67 67 GLU D 63 SER D 71 1 9
HELIX 68 68 HIS D 94 PHE D 96 5 3
HELIX 69 69 ASN D 100 ALA D 109 1 10
HELIX 70 70 GLY D 110 MET D 115 5 6
HELIX 71 71 PRO D 129 ARG D 134 1 6
HELIX 72 72 PHE D 141 GLU D 151 1 11
HELIX 73 73 SER D 169 ASN D 183 1 15
HELIX 74 74 ARG D 201 GLY D 221 1 21
HELIX 75 75 ASP D 233 GLY D 248 1 16
HELIX 76 76 VAL D 256 GLY D 260 1 5
HELIX 77 77 GLY D 260 TYR D 274 1 15
HELIX 78 78 HIS D 285 ARG D 290 1 6
HELIX 79 79 SER D 297 GLY D 309 1 13
HELIX 80 80 GLU D 326 GLU D 339 1 14
HELIX 81 81 HIS D 371 ASN D 374 5 4
HELIX 82 82 ILE D 375 GLY D 383 1 9
HELIX 83 83 GLY D 391 GLY D 396 1 6
HELIX 84 84 GLY D 400 GLY D 418 1 19
HELIX 85 85 PRO D 420 ALA D 425 1 6
HELIX 86 86 HIS D 428 GLY D 439 1 12
HELIX 87 87 ILE E 8 VAL E 13 5 6
HELIX 88 88 THR E 38 SER E 50 1 13
HELIX 89 89 GLU E 63 SER E 71 1 9
HELIX 90 90 HIS E 94 PHE E 96 5 3
HELIX 91 91 ASN E 100 ALA E 109 1 10
HELIX 92 92 GLY E 110 MET E 115 5 6
HELIX 93 93 PRO E 129 ARG E 134 1 6
HELIX 94 94 PHE E 141 GLU E 151 1 11
HELIX 95 95 SER E 169 ASN E 183 1 15
HELIX 96 96 ARG E 201 GLY E 221 1 21
HELIX 97 97 ASP E 233 LEU E 247 1 15
HELIX 98 98 VAL E 256 GLY E 260 1 5
HELIX 99 99 GLY E 260 GLY E 275 1 16
HELIX 100 100 HIS E 285 ARG E 290 1 6
HELIX 101 101 SER E 297 GLY E 309 1 13
HELIX 102 102 GLU E 326 GLU E 339 1 14
HELIX 103 103 ASN E 374 GLY E 383 1 10
HELIX 104 104 GLY E 391 GLY E 396 1 6
HELIX 105 105 GLY E 400 GLN E 417 1 18
HELIX 106 106 PRO E 420 LYS E 426 1 7
HELIX 107 107 HIS E 428 GLY E 439 1 12
HELIX 108 108 TYR F 9 VAL F 13 5 5
HELIX 109 109 THR F 38 SER F 50 1 13
HELIX 110 110 GLU F 63 LEU F 70 1 8
HELIX 111 111 HIS F 94 PHE F 96 5 3
HELIX 112 112 ASN F 100 ALA F 109 1 10
HELIX 113 113 GLY F 110 MET F 115 5 6
HELIX 114 114 PRO F 129 ARG F 134 1 6
HELIX 115 115 PHE F 141 GLU F 151 1 11
HELIX 116 116 SER F 169 ASN F 183 1 15
HELIX 117 117 ARG F 201 GLY F 221 1 21
HELIX 118 118 ASP F 233 LEU F 247 1 15
HELIX 119 119 VAL F 256 GLY F 260 1 5
HELIX 120 120 GLY F 260 TYR F 274 1 15
HELIX 121 121 HIS F 285 ARG F 290 1 6
HELIX 122 122 SER F 297 GLY F 309 1 13
HELIX 123 123 GLU F 326 GLU F 339 1 14
HELIX 124 124 HIS F 371 ASN F 374 5 4
HELIX 125 125 ILE F 375 GLY F 383 1 9
HELIX 126 126 GLY F 391 GLY F 396 1 6
HELIX 127 127 GLY F 400 GLN F 417 1 18
HELIX 128 128 PRO F 420 LYS F 426 1 7
HELIX 129 129 HIS F 428 GLY F 439 1 12
