HEADER ISOMERASE 18-SEP-09 3JW7
TITLE CRYSTAL STRUCTURE OF DIPEPTIDE EPIMERASE FROM ENTEROCOCCUS FAECALIS
TITLE 2 V583 COMPLEXED WITH MG AND DIPEPTIDE L-ILE-L-TYR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDE EPIMERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: MANDELATE RACEMASE/MUCONATE LACTONIZING ENZYME FAMILY
COMPND 5 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS V583;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS FAECALIS;
SOURCE 4 ORGANISM_TAXID: 226185;
SOURCE 5 GENE: EF_1511;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIPEPTIDE EPIMERASE, ENOLASE SUPERFAMILY, DIPEPTIDE L-ILE-L-TYR,
KEYWDS 2 ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,H.J.IMKER,A.SAKAI,J.A.GERLT,S.C.ALMO
REVDAT 4 06-SEP-23 3JW7 1 REMARK LINK
REVDAT 3 23-MAY-12 3JW7 1 JRNL
REVDAT 2 21-MAR-12 3JW7 1 JRNL VERSN
REVDAT 1 11-AUG-10 3JW7 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. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1603533.100
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 299981
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 SET) : 0.221
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 15157
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 26180
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1362
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 224
REMARK 3 SOLVENT ATOMS : 1625
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.10000
REMARK 3 B22 (A**2) : -3.07000
REMARK 3 B33 (A**2) : -3.03000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.130 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.570 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.940 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 40.48
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : GOL_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : GOL_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3JW7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 299981
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 3JVA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM CITRATE, 0.1M HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 97.45900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 93.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 97.45900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 93.72100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1358 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1321 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 354
REMARK 465 HIS B 354
REMARK 465 HIS C 354
REMARK 465 HIS D 354
REMARK 465 HIS E 354
REMARK 465 HIS F 354
REMARK 465 HIS G 354
REMARK 465 HIS H 354
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU C 337 OE1 GLU C 337 2455 2.18
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 PHE A 94 110.69 -165.26
REMARK 500 ALA A 95 61.40 -169.52
REMARK 500 GLN A 216 70.83 24.72
REMARK 500 ASP A 240 -84.26 -130.01
REMARK 500 THR A 297 -149.12 -132.36
REMARK 500 PHE B 94 112.43 -162.22
REMARK 500 ALA B 95 61.23 -171.79
REMARK 500 GLN B 216 71.66 22.86
REMARK 500 ASP B 240 -81.78 -129.79
REMARK 500 THR B 297 -155.34 -134.34
REMARK 500 PHE C 94 115.85 -161.43
REMARK 500 ALA C 95 63.47 -175.85
REMARK 500 ASP C 208 27.13 -79.25
REMARK 500 GLN C 210 70.20 49.16
REMARK 500 GLN C 216 73.75 27.93
REMARK 500 ASP C 240 -82.19 -130.30
REMARK 500 THR C 297 -139.83 -131.98
REMARK 500 PHE D 94 115.22 -163.59
REMARK 500 ALA D 95 63.43 -175.02
REMARK 500 GLN D 210 71.42 49.50
REMARK 500 GLN D 216 73.30 27.40
REMARK 500 ASP D 240 -85.00 -130.91
REMARK 500 THR D 297 -145.52 -126.80
REMARK 500 LEU D 319 79.36 -118.68
REMARK 500 PHE E 94 112.95 -166.30
REMARK 500 ALA E 95 63.99 -170.88
REMARK 500 GLN E 216 75.11 27.20
REMARK 500 ASP E 240 -82.91 -127.11
REMARK 500 THR E 297 -144.72 -126.49
REMARK 500 PHE F 94 109.19 -168.23
REMARK 500 ALA F 95 65.16 -167.51
REMARK 500 GLN F 216 69.11 30.36
REMARK 500 ASP F 240 -84.75 -128.43
REMARK 500 THR F 297 -149.05 -120.93
REMARK 500 LEU F 319 77.09 -119.10
REMARK 500 PHE G 94 111.68 -166.07
REMARK 500 ALA G 95 63.39 -170.20
REMARK 500 GLN G 216 68.22 28.81
REMARK 500 ASP G 240 -85.34 -128.61
REMARK 500 THR G 297 -154.92 -124.84
REMARK 500 LEU G 319 75.52 -117.48
REMARK 500 PHE H 94 113.43 -167.60
