HEADER ISOMERASE 19-FEB-07 2OX4
TITLE CRYSTAL STRUCTURE OF PUTATIVE DEHYDRATASE FROM ZYMOMONAS MOBILIS ZM4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE MANDELATE RACEMASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 5.1.2.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 542;
SOURCE 4 STRAIN: ZM4, CP4;
SOURCE 5 ATCC: 31821;
SOURCE 6 GENE: RSPA, ZMO1264;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS ENOLASE, DEHYDRATASE, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, PSI, NYSGRC, NEW YORK STRUCTURAL GENOMICS RESEARCH
KEYWDS 3 CONSORTIUM, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 4 NYSGXRC, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,J.M.SAUDER,J.C.FREEMAN,K.BAIN,T.GHEYI,
AUTHOR 2 S.R.WASSERMAN,D.SMITH,J.GERLT,S.K.BURLEY,S.C.ALMO,NEW YORK SGX
AUTHOR 3 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 7 30-AUG-23 2OX4 1 REMARK
REVDAT 6 03-FEB-21 2OX4 1 AUTHOR JRNL REMARK SEQADV
REVDAT 6 2 1 LINK
REVDAT 5 14-NOV-18 2OX4 1 AUTHOR
REVDAT 4 18-OCT-17 2OX4 1 REMARK
REVDAT 3 13-JUL-11 2OX4 1 VERSN
REVDAT 2 24-FEB-09 2OX4 1 VERSN
REVDAT 1 06-MAR-07 2OX4 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,J.M.SAUDER,J.C.FREEMAN,K.BAIN,T.GHEYI,
JRNL AUTH 2 S.R.WASSERMAN,D.SMITH,J.GERLT,S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE DEHYDRATASE FROM ZYMOMONAS
JRNL TITL 2 MOBILIS ZM4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0028
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 278981
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8758
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19564
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 629
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 3160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.05000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.215
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25912 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 35150 ; 1.171 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3313 ; 7.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1186 ;36.120 ;24.376
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4503 ;15.781 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 130 ;18.864 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3825 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19732 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 13410 ; 0.181 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 17680 ; 0.309 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 5250 ; 0.174 ; 0.500
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): 86 ; 0.155 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 86 ; 0.169 ; 0.500
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): 16276 ; 3.180 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25616 ; 4.108 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10812 ; 6.099 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9459 ; 8.560 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 392 1
REMARK 3 2 B 2 B 392 1
REMARK 3 3 C 2 C 392 1
REMARK 3 4 D 2 D 392 1
REMARK 3 5 E 2 E 392 1
REMARK 3 6 F 2 F 392 1
REMARK 3 7 G 2 G 392 1
REMARK 3 8 H 2 H 392 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2956 ; 0.28 ; 0.30
REMARK 3 TIGHT POSITIONAL 1 B (A): 2956 ; 0.43 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 C (A): 2956 ; 0.32 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 D (A): 2956 ; 0.30 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 E (A): 2956 ; 0.32 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 F (A): 2956 ; 0.29 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 G (A): 2956 ; 0.47 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 H (A): 2956 ; 0.29 ; 0.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 2956 ; 2.94 ; 2.00
REMARK 3 TIGHT THERMAL 1 B (A**2): 2956 ; 3.16 ; 0.00
REMARK 3 TIGHT THERMAL 1 C (A**2): 2956 ; 3.38 ; 0.00
REMARK 3 TIGHT THERMAL 1 D (A**2): 2956 ; 2.91 ; 0.00
REMARK 3 TIGHT THERMAL 1 E (A**2): 2956 ; 3.31 ; 0.00
REMARK 3 TIGHT THERMAL 1 F (A**2): 2956 ; 2.61 ; 0.00
REMARK 3 TIGHT THERMAL 1 G (A**2): 2956 ; 3.17 ; 0.00
REMARK 3 TIGHT THERMAL 1 H (A**2): 2956 ; 2.45 ; 0.00
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 2OX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97960
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 288410
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : 0.43000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 2GL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL, PH 8.5, 30% PEG 4000,
REMARK 280 200MM LITHIUM SULFATE, 10% GLYCEROL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 294K
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 95.08900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 95.20450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 95.08900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 95.20450
REMARK 290 SMTRY3 4 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 300 REMARK: OCTAMER, THE ASU CONTAINS THE WHOLE OCTAMER
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 41950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 SER A 393
REMARK 465 GLU A 394
REMARK 465 GLY A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
REMARK 465 MET B -1
REMARK 465 SER B 393
REMARK 465 GLU B 394
REMARK 465 GLY B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 HIS B 400
REMARK 465 HIS B 401
REMARK 465 MET C -1
REMARK 465 SER C 393
REMARK 465 GLU C 394
REMARK 465 HIS C 399
REMARK 465 HIS C 400
REMARK 465 HIS C 401
REMARK 465 MET D -1
REMARK 465 SER D 393
REMARK 465 GLU D 394
REMARK 465 HIS D 399
REMARK 465 HIS D 400
REMARK 465 HIS D 401
REMARK 465 MET E -1
REMARK 465 SER E 393
REMARK 465 GLU E 394
REMARK 465 GLY E 395
REMARK 465 HIS E 396
REMARK 465 HIS E 397
REMARK 465 HIS E 398
REMARK 465 HIS E 399
REMARK 465 HIS E 400
REMARK 465 HIS E 401
REMARK 465 MET F -1
REMARK 465 SER F 393
REMARK 465 GLU F 394
REMARK 465 GLY F 395
REMARK 465 HIS F 396
REMARK 465 HIS F 397
REMARK 465 HIS F 398
REMARK 465 HIS F 399
REMARK 465 HIS F 400
REMARK 465 HIS F 401