HELIX 130 130 ILE G 8 VAL G 13 5 6
HELIX 131 131 THR G 38 SER G 50 1 13
HELIX 132 132 GLU G 63 SER G 71 1 9
HELIX 133 133 HIS G 94 PHE G 96 5 3
HELIX 134 134 ASN G 100 ALA G 109 1 10
HELIX 135 135 GLY G 110 MET G 115 5 6
HELIX 136 136 PRO G 129 ARG G 134 1 6
HELIX 137 137 PHE G 141 GLU G 151 1 11
HELIX 138 138 SER G 169 ASN G 183 1 15
HELIX 139 139 ARG G 201 GLY G 221 1 21
HELIX 140 140 ASP G 233 LEU G 247 1 15
HELIX 141 141 VAL G 256 GLY G 260 1 5
HELIX 142 142 GLY G 260 TYR G 274 1 15
HELIX 143 143 HIS G 285 ARG G 290 1 6
HELIX 144 144 SER G 297 GLY G 309 1 13
HELIX 145 145 GLU G 326 GLU G 339 1 14
HELIX 146 146 HIS G 371 ASN G 374 5 4
HELIX 147 147 ILE G 375 GLY G 383 1 9
HELIX 148 148 GLY G 391 GLY G 396 1 6
HELIX 149 149 GLY G 400 GLY G 418 1 19
HELIX 150 150 PRO G 420 ALA G 425 1 6
HELIX 151 151 HIS G 428 GLY G 439 1 12
HELIX 152 152 THR H 7 VAL H 13 5 7
HELIX 153 153 THR H 38 SER H 50 1 13
HELIX 154 154 GLU H 63 SER H 71 1 9
HELIX 155 155 HIS H 94 PHE H 96 5 3
HELIX 156 156 ASN H 100 ALA H 109 1 10
HELIX 157 157 GLY H 110 MET H 115 5 6
HELIX 158 158 PRO H 129 ARG H 134 1 6
HELIX 159 159 PHE H 141 GLU H 151 1 11
HELIX 160 160 SER H 169 ASN H 183 1 15
HELIX 161 161 ARG H 201 GLY H 221 1 21
HELIX 162 162 ASP H 233 LEU H 247 1 15
HELIX 163 163 VAL H 256 GLY H 260 1 5
HELIX 164 164 GLY H 260 TYR H 274 1 15
HELIX 165 165 HIS H 285 ARG H 290 1 6
HELIX 166 166 SER H 297 GLY H 309 1 13
HELIX 167 167 GLU H 326 GLU H 339 1 14
HELIX 168 168 ILE H 375 GLY H 383 1 9
HELIX 169 169 GLY H 391 GLY H 396 1 6
HELIX 170 170 GLY H 400 GLN H 417 1 18
HELIX 171 171 PRO H 420 LYS H 426 1 7
HELIX 172 172 HIS H 428 GLY H 439 1 12
HELIX 173 173 TYR I 9 VAL I 13 5 5
HELIX 174 174 THR I 38 SER I 50 1 13
HELIX 175 175 GLU I 63 SER I 71 1 9
HELIX 176 176 HIS I 94 PHE I 96 5 3
HELIX 177 177 ASN I 100 ALA I 109 1 10
HELIX 178 178 GLY I 110 MET I 115 5 6
HELIX 179 179 PRO I 129 ARG I 134 1 6
HELIX 180 180 PHE I 141 GLU I 151 1 11
HELIX 181 181 SER I 169 ASN I 183 1 15
HELIX 182 182 ARG I 201 GLY I 221 1 21
HELIX 183 183 ASP I 233 GLY I 248 1 16
HELIX 184 184 VAL I 256 GLY I 260 1 5
HELIX 185 185 GLY I 260 TYR I 274 1 15
HELIX 186 186 HIS I 285 ARG I 290 1 6
HELIX 187 187 SER I 297 GLY I 309 1 13
HELIX 188 188 GLU I 326 GLU I 339 1 14
HELIX 189 189 HIS I 371 ASN I 374 5 4
HELIX 190 190 ILE I 375 GLY I 383 1 9