REMARK 500 ALA H 95 63.92 -171.52
REMARK 500 ASP H 138 -178.29 -172.20
REMARK 500 GLN H 216 73.45 24.87
REMARK 500 ASP H 240 -83.55 -127.16
REMARK 500 THR H 297 -150.27 -130.86
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 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 189 OD2
REMARK 620 2 GLU A 215 OE2 94.3
REMARK 620 3 ASP A 240 OD2 165.7 98.8
REMARK 620 4 TYR A 356 OXT 85.1 149.9 86.6
REMARK 620 5 TYR A 356 O 99.9 100.4 83.6 50.5
REMARK 620 6 HOH A 360 O 86.3 104.6 84.7 105.4 153.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 189 OD2
REMARK 620 2 GLU B 215 OE2 92.3
REMARK 620 3 ASP B 240 OD2 169.1 97.1
REMARK 620 4 TYR B 356 OXT 87.7 148.1 87.2
REMARK 620 5 TYR B 356 O 100.7 97.7 83.5 51.3
REMARK 620 6 HOH B 359 O 87.4 105.5 84.9 106.4 155.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 189 OD2
REMARK 620 2 GLU C 215 OE2 101.2
REMARK 620 3 ASP C 240 OD2 161.5 97.1
REMARK 620 4 TYR C 356 OXT 77.8 145.0 85.9
REMARK 620 5 TYR C 356 O 93.6 96.7 82.0 49.0
REMARK 620 6 HOH C 363 O 83.0 114.3 91.5 100.5 149.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 189 OD2
REMARK 620 2 GLU D 215 OE2 101.7
REMARK 620 3 ASP D 240 OD2 157.5 100.7
REMARK 620 4 TYR D 356 OXT 79.0 146.5 83.5
REMARK 620 5 TYR D 356 O 93.6 98.1 85.3 48.8
REMARK 620 6 HOH D 925 O 81.5 113.4 87.7 100.0 148.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 189 OD2
REMARK 620 2 GLU E 215 OE2 93.2
REMARK 620 3 ASP E 240 OD2 164.1 100.7
REMARK 620 4 TYR E 356 OXT 82.1 144.3 90.7
REMARK 620 5 TYR E 356 O 100.2 95.1 86.2 51.8
REMARK 620 6 HOH E 368 O 85.2 105.9 83.7 108.9 158.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 189 OD2
REMARK 620 2 GLU F 215 OE2 94.7
REMARK 620 3 ASP F 240 OD2 162.0 103.0
REMARK 620 4 TYR F 356 OXT 80.8 143.1 86.9
REMARK 620 5 TYR F 356 O 95.6 95.0 86.2 49.7
REMARK 620 6 HOH F 393 O 81.2 110.2 89.5 105.3 154.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 189 OD2
REMARK 620 2 GLU G 215 OE2 93.2
REMARK 620 3 ASP G 240 OD2 165.6 101.1
REMARK 620 4 TYR G 356 OXT 80.8 142.7 88.6
REMARK 620 5 TYR G 356 O 94.3 95.1 86.0 49.3
REMARK 620 6 HOH G 384 O 83.7 111.3 89.7 104.6 153.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 358 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 189 OD2
REMARK 620 2 GLU H 215 OE2 92.6
REMARK 620 3 ASP H 240 OD2 167.4 98.9
REMARK 620 4 TYR H 356 OXT 82.5 146.2 90.8
REMARK 620 5 TYR H 356 O 98.4 96.6 85.6 51.7
REMARK 620 6 HOH H 359 O 86.8 104.0 85.3 109.0 158.5
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 ILE A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR A 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE B 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR B 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE C 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR C 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE D 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR D 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE E 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR E 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE F 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR F 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE G 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR G 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ILE H 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYR H 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 358
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JVA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT BOUND DIPEPTIDE
DBREF 3JW7 A 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 B 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 C 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 D 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 E 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 F 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 G 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
DBREF 3JW7 H 1 354 UNP Q834W6 Q834W6_ENTFA 1 354
