HEADER ISOMERASE 22-DEC-10 3Q45
TITLE CRYSTAL STRUCTURE OF DIPEPTIDE EPIMERASE FROM CYTOPHAGA HUTCHINSONII
TITLE 2 COMPLEXED WITH MG AND DIPEPTIDE D-ALA-L-VAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANDELATE RACEMASE/MUCONATE LACTONIZING ENZYME FAMILY;
COMPND 3 POSSIBLE CHLOROMUCONATE CYCLOISOMERASE;
COMPND 4 CHAIN: A, B, C, D, E, F, G, H, I;
COMPND 5 EC: 5.5.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYTOPHAGA HUTCHINSONII;
SOURCE 3 ORGANISM_TAXID: 269798;
SOURCE 4 STRAIN: ATCC 33406;
SOURCE 5 GENE: CHU2140, CHU_2140, TFDD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-17B
KEYWDS (BETA/ALPHA)8-BARREL, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LUKK,J.A.GERLT,S.K.NAIR
REVDAT 7 13-SEP-23 3Q45 1 REMARK LINK
REVDAT 6 11-OCT-17 3Q45 1 REMARK
REVDAT 5 28-MAR-12 3Q45 1 JRNL
REVDAT 4 21-MAR-12 3Q45 1 JRNL
REVDAT 3 14-MAR-12 3Q45 1 JRNL
REVDAT 2 22-FEB-12 3Q45 1 JRNL VERSN
REVDAT 1 16-FEB-11 3Q45 0
JRNL AUTH T.LUKK,A.SAKAI,C.KALYANARAMAN,S.D.BROWN,H.J.IMKER,L.SONG,
JRNL AUTH 2 A.A.FEDOROV,E.V.FEDOROV,R.TORO,B.HILLERICH,R.SEIDEL,
JRNL AUTH 3 Y.PATSKOVSKY,M.W.VETTING,S.K.NAIR,P.C.BABBITT,S.C.ALMO,
JRNL AUTH 4 J.A.GERLT,M.P.JACOBSON
JRNL TITL HOMOLOGY MODELS GUIDE DISCOVERY OF DIVERSE ENZYME
JRNL TITL 2 SPECIFICITIES AMONG DIPEPTIDE EPIMERASES IN THE ENOLASE
JRNL TITL 3 SUPERFAMILY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 4122 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22392983
JRNL DOI 10.1073/PNAS.1112081109
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 99570
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5241
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7209
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 380
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25434
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.388
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25983 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 35154 ; 1.026 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3312 ; 4.892 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1062 ;36.441 ;24.746
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4608 ;17.341 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 117 ;23.647 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4095 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19161 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 16506 ; 5.792 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 26604 ; 7.843 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9477 ; 8.538 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8550 ;11.381 ; 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 : 1.40
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 3Q45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104809
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.560
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1TKK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT CONTAINED 12% PEG 10000
REMARK 280 AND 0.1M NA-CITRATE, PROTEIN SOLUTION CONTAINED 0.1M NACL, 10%
REMARK 280 GLYCEROL, AND 0.02M D-ALA-L-VAL. PROTEIN CONCENTRATION WAS 40 MG/
REMARK 280 ML, PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 79.10000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
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: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU G 73 O HOH G 369 2.18
REMARK 500 O GLN B 255 NE2 GLN G 284 2.19
REMARK 500 NE2 GLN B 284 O GLN G 255 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 54 -46.91 -130.58
REMARK 500 ALA A 181 -15.20 -147.12
REMARK 500 ASN A 211 73.90 54.07
REMARK 500 GLU A 217 76.89 36.64
REMARK 500 ALA A 233 47.83 -100.15
REMARK 500 CYS A 234 122.73 -174.14
REMARK 500 ASP A 241 -84.34 -112.91
REMARK 500 GLN A 257 60.66 39.86
REMARK 500 PHE A 294 -109.92 -118.79
REMARK 500 ASP A 357 17.90 51.69
REMARK 500 ILE B 54 -50.35 -127.72
REMARK 500 ALA B 181 -15.87 -144.40
REMARK 500 ASN B 211 71.07 54.96
REMARK 500 GLU B 217 75.75 37.45
REMARK 500 ASP B 241 -85.04 -114.57
REMARK 500 PHE B 294 -110.59 -113.17
REMARK 500 CYS B 315 1.19 -150.77
REMARK 500 ASP B 357 20.21 47.33
REMARK 500 CYS C 78 0.06 -68.36
REMARK 500 ALA C 181 -16.26 -146.54
REMARK 500 ASN C 211 72.09 54.30
REMARK 500 GLU C 217 76.87 40.46
REMARK 500 ASP C 241 -86.11 -111.35
REMARK 500 PHE C 294 -113.09 -119.39
REMARK 500 CYS C 315 -0.66 -150.34
REMARK 500 GLN C 355 150.43 -49.57
REMARK 500 ASP C 357 19.34 51.49
REMARK 500 CYS D 78 0.97 -67.50
REMARK 500 ALA D 181 -16.05 -147.33
REMARK 500 ASN D 211 72.05 54.95
REMARK 500 GLU D 217 76.62 38.43
REMARK 500 ASP D 241 -85.04 -110.96
REMARK 500 PHE D 294 -112.44 -115.47
REMARK 500 CYS D 315 0.17 -150.21
REMARK 500 GLN D 355 153.58 -49.41
REMARK 500 ASP D 357 18.18 49.59
REMARK 500 CYS E 78 1.37 -67.78
REMARK 500 ALA E 181 -14.48 -147.02
REMARK 500 ASN E 211 74.52 55.01
REMARK 500 GLU E 217 74.22 39.33
REMARK 500 ASP E 241 -86.22 -111.55
REMARK 500 PHE E 294 -110.86 -118.15
REMARK 500 CYS E 315 2.58 -150.44
REMARK 500 GLN E 355 153.34 -47.26
REMARK 500 ASP E 357 20.29 47.59
REMARK 500 CYS F 78 3.43 -67.36
REMARK 500 ALA F 181 -15.74 -144.26
REMARK 500 ASN F 211 72.82 56.67
REMARK 500 GLU F 217 77.72 36.59
REMARK 500 ASP F 241 -88.32 -108.74
REMARK 500
REMARK 500 THIS ENTRY HAS 83 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 A1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 190 OD2
REMARK 620 2 GLU A 216 OE1 70.4