HELIX 191 191 GLY I 391 GLY I 396 1 6
HELIX 192 192 GLY I 400 GLY I 418 1 19
HELIX 193 193 PRO I 420 ALA I 425 1 6
HELIX 194 194 HIS I 428 GLY I 439 1 12
HELIX 195 195 ILE J 8 VAL J 13 5 6
HELIX 196 196 THR J 38 SER J 50 1 13
HELIX 197 197 GLU J 63 SER J 71 1 9
HELIX 198 198 HIS J 94 PHE J 96 5 3
HELIX 199 199 ASN J 100 ALA J 109 1 10
HELIX 200 200 GLY J 110 MET J 115 5 6
HELIX 201 201 PRO J 129 ARG J 134 1 6
HELIX 202 202 PHE J 141 GLU J 151 1 11
HELIX 203 203 SER J 169 ASN J 183 1 15
HELIX 204 204 ARG J 201 GLY J 221 1 21
HELIX 205 205 ASP J 233 LEU J 247 1 15
HELIX 206 206 VAL J 256 GLY J 260 1 5
HELIX 207 207 GLY J 260 TYR J 274 1 15
HELIX 208 208 HIS J 285 ARG J 290 1 6
HELIX 209 209 SER J 297 GLY J 309 1 13
HELIX 210 210 GLU J 326 GLU J 339 1 14
HELIX 211 211 ASN J 374 GLY J 383 1 10
HELIX 212 212 GLY J 391 GLY J 396 1 6
HELIX 213 213 GLY J 400 GLN J 417 1 18
HELIX 214 214 PRO J 420 LYS J 426 1 7
HELIX 215 215 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 ILE A 25 O TYR A 91
SHEET 4 A 5 VAL A 118 TYR A 127 -1 O TYR A 127 N ILE A 26
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 279 N ALA A 252
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 PHE B 29 O VAL B 87
SHEET 4 D 5 VAL B 118 TYR B 127 -1 O GLU B 124 N VAL B 28
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 ILE C 86 N HIS C 78
SHEET 3 G 5 ASP C 24 PRO C 33 -1 N ILE C 25 O TYR C 91
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 123
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 281 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 HIS D 279 N VAL D 254
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 THR E 365 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 79 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 121
SHEET 1 Q 9 ILE F 157 VAL F 160 0
SHEET 2 Q 9 TYR F 187 KCX F 189 1 O KCX F 189 N VAL F 160
SHEET 3 Q 9 THR F 225 ASN F 229 1 O PHE F 227 N MET F 188
SHEET 4 Q 9 HIS F 251 ASP F 255 1 O MET F 253 N ALA F 228
SHEET 5 Q 9 ALA F 277 HIS F 281 1 O HIS F 281 N VAL F 254
SHEET 6 Q 9 GLN F 312 HIS F 314 1 O GLN F 312 N GLY F 280
SHEET 7 Q 9 PHE F 363 SER F 367 1 O THR F 365 N LEU F 313
SHEET 8 Q 9 VAL F 387 GLN F 389 1 O VAL F 387 N SER F 366
SHEET 9 Q 9 ILE F 157 VAL F 160 1 N ILE F 157 O LEU F 388
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 123