SEQRES 1 A 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 A 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 A 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 A 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 A 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 A 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 A 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 A 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 A 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 A 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 A 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 A 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 A 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 A 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 A 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 A 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 A 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 A 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 A 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 A 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 A 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 A 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 A 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 A 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 A 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 A 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 A 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 A 354 ILE SER HIS
SEQRES 1 B 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 B 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 B 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 B 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 B 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 B 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 B 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 B 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 B 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 B 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 B 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 B 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 B 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 B 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 B 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 B 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 B 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 B 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 B 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 B 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 B 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 B 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 B 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 B 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 B 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 B 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 B 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 B 354 ILE SER HIS
SEQRES 1 C 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 C 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 C 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 C 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 C 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 C 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 C 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 C 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 C 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 C 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 C 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 C 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 C 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 C 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 C 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 C 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 C 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 C 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 C 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 C 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 C 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 C 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 C 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 C 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 C 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 C 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 C 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 C 354 ILE SER HIS
SEQRES 1 D 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 D 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 D 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 D 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 D 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 D 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 D 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 D 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 D 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 D 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 D 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 D 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 D 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 D 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 D 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 D 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 D 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 D 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 D 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 D 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 D 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 D 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 D 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 D 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 D 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 D 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 D 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 D 354 ILE SER HIS
SEQRES 1 E 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 E 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 E 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 E 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 E 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 E 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 E 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 E 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 E 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 E 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 E 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 E 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 E 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 E 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 E 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 E 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 E 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 E 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 E 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 E 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 E 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 E 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 E 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 E 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 E 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 E 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 E 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 E 354 ILE SER HIS
SEQRES 1 F 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 F 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 F 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 F 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 F 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 F 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 F 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 F 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 F 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 F 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 F 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 F 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 F 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 F 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 F 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 F 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 F 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 F 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 F 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 F 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 F 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 F 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 F 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 F 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 F 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 F 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 F 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 F 354 ILE SER HIS