REMARK 620 3 ASP A 241 OD2 146.5 84.6
REMARK 620 4 VAL A2471 OXT 61.3 103.0 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 190 OD2
REMARK 620 2 GLU B 216 OE1 77.9
REMARK 620 3 ASP B 241 OD2 166.3 89.3
REMARK 620 4 VAL B2473 O 95.2 101.3 92.1
REMARK 620 5 VAL B2473 OXT 74.5 132.0 118.4 44.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 190 OD2
REMARK 620 2 GLU C 216 OE1 63.6
REMARK 620 3 ASP C 241 OD2 126.3 76.5
REMARK 620 4 VAL C2475 O 69.2 65.6 62.1
REMARK 620 5 VAL C2475 OXT 56.0 95.5 96.7 42.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 190 OD2
REMARK 620 2 GLU D 216 OE1 66.8
REMARK 620 3 ASP D 241 OD2 144.7 84.4
REMARK 620 4 VAL D2477 OXT 90.2 97.0 72.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E1605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 190 OD2
REMARK 620 2 GLU E 216 OE1 68.0
REMARK 620 3 ASP E 241 OD2 138.0 73.8
REMARK 620 4 VAL E2479 OXT 63.7 103.2 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F1606 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 190 OD2
REMARK 620 2 GLU F 216 OE1 82.8
REMARK 620 3 ASP F 241 OD2 153.5 90.7
REMARK 620 4 VAL F2481 OXT 63.9 92.3 91.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G1607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 190 OD2
REMARK 620 2 GLU G 216 OE1 84.0
REMARK 620 3 ASP G 241 OD2 165.4 90.9
REMARK 620 4 HOH G 379 O 88.8 129.2 105.0
REMARK 620 5 VAL G2483 O 86.5 95.3 80.4 134.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H1608 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 190 OD2
REMARK 620 2 GLU H 216 OE1 69.9
REMARK 620 3 ASP H 241 OD2 139.6 72.4
REMARK 620 4 VAL H2485 O 84.3 81.2 75.9
REMARK 620 5 VAL H2485 OXT 68.8 112.3 114.1 43.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I1609 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 190 OD2
REMARK 620 2 GLU I 216 OE1 77.3
REMARK 620 3 ASP I 241 OD2 151.4 82.6
REMARK 620 4 VAL I2487 OXT 80.2 128.1 96.8
REMARK 620 5 VAL I2487 O 80.0 85.9 78.5 44.1
REMARK 620 N 1 2 3 4
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 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL A 2470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL A 2471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL B 2472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL B 2473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL C 2474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL C 2475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL D 2476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL D 2477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL E 2478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL E 2479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL F 2480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL F 2481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL G 2482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL G 2483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL H 2484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL H 2485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAL I 2486
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL I 2487
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q4D RELATED DB: PDB
DBREF 3Q45 A 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 B 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 C 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 D 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 E 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 F 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 G 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 H 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
DBREF 3Q45 I 1 368 UNP Q11T61 Q11T61_CYTH3 1 368
SEQRES 1 A 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 A 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 A 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 A 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 A 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 A 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 A 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 A 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 A 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 A 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 A 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 A 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 A 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 A 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 A 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 A 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 A 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 A 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 A 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 A 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 A 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 A 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 A 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 A 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 A 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 A 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 A 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 A 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 A 368 ILE CYS ILE ASN