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 281 N VAL G 254
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 ILE H 25 O TYR H 91
SHEET 4 V 5 VAL H 118 TYR H 127 -1 O TYR H 127 N ILE H 26
SHEET 5 V 5 GLY H 295 ILE H 296 1 O GLY H 295 N LEU H 121
SHEET 1 W 9 ILE H 157 VAL H 160 0
SHEET 2 W 9 TYR H 187 KCX H 189 1 O KCX H 189 N VAL H 160
SHEET 3 W 9 THR H 225 ASN H 229 1 O PHE H 227 N MET H 188
SHEET 4 W 9 HIS H 251 ASP H 255 1 O MET H 253 N ALA H 228
SHEET 5 W 9 ALA H 277 HIS H 281 1 O HIS H 281 N VAL H 254
SHEET 6 W 9 GLN H 312 HIS H 314 1 O GLN H 312 N GLY H 280
SHEET 7 W 9 PHE H 363 SER H 367 1 O THR H 365 N LEU H 313
SHEET 8 W 9 VAL H 387 GLN H 389 1 O VAL H 387 N PRO H 364
SHEET 9 W 9 ILE H 157 VAL H 160 1 N ILE H 157 O LEU H 388
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 ALA I 90 N LYS I 73
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 121
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 HIS I 279 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 LYS J 119 N THR J 32
SHEET 5 AB 5 GLY J 295 ILE J 296 1 O GLY J 295 N LEU J 121
SHEET 1 AC 9 ILE J 157 VAL J 160 0
SHEET 2 AC 9 TYR J 187 KCX J 189 1 O KCX J 189 N VAL J 160
SHEET 3 AC 9 THR J 225 ASN J 229 1 O PHE J 227 N MET J 188
SHEET 4 AC 9 HIS J 251 ASP J 255 1 O MET J 253 N ALA J 228
SHEET 5 AC 9 ALA J 277 HIS J 281 1 O HIS J 281 N VAL J 254
SHEET 6 AC 9 GLN J 312 HIS J 314 1 O GLN J 312 N GLY J 280
SHEET 7 AC 9 PHE J 363 SER J 367 1 O PHE J 363 N LEU J 313
SHEET 8 AC 9 VAL J 387 GLN J 389 1 O VAL J 387 N SER J 366
SHEET 9 AC 9 ILE J 157 VAL J 160 1 N ILE J 157 O LEU J 388
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 1.33
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 1.33
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 500 1555 1555 1.96
LINK OD1 ASP A 191 MG MG A 500 1555 1555 2.07
LINK OE1 GLU A 192 MG MG A 500 1555 1555 1.82
LINK MG MG A 500 O3 CAP A 600 1555 1555 2.10
LINK MG MG A 500 O2 CAP A 600 1555 1555 2.26
LINK MG MG A 500 O7 CAP A 600 1555 1555 2.30
LINK OQ2 KCX B 189 MG MG B 500 1555 1555 1.98
LINK OD1 ASP B 191 MG MG B 500 1555 1555 2.05
LINK OE1 GLU B 192 MG MG B 500 1555 1555 2.04
LINK MG MG B 500 O3 CAP B 600 1555 1555 2.21
LINK MG MG B 500 O7 CAP B 600 1555 1555 2.11
LINK MG MG B 500 O2 CAP B 600 1555 1555 2.23