SEQRES 1 G 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 G 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 G 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 G 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 G 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 G 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 G 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 G 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 G 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 G 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 G 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 G 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 G 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 G 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 G 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 G 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 G 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 G 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 G 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 G 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 G 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 G 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 G 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 G 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 G 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 G 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 G 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 G 354 ILE SER HIS
SEQRES 1 H 354 MET LYS ILE LYS GLN VAL HIS VAL ARG ALA SER LYS ILE
SEQRES 2 H 354 LYS LEU LYS GLU THR PHE THR ILE ALA LEU GLY THR ILE
SEQRES 3 H 354 GLU SER ALA ASP SER ALA ILE VAL GLU ILE GLU THR GLU
SEQRES 4 H 354 GLU GLY LEU VAL GLY TYR GLY GLU GLY GLY PRO GLY ILE
SEQRES 5 H 354 PHE ILE THR GLY GLU THR LEU ALA GLY THR LEU GLU THR
SEQRES 6 H 354 ILE GLU LEU PHE GLY GLN ALA ILE ILE GLY LEU ASN PRO
SEQRES 7 H 354 PHE ASN ILE GLU LYS ILE HIS GLU VAL MET ASP LYS ILE
SEQRES 8 H 354 SER ALA PHE ALA PRO ALA ALA LYS ALA ALA ILE ASP ILE
SEQRES 9 H 354 ALA CYS TYR ASP LEU MET GLY GLN LYS ALA GLN LEU PRO
SEQRES 10 H 354 LEU TYR GLN LEU LEU GLY GLY TYR ASP ASN GLN VAL ILE
SEQRES 11 H 354 THR ASP ILE THR LEU GLY ILE ASP GLU PRO ASN VAL MET
SEQRES 12 H 354 ALA GLN LYS ALA VAL GLU LYS VAL LYS LEU GLY PHE ASP
SEQRES 13 H 354 THR LEU LYS ILE LYS VAL GLY THR GLY ILE GLU ALA ASP
SEQRES 14 H 354 ILE ALA ARG VAL LYS ALA ILE ARG GLU ALA VAL GLY PHE
SEQRES 15 H 354 ASP ILE LYS LEU ARG LEU ASP ALA ASN GLN ALA TRP THR
SEQRES 16 H 354 PRO LYS ASP ALA VAL LYS ALA ILE GLN ALA LEU ALA ASP
SEQRES 17 H 354 TYR GLN ILE GLU LEU VAL GLU GLN PRO VAL LYS ARG ARG
SEQRES 18 H 354 ASP LEU GLU GLY LEU LYS TYR VAL THR SER GLN VAL ASN
SEQRES 19 H 354 THR THR ILE MET ALA ASP GLU SER CYS PHE ASP ALA GLN
SEQRES 20 H 354 ASP ALA LEU GLU LEU VAL LYS LYS GLY THR VAL ASP VAL
SEQRES 21 H 354 ILE ASN ILE LYS LEU MET LYS CYS GLY GLY ILE HIS GLU
SEQRES 22 H 354 ALA LEU LYS ILE ASN GLN ILE CYS GLU THR ALA GLY ILE
SEQRES 23 H 354 GLU CYS MET ILE GLY CYS MET ALA GLU GLU THR THR ILE
SEQRES 24 H 354 GLY ILE THR ALA ALA ALA HIS LEU ALA ALA ALA GLN LYS
SEQRES 25 H 354 ASN ILE THR ARG ALA ASP LEU ASP ALA THR PHE GLY LEU
SEQRES 26 H 354 GLU THR ALA PRO VAL THR GLY GLY VAL SER LEU GLU ALA
SEQRES 27 H 354 LYS PRO LEU LEU GLU LEU GLY GLU ALA ALA GLY LEU GLY
SEQRES 28 H 354 ILE SER HIS
HET ILE A 355 8
HET TYR A 356 13
HET GOL A 357 6
HET MG A 358 1
HET ILE B 355 8
HET TYR B 356 13
HET GOL B 357 6
HET MG B 358 1
HET ILE C 355 8
HET TYR C 356 13
HET GOL C 357 6
HET MG C 358 1
HET ILE D 355 8
HET TYR D 356 13
HET GOL D 357 6
HET MG D 358 1
HET ILE E 355 8
HET TYR E 356 13
HET GOL E 357 6
HET MG E 358 1
HET ILE F 355 8