SEQRES 1 B 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 B 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 B 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 B 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 B 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 B 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 B 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 B 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 B 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 B 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 B 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 B 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 B 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 B 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 B 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 B 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 B 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 B 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 B 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 B 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 B 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 B 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 B 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 B 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 B 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 B 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 B 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 B 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 B 368 ILE CYS ILE ASN
SEQRES 1 C 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 C 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 C 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 C 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 C 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 C 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 C 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 C 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 C 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 C 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 C 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 C 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 C 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 C 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 C 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 C 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 C 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 C 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 C 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 C 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 C 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 C 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 C 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 C 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 C 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 C 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 C 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 C 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 C 368 ILE CYS ILE ASN
SEQRES 1 D 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 D 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 D 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 D 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 D 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 D 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 D 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 D 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 D 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 D 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 D 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 D 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 D 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 D 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 D 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 D 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 D 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 D 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 D 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 D 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 D 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 D 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 D 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 D 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 D 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 D 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 D 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 D 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 D 368 ILE CYS ILE ASN
SEQRES 1 E 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 E 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 E 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 E 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 E 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 E 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 E 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 E 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 E 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 E 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 E 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 E 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 E 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 E 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 E 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 E 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 E 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 E 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 E 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 E 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 E 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 E 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 E 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 E 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 E 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 E 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 E 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 E 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 E 368 ILE CYS ILE ASN
SEQRES 1 F 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 F 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 F 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 F 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 F 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 F 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 F 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 F 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 F 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 F 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 F 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 F 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 F 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 F 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 F 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 F 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 F 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 F 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 F 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 F 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 F 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 F 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 F 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 F 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 F 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 F 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 F 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 F 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 F 368 ILE CYS ILE ASN
SEQRES 1 G 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 G 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 G 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 G 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 G 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 G 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 G 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 G 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 G 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 G 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 G 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 G 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 G 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 G 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 G 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 G 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 G 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 G 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 G 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 G 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 G 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 G 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 G 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 G 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 G 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 G 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 G 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 G 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 G 368 ILE CYS ILE ASN
SEQRES 1 H 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 H 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 H 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 H 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 H 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 H 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 H 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 H 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 H 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 H 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 H 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 H 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 H 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 H 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 H 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 H 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 H 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 H 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 H 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 H 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 H 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 H 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 H 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 H 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 H 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 H 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 H 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 H 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 H 368 ILE CYS ILE ASN