LINK OQ2 KCX C 189 MG MG C 500 1555 1555 1.93
LINK OD1 ASP C 191 MG MG C 500 1555 1555 2.03
LINK OE1 GLU C 192 MG MG C 500 1555 1555 2.03
LINK MG MG C 500 O2 CAP C 600 1555 1555 2.38
LINK MG MG C 500 O7 CAP C 600 1555 1555 2.00
LINK MG MG C 500 O3 CAP C 600 1555 1555 2.17
LINK OQ2 KCX D 189 MG MG D 500 1555 1555 1.90
LINK OD1 ASP D 191 MG MG D 500 1555 1555 1.90
LINK OE1 GLU D 192 MG MG D 500 1555 1555 1.99
LINK MG MG D 500 O3 CAP D 600 1555 1555 2.09
LINK MG MG D 500 O2 CAP D 600 1555 1555 2.36
LINK MG MG D 500 O7 CAP D 600 1555 1555 2.08
LINK OQ2 KCX E 189 MG MG E 500 1555 1555 2.06
LINK OD1 ASP E 191 MG MG E 500 1555 1555 1.99
LINK OE1 GLU E 192 MG MG E 500 1555 1555 2.10
LINK MG MG E 500 O3 CAP E 600 1555 1555 2.07
LINK MG MG E 500 O2 CAP E 600 1555 1555 2.27
LINK MG MG E 500 O7 CAP E 600 1555 1555 1.89
LINK OQ2 KCX F 189 MG MG F 500 1555 1555 1.99
LINK OD1 ASP F 191 MG MG F 500 1555 1555 1.93
LINK OE1 GLU F 192 MG MG F 500 1555 1555 2.04
LINK MG MG F 500 O3 CAP F 600 1555 1555 2.09
LINK MG MG F 500 O2 CAP F 600 1555 1555 2.39
LINK MG MG F 500 O7 CAP F 600 1555 1555 2.01
LINK OQ2 KCX G 189 MG MG G 500 1555 1555 2.02
LINK OD1 ASP G 191 MG MG G 500 1555 1555 2.00
LINK OE1 GLU G 192 MG MG G 500 1555 1555 1.91
LINK MG MG G 500 O3 CAP G 600 1555 1555 2.07
LINK MG MG G 500 O7 CAP G 600 1555 1555 1.98
LINK MG MG G 500 O2 CAP G 600 1555 1555 2.33
LINK OQ2 KCX H 189 MG MG H 500 1555 1555 2.08
LINK OD2 ASP H 191 MG MG H 500 1555 1555 2.66
LINK OE1 GLU H 192 MG MG H 500 1555 1555 1.97
LINK MG MG H 500 O2 CAP H 600 1555 1555 2.34
LINK MG MG H 500 O7 CAP H 600 1555 1555 2.21
LINK MG MG H 500 O3 CAP H 600 1555 1555 2.17
LINK OQ2 KCX I 189 MG MG I 500 1555 1555 1.94
LINK OD1 ASP I 191 MG MG I 500 1555 1555 2.03
LINK OE1 GLU I 192 MG MG I 500 1555 1555 2.08
LINK MG MG I 500 O2 CAP I 600 1555 1555 2.29
LINK MG MG I 500 O3 CAP I 600 1555 1555 2.10
LINK MG MG I 500 O7 CAP I 600 1555 1555 2.19
LINK OQ2 KCX J 189 MG MG J 500 1555 1555 2.05
LINK OD2 ASP J 191 MG MG J 500 1555 1555 1.99
LINK OE1 GLU J 192 MG MG J 500 1555 1555 2.09
LINK MG MG J 500 O3 CAP J 600 1555 1555 2.19
LINK MG MG J 500 O2 CAP J 600 1555 1555 2.24
LINK MG MG J 500 O7 CAP J 600 1555 1555 1.90
CISPEP 1 LYS A 163 PRO A 164 0 5.99
CISPEP 2 LYS B 163 PRO B 164 0 6.80
CISPEP 3 LYS C 163 PRO C 164 0 6.37
CISPEP 4 LYS D 163 PRO D 164 0 8.12