HET TYR F 356 13
HET GOL F 357 6
HET MG F 358 1
HET ILE G 355 8
HET TYR G 356 13
HET GOL G 357 6
HET MG G 358 1
HET ILE H 355 8
HET TYR H 356 13
HET GOL H 357 6
HET MG H 358 1
HETNAM ILE ISOLEUCINE
HETNAM TYR TYROSINE
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 ILE 8(C6 H13 N O2)
FORMUL 10 TYR 8(C9 H11 N O3)
FORMUL 11 GOL 8(C3 H8 O3)
FORMUL 12 MG 8(MG 2+)
FORMUL 41 HOH *1625(H2 O)
HELIX 1 1 THR A 58 ILE A 73 1 16
HELIX 2 2 ASN A 80 SER A 92 1 13
HELIX 3 3 ALA A 95 GLN A 115 1 21
HELIX 4 4 PRO A 117 LEU A 122 1 6
HELIX 5 5 GLU A 139 LEU A 153 1 15
HELIX 6 6 GLY A 165 GLY A 181 1 17
HELIX 7 7 THR A 195 LEU A 206 1 12
HELIX 8 8 ALA A 207 TYR A 209 5 3
HELIX 9 9 ASP A 222 VAL A 233 1 12
HELIX 10 10 ASP A 245 GLY A 256 1 12
HELIX 11 11 LYS A 264 GLY A 269 1 6
HELIX 12 12 GLY A 270 GLY A 285 1 16
HELIX 13 13 THR A 297 GLN A 311 1 15
HELIX 14 14 ASP A 320 LEU A 325 5 6
HELIX 15 15 GLY B 51 GLY B 56 1 6
HELIX 16 16 THR B 58 ILE B 74 1 17
HELIX 17 17 ASN B 80 SER B 92 1 13
HELIX 18 18 ALA B 95 GLN B 115 1 21
HELIX 19 19 PRO B 117 LEU B 122 1 6
HELIX 20 20 GLU B 139 LEU B 153 1 15
HELIX 21 21 GLY B 165 GLY B 181 1 17
HELIX 22 22 THR B 195 LEU B 206 1 12
HELIX 23 23 ALA B 207 TYR B 209 5 3
HELIX 24 24 ASP B 222 VAL B 233 1 12
HELIX 25 25 ASP B 245 GLY B 256 1 12
HELIX 26 26 LYS B 264 GLY B 269 1 6
HELIX 27 27 GLY B 270 GLY B 285 1 16
HELIX 28 28 THR B 297 GLN B 311 1 15
HELIX 29 29 ASP B 320 LEU B 325 5 6
HELIX 30 30 THR C 58 ILE C 74 1 17
HELIX 31 31 ASN C 80 SER C 92 1 13
HELIX 32 32 ALA C 95 GLN C 115 1 21
HELIX 33 33 PRO C 117 LEU C 121 5 5
HELIX 34 34 GLU C 139 LEU C 153 1 15
HELIX 35 35 GLY C 165 GLY C 181 1 17
HELIX 36 36 THR C 195 LEU C 206 1 12
HELIX 37 37 ALA C 207 TYR C 209 5 3
HELIX 38 38 ASP C 222 SER C 231 1 10
HELIX 39 39 ASP C 245 GLY C 256 1 12
HELIX 40 40 LYS C 264 GLY C 269 1 6
HELIX 41 41 GLY C 270 GLY C 285 1 16
HELIX 42 42 THR C 297 GLN C 311 1 15
HELIX 43 43 ASP C 320 LEU C 325 5 6
HELIX 44 44 THR D 58 ILE D 74 1 17
HELIX 45 45 ASN D 80 SER D 92 1 13
HELIX 46 46 ALA D 95 ALA D 114 1 20
HELIX 47 47 PRO D 117 LEU D 122 1 6
HELIX 48 48 GLU D 139 LYS D 152 1 14
HELIX 49 49 GLY D 165 GLY D 181 1 17
HELIX 50 50 THR D 195 LEU D 206 1 12
HELIX 51 51 ALA D 207 TYR D 209 5 3
HELIX 52 52 ASP D 222 SER D 231 1 10
HELIX 53 53 ASP D 245 GLY D 256 1 12
HELIX 54 54 LYS D 264 GLY D 269 1 6
HELIX 55 55 GLY D 270 GLY D 285 1 16
HELIX 56 56 THR D 297 GLN D 311 1 15
HELIX 57 57 ASP D 320 LEU D 325 5 6
HELIX 58 58 GLY E 51 GLY E 56 1 6
HELIX 59 59 THR E 58 ILE E 73 1 16
HELIX 60 60 ASN E 80 SER E 92 1 13
HELIX 61 61 ALA E 95 GLN E 115 1 21
HELIX 62 62 PRO E 117 LEU E 122 1 6
HELIX 63 63 GLU E 139 LYS E 152 1 14
HELIX 64 64 GLY E 165 GLY E 181 1 17
HELIX 65 65 THR E 195 LEU E 206 1 12
HELIX 66 66 ALA E 207 TYR E 209 5 3
HELIX 67 67 ASP E 222 VAL E 233 1 12
HELIX 68 68 ASP E 245 GLY E 256 1 12
HELIX 69 69 LYS E 264 GLY E 269 1 6
HELIX 70 70 GLY E 270 GLY E 285 1 16
HELIX 71 71 THR E 297 GLN E 311 1 15
HELIX 72 72 ASP E 320 LEU E 325 5 6
HELIX 73 73 THR F 58 ILE F 73 1 16
HELIX 74 74 ASN F 80 SER F 92 1 13
HELIX 75 75 ALA F 95 GLN F 115 1 21
HELIX 76 76 PRO F 117 LEU F 122 1 6
HELIX 77 77 GLU F 139 LEU F 153 1 15
HELIX 78 78 GLY F 165 GLY F 181 1 17
HELIX 79 79 THR F 195 LEU F 206 1 12
HELIX 80 80 ALA F 207 TYR F 209 5 3
HELIX 81 81 ASP F 222 VAL F 233 1 12
HELIX 82 82 ASP F 245 GLY F 256 1 12
HELIX 83 83 LYS F 264 GLY F 269 1 6
HELIX 84 84 GLY F 270 ALA F 284 1 15
HELIX 85 85 THR F 297 GLN F 311 1 15
HELIX 86 86 ASP F 320 LEU F 325 5 6
HELIX 87 87 GLY G 51 GLY G 56 1 6
HELIX 88 88 THR G 58 ILE G 73 1 16
HELIX 89 89 ASN G 80 SER G 92 1 13
HELIX 90 90 ALA G 95 GLN G 115 1 21
HELIX 91 91 PRO G 117 LEU G 122 1 6
HELIX 92 92 GLU G 139 LEU G 153 1 15
HELIX 93 93 GLY G 165 GLY G 181 1 17
HELIX 94 94 THR G 195 LEU G 206 1 12
HELIX 95 95 ALA G 207 TYR G 209 5 3
HELIX 96 96 ASP G 222 VAL G 233 1 12
HELIX 97 97 ASP G 245 GLY G 256 1 12
HELIX 98 98 LYS G 264 GLY G 269 1 6
HELIX 99 99 GLY G 270 GLY G 285 1 16
HELIX 100 100 THR G 297 GLN G 311 1 15
HELIX 101 101 ASP G 320 LEU G 325 5 6
HELIX 102 102 GLY H 51 GLY H 56 1 6
HELIX 103 103 THR H 58 ILE H 73 1 16
HELIX 104 104 ASN H 80 SER H 92 1 13
HELIX 105 105 ALA H 95 GLN H 115 1 21
HELIX 106 106 PRO H 117 LEU H 122 1 6
HELIX 107 107 GLU H 139 LYS H 152 1 14