SEQRES 1 I 368 MET ILE ILE THR GLN VAL GLU LEU TYR LYS SER PRO VAL
SEQRES 2 I 368 LYS LEU LYS GLU PRO PHE LYS ILE SER LEU GLY ILE LEU
SEQRES 3 I 368 THR HIS ALA ASN ASN VAL ILE VAL ARG ILE HIS THR ALA
SEQRES 4 I 368 SER GLY HIS ILE GLY TYR GLY GLU CYS SER PRO PHE MET
SEQRES 5 I 368 THR ILE HIS GLY GLU SER MET ASP THR ALA PHE ILE VAL
SEQRES 6 I 368 GLY GLN TYR LEU ALA LYS GLY LEU ILE GLY THR SER CYS
SEQRES 7 I 368 LEU ASP ILE VAL SER ASN SER LEU LEU MET ASP ALA ILE
SEQRES 8 I 368 ILE TYR GLY ASN SER CYS ILE LYS SER ALA PHE ASN ILE
SEQRES 9 I 368 ALA LEU TYR ASP LEU ALA ALA GLN HIS ALA GLY LEU PRO
SEQRES 10 I 368 LEU TYR ALA PHE LEU GLY GLY LYS LYS ASP LYS ILE ILE
SEQRES 11 I 368 GLN THR ASP TYR THR VAL SER ILE ASP GLU PRO HIS LYS
SEQRES 12 I 368 MET ALA ALA ASP ALA VAL GLN ILE LYS LYS ASN GLY PHE
SEQRES 13 I 368 GLU ILE ILE LYS VAL LYS VAL GLY GLY SER LYS GLU LEU
SEQRES 14 I 368 ASP VAL GLU ARG ILE ARG MET ILE ARG GLU ALA ALA GLY
SEQRES 15 I 368 ASP SER ILE THR LEU ARG ILE ASP ALA ASN GLN GLY TRP
SEQRES 16 I 368 SER VAL GLU THR ALA ILE GLU THR LEU THR LEU LEU GLU
SEQRES 17 I 368 PRO TYR ASN ILE GLN HIS CYS GLU GLU PRO VAL SER ARG
SEQRES 18 I 368 ASN LEU TYR THR ALA LEU PRO LYS ILE ARG GLN ALA CYS
SEQRES 19 I 368 ARG ILE PRO ILE MET ALA ASP GLU SER CYS CYS ASN SER
SEQRES 20 I 368 PHE ASP ALA GLU ARG LEU ILE GLN ILE GLN ALA CYS ASP
SEQRES 21 I 368 SER PHE ASN LEU LYS LEU SER LYS SER ALA GLY ILE THR
SEQRES 22 I 368 ASN ALA LEU ASN ILE ILE ARG LEU ALA GLU GLN ALA HIS
SEQRES 23 I 368 MET PRO VAL GLN VAL GLY GLY PHE LEU GLU SER ARG LEU
SEQRES 24 I 368 GLY PHE THR ALA ALA ALA HIS VAL ALA LEU VAL SER LYS
SEQRES 25 I 368 THR ILE CYS TYR TYR ASP PHE ASP THR PRO LEU MET PHE
SEQRES 26 I 368 GLU ALA ASP PRO VAL ARG GLY GLY ILE VAL TYR GLN GLN
SEQRES 27 I 368 ARG GLY ILE ILE GLU VAL PRO GLU THR ALA GLY LEU GLY
SEQRES 28 I 368 ALA GLY TYR GLN LYS ASP TYR LEU SER GLY LEU GLU LYS
SEQRES 29 I 368 ILE CYS ILE ASN
HET MG A1601 1
HET DAL A2470 5
HET VAL A2471 8
HET MG B1602 1
HET DAL B2472 5
HET VAL B2473 8
HET MG C1603 1
HET DAL C2474 5
HET VAL C2475 8
HET MG D1604 1
HET DAL D2476 5
HET VAL D2477 8
HET MG E1605 1
HET DAL E2478 5
HET VAL E2479 8
HET MG F1606 1
HET DAL F2480 5
HET VAL F2481 8
HET MG G1607 1
HET DAL G2482 5
HET VAL G2483 8
HET MG H1608 1
HET DAL H2484 5
HET VAL H2485 8
HET MG I1609 1
HET DAL I2486 5
HET VAL I2487 8
HETNAM MG MAGNESIUM ION
HETNAM DAL D-ALANINE
HETNAM VAL VALINE
FORMUL 10 MG 9(MG 2+)
FORMUL 11 DAL 9(C3 H7 N O2)
FORMUL 12 VAL 9(C5 H11 N O2)
FORMUL 37 HOH *103(H2 O)
HELIX 1 1 PHE A 51 GLY A 56 1 6
HELIX 2 2 SER A 58 ILE A 74 1 17
HELIX 3 3 ASP A 80 ILE A 92 1 13
HELIX 4 4 ASN A 95 GLY A 115 1 21
HELIX 5 5 PRO A 117 LEU A 122 1 6
HELIX 6 6 GLU A 140 ASN A 154 1 15
HELIX 7 7 SER A 166 GLY A 182 1 17
HELIX 8 8 SER A 196 GLU A 208 1 13
HELIX 9 9 PRO A 209 ASN A 211 5 3
HELIX 10 10 SER A 220 THR A 225 5 6
HELIX 11 11 ALA A 226 ALA A 233 1 8
HELIX 12 12 ASN A 246 ILE A 256 1 11
HELIX 13 13 GLY A 271 ALA A 285 1 15
HELIX 14 14 SER A 297 LEU A 309 1 13
HELIX 15 15 ASP A 320 PHE A 325 5 6
HELIX 16 16 TYR A 358 LEU A 362 5 5
HELIX 17 17 PHE B 51 GLY B 56 1 6
HELIX 18 18 SER B 58 ILE B 74 1 17
HELIX 19 19 ASP B 80 ILE B 92 1 13
HELIX 20 20 ASN B 95 GLY B 115 1 21
HELIX 21 21 PRO B 117 LEU B 122 1 6
HELIX 22 22 GLU B 140 ASN B 154 1 15
HELIX 23 23 SER B 166 GLY B 182 1 17
HELIX 24 24 SER B 196 GLU B 208 1 13
HELIX 25 25 PRO B 209 ASN B 211 5 3
HELIX 26 26 SER B 220 THR B 225 5 6
HELIX 27 27 ALA B 226 CYS B 234 1 9
HELIX 28 28 ASN B 246 ILE B 256 1 11
HELIX 29 29 GLY B 271 ALA B 285 1 15
HELIX 30 30 SER B 297 LEU B 309 1 13
HELIX 31 31 ASP B 320 PHE B 325 5 6
HELIX 32 32 TYR B 358 LEU B 362 5 5
HELIX 33 33 PHE C 51 GLY C 56 1 6
HELIX 34 34 SER C 58 ILE C 74 1 17
HELIX 35 35 ASP C 80 ILE C 92 1 13
HELIX 36 36 ASN C 95 GLY C 115 1 21
HELIX 37 37 PRO C 117 LEU C 122 1 6
HELIX 38 38 GLU C 140 ASN C 154 1 15
HELIX 39 39 SER C 166 GLY C 182 1 17
HELIX 40 40 SER C 196 GLU C 208 1 13
HELIX 41 41 PRO C 209 ASN C 211 5 3
HELIX 42 42 SER C 220 THR C 225 5 6
HELIX 43 43 ALA C 226 CYS C 234 1 9
HELIX 44 44 ASN C 246 ILE C 256 1 11
HELIX 45 45 LYS C 265 ALA C 270 1 6
HELIX 46 46 GLY C 271 ALA C 285 1 15
HELIX 47 47 SER C 297 LEU C 309 1 13
HELIX 48 48 ASP C 320 PHE C 325 5 6
HELIX 49 49 TYR C 358 LEU C 362 5 5
HELIX 50 50 PHE D 51 GLY D 56 1 6
HELIX 51 51 SER D 58 ILE D 74 1 17
HELIX 52 52 ASP D 80 ILE D 92 1 13
HELIX 53 53 ASN D 95 GLY D 115 1 21
HELIX 54 54 PRO D 117 LEU D 122 1 6
HELIX 55 55 GLU D 140 ASN D 154 1 15
HELIX 56 56 SER D 166 GLY D 182 1 17
HELIX 57 57 SER D 196 GLU D 208 1 13
HELIX 58 58 PRO D 209 ASN D 211 5 3
HELIX 59 59 SER D 220 THR D 225 5 6
HELIX 60 60 ALA D 226 CYS D 234 1 9
HELIX 61 61 ASN D 246 ILE D 256 1 11
HELIX 62 62 GLY D 271 ALA D 285 1 15
HELIX 63 63 SER D 297 LEU D 309 1 13
HELIX 64 64 ASP D 320 PHE D 325 5 6
HELIX 65 65 TYR D 358 LEU D 362 5 5
HELIX 66 66 PHE E 51 GLY E 56 1 6
HELIX 67 67 SER E 58 ILE E 74 1 17
HELIX 68 68 ASP E 80 ILE E 92 1 13
HELIX 69 69 ASN E 95 GLY E 115 1 21
HELIX 70 70 PRO E 117 LEU E 122 1 6
HELIX 71 71 GLU E 140 ASN E 154 1 15
HELIX 72 72 SER E 166 GLY E 182 1 17
HELIX 73 73 SER E 196 GLU E 208 1 13