CISPEP 5 LYS E 163 PRO E 164 0 5.64
CISPEP 6 LYS F 163 PRO F 164 0 6.30
CISPEP 7 LYS G 163 PRO G 164 0 5.38
CISPEP 8 LYS H 163 PRO H 164 0 6.42
CISPEP 9 LYS I 163 PRO I 164 0 6.65
CISPEP 10 LYS J 163 PRO J 164 0 5.79
SITE 1 AC1 6 LYS A 165 KCX A 189 ASP A 191 GLU A 192
SITE 2 AC1 6 CAP A 600 ASN H 111
SITE 1 AC2 26 VAL A 161 LYS A 163 LYS A 165 KCX A 189
SITE 2 AC2 26 ASP A 191 GLU A 192 HIS A 281 ARG A 282
SITE 3 AC2 26 HIS A 314 LYS A 322 LEU A 323 SER A 367
SITE 4 AC2 26 GLY A 368 GLY A 369 GLN A 389 GLY A 391
SITE 5 AC2 26 GLY A 392 HOH A 495 MG A 500 HOH A 645
SITE 6 AC2 26 HOH A1278 HOH A1893 HOH A2850 THR H 54
SITE 7 AC2 26 TRP H 55 ASN H 111
SITE 1 AC3 4 KCX B 189 ASP B 191 GLU B 192 CAP B 600
SITE 1 AC4 28 LYS B 163 LYS B 165 KCX B 189 ASP B 191
SITE 2 AC4 28 GLU B 192 HIS B 281 ARG B 282 HIS B 314
SITE 3 AC4 28 LYS B 322 LEU B 323 SER B 367 GLY B 368
SITE 4 AC4 28 GLY B 369 GLN B 389 GLY B 391 GLY B 392
SITE 5 AC4 28 HOH B 467 HOH B 468 HOH B 472 HOH B 499
SITE 6 AC4 28 MG B 500 HOH B2398 HOH B2720 HOH B2839
SITE 7 AC4 28 GLU G 49 TRP G 55 ASN G 111 HOH G 466
SITE 1 AC5 5 KCX C 189 ASP C 191 GLU C 192 CAP C 600
SITE 2 AC5 5 ASN F 111
SITE 1 AC6 29 LYS C 163 LYS C 165 KCX C 189 ASP C 191
SITE 2 AC6 29 GLU C 192 HIS C 281 ARG C 282 HIS C 314
SITE 3 AC6 29 LYS C 322 LEU C 323 SER C 367 GLY C 368
SITE 4 AC6 29 GLY C 369 GLN C 389 GLY C 391 GLY C 392
SITE 5 AC6 29 HOH C 445 HOH C 457 HOH C 461 HOH C 487
SITE 6 AC6 29 MG C 500 HOH C 616 HOH C 691 HOH C2321
SITE 7 AC6 29 GLU F 49 TRP F 55 ASN F 111 HOH F 503
SITE 8 AC6 29 HOH F1009
SITE 1 AC7 4 KCX D 189 ASP D 191 GLU D 192 CAP D 600
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 HOH D 445 HOH D 452 HOH D 458 MG D 500
SITE 6 AC8 28 HOH D 510 HOH D1721 HOH D2695 HOH D2855
SITE 7 AC8 28 GLU J 49 TRP J 55 ASN J 111 HOH J2762
SITE 1 AC9 4 KCX E 189 ASP E 191 GLU E 192 CAP E 600
SITE 1 BC1 28 LYS E 163 LYS E 165 KCX E 189 ASP E 191
SITE 2 BC1 28 GLU E 192 HIS E 281 ARG E 282 HIS E 314
SITE 3 BC1 28 LYS E 322 LEU E 323 SER E 367 GLY E 368
SITE 4 BC1 28 GLY E 369 GLN E 389 GLY E 391 GLY E 392
SITE 5 BC1 28 HOH E 483 HOH E 494 MG E 500 HOH E 654
SITE 6 BC1 28 HOH E 676 HOH E1879 HOH E2240 GLU I 49
SITE 7 BC1 28 TRP I 55 ASN I 111 HOH I 463 HOH I 465
SITE 1 BC2 5 ASN C 111 KCX F 189 ASP F 191 GLU F 192
SITE 2 BC2 5 CAP F 600