HELIX 108 108 GLY H 165 GLY H 181 1 17
HELIX 109 109 THR H 195 LEU H 206 1 12
HELIX 110 110 ALA H 207 TYR H 209 5 3
HELIX 111 111 ASP H 222 VAL H 233 1 12
HELIX 112 112 ASP H 245 GLY H 256 1 12
HELIX 113 113 LYS H 264 GLY H 269 1 6
HELIX 114 114 GLY H 270 GLY H 285 1 16
HELIX 115 115 THR H 297 GLN H 311 1 15
HELIX 116 116 ASP H 320 LEU H 325 5 6
SHEET 1 A 3 ILE A 3 ILE A 21 0
SHEET 2 A 3 GLY A 24 THR A 38 -1 O ALA A 29 N ILE A 13
SHEET 3 A 3 VAL A 43 GLY A 48 -1 O GLY A 46 N VAL A 34
SHEET 1 B 2 GLN A 128 ILE A 130 0
SHEET 2 B 2 LEU A 341 GLU A 343 -1 O LEU A 342 N VAL A 129
SHEET 1 C 8 ILE A 133 LEU A 135 0
SHEET 2 C 8 THR A 157 LYS A 161 1 O LYS A 159 N ILE A 133
SHEET 3 C 8 LYS A 185 ASP A 189 1 O ARG A 187 N ILE A 160
SHEET 4 C 8 ILE A 211 GLU A 215 1 O GLU A 215 N LEU A 188
SHEET 5 C 8 THR A 236 ALA A 239 1 O MET A 238 N VAL A 214
SHEET 6 C 8 VAL A 260 ILE A 263 1 O ASN A 262 N ALA A 239
SHEET 7 C 8 GLU A 287 ILE A 290 1 O MET A 289 N ILE A 263
SHEET 8 C 8 ILE A 314 ALA A 317 1 O ARG A 316 N ILE A 290
SHEET 1 D 2 THR A 331 GLY A 332 0
SHEET 2 D 2 ILE A 352 SER A 353 -1 O SER A 353 N THR A 331
SHEET 1 E 3 ILE B 3 ILE B 21 0
SHEET 2 E 3 GLY B 24 THR B 38 -1 O ALA B 29 N ILE B 13
SHEET 3 E 3 VAL B 43 GLY B 48 -1 O GLY B 46 N VAL B 34
SHEET 1 F 2 GLN B 128 ILE B 130 0
SHEET 2 F 2 LEU B 341 GLU B 343 -1 O LEU B 342 N VAL B 129
SHEET 1 G 8 ILE B 133 LEU B 135 0
SHEET 2 G 8 THR B 157 LYS B 161 1 O LYS B 159 N ILE B 133
SHEET 3 G 8 LYS B 185 ASP B 189 1 O ARG B 187 N ILE B 160
SHEET 4 G 8 ILE B 211 GLU B 215 1 O GLU B 212 N LEU B 186
SHEET 5 G 8 THR B 236 ALA B 239 1 O MET B 238 N VAL B 214
SHEET 6 G 8 VAL B 260 ILE B 263 1 O ASN B 262 N ALA B 239
SHEET 7 G 8 GLU B 287 ILE B 290 1 O MET B 289 N ILE B 263
SHEET 8 G 8 ILE B 314 ALA B 317 1 O ARG B 316 N ILE B 290
SHEET 1 H 2 THR B 331 GLY B 332 0
SHEET 2 H 2 ILE B 352 SER B 353 -1 O SER B 353 N THR B 331
SHEET 1 I 3 ILE C 3 ILE C 21 0
SHEET 2 I 3 GLY C 24 THR C 38 -1 O ALA C 29 N ILE C 13
SHEET 3 I 3 VAL C 43 GLY C 48 -1 O GLY C 46 N VAL C 34
SHEET 1 J 2 GLN C 128 ILE C 130 0
SHEET 2 J 2 LEU C 341 GLU C 343 -1 O LEU C 342 N VAL C 129
SHEET 1 K 8 ILE C 133 LEU C 135 0
SHEET 2 K 8 THR C 157 LYS C 161 1 O LYS C 159 N ILE C 133
SHEET 3 K 8 LYS C 185 ASP C 189 1 O ARG C 187 N ILE C 160
SHEET 4 K 8 ILE C 211 GLU C 215 1 O LEU C 213 N LEU C 188
SHEET 5 K 8 THR C 236 ALA C 239 1 O MET C 238 N VAL C 214
SHEET 6 K 8 VAL C 260 ILE C 263 1 O ASN C 262 N ALA C 239
SHEET 7 K 8 GLU C 287 ILE C 290 1 O MET C 289 N ILE C 263
SHEET 8 K 8 ILE C 314 ALA C 317 1 O ARG C 316 N ILE C 290
SHEET 1 L 2 THR C 331 GLY C 332 0
SHEET 2 L 2 ILE C 352 SER C 353 -1 O SER C 353 N THR C 331
SHEET 1 M 3 ILE D 3 ILE D 21 0
SHEET 2 M 3 GLY D 24 THR D 38 -1 O ALA D 29 N ILE D 13
SHEET 3 M 3 VAL D 43 GLY D 48 -1 O GLY D 46 N VAL D 34
SHEET 1 N 2 GLN D 128 ILE D 130 0
SHEET 2 N 2 LEU D 341 GLU D 343 -1 O LEU D 342 N VAL D 129
SHEET 1 O 8 ILE D 133 LEU D 135 0
SHEET 2 O 8 THR D 157 LYS D 161 1 O LYS D 159 N LEU D 135
SHEET 3 O 8 LYS D 185 ASP D 189 1 O ARG D 187 N ILE D 160
SHEET 4 O 8 ILE D 211 GLU D 215 1 O GLU D 215 N LEU D 188
SHEET 5 O 8 THR D 236 ALA D 239 1 O MET D 238 N VAL D 214
SHEET 6 O 8 VAL D 260 ILE D 263 1 O ASN D 262 N ALA D 239
SHEET 7 O 8 GLU D 287 ILE D 290 1 O MET D 289 N ILE D 263
SHEET 8 O 8 ILE D 314 ALA D 317 1 O ARG D 316 N ILE D 290
SHEET 1 P 3 ILE E 3 ILE E 21 0
SHEET 2 P 3 GLY E 24 THR E 38 -1 O ALA E 29 N ILE E 13
SHEET 3 P 3 VAL E 43 GLY E 48 -1 O GLY E 44 N ILE E 36
SHEET 1 Q 2 GLN E 128 ILE E 130 0
SHEET 2 Q 2 LEU E 341 GLU E 343 -1 O LEU E 342 N VAL E 129
SHEET 1 R 8 ILE E 133 LEU E 135 0
SHEET 2 R 8 THR E 157 LYS E 161 1 O LYS E 159 N LEU E 135
SHEET 3 R 8 LYS E 185 ASP E 189 1 O ARG E 187 N ILE E 160
SHEET 4 R 8 ILE E 211 GLU E 215 1 O LEU E 213 N LEU E 188
SHEET 5 R 8 THR E 236 ALA E 239 1 O MET E 238 N VAL E 214
SHEET 6 R 8 VAL E 260 ILE E 263 1 O ASN E 262 N ALA E 239
SHEET 7 R 8 GLU E 287 ILE E 290 1 O MET E 289 N ILE E 263
SHEET 8 R 8 ILE E 314 ALA E 317 1 O ARG E 316 N ILE E 290
SHEET 1 S 2 THR E 331 GLY E 332 0
SHEET 2 S 2 ILE E 352 SER E 353 -1 O SER E 353 N THR E 331
SHEET 1 T 3 ILE F 3 ILE F 21 0
SHEET 2 T 3 GLY F 24 THR F 38 -1 O GLY F 24 N ILE F 21
SHEET 3 T 3 VAL F 43 GLY F 48 -1 O GLY F 46 N VAL F 34
SHEET