REMARK 465 MET G -1
REMARK 465 SER G 393
REMARK 465 GLU G 394
REMARK 465 GLY G 395
REMARK 465 HIS G 396
REMARK 465 HIS G 397
REMARK 465 HIS G 398
REMARK 465 HIS G 399
REMARK 465 HIS G 400
REMARK 465 HIS G 401
REMARK 465 MET H -1
REMARK 465 SER H 393
REMARK 465 GLU H 394
REMARK 465 GLY H 395
REMARK 465 HIS H 396
REMARK 465 HIS H 397
REMARK 465 HIS H 398
REMARK 465 HIS H 399
REMARK 465 HIS H 400
REMARK 465 HIS H 401
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 PHE A 80 -57.41 71.86
REMARK 500 GLN A 130 54.27 73.48
REMARK 500 SER A 269 168.51 68.95
REMARK 500 ALA A 317 56.29 -160.26
REMARK 500 ASN A 335 49.15 -102.51
REMARK 500 CYS A 337 -63.83 -97.13
REMARK 500 GLU A 391 -158.49 -130.52
REMARK 500 THR B 13 119.93 -38.56
REMARK 500 PHE B 80 -54.25 72.17
REMARK 500 GLN B 130 51.95 73.92
REMARK 500 ASN B 234 66.78 60.87
REMARK 500 SER B 269 167.51 70.88
REMARK 500 ALA B 317 55.02 -160.23
REMARK 500 ASN B 335 51.58 -101.36
REMARK 500 CYS B 337 -64.88 -97.69
REMARK 500 LYS B 344 -25.70 -35.15
REMARK 500 GLU B 369 54.00 -109.68
REMARK 500 PHE C 80 -54.41 73.51
REMARK 500 GLN C 130 56.66 74.20
REMARK 500 TRP C 135 76.18 -102.59
REMARK 500 SER C 269 165.26 67.80
REMARK 500 ALA C 317 52.18 -161.61
REMARK 500 ASN C 335 48.53 -98.58
REMARK 500 CYS C 337 -63.36 -96.33
REMARK 500 PHE D 80 -55.75 71.59
REMARK 500 GLN D 130 55.66 75.66
REMARK 500 SER D 269 164.47 71.76
REMARK 500 ALA D 317 54.69 -159.96
REMARK 500 ASN D 335 47.47 -100.82
REMARK 500 CYS D 337 -64.25 -95.27
REMARK 500 PHE E 80 -54.27 73.70
REMARK 500 GLN E 130 53.13 70.73
REMARK 500 SER E 269 166.29 68.99
REMARK 500 ALA E 317 56.55 -165.50
REMARK 500 ASN E 335 52.63 -96.60
REMARK 500 CYS E 337 -63.96 -94.94
REMARK 500 ASP F 29 1.41 -68.98
REMARK 500 PHE F 80 -56.67 74.07
REMARK 500 GLN F 130 50.45 74.06
REMARK 500 SER F 269 165.58 73.77
REMARK 500 ALA F 317 61.00 -161.05
REMARK 500 ASN F 335 49.05 -99.22
REMARK 500 CYS F 337 -63.11 -96.95
REMARK 500 PHE G 80 -57.17 73.14
REMARK 500 ASN G 242 -164.76 -160.24
REMARK 500 SER G 269 165.63 70.60
REMARK 500 ASN G 335 48.44 -99.09
REMARK 500 CYS G 337 -61.91 -97.67
REMARK 500 LYS G 344 -39.94 -35.30
REMARK 500 GLU G 369 75.40 -101.93
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP A 135 GLY A 136 -30.12
REMARK 500 LYS B 137 GLU B 138 136.83
REMARK 500 LEU B 346 LEU B 347 140.71
REMARK 500 GLU B 391 ALA B 392 -133.56
REMARK 500 TRP C 135 GLY C 136 70.76
REMARK 500 GLU D 391 ALA D 392 -108.89
REMARK 500 TRP F 135 GLY F 136 -62.01
REMARK 500 GLU F 391 ALA F 392 -93.31
REMARK 500 LYS G 137 GLU G 138 -125.51
REMARK 500 GLU G 138 ARG G 139 -149.31
REMARK 500 TRP H 135 GLY H 136 -58.54
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 213 OE1
REMARK 620 2 GLU A 213 OE1 17.1
REMARK 620 3 GLU A 239 OE2 83.4 100.5
REMARK 620 4 GLU A 265 OE1 165.2 160.3 92.6
REMARK 620 5 HOH A3470 O 81.1 77.7 99.9 85.6
REMARK 620 6 HOH A3504 O 94.1 77.0 175.3 90.8 83.5
REMARK 620 7 HOH A3575 O 91.6 90.9 94.2 102.9 163.2 81.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 213 OE1
REMARK 620 2 GLU B 213 OE1 18.5
REMARK 620 3 GLU B 239 OE2 84.4 102.5
REMARK 620 4 GLU B 265 OE1 167.3 160.8 89.8
REMARK 620 5 HOH B3509 O 85.1 78.6 100.1 84.9
REMARK 620 6 HOH B3594 O 94.0 76.6 171.0 93.5 88.5
REMARK 620 7 HOH B3766 O 89.7 91.3 95.7 102.1 162.7 75.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 213 OE1
REMARK 620 2 GLU C 239 OE2 88.3
REMARK 620 3 GLU C 265 OE1 167.3 91.1
REMARK 620 4 HOH C3447 O 83.3 99.5 84.4
REMARK 620 5 HOH C3506 O 91.8 175.1 89.9 85.3
REMARK 620 6 HOH C3576 O 93.1 94.8 99.6 165.0 80.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 213 OE1
REMARK 620 2 GLU D 239 OE2 85.5
REMARK 620 3 GLU D 265 OE1 167.3 91.9
REMARK 620 4 HOH D3519 O 83.4 100.7 84.9
REMARK 620 5 HOH D3550 O 95.0 176.7 88.3 82.6
REMARK 620 6 HOH D3564 O 90.9 95.3 101.7 162.5 81.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 213 OE1
REMARK 620 2 GLU E 213 OE2 18.2
REMARK 620 3 GLU E 239 OE2 85.7 103.9
REMARK 620 4 GLU E 265 OE1 168.1 161.3 90.1
REMARK 620 5 HOH E3453 O 82.7 79.4 96.7 86.7
REMARK 620 6 HOH E3534 O 91.7 91.5 95.0 99.8 166.6
REMARK 620 7 HOH E3574 O 94.4 76.5 174.1 90.9 89.1 79.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 213 OE1
REMARK 620 2 GLU F 239 OE2 87.4
REMARK 620 3 GLU F 265 OE1 169.2 91.5
REMARK 620 4 HOH F3486 O 85.3 98.1 84.2
REMARK 620 5 HOH F3534 O 92.2 173.6 90.1 88.2
REMARK 620 6 HOH F3536 O 86.4 94.4 104.4 164.6 79.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 213 OE1
REMARK 620 2 GLU G 213 OE2 16.3
REMARK 620 3 GLU G 239 OE2 84.4 100.5
REMARK 620 4 GLU G 265 OE1 168.0 165.9 90.5
REMARK 620 5 HOH G3525 O 81.6 82.1 95.5 88.2
REMARK 620 6 HOH G3539 O 90.6 86.5 98.1 100.8 163.6
REMARK 620 7 HOH G3586 O 98.5 82.2 173.1 87.9 91.1 75.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 213 OE1
REMARK 620 2 GLU H 239 OE2 86.9
REMARK 620 3 GLU H 265 OE1 169.8 89.7
REMARK 620 4 HOH H3494 O 85.8 99.0 85.2
REMARK 620 5 HOH H3520 O 91.0 92.2 98.7 168.1
REMARK 620 6 HOH H3593 O 94.7 174.6 89.5 86.3 82.6
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 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 3403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 3404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 3406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 3413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 3407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 3409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 3411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 3405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 3408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 3412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 3410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-9270C RELATED DB: TARGETDB
DBREF 2OX4 A 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 B 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 C 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 D 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 E 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 F 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 G 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