SITE 1 BC3 28 GLU C 49 THR C 54 TRP C 55 ASN C 111
SITE 2 BC3 28 HOH C 451 HOH C 478 LYS F 163 LYS F 165
SITE 3 BC3 28 KCX F 189 ASP F 191 GLU F 192 HIS F 281
SITE 4 BC3 28 ARG F 282 HIS F 314 LYS F 322 LEU F 323
SITE 5 BC3 28 SER F 367 GLY F 368 GLY F 369 GLN F 389
SITE 6 BC3 28 GLY F 391 GLY F 392 HOH F 445 HOH F 464
SITE 7 BC3 28 HOH F 490 HOH F 495 HOH F 498 MG F 500
SITE 1 BC4 5 ASN B 111 KCX G 189 ASP G 191 GLU G 192
SITE 2 BC4 5 CAP G 600
SITE 1 BC5 28 GLU B 49 TRP B 55 ASN B 111 HOH B 448
SITE 2 BC5 28 HOH B 454 LYS G 163 LYS G 165 KCX G 189
SITE 3 BC5 28 ASP G 191 GLU G 192 HIS G 281 ARG G 282
SITE 4 BC5 28 HIS G 314 LYS G 322 LEU G 323 SER G 367
SITE 5 BC5 28 GLY G 368 GLY G 369 GLN G 389 GLY G 391
SITE 6 BC5 28 GLY G 392 HOH G 446 HOH G 456 HOH G 469
SITE 7 BC5 28 HOH G 485 MG G 500 HOH G 530 HOH G1761
SITE 1 BC6 4 KCX H 189 ASP H 191 GLU H 192 CAP H 600
SITE 1 BC7 25 TRP A 55 ASN A 111 HOH A1659 LYS H 163
SITE 2 BC7 25 LYS H 165 KCX H 189 ASP H 191 GLU H 192
SITE 3 BC7 25 HIS H 281 ARG H 282 HIS H 314 LYS H 322
SITE 4 BC7 25 LEU H 323 SER H 367 GLY H 368 GLY H 369
SITE 5 BC7 25 GLN H 389 GLY H 391 GLY H 392 HOH H 457
SITE 6 BC7 25 MG H 500 HOH H1169 HOH H1230 HOH H2657
SITE 7 BC7 25 HOH H2710
SITE 1 BC8 4 KCX I 189 ASP I 191 GLU I 192 CAP I 600
SITE 1 BC9 28 GLU E 49 TRP E 55 ASN E 111 HOH E 505
SITE 2 BC9 28 LYS I 163 LYS I 165 KCX I 189 ASP I 191
SITE 3 BC9 28 GLU I 192 HIS I 281 ARG I 282 HIS I 314
SITE 4 BC9 28 LYS I 322 LEU I 323 SER I 367 GLY I 368
SITE 5 BC9 28 GLY I 369 GLN I 389 GLY I 391 GLY I 392
SITE 6 BC9 28 HOH I 445 HOH I 451 HOH I 471 HOH I 478
SITE 7 BC9 28 HOH I 482 HOH I 483 HOH I 491 MG I 500
SITE 1 CC1 5 ASN D 111 KCX J 189 ASP J 191 GLU J 192
SITE 2 CC1 5 CAP J 600
SITE 1 CC2 28 GLU D 49 TRP D 55 ASN D 111 HOH D 482
SITE 2 CC2 28 HOH D 484 LYS J 163 LYS J 165 KCX J 189
SITE 3 CC2 28 ASP J 191 GLU J 192 HIS J 281 ARG J 282
SITE 4 CC2 28 HIS J 314 LYS J 322 LEU J 323 SER J 367
SITE 5 CC2 28 GLY J 368 GLY J 369 GLN J 389 GLY J 391
SITE 6 CC2 28 GLY J 392 HOH J 445 HOH J 481 MG J 500
SITE 7 CC2 28 HOH J 578 HOH J 602 HOH J1892 HOH J1895
CRYST1 97.474 246.241 133.080 90.00 104.10 90.00 P 1 21 1 20
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 0.010259 0.000000 0.002577 0.00000
SCALE2 0.000000 0.004061 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