HELIX 74 74 PRO E 209 ASN E 211 5 3
HELIX 75 75 SER E 220 THR E 225 5 6
HELIX 76 76 ALA E 226 CYS E 234 1 9
HELIX 77 77 ASN E 246 ILE E 256 1 11
HELIX 78 78 GLY E 271 ALA E 285 1 15
HELIX 79 79 SER E 297 LEU E 309 1 13
HELIX 80 80 ASP E 320 PHE E 325 5 6
HELIX 81 81 TYR E 358 LEU E 362 5 5
HELIX 82 82 PHE F 51 GLY F 56 1 6
HELIX 83 83 SER F 58 ILE F 74 1 17
HELIX 84 84 ASP F 80 ILE F 92 1 13
HELIX 85 85 ASN F 95 GLY F 115 1 21
HELIX 86 86 PRO F 117 LEU F 122 1 6
HELIX 87 87 GLU F 140 ASN F 154 1 15
HELIX 88 88 SER F 166 GLY F 182 1 17
HELIX 89 89 SER F 196 GLU F 208 1 13
HELIX 90 90 PRO F 209 ASN F 211 5 3
HELIX 91 91 SER F 220 THR F 225 5 6
HELIX 92 92 ALA F 226 CYS F 234 1 9
HELIX 93 93 ASN F 246 ILE F 256 1 11
HELIX 94 94 LYS F 265 ALA F 270 1 6
HELIX 95 95 GLY F 271 ALA F 285 1 15
HELIX 96 96 SER F 297 LEU F 309 1 13
HELIX 97 97 ASP F 320 PHE F 325 5 6
HELIX 98 98 TYR F 358 LEU F 362 5 5
HELIX 99 99 PHE G 51 GLY G 56 1 6
HELIX 100 100 SER G 58 ILE G 74 1 17
HELIX 101 101 ASP G 80 ILE G 92 1 13
HELIX 102 102 ASN G 95 GLY G 115 1 21
HELIX 103 103 PRO G 117 LEU G 122 1 6
HELIX 104 104 GLU G 140 ASN G 154 1 15
HELIX 105 105 SER G 166 GLY G 182 1 17
HELIX 106 106 SER G 196 GLU G 208 1 13
HELIX 107 107 PRO G 209 ASN G 211 5 3
HELIX 108 108 SER G 220 THR G 225 5 6
HELIX 109 109 ALA G 226 CYS G 234 1 9
HELIX 110 110 ASN G 246 ILE G 256 1 11
HELIX 111 111 GLY G 271 ALA G 285 1 15
HELIX 112 112 SER G 297 LEU G 309 1 13
HELIX 113 113 ASP G 320 PHE G 325 5 6
HELIX 114 114 TYR G 358 LEU G 362 5 5
HELIX 115 115 PHE H 51 GLY H 56 1 6
HELIX 116 116 SER H 58 ILE H 74 1 17
HELIX 117 117 ASP H 80 ILE H 92 1 13
HELIX 118 118 ASN H 95 GLY H 115 1 21
HELIX 119 119 PRO H 117 LEU H 122 1 6
HELIX 120 120 GLU H 140 ASN H 154 1 15
HELIX 121 121 SER H 166 GLY H 182 1 17
HELIX 122 122 SER H 196 GLU H 208 1 13
HELIX 123 123 PRO H 209 ASN H 211 5 3
HELIX 124 124 SER H 220 THR H 225 5 6
HELIX 125 125 ALA H 226 CYS H 234 1 9
HELIX 126 126 ASN H 246 ILE H 256 1 11
HELIX 127 127 GLY H 271 ALA H 285 1 15
HELIX 128 128 SER H 297 LEU H 309 1 13
HELIX 129 129 ASP H 320 PHE H 325 5 6
HELIX 130 130 TYR H 358 LEU H 362 5 5
HELIX 131 131 PHE I 51 GLY I 56 1 6
HELIX 132 132 SER I 58 ILE I 74 1 17
HELIX 133 133 ASP I 80 ILE I 92 1 13
HELIX 134 134 ASN I 95 GLY I 115 1 21
HELIX 135 135 PRO I 117 LEU I 122 1 6
HELIX 136 136 GLU I 140 ASN I 154 1 15
HELIX 137 137 SER I 166 GLY I 182 1 17
HELIX 138 138 SER I 196 GLU I 208 1 13
HELIX 139 139 PRO I 209 ASN I 211 5 3
HELIX 140 140 SER I 220 THR I 225 5 6
HELIX 141 141 ALA I 226 CYS I 234 1 9
HELIX 142 142 ASN I 246 ILE I 256 1 11
HELIX 143 143 GLY I 271 ALA I 285 1 15
HELIX 144 144 SER I 297 LEU I 309 1 13
HELIX 145 145 ASP I 320 PHE I 325 5 6
HELIX 146 146 TYR I 358 LEU I 362 5 5
SHEET 1 A 4 ILE A 43 CYS A 48 0
SHEET 2 A 4 GLY A 24 THR A 38 -1 N VAL A 34 O GLY A 46
SHEET 3 A 4 ILE A 3 ILE A 21 -1 N PHE A 19 O LEU A 26
SHEET 4 A 4 GLU A 363 ILE A 367 -1 O ILE A 367 N VAL A 6
SHEET 1 B 3 ILE A 130 GLN A 131 0
SHEET 2 B 3 ILE A 341 GLU A 343 -1 O ILE A 342 N ILE A 130
SHEET 3 B 3 VAL A 335 TYR A 336 -1 N VAL A 335 O GLU A 343
SHEET 1 C 8 TYR A 134 VAL A 136 0
SHEET 2 C 8 ILE A 158 LYS A 162 1 O LYS A 160 N TYR A 134
SHEET 3 C 8 THR A 186 ASP A 190 1 O ARG A 188 N VAL A 161
SHEET 4 C 8 CYS A 215 GLU A 216 1 O GLU A 216 N ILE A 189
SHEET 5 C 8 ILE A 238 ALA A 240 1 O MET A 239 N CYS A 215
SHEET 6 C 8 SER A 261 LEU A 264 1 O SER A 261 N ALA A 240
SHEET 7 C 8 VAL A 289 VAL A 291 1 O GLN A 290 N LEU A 264
SHEET 8 C 8 ILE A 314 TYR A 317 1 O CYS A 315 N VAL A 289
SHEET 1 D 2 VAL A 330 GLY A 332 0
SHEET 2 D 2 ALA A 352 TYR A 354 -1 O GLY A 353 N ARG A 331
SHEET 1 E 4 ILE B 43 CYS B 48 0
SHEET 2 E 4 GLY B 24 THR B 38 -1 N VAL B 34 O GLY B 46
SHEET 3 E 4 ILE B 3 ILE B 21 -1 N PHE B 19 O LEU B 26
SHEET 4 E 4 GLU B 363 ILE B 367 -1 O ILE B 367 N VAL B 6
SHEET 1 F 3 ILE B 130 GLN B 131 0
SHEET 2 F 3 ILE B 341 GLU B 343 -1 O ILE B 342 N ILE B 130
SHEET 3 F 3 VAL B 335 TYR B 336 -1 N VAL B 335 O GLU B 343
SHEET 1 G 8 TYR B 134 VAL B 136 0
SHEET 2 G 8 ILE B 158 LYS B 162 1 O LYS B 160 N TYR B 134
SHEET 3 G 8 THR B 186 ASP B 190 1 O ARG B 188 N VAL B 161
SHEET 4 G 8 CYS B 215 GLU B 216 1 O GLU B 216 N ILE B 189
SHEET 5 G 8 ILE B 238 ALA B 240 1 O MET B 239 N CYS B 215
SHEET 6 G 8 SER B 261 LEU B 264 1 O ASN B 263 N ALA B 240
SHEET 7 G 8 VAL B 289 VAL B 291 1 O GLN B 290 N PHE B 262
SHEET 8 G 8 ILE B 314 TYR B 317 1 O CYS B 315 N VAL B 289
SHEET 1 H 2 VAL B 330 GLY B 332 0
SHEET 2 H 2 ALA B 352 TYR B 354 -1 O GLY B 353 N ARG B 331
SHEET 1 I 4 ILE C 43 CYS C 48 0
SHEET 2 I 4 GLY C 24 THR C 38 -1 N VAL C 34 O GLY C 46
SHEET 3 I 4 ILE C 3 ILE C 21 -1 N PHE C 19 O LEU C 26
SHEET 4 I 4 LYS C 364 ILE C 367 -1 O ILE C 367 N VAL C 6
SHEET 1 J 3 ILE C 130 GLN C 131 0
SHEET 2 J 3 ILE C 341 GLU C 343 -1 O ILE C 342 N ILE C 130
SHEET 3 J 3 VAL C 335 TYR C 336 -1 N VAL C 335 O GLU C 343
SHEET 1 K 8 TYR C 134 VAL C 136 0
SHEET 2 K 8 ILE C 158 LYS C 162 1 O LYS C 160 N TYR C 134
SHEET 3 K 8 THR C 186 ASP C 190 1 O ARG C 188 N VAL C 161
SHEET 4 K 8 CYS C 215 GLU C 216 1 O GLU C 216 N ILE C 189
SHEET 5 K 8 ILE C 238 ALA C 240 1 O MET C 239 N CYS C 215
SHEET 6 K 8 SER C 261 LEU C 264 1 O ASN C 263 N ALA C 240
SHEET 7 K 8 VAL C 289 VAL C 291 1 O GLN C 290 N LEU C 264
SHEET 8 K 8 ILE C 314 TYR C 317 1 O CYS C 315 N VAL C 289
SHEET 1 L 2 VAL C 330 GLY C 332 0
SHEET 2 L 2 ALA C 352 TYR C 354 -1 O GLY C 353 N ARG C 331
SHEET 1 M 4 ILE D 43 CYS D 48 0