DBREF 2OX4 H 2 393 UNP Q5NN22 Q5NN22_ZYMMO 2 393
SEQADV 2OX4 MET A -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER A 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU A 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU A 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY A 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS A 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET B -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER B 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU B 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU B 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY B 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS B 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET C -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER C 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU C 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU C 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY C 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS C 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET D -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER D 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU D 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU D 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY D 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS D 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET E -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER E 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU E 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU E 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY E 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS E 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET F -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER F 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU F 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU F 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY F 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS F 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET G -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER G 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU G 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU G 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY G 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS G 401 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 MET H -1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 SER H 0 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 LEU H 1 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLU H 394 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 GLY H 395 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 396 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 397 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 398 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 399 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 400 UNP Q5NN22 EXPRESSION TAG
SEQADV 2OX4 HIS H 401 UNP Q5NN22 EXPRESSION TAG
SEQRES 1 A 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 A 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 A 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 A 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 A 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 A 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 A 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 A 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 A 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 A 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 A 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 A 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 A 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 A 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 A 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 A 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 A 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 A 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 A 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 A 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 A 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 A 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 A 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 A 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 A 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 A 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 A 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 A 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 A 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 A 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 A 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 B 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 B 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 B 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 B 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 B 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 B 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 B 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 B 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 B 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 B 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 B 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 B 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 B 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 B 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 B 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 B 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 B 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 B 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 B 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 B 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 B 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 