SHEET 2 M 4 GLY D 24 THR D 38 -1 N VAL D 34 O GLY D 46
SHEET 3 M 4 ILE D 3 ILE D 21 -1 N GLN D 5 O HIS D 37
SHEET 4 M 4 GLU D 363 ILE D 367 -1 O ILE D 367 N VAL D 6
SHEET 1 N 3 ILE D 130 GLN D 131 0
SHEET 2 N 3 ILE D 341 GLU D 343 -1 O ILE D 342 N ILE D 130
SHEET 3 N 3 VAL D 335 TYR D 336 -1 N VAL D 335 O GLU D 343
SHEET 1 O 8 TYR D 134 VAL D 136 0
SHEET 2 O 8 ILE D 158 LYS D 162 1 O LYS D 160 N TYR D 134
SHEET 3 O 8 THR D 186 ASP D 190 1 O ARG D 188 N VAL D 161
SHEET 4 O 8 CYS D 215 GLU D 216 1 O GLU D 216 N ILE D 189
SHEET 5 O 8 ILE D 238 ALA D 240 1 O MET D 239 N CYS D 215
SHEET 6 O 8 SER D 261 LEU D 264 1 O ASN D 263 N ALA D 240
SHEET 7 O 8 VAL D 289 VAL D 291 1 O GLN D 290 N LEU D 264
SHEET 8 O 8 ILE D 314 TYR D 317 1 O CYS D 315 N VAL D 289
SHEET 1 P 2 VAL D 330 GLY D 332 0
SHEET 2 P 2 ALA D 352 TYR D 354 -1 O GLY D 353 N ARG D 331
SHEET 1 Q 4 ILE E 43 CYS E 48 0
SHEET 2 Q 4 GLY E 24 THR E 38 -1 N VAL E 34 O GLY E 46
SHEET 3 Q 4 ILE E 3 ILE E 21 -1 N GLN E 5 O HIS E 37
SHEET 4 Q 4 GLU E 363 ILE E 367 -1 O ILE E 367 N VAL E 6
SHEET 1 R 3 ILE E 130 GLN E 131 0
SHEET 2 R 3 ILE E 341 GLU E 343 -1 O ILE E 342 N ILE E 130
SHEET 3 R 3 VAL E 335 TYR E 336 -1 N VAL E 335 O GLU E 343
SHEET 1 S 8 TYR E 134 VAL E 136 0
SHEET 2 S 8 ILE E 158 LYS E 162 1 O LYS E 160 N TYR E 134
SHEET 3 S 8 THR E 186 ASP E 190 1 O ARG E 188 N VAL E 161
SHEET 4 S 8 CYS E 215 GLU E 216 1 O GLU E 216 N ILE E 189
SHEET 5 S 8 ILE E 238 ALA E 240 1 O MET E 239 N CYS E 215
SHEET 6 S 8 SER E 261 LEU E 264 1 O ASN E 263 N ALA E 240
SHEET 7 S 8 VAL E 289 VAL E 291 1 O GLN E 290 N PHE E 262
SHEET 8 S 8 ILE E 314 TYR E 317 1 O CYS E 315 N VAL E 289
SHEET 1 T 2 VAL E 330 GLY E 332 0
SHEET 2 T 2 ALA E 352 TYR E 354 -1 O GLY E 353 N ARG E 331
SHEET 1 U 4 ILE F 43 CYS F 48 0
SHEET 2 U 4 GLY F 24 THR F 38 -1 N VAL F 34 O GLY F 46
SHEET 3 U 4 ILE F 3 ILE F 21 -1 N SER F 11 O ASN F 31
SHEET 4 U 4 LYS F 364 ILE F 367 -1 O ILE F 367 N VAL F 6
SHEET 1 V 3 ILE F 130 GLN F 131 0
SHEET 2 V 3 ILE F 341 GLU F 343 -1 O ILE F 342 N ILE F 130
SHEET 3 V 3 VAL F 335 TYR F 336 -1 N VAL F 335 O GLU F 343
SHEET 1 W 8 TYR F 134 VAL F 136 0
SHEET 2 W 8 ILE F 158 LYS F 162 1 O LYS F 160 N TYR F 134
SHEET 3 W 8 THR F 186 ASP F 190 1 O ARG F 188 N VAL F 161
SHEET 4 W 8 CYS F 215 GLU F 216 1 O GLU F 216 N ILE F 189
SHEET 5 W 8 ILE F 238 ALA F 240 1 O MET F 239 N CYS F 215
SHEET 6 W 8 SER F 261 LEU F 264 1 O SER F 261 N ALA F 240
SHEET 7 W 8 VAL F 289 VAL F 291 1 O GLN F 290 N LEU F 264
SHEET 8 W 8 ILE F 314 TYR F 317 1 O CYS F 315 N VAL F 289
SHEET 1 X 2 VAL F 330 GLY F 332 0
SHEET 2 X 2 ALA F 352 TYR F 354 -1 O GLY F 353 N ARG F 331
SHEET 1 Y 4 ILE G 43 CYS G 48 0
SHEET 2 Y 4 GLY G 24 THR G 38 -1 N VAL G 34 O GLY G 46
SHEET 3 Y 4 ILE G 3 ILE G 21 -1 N PHE G 19 O LEU G 26
SHEET 4 Y 4 GLU G 363 ILE G 367 -1 O ILE G 367 N VAL G 6
SHEET 1 Z 3 ILE G 130 GLN G 131 0
SHEET 2 Z 3 ILE G 341 GLU G 343 -1 O ILE G 342 N ILE G 130
SHEET 3 Z 3 VAL G 335 TYR G 336 -1 N VAL G 335 O GLU G 343
SHEET 1 AA 8 TYR G 134 VAL G 136 0
SHEET 2 AA 8 ILE G 158 LYS G 162 1 O LYS G 160 N TYR G 134
SHEET 3 AA 8 THR G 186 ASP G 190 1 O ARG G 188 N VAL G 161
SHEET 4 AA 8 CYS G 215 GLU G 216 1 O GLU G 216 N ILE G 189
SHEET 5 AA 8 ILE G 238 ALA G 240 1 O MET G 239 N CYS G 215
SHEET 6 AA 8 SER G 261 LEU G 264 1 O SER G 261 N ALA G 240
SHEET 7 AA 8 VAL G 289 VAL G 291 1 O GLN G 290 N LEU G 264
SHEET 8 AA 8 ILE G 314 TYR G 317 1 O TYR G 316 N VAL G 291
SHEET 1 AB 2 VAL G 330 GLY G 332 0
SHEET 2 AB 2 ALA G 352 TYR G 354 -1 O GLY G 353 N ARG G 331
SHEET 1 AC 4 ILE H 43 CYS H 48 0
SHEET 2 AC 4 GLY H 24 THR H 38 -1 N VAL H 34 O GLY H 46
SHEET 3 AC 4 ILE H 3 ILE H 21 -1 N GLN H 5 O HIS H 37
SHEET 4 AC 4 LYS H 364 ILE H 367 -1 O ILE H 367 N VAL H 6
SHEET 1 AD 3 ILE H 130 GLN H 131 0
SHEET 2 AD 3 ILE H 341 GLU H 343 -1 O ILE H 342 N ILE H 130
SHEET 3 AD 3 VAL H 335 TYR H 336 -1 N VAL H 335 O GLU H 343
SHEET 1 AE 8 TYR H 134 VAL H 136 0
SHEET 2 AE 8 ILE H 158 LYS H 162 1 O LYS H 160 N TYR H 134
SHEET 3 AE 8 THR H 186 ASP H 190 1 O ARG H 188 N VAL H 161
SHEET 4 AE 8 CYS H 215 GLU H 216 1 O GLU H 216 N ILE H 189
SHEET 5 AE 8 ILE H 238 ALA H 240 1 O MET H 239 N CYS H 215
SHEET 6 AE 8 SER H 261 LEU H 264 1 O ASN H 263 N ALA H 240
SHEET 7 AE 8 VAL H 289 VAL H 291 1 O GLN H 290 N PHE H 262
SHEET 8 AE 8 ILE H 314 TYR H 317 1 O CYS H 315 N VAL H 289
SHEET 1 AF 2 VAL H 330 GLY H 332 0
SHEET 2 AF 2 ALA H 352 TYR H 354 -1 O GLY H 353 N ARG H 331
SHEET 1 AG 4 ILE I 43 CYS I 48 0
SHEET 2 AG 4 GLY I 24 THR I 38 -1 N VAL I 34 O GLY I 46
SHEET 3 AG 4 ILE I 3 ILE I 21 -1 N GLN I 5 O HIS I 37
SHEET 4 AG 4 GLU I 363 ILE I 367 -1 O ILE I 367 N VAL I 6
SHEET 1 AH 3 ILE I 130 GLN I 131 0
SHEET 2 AH 3 ILE I 341 GLU I 343 -1 O ILE I 342 N ILE I 130
SHEET 3 AH 3 VAL I 335 TYR I 336 -1 N VAL I 335 O GLU I 343
SHEET 1 AI 8 TYR I 134 VAL I 136 0
SHEET 2 AI 8 ILE I 158 LYS I 162 1 O LYS I 160 N TYR I 134
SHEET 3 AI 8 THR I 186 ASP I 190 1 O ARG I 188 N VAL I 161
SHEET 4 AI 8 CYS I 215 GLU I 216 1 O GLU I 216 N ILE I 189
SHEET 5 AI 8 ILE I 238 ALA I 240 1 O MET I 239 N CYS I 215
SHEET 6 AI 8 SER I 261 LEU I 264 1 O ASN I 263 N ALA I 240
SHEET 7 AI 8 VAL I 289 VAL I 291 1 O GLN I 290 N PHE I 262
SHEET 8 AI 8 ILE I 314 TYR I 317 1 O CYS I 315 N VAL I 289
SHEET 1 AJ 2 VAL I 330 GLY I 332 0
SHEET 2 AJ 2 ALA I 352 TYR I 354 -1 O GLY I 353 N ARG I 331
LINK C DAL A2470 N VAL A2471 1555 1555 1.34
LINK C DAL B2472 N VAL B2473 1555 1555 1.33
LINK C DAL C2474 N VAL C2475 1555 1555 1.34