B 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 B 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 B 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 B 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 B 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 B 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 B 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 B 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 B 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 C 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 C 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 C 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 C 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 C 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 C 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 C 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 C 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 C 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 C 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 C 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 C 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 C 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 C 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 C 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 C 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 C 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 C 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 C 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 C 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 C 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 C 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 C 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 C 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 C 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 C 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 C 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 C 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 C 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 C 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 D 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 D 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 D 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 D 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 D 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 D 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 D 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 D 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 D 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 D 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 D 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 D 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 D 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 D 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 D 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 D 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 D 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 D 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 D 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 D 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 D 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 D 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 D 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 D 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 D 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 D 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 D 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 D 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 D 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 D 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 E 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 E 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 E 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 E 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 E 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 E 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 E 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 E 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 E 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 E 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 E 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 E 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 E 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 E 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 E 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 E 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 E 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 E 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 E 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 E 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 E 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 E 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 E 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 E 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 E 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 E 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 E 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 E 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 E 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 E 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 E 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 F 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 F 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 F 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 F 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 F 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 F 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 F 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 F 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 F 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 F 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 F 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 F 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 F 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 F 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 F 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 F 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 F 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 F 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 F 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 F 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 F 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 F 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 F 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 F 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 F 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 F 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 F 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 F 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 F 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 F 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 F 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 G 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 G 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 G 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 G 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 G 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 G 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 G 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 G 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 G 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 G 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 G 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 G 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 G 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 G 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 G 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 G 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 G 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 G 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 G 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 G 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 G 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 G 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 G 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 G 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 G 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 G 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 G 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 G 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 G 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 G 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 G 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 H 403 MET SER LEU LYS ILE THR LYS ILE GLU ILE PHE HIS VAL
SEQRES 2 H 403 HIS THR ARG PRO GLN SER GLY GLN ARG PRO ILE LEU VAL
SEQRES 3 H 403 LYS VAL SER THR ASP GLU GLY ILE TYR GLY LEU GLY GLU
SEQRES 4 H 403 ALA GLY ILE ALA TYR GLY VAL GLY GLY SER ALA ALA ALA
SEQRES 5 H 403 GLY ILE LEU LYS ASP TYR ALA ALA LEU LEU ILE GLY GLU
SEQRES 6 H 403 ASP PRO PHE ASN THR GLU ALA ILE TRP GLU LYS LEU PHE
SEQRES 7 H 403 LYS LYS THR PHE TRP GLY GLN GLY GLY GLY THR VAL ILE
SEQRES 8 H 403 PHE SER GLY ILE SER ALA PHE ASP ILE ALA PHE TRP ASP
SEQRES 9 H 403 ILE LYS GLY LYS ALA LEU ASN LEU PRO VAL TYR LYS LEU
SEQRES 10 H 403 LEU GLY GLY LYS ASN ARG GLU ASP LEU ARG VAL TYR ALA
SEQRES 11 H 403 SER GLN LEU GLN PHE GLY TRP GLY LYS GLU ARG LYS SER
SEQRES 12 H 403 LYS GLY ARG LYS GLU GLU TYR ALA GLU GLU ALA LEU LYS
SEQRES 13 H 403 ALA VAL ALA GLU GLY TYR ASP ALA VAL LYS VAL ASP VAL
SEQRES 14 H 403 LEU ALA HIS ASP ARG ASN GLY SER ARG GLU GLY VAL PHE
SEQRES 15 H 403 LEU GLU GLY PRO LEU PRO SER GLU THR ILE LYS ILE GLY
SEQRES 16 H 403 VAL GLU ARG VAL GLU ALA ILE ARG ASN ALA VAL GLY PRO
SEQRES 17 H 403 ASP VAL ASP ILE ILE VAL GLU ASN HIS GLY HIS THR ASP
SEQRES 18 H 403 LEU VAL SER ALA ILE GLN PHE ALA LYS ALA ILE GLU GLU
SEQRES 19 H 403 PHE ASN ILE PHE PHE TYR GLU GLU ILE ASN THR PRO LEU
SEQRES 20 H 403 ASN PRO ARG LEU LEU LYS GLU ALA LYS LYS LYS ILE ASP
SEQRES 21 H 403 ILE PRO LEU ALA SER GLY GLU ARG ILE TYR SER ARG TRP
SEQRES 22 H 403 GLY PHE LEU PRO PHE LEU GLU ASP ARG SER ILE ASP VAL
SEQRES 23 H 403 ILE GLN PRO ASP LEU GLY THR CYS GLY GLY PHE THR GLU
SEQRES 24 H 403 PHE LYS LYS ILE ALA ASP MET ALA HIS ILE PHE GLU VAL
SEQRES 25 H 403 THR VAL GLN ALA HIS VAL ALA GLY THR GLY VAL ALA GLU
SEQRES 26 H 403 ALA ALA SER LEU HIS ALA GLU ILE ALA ILE PRO ASN PHE
SEQRES 27 H 403 CYS ILE HIS GLU HIS HIS GLN LYS THR LEU LEU PRO GLU
SEQRES 28 H 403 TYR GLU GLU LEU CYS VAL HIS ASN TYR GLN PRO VAL LYS
SEQRES 29 H 403 GLY ARG TYR LYS VAL PRO GLU LEU PRO GLY ILE GLY GLN
SEQRES 30 H 403 ASP ILE THR GLU LYS LEU TYR GLN ILE SER ASP TYR VAL
SEQRES 31 H 403 SER ILE GLU ALA SER GLU GLY HIS HIS HIS HIS HIS HIS
HET MG A 402 1
HET GOL A3401 6
HET GOL A3414 6
HET CL B 501 1
HET MG B 502 1
HET GOL B3402 6
HET MG C 402 1
HET GOL C3403 6
HET GOL C3404 6
HET MG D 402 1
HET CL D 501 1
HET GOL D3406 6
HET GOL D3413 6
HET MG E 402 1
HET GOL E3407 6
HET MG F 402 1
HET CL F 501 1
HET GOL F3409 6
HET GOL F3411 6
HET CL G 501 1
HET MG G 502 1
HET GOL G3405 6
HET GOL G3408 6
HET GOL G3412 6
HET MG H 402 1
HET GOL H3410 6
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 MG 8(MG 2+)
FORMUL 10 GOL 14(C3 H8 O3)
FORMUL 12 CL 4(CL 1-)
FORMUL 35 HOH *3160(H2 O)
HELIX 1 1 GLY A 45 ILE A 61 1 17
HELIX 2 2 ASN A 67 LYS A 78 1 12
HELIX 3 3 PHE A 80 GLY A 84 5 5
HELIX 4 4 GLY A 86 ASN A 109 1 24
HELIX 5 5 PRO A 111 LEU A 116 1 6
HELIX 6 6 LEU A 131 GLY A 134 5 4
HELIX 7 7 ARG A 144 GLU A 158 1 15
HELIX 8 8 PRO A 186 GLY A 205 1 20
HELIX 9 9 ASP A 219 GLU A 231 1 13
HELIX 10 10 PRO A 247 LYS A 256 1 10
HELIX 11 11 TYR A 268 ASP A 279 1 12
HELIX 12 12 ASP A 288 GLY A 293 1 6
HELIX 13 13 GLY A 293 PHE A 308 1 16
HELIX 14 14 THR A 319 ALA A 332 1 14
HELIX 15 15 LYS A 344 LEU A 346 5 3
HELIX 16 16 LEU A 347 GLU A 352 1 6
HELIX 17 17 THR A 378 GLN A 383 5 6
HELIX 18 18 GLY B 45 ALA B 58 1 14
HELIX 19 19 ASN B 67 LYS B 78 1 12
HELIX 20 20 PHE B 80 GLY B 85 5 6
HELIX 21 21 GLY B 86 ASN B 109 1 24
HELIX 22 22 PRO B 111 LEU B 116 1 6
HELIX 23 23 LEU B 131 GLY B 134 5 4
HELIX 24 24 ARG B 144 GLU B 158 1 15
HELIX 25 25 PRO B 186 GLY B 205 1 20
HELIX 26 26 ASP B 219 GLU B 231 1 13
HELIX 27 27 PRO B 247 ILE B 257 1 11
HELIX 28 28 TYR B 268 ASP B 279 1 12
HELIX 29 29 ASP B 288 GLY B 293 1 6
HELIX 30 30 GLY B 293 PHE B 308 1 16
HELIX 31 31 THR B 319 ALA B 332 1 14
HELIX 32 32 HIS B 342 LEU B 346 5 5
HELIX 33 33 LEU B 347 GLU B 352 1 6
HELIX 34 34 THR B 378 GLN B 383 5 6
HELIX 35 35 GLY C 45 ILE C 61 1 17
HELIX 36 36 ASN C 67 LYS C 78 1 12
HELIX 37 37 PHE C 80 GLY C 85 5 6
HELIX 38 38 GLY C 86 ASN C 109 1 24
HELIX 39 39 PRO C 111 LEU C 116 5 6
HELIX 40 40 LEU C 131 GLY C 134 5 4
HELIX 41 41 ARG C 144 GLU C 158 1 15
HELIX 42 42 PRO C 186 GLY C 205 1 20
HELIX 43 43 ASP C 219 GLU C 231 1 13
HELIX 44 44 PRO C 247 ILE C 257 1 11
HELIX 45 45 TYR C 268 ASP C 279 1 12
HELIX 46 46 ASP C 288 GLY C 293 1 6
HELIX 47 47 GLY C 293 PHE C 308 1 16
HELIX 48 48 THR C 319 ALA C 332 1 14
HELIX 49 49 LYS C 344 LEU C 346 5 3
HELIX 50 50 LEU C 347 GLU C 352 1 6
HELIX 51 51 THR C 378 GLN C 383 5 6
HELIX 52 52 GLY D 45 ILE D 61 1 17
HELIX 53 53 ASN D 67 LYS D 78 1 12
HELIX 54 54 PHE D 80 GLY D 84 5 5
HELIX 55 55 GLY D 86 LEU D 108 1 23
HELIX 56 56 PRO D 111 LEU D 116 5 6
HELIX 57 57 LEU D 131 GLY D 134 5 4
HELIX 58 58 ARG D 144 GLU D 158 1 15
HELIX 59 59 PRO D 186 GLY D 205 1 20
HELIX 60 60 ASP D 219 GLU D 231 1 13
HELIX 61 61 PRO D 247 LYS D 255 1 9
HELIX 62 62 TYR D 268 ASP D 279 1 12
HELIX 63 63 ASP D 288 GLY D 293 1 6
HELIX 64 64 GLY D 293 ILE D 307 1 15
HELIX 65 65 THR D 319 ALA D 332 1 14
HELIX 66 66 LYS D 344 LEU D 346 5 3
HELIX 67 67 LEU D 347 GLU D 352 1 6
HELIX 68 68 THR D 378 GLN D 383 5 6
HELIX 69 69 GLY E 45 ILE E 61 1 17
HELIX 70 70 ASN E 67 LYS E 78 1 12
HELIX 71 71 PHE E 80 GLY E 85 5 6
HELIX 72 72 GLY E 86 LEU E 108 1 23
HELIX 73 73 PRO E 111 LEU E 116 5 6
HELIX 74 74 LEU E 131 GLY E 134 5 4
HELIX 75 75 ARG E 144 GLU E 158 1 15
HELIX 76 76 PRO E 186 GLY E 205 1 20
HELIX 77 77 ASP E 219 GLU E 231 1 13
HELIX 78 78 GLU E 232 ASN E 234 5 3
HELIX 79 79 PRO E 247 LYS E 255 1 9
HELIX 80 80 TYR E 268 ASP E 279 1 12
HELIX 81 81 GLY E 293 PHE E 308 1 16
HELIX 82 82 THR E 319 ALA E 332 1 14
HELIX 83 83 LYS E 344 LEU E 346 5 3
HELIX 84 84 LEU E 347 GLU E 352 1 6
HELIX 85 85 THR E 378 GLN E 383 5 6
HELIX 86 86 GLY F 45 ILE F 61 1 17
HELIX 87 87 ASN F 67 LYS F 78 1 12
HELIX 88 88 PHE F 80 GLY F 85 5 6
HELIX 89 89 GLY F 86 ASN F 109 1 24
HELIX 90 90 PRO F 111 LEU F 116 5 6
HELIX 91 91 LEU F 131 GLY F 134 5 4
HELIX 92 92 ARG F 144 GLU F 158 1 15
HELIX 93 93 PRO F 186 GLY F 205 1 20
HELIX 94 94 ASP F 219 GLU F 231 1 13
HELIX 95 95 PRO F 247 LYS F 256 1 10
HELIX 96 96 TYR F 268 ASP F 279 1 12
HELIX 97 97 ASP F 288 GLY F 293 1 6
HELIX 98 98 GLY F 293 ILE F 307 1 15
HELIX 99 99 THR F 319 ALA F 332 1 14
HELIX 100 100 LYS F 344 LEU F 346 5 3
HELIX 101 101 LEU F 347 GLU F 352 1 6
HELIX 102 102 THR F 378 GLN F 383 5 6
HELIX 103 103 GLY G 45 ALA G 58 1 14
HELIX 104 104 ASN G 67 LYS G 78 1 12
HELIX 105 105 PHE G 80 GLY G 84 5 5
HELIX 106 106 GLY G 86 ASN G 109 1 24
HELIX 107 107 PRO G 111 LEU G 116 1 6
HELIX 108 108 GLN G 130 GLY G 134 5 5
HELIX 109 109 ARG G 144 GLU G 158 1 15
HELIX 110 110 PRO G 186 GLY G 205 1 20
HELIX 111 111 ASP G 219 GLU G 231 1 13
HELIX 112 112 PRO G 247 LYS G 255 1 9
HELIX 113 113 TYR G 268 ASP G 279 1 12
HELIX 114 114 ASP G 288 GLY G 293 1 6
HELIX 115 115 GLY G 293 PHE G 308 1 16
HELIX 116 116 THR G 319 ALA G 332 1 14
HELIX 117 117 GLN G 343 LEU G 346 5 4
HELIX 118 118 LEU G 347 GLU G 352 1 6
HELIX 119 119 GLU G 379 GLN G 383 5 5
HELIX 120 120 GLY H 45 ALA H 58 1 14
HELIX 121 121 ASN H 67 LYS H 78 1 12
HELIX 122 122 PHE H 80 GLY H 85 5 6
HELIX 123 123 GLY H 86 LEU H 108 1 23
HELIX 124 124 PRO H 111 LEU H 116 5 6
HELIX 125 125 LEU H 131 GLY H 134 5 4
HELIX 126 126 ARG H 144 GLU H 158 1 15
HELIX 127 127 PRO H 186 GLY H 205 1 20
HELIX 128 128 ASP H 219 GLU H 231 1 13
HELIX 129 129 PRO H 247 LYS H 256 1 10
HELIX 130 130 TYR H 268 ASP H 279 1 12
HELIX 131 131 ASP H 288 GLY H 293 1 6
HELIX 132 132 GLY H 293 PHE H 308 1 16
HELIX 133 133 THR H 319 ALA H 332 1 14
HELIX 134 134 LYS H 344 LEU H 346 5 3
HELIX 135 135 LEU H 347 GLU H 352 1 6
HELIX 136 136 LYS H 380 GLN H 383 5 4
SHEET 1 A 4 TYR A 33 ALA A 38 0
SHEET 2 A 4 ILE A 22 THR A 28 -1 N VAL A 26 O GLY A 34
SHEET 3 A 4 ILE A 3 VAL A 11 -1 N LYS A 5 O SER A 27
SHEET 4 A 4 SER A 385 ILE A 390 -1 O VAL A 388 N ILE A 8
SHEET 1 B 8 THR A 311 VAL A 312 0
SHEET 2 B 8 VAL A 284 ILE A 285 1 N ILE A 285 O THR A 311
SHEET 3 B 8 LEU A 261 SER A 263 1 O LEU A 261 N VAL A 284
SHEET 4 B 8 ILE A 235 GLU A 239 1 N TYR A 238 O ALA A 262
SHEET 5 B 8 ASP A 209 GLU A 213 1 N VAL A 212 O GLU A 239
SHEET 6 B 8 ALA A 162 VAL A 165 1 N VAL A 163 O ILE A 211
SHEET 7 B 8 LEU A 124 SER A 129 1 N ALA A 128 O LYS A 164
SHEET 8 B 8 HIS A 339 HIS A 342 1 O HIS A 339 N TYR A 127
SHEET 1 C 8 THR A 311 VAL A 312 0
SHEET 2 C 8 VAL A 284 ILE A 285 1 N ILE A 285 O THR A 311
SHEET 3 C 8 LEU A 261 SER A 263 1 O LEU A 261 N VAL A 284
SHEET 4 C 8 ILE A 235 GLU A 239 1 N TYR A 238 O ALA A 262
SHEET 5 C 8 ASP A 209 GLU A 213 1 N VAL A 212 O GLU A 239
SHEET 6 C 8 ALA A 162 VAL A 165 1 N VAL A 163 O ILE A 211
SHEET 7 C 8 LEU A 124 SER A 129 1 N ALA A 128 O LYS A 164
SHEET 8 C 8 ARG A 364 TYR A 365 -1 O TYR A 365 N LEU A 124
SHEET 1 D 4 TYR B 33 ALA B 38 0
SHEET 2 D 4 ILE B 22 THR B 28 -1 N VAL B 26 O GLY B 34
SHEET 3 D 4 ILE B 3 VAL B 11 -1 N PHE B 9 O LEU B 23
SHEET 4 D 4 SER B 385 GLU B 391 -1 O VAL B 388 N ILE B 8
SHEET 1 E 8 THR B 311 VAL B 312 0
SHEET 2 E 8 VAL B 284 ILE B 285 1 N ILE B 285 O THR B 311
SHEET 3 E 8 LEU B 261 SER B 263 1 O LEU B 261 N VAL B 284
SHEET 4 E 8 ILE B 235 GLU B 239 1 N TYR B 238 O ALA B 262
SHEET 5 E 8 ASP B 209 GLU B 213 1 N VAL B 212 O GLU B 239
SHEET 6 E 8 ALA B 162 VAL B 165 1 N VAL B 163 O ILE B 211