LINK C DAL D2476 N VAL D2477 1555 1555 1.33
LINK C DAL E2478 N VAL E2479 1555 1555 1.34
LINK C DAL F2480 N VAL F2481 1555 1555 1.32
LINK C DAL G2482 N VAL G2483 1555 1555 1.33
LINK C DAL H2484 N VAL H2485 1555 1555 1.34
LINK C DAL I2486 N VAL I2487 1555 1555 1.34
LINK OD2 ASP A 190 MG MG A1601 1555 1555 2.61
LINK OE1 GLU A 216 MG MG A1601 1555 1555 2.56
LINK OD2 ASP A 241 MG MG A1601 1555 1555 2.17
LINK MG MG A1601 OXT VAL A2471 1555 1555 2.75
LINK OD2 ASP B 190 MG MG B1602 1555 1555 2.38
LINK OE1 GLU B 216 MG MG B1602 1555 1555 2.31
LINK OD2 ASP B 241 MG MG B1602 1555 1555 2.26
LINK MG MG B1602 O VAL B2473 1555 1555 2.74
LINK MG MG B1602 OXT VAL B2473 1555 1555 2.80
LINK OD2 ASP C 190 MG MG C1603 1555 1555 2.76
LINK OE1 GLU C 216 MG MG C1603 1555 1555 2.78
LINK OD2 ASP C 241 MG MG C1603 1555 1555 2.37
LINK MG MG C1603 O VAL C2475 1555 1555 2.85
LINK MG MG C1603 OXT VAL C2475 1555 1555 2.89
LINK OD2 ASP D 190 MG MG D1604 1555 1555 2.74
LINK OE1 GLU D 216 MG MG D1604 1555 1555 2.68
LINK OD2 ASP D 241 MG MG D1604 1555 1555 2.01
LINK MG MG D1604 OXT VAL D2477 1555 1555 2.40
LINK OD2 ASP E 190 MG MG E1605 1555 1555 2.59
LINK OE1 GLU E 216 MG MG E1605 1555 1555 2.92
LINK OD2 ASP E 241 MG MG E1605 1555 1555 2.29
LINK MG MG E1605 OXT VAL E2479 1555 1555 2.41
LINK OD2 ASP F 190 MG MG F1606 1555 1555 2.42
LINK OE1 GLU F 216 MG MG F1606 1555 1555 2.18
LINK OD2 ASP F 241 MG MG F1606 1555 1555 2.30
LINK MG MG F1606 OXT VAL F2481 1555 1555 2.96
LINK OD2 ASP G 190 MG MG G1607 1555 1555 2.38
LINK OE1 GLU G 216 MG MG G1607 1555 1555 2.23
LINK OD2 ASP G 241 MG MG G1607 1555 1555 2.27
LINK O HOH G 379 MG MG G1607 1555 1555 2.72
LINK MG MG G1607 O VAL G2483 1555 1555 2.81
LINK OD2 ASP H 190 MG MG H1608 1555 1555 2.41
LINK OE1 GLU H 216 MG MG H1608 1555 1555 2.84
LINK OD2 ASP H 241 MG MG H1608 1555 1555 2.50
LINK MG MG H1608 O VAL H2485 1555 1555 2.63
LINK MG MG H1608 OXT VAL H2485 1555 1555 2.91
LINK OD2 ASP I 190 MG MG I1609 1555 1555 2.35
LINK OE1 GLU I 216 MG MG I1609 1555 1555 2.44
LINK OD2 ASP I 241 MG MG I1609 1555 1555 2.36
LINK MG MG I1609 OXT VAL I2487 1555 1555 2.73
LINK MG MG I1609 O VAL I2487 1555 1555 2.85
SITE 1 AC1 6 ASP A 190 ASN A 192 GLU A 216 ASP A 241
SITE 2 AC1 6 GLU A 242 VAL A2471
SITE 1 AC2 6 PHE A 19 THR A 135 LYS A 162 ASP A 318
SITE 2 AC2 6 ASP A 320 VAL A2471
SITE 1 AC3 13 PHE A 19 LYS A 160 LYS A 162 ASP A 190
SITE 2 AC3 13 ASN A 192 GLU A 216 ASP A 241 ASN A 263
SITE 3 AC3 13 LYS A 265 GLY A 293 HOH A 377 MG A1601
SITE 4 AC3 13 DAL A2470
SITE 1 AC4 4 ASP B 190 GLU B 216 ASP B 241 VAL B2473
SITE 1 AC5 7 PHE B 19 THR B 135 LYS B 162 GLY B 293
SITE 2 AC5 7 ASP B 318 ASP B 320 VAL B2473
SITE 1 AC6 12 PHE B 19 PHE B 51 ILE B 54 LYS B 160
SITE 2 AC6 12 LYS B 162 ASP B 190 ASN B 192 ASP B 241
SITE 3 AC6 12 LYS B 265 GLY B 293 MG B1602 DAL B2472
SITE 1 AC7 6 ASP C 190 ASN C 192 GLU C 216 ASP C 241
SITE 2 AC7 6 GLU C 242 VAL C2475
SITE 1 AC8 7 THR C 135 LYS C 160 LYS C 162 GLY C 293
SITE 2 AC8 7 ASP C 318 ASP C 320 VAL C2475
SITE 1 AC9 12 LYS C 160 LYS C 162 ASP C 190 ASN C 192
SITE 2 AC9 12 GLU C 216 ASP C 241 ASN C 263 LYS C 265
SITE 3 AC9 12 GLY C 293 ASP C 318 MG C1603 DAL C2474
SITE 1 BC1 6 ASP D 190 ASN D 192 GLU D 216 ASP D 241
SITE 2 BC1 6 GLU D 242 VAL D2477
SITE 1 BC2 7 PHE D 19 THR D 135 LYS D 162 GLY D 293
SITE 2 BC2 7 ASP D 318 ASP D 320 VAL D2477
SITE 1 BC3 9 PHE D 19 LYS D 160 LYS D 162 ASP D 190
SITE 2 BC3 9 ASP D 241 LYS D 265 GLY D 293 MG D1604
SITE 3 BC3 9 DAL D2476
SITE 1 BC4 6 ASP E 190 ASN E 192 GLU E 216 ASP E 241
SITE 2 BC4 6 GLU E 242 VAL E2479
SITE 1 BC5 7 THR E 135 LYS E 160 LYS E 162 GLY E 293
SITE 2 BC5 7 ASP E 318 ASP E 320 VAL E2479
SITE 1 BC6 12 PHE E 19 ILE E 54 LYS E 160 LYS E 162
SITE 2 BC6 12 ASP E 190 ASN E 192 GLU E 216 ASP E 241
SITE 3 BC6 12 LYS E 265 GLY E 293 MG E1605 DAL E2478
SITE 1 BC7 4 ASP F 190 GLU F 216 ASP F 241 VAL F2481
SITE 1 BC8 7 THR F 135 LYS F 160 LYS F 162 GLY F 293
SITE 2 BC8 7 ASP F 318 ASP F 320 VAL F2481
SITE 1 BC9 9 ILE F 54 LYS F 160 LYS F 162 ASP F 190
SITE 2 BC9 9 ASP F 241 LYS F 265 GLY F 293 MG F1606
SITE 3 BC9 9 DAL F2480
SITE 1 CC1 5 ASP G 190 GLU G 216 ASP G 241 HOH G 379
SITE 2 CC1 5 VAL G2483
SITE 1 CC2 7 PHE G 19 THR G 135 LYS G 162 GLY G 293
SITE 2 CC2 7 ASP G 318 ASP G 320 VAL G2483
SITE 1 CC3 13 PHE G 19 PHE G 51 ILE G 54 LYS G 160
SITE 2 CC3 13 LYS G 162 ASP G 190 ASN G 192 ASP G 241
SITE 3 CC3 13 LYS G 265 GLY G 293 PHE G 294 MG G1607
SITE 4 CC3 13 DAL G2482
SITE 1 CC4 6 ASP H 190 ASN H 192 GLU H 216 ASP H 241
SITE 2 CC4 6 GLU H 242 VAL H2485
SITE 1 CC5 8 PHE H 19 THR H 135 LYS H 160 LYS H 162
SITE 2 CC5 8 GLY H 293 ASP H 318 ASP H 320 VAL H2485
SITE 1 CC6 12 PHE H 19 LYS H 160 LYS H 162 ASP H 190
SITE 2 CC6 12 ASN H 192 GLU H 216 ASP H 241 LYS H 265
SITE 3 CC6 12 GLY H 293 LEU H 295 MG H1608 DAL H2484
SITE 1 CC7 5 ASP I 190 ASN I 192 GLU I 216 ASP I 241
SITE 2 CC7 5 VAL I2487
SITE 1 CC8 8 THR I 135 LYS I 160 LYS I 162 GLY I 293
SITE 2 CC8 8 PHE I 294 ASP I 318 ASP I 320 VAL I2487
SITE 1 CC9 13 PHE I 51 ILE I 54 LYS I 160 LYS I 162
SITE 2 CC9 13 ASP I 190 ASN I 192 GLU I 216 ASP I 241
SITE 3 CC9 13 LYS I 265 GLY I 293 PHE I 294 MG I1609
SITE 4 CC9 13 DAL I2486
CRYST1 94.000 158.200 182.740 90.00 100.28 90.00 P 1 21 1 18
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010638 0.000000 0.001929 0.00000
SCALE2 0.000000 0.006321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005561 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