SHEET 7 E 8 LEU B 124 SER B 129 1 N ALA B 128 O LYS B 164
SHEET 8 E 8 HIS B 339 HIS B 341 1 O HIS B 341 N SER B 129
SHEET 1 F 8 THR B 311 VAL B 312 0
SHEET 2 F 8 VAL B 284 ILE B 285 1 N ILE B 285 O THR B 311
SHEET 3 F 8 LEU B 261 SER B 263 1 O LEU B 261 N VAL B 284
SHEET 4 F 8 ILE B 235 GLU B 239 1 N TYR B 238 O ALA B 262
SHEET 5 F 8 ASP B 209 GLU B 213 1 N VAL B 212 O GLU B 239
SHEET 6 F 8 ALA B 162 VAL B 165 1 N VAL B 163 O ILE B 211
SHEET 7 F 8 LEU B 124 SER B 129 1 N ALA B 128 O LYS B 164
SHEET 8 F 8 ARG B 364 TYR B 365 -1 O TYR B 365 N LEU B 124
SHEET 1 G 5 TYR C 33 ALA C 38 0
SHEET 2 G 5 ILE C 22 THR C 28 -1 N VAL C 26 O GLY C 34
SHEET 3 G 5 ILE C 3 VAL C 11 -1 N PHE C 9 O LEU C 23
SHEET 4 G 5 SER C 385 GLU C 391 -1 O VAL C 388 N ILE C 8
SHEET 5 G 5 HIS C 396 HIS C 397 -1 O HIS C 397 N SER C 389
SHEET 1 H 8 THR C 311 VAL C 312 0
SHEET 2 H 8 VAL C 284 ILE C 285 1 N ILE C 285 O THR C 311
SHEET 3 H 8 LEU C 261 SER C 263 1 O LEU C 261 N VAL C 284
SHEET 4 H 8 ILE C 235 GLU C 239 1 N TYR C 238 O ALA C 262
SHEET 5 H 8 ASP C 209 GLU C 213 1 N ILE C 210 O PHE C 236
SHEET 6 H 8 ALA C 162 VAL C 165 1 N VAL C 163 O ILE C 211
SHEET 7 H 8 LEU C 124 SER C 129 1 N ALA C 128 O LYS C 164
SHEET 8 H 8 HIS C 339 HIS C 342 1 O HIS C 339 N TYR C 127
SHEET 1 I 8 THR C 311 VAL C 312 0
SHEET 2 I 8 VAL C 284 ILE C 285 1 N ILE C 285 O THR C 311
SHEET 3 I 8 LEU C 261 SER C 263 1 O LEU C 261 N VAL C 284
SHEET 4 I 8 ILE C 235 GLU C 239 1 N TYR C 238 O ALA C 262
SHEET 5 I 8 ASP C 209 GLU C 213 1 N ILE C 210 O PHE C 236
SHEET 6 I 8 ALA C 162 VAL C 165 1 N VAL C 163 O ILE C 211
SHEET 7 I 8 LEU C 124 SER C 129 1 N ALA C 128 O LYS C 164
SHEET 8 I 8 ARG C 364 TYR C 365 -1 O TYR C 365 N LEU C 124
SHEET 1 J 5 TYR D 33 ALA D 38 0
SHEET 2 J 5 ILE D 22 THR D 28 -1 N VAL D 26 O GLY D 34
SHEET 3 J 5 ILE D 3 VAL D 11 -1 N GLU D 7 O LYS D 25
SHEET 4 J 5 SER D 385 GLU D 391 -1 O VAL D 388 N ILE D 8
SHEET 5 J 5 HIS D 396 HIS D 397 -1 O HIS D 397 N SER D 389
SHEET 1 K 8 THR D 311 VAL D 312 0
SHEET 2 K 8 VAL D 284 ILE D 285 1 N ILE D 285 O THR D 311
SHEET 3 K 8 LEU D 261 SER D 263 1 O LEU D 261 N VAL D 284
SHEET 4 K 8 ILE D 235 GLU D 239 1 N TYR D 238 O ALA D 262
SHEET 5 K 8 ASP D 209 GLU D 213 1 N VAL D 212 O GLU D 239
SHEET 6 K 8 ALA D 162 VAL D 165 1 N VAL D 163 O ILE D 211
SHEET 7 K 8 LEU D 124 SER D 129 1 N ALA D 128 O LYS D 164
SHEET 8 K 8 HIS D 339 HIS D 342 1 O HIS D 339 N TYR D 127
SHEET 1 L 8 THR D 311 VAL D 312 0
SHEET 2 L 8 VAL D 284 ILE D 285 1 N ILE D 285 O THR D 311
SHEET 3 L 8 LEU D 261 SER D 263 1 O LEU D 261 N VAL D 284
SHEET 4 L 8 ILE D 235 GLU D 239 1 N TYR D 238 O ALA D 262
SHEET 5 L 8 ASP D 209 GLU D 213 1 N VAL D 212 O GLU D 239
SHEET 6 L 8 ALA D 162 VAL D 165 1 N VAL D 163 O ILE D 211
SHEET 7 L 8 LEU D 124 SER D 129 1 N ALA D 128 O LYS D 164
SHEET 8 L 8 ARG D 364 TYR D 365 -1 O TYR D 365 N LEU D 124
SHEET 1 M 4 TYR E 33 ALA E 38 0
SHEET 2 M 4 ILE E 22 THR E 28 -1 N VAL E 26 O GLY E 34
SHEET 3 M 4 ILE E 3 VAL E 11 -1 N LYS E 5 O SER E 27
SHEET 4 M 4 SER E 385 GLU E 391 -1 O VAL E 388 N ILE E 8
SHEET 1 N 8 THR E 311 VAL E 312 0
SHEET 2 N 8 VAL E 284 ILE E 285 1 N ILE E 285 O THR E 311
SHEET 3 N 8 LEU E 261 SER E 263 1 O LEU E 261 N VAL E 284
SHEET 4 N 8 TYR E 238 GLU E 239 1 N TYR E 238 O ALA E 262
SHEET 5 N 8 ASP E 209 GLU E 213 1 N VAL E 212 O GLU E 239
SHEET 6 N 8 ALA E 162 VAL E 165 1 N VAL E 163 O ILE E 211
SHEET 7 N 8 LEU E 124 SER E 129 1 N ALA E 128 O LYS E 164
SHEET 8 N 8 HIS E 339 HIS E 342 1 O HIS E 339 N TYR E 127
SHEET 1 O 8 THR E 311 VAL E 312 0
SHEET 2 O 8 VAL E 284 ILE E 285 1 N ILE E 285 O THR E 311
SHEET 3 O 8 LEU E 261 SER E 263 1 O LEU E 261 N VAL E 284
SHEET 4 O 8 TYR E 238 GLU E 239 1 N TYR E 238 O ALA E 262
SHEET 5 O 8 ASP E 209 GLU E 213 1 N VAL E 212 O GLU E 239
SHEET 6 O 8 ALA E 162 VAL E 165 1 N VAL E 163 O ILE E 211
SHEET 7 O 8 LEU E 124 SER E 129 1 N ALA E 128 O LYS E 164
SHEET 8 O 8 ARG E 364 TYR E 365 -1 O TYR E 365 N LEU E 124
SHEET 1 P 4 TYR F 33 ALA F 38 0
SHEET 2 P 4 ILE F 22 THR F 28 -1 N VAL F 26 O GLY F 34
SHEET 3 P 4 ILE F 3 VAL F 11 -1 N LYS F 5 O SER F 27
SHEET 4 P 4 SER F 385 ILE F 390 -1 O VAL F 388 N ILE F 8
SHEET 1 Q 8 THR F 311 VAL F 312 0
SHEET 2 Q 8 VAL F 284 ILE F 285 1 N ILE F 285 O THR F 311
SHEET 3 Q 8 LEU F 261 SER F 263 1 O LEU F 261 N VAL F 284
SHEET 4 Q 8 ILE F 235 GLU F 239 1 N TYR F 238 O ALA F 262
SHEET 5 Q 8 ASP F 209 GLU F 213 1 N VAL F 212 O GLU F 239
SHEET 6 Q 8 ALA F 162 VAL F 165 1 N VAL F 163 O ILE F 211
SHEET 7 Q 8 LEU F 124 SER F 129 1 N ALA F 128 O LYS F 164
SHEET 8 Q 8 HIS F 339 HIS F 342 1 O HIS F 339 N TYR F 127
SHEET 1 R 8 THR F 311 VAL F 312 0
SHEET 2 R 8 VAL F 284 ILE F 285 1 N ILE F 285 O THR F 311
SHEET 3 R 8 LEU F 261 SER F 263 1 O LEU F 261 N VAL F 284
SHEET 4 R 8 ILE F 235 GLU F 239 1 N TYR F 238 O ALA F 262
SHEET 5 R 8 ASP F 209 GLU F 213 1 N VAL F 212 O GLU F 239
SHEET 6 R 8 ALA F 162 VAL F 165 1 N VAL F 163 O ILE F 211
SHEET 7 R 8 LEU F 124 SER F 129 1 N ALA F 128 O LYS F 164
SHEET 8 R 8 ARG F 364 TYR F 365 -1 O TYR F 365 N LEU F 124
SHEET 1 S 4 TYR G 33 ALA G 38 0
SHEET 2 S 4 ILE G 22 THR G 28 -1 N VAL G 26 O GLY G 34
SHEET 3 S 4 ILE G 3 VAL G 11 -1 N LYS G 5 O SER G 27
SHEET 4 S 4 SER G 385 GLU G 391 -1 O ASP G 386 N HIS G 10
SHEET 1 T 3 HIS G 339 HIS G 341 0
SHEET 2 T 3 LEU G 124 ALA G 128 1 N TYR G 127 O HIS G 339
SHEET 3 T 3 ARG G 364 TYR G 365 -1 O TYR G 365 N LEU G 124
SHEET 1 U 6 ALA G 162 VAL G 165 0
SHEET 2 U 6 ASP G 209 GLU G 213 1 O ILE G 211 N VAL G 163
SHEET 3 U 6 ILE G 235 GLU G 239 1 O GLU G 239 N VAL G 212
SHEET 4 U 6 LEU G 261 SER G 263 1 O ALA G 262 N TYR G 238
SHEET 5 U 6 VAL G 284 ILE G 285 1 N VAL G 284 O LEU G 261
SHEET 6 U 6 THR G 311 VAL G 312 1 O THR G 311 N ILE G 285
SHEET 1 V 4 TYR H 33 ALA H 38 0
SHEET 2 V 4 ILE H 22 THR H 28 -1 N VAL H 26 O GLY H 34
SHEET 3 V 4 ILE H 3 VAL H 11 -1 N LYS H 5 O SER H 27
SHEET 4 V 4 SER H 385 GLU H 391 -1 O VAL H 388 N ILE H 8
SHEET 1 W 8 THR H 311 VAL H 312 0
SHEET 2 W 8 VAL H 284 ILE H 285 1 N ILE H 285 O THR H 311
SHEET 3 W 8 LEU H 261 SER H 263 1 O LEU H 261 N VAL H 284
SHEET 4 W 8 ILE H 235 GLU H 239 1 N TYR H 238 O ALA H 262
SHEET 5 W 8 ASP H 209 GLU H 213 1 N VAL H 212 O GLU H 239
SHEET 6 W 8 ALA H 162 VAL H 165 1 N VAL H 163 O ILE H 211
SHEET 7 W 8 LEU H 124 SER H 129 1 N ALA H 128 O LYS H 164
SHEET 8 W 8 HIS H 339 HIS H 342 1 O HIS H 339 N TYR H 127
SHEET 1 X 8 THR H 311 VAL H 312 0
SHEET 2 X 8 VAL H 284 ILE H 285 1 N ILE H 285 O THR H 311
SHEET 3 X 8 LEU H 261 SER H 263 1 O LEU H 261 N VAL H 284
SHEET 4 X 8 ILE H 235 GLU H 239 1 N TYR H 238 O ALA H 262
SHEET 5 X 8 ASP H 209 GLU H 213 1 N VAL H 212 O GLU H 239
SHEET 6 X 8 ALA H 162 VAL H 165 1 N VAL H 163 O ILE H 211
SHEET 7 X 8 LEU H 124 SER H 129 1 N ALA H 128 O LYS H 164
SHEET 8 X 8 ARG H 364 TYR H 365 -1 O TYR H 365 N LEU H 124
LINK OE1AGLU A 213 MG MG A 402 1555 1555 2.38
LINK OE1BGLU A 213 MG MG A 402 1555 1555 2.25
LINK OE2 GLU A 239 MG MG A 402 1555 1555 2.12
LINK OE1 GLU A 265 MG MG A 402 1555 1555 2.06
LINK MG MG A 402 O HOH A3470 1555 1555 2.12
LINK MG MG A 402 O HOH A3504 1555 1555 2.36
LINK MG MG A 402 O HOH A3575 1555 1555 2.20
LINK OE1AGLU B 213 MG MG B 502 1555 1555 2.36
LINK OE1BGLU B 213 MG MG B 502 1555 1555 2.25
LINK OE2 GLU B 239 MG MG B 502 1555 1555 2.17
LINK OE1 GLU B 265 MG MG B 502 1555 1555 2.09
LINK MG MG B 502 O HOH B3509 1555 1555 2.14
LINK MG MG B 502 O HOH B3594 1555 1555 2.36
LINK MG MG B 502 O HOH B3766 1555 1555 2.17
LINK OE1 GLU C 213 MG MG C 402 1555 1555 2.24
LINK OE2 GLU C 239 MG MG C 402 1555 1555 2.09
LINK OE1 GLU C 265 MG MG C 402 1555 1555 2.11
LINK MG MG C 402 O HOH C3447 1555 1555 2.21
LINK MG MG C 402 O HOH C3506 1555 1555 2.36
LINK MG MG C 402 O HOH C3576 1555 1555 2.10
LINK OE1 GLU D 213 MG MG D 402 1555 1555 2.26
LINK OE2 GLU D 239 MG MG D 402 1555 1555 2.16
LINK OE1 GLU D 265 MG MG D 402 1555 1555 2.11
LINK MG MG D 402 O HOH D3519 1555 1555 2.18
LINK MG MG D 402 O HOH D3550 1555 1555 2.23
LINK MG MG D 402 O HOH D3564 1555 1555 2.04
LINK OE1AGLU E 213 MG MG E 402 1555 1555 2.31
LINK OE2BGLU E 213 MG MG E 402 1555 1555 2.18
LINK OE2 GLU E 239 MG MG E 402 1555 1555 2.12
LINK OE1 GLU E 265 MG MG E 402 1555 1555 2.14
LINK MG MG E 402 O HOH E3453 1555 1555 2.24
LINK MG MG E 402 O HOH E3534 1555 1555 2.14
LINK MG MG E 402 O HOH E3574 1555 1555 2.24
LINK OE1 GLU F 213 MG MG F 402 1555 1555 2.35
LINK OE2 GLU F 239 MG MG F 402 1555 1555 2.08
LINK OE1 GLU F 265 MG MG F 402 1555 1555 2.11
LINK MG MG F 402 O HOH F3486 1555 1555 2.15
LINK MG MG F 402 O HOH F3534 1555 1555 2.18
LINK MG MG F 402 O HOH F3536 1555 1555 2.16
LINK OE1AGLU G 213 MG MG G 502 1555 1555 2.31
LINK OE2BGLU G 213 MG MG G 502 1555 1555 2.16
LINK OE2 GLU G 239 MG MG G 502 1555 1555 2.11
LINK OE1 GLU G 265 MG MG G 502 1555 1555 2.05
LINK MG MG G 502 O HOH G3525 1555 1555 2.08
LINK MG MG G 502 O HOH G3539 1555 1555 2.22
LINK MG MG G 502 O HOH G3586 1555 1555 2.31
LINK OE1 GLU H 213 MG MG H 402 1555 1555 2.32
LINK OE2 GLU H 239 MG MG H 402 1555 1555 2.05
LINK OE1 GLU H 265 MG MG H 402 1555 1555 2.13
LINK MG MG H 402 O HOH H3494 1555 1555 2.07
LINK MG MG H 402 O HOH H3520 1555 1555 2.08
LINK MG MG H 402 O HOH H3593 1555 1555 2.18
SITE 1 AC1 6 GLU A 213 GLU A 239 GLU A 265 HOH A3470
SITE 2 AC1 6 HOH A3504 HOH A3575
SITE 1 AC2 8 GLY A 86 THR A 87 VAL A 88 ILE A 89
SITE 2 AC2 8 GLY B 86 THR B 87 VAL B 88 ILE B 89
SITE 1 AC3 6 GLU B 213 GLU B 239 GLU B 265 HOH B3509
SITE 2 AC3 6 HOH B3594 HOH B3766
SITE 1 AC4 6 GLU C 213 GLU C 239 GLU C 265 HOH C3447
SITE 2 AC4 6 HOH C3506 HOH C3576
SITE 1 AC5 6 GLU D 213 GLU D 239 GLU D 265 HOH D3519
SITE 2 AC5 6 HOH D3550 HOH D3564
SITE 1 AC6 8 GLY D 86 THR D 87 VAL D 88 ILE D 89
SITE 2 AC6 8 GLY E 86 THR E 87 VAL E 88 ILE E 89
SITE 1 AC7 6 GLU E 213 GLU E 239 GLU E 265 HOH E3453
SITE 2 AC7 6 HOH E3534 HOH E3574
SITE 1 AC8 6 GLU F 213 GLU F 239 GLU F 265 HOH F3486
SITE 2 AC8 6 HOH F3534 HOH F3536
SITE 1 AC9 8 GLY F 86 THR F 87 VAL F 88 ILE F 89
SITE 2 AC9 8 GLY H 86 THR H 87 VAL H 88 ILE H 89
SITE 1 BC1 8 GLY C 86 THR C 87 VAL C 88 ILE C 89
SITE 2 BC1 8 GLY G 86 THR G 87 VAL G 88 ILE G 89
SITE 1 BC2 6 GLU G 213 GLU G 239 GLU G 265 HOH G3525
SITE 2 BC2 6 HOH G3539 HOH G3586
SITE 1 BC3 6 GLU H 213 GLU H 239 GLU H 265 HOH H3494
SITE 2 BC3 6 HOH H3520 HOH H3593
SITE 1 BC4 11 HIS A 10 ARG A 20 GLY A 43 VAL A 44
SITE 2 BC4 11 GLY A 45 GLY A 46 HOH A3473 HOH A3733
SITE 3 BC4 11 HOH A3736 ASP B 55 HOH B3504
SITE 1 BC5 11 TRP A 101 LEU A 115 LEU A 116 GLY A 117
SITE 2 BC5 11 LYS A 299 TRP H 101 LEU H 115 LEU H 116
SITE 3 BC5 11 GLY H 117 LYS H 299 HOH H3578
SITE 1 BC6 11 ASP A 55 HOH A3502 HIS B 10 ARG B 20
SITE 2 BC6 11 GLY B 43 VAL B 44 GLY B 45 GLY B 46
SITE 3 BC6 11 HOH B3510 HOH B3760 HOH B3796
SITE 1 BC7 11 TRP B 101 LEU B 115 LEU B 116 HOH B3670
SITE 2 BC7 11 TRP C 101 LEU C 115 LEU C 116 GLY C 117
SITE 3 BC7 11 LYS C 299 HOH C3633 HOH C3783
SITE 1 BC8 11 HIS C 10 ARG C 20 GLY C 43 VAL C 44
SITE 2 BC8 11 GLY C 45 GLY C 46 HOH C3454 HOH C3599
SITE 3 BC8 11 HOH C3785 ASP G 55 HOH G3497
SITE 1 BC9 11 HIS D 10 ARG D 20 GLY D 43 VAL D 44
SITE 2 BC9 11 GLY D 45 GLY D 46 HOH D3499 HOH D3655
SITE 3 BC9 11 HOH D3746 ASP E 55 HOH E3565
SITE 1 CC1 7 GLN D 19 TYR D 42 ARG D 139 ALA D 317
SITE 2 CC1 7 HIS D 342 LYS D 344 HOH D3616
SITE 1 CC2 10 ASP D 55 HOH D3488 HIS E 10 ARG E 20
SITE 2 CC2 10 GLY E 43 VAL E 44 GLY E 45 GLY E 46
SITE 3 CC2 10 HOH E3558 HOH E3642
SITE 1 CC3 10 HIS F 10 ARG F 20 GLY F 43 VAL F 44
SITE 2 CC3 10 GLY F 45 GLY F 46 HOH F3471 HOH F3523
SITE 3 CC3 10 HOH F3800 ASP H 55
SITE 1 CC4 7 LYS F 25 TYR F 33 ASP F 376 ILE F 377
SITE 2 CC4 7 GLU F 379 TYR F 382 HOH F3684
SITE 1 CC5 10 ASP C 55 HOH C3571 HIS G 10 ARG G 20
SITE 2 CC5 10 GLY G 43 VAL G 44 GLY G 45 GLY G 46
SITE 3 CC5 10 HOH G3551 HOH G3585
SITE 1 CC6 6 LYS D 114 SER G 0 LEU G 1 ASP G 64
SITE 2 CC6 6 PHE G 66 HOH G3747
SITE 1 CC7 8 GLY G 178 VAL G 179 PHE G 180 PRO G 186
SITE 2 CC7 8 THR G 189 HOH G3564 HOH G3615 HOH G3637
SITE 1 CC8 11 ASP F 55 HOH F3487 HIS H 10 ARG H 20
SITE 2 CC8 11 GLY H 43 VAL H 44 GLY H 45 GLY H 46
SITE 3 CC8 11 HOH H3533 HOH H3701 HOH H3704
CRYST1 190.178 190.409 85.922 90.00 90.00 90.00 P 21 21 2 32
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 0.005258 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011638 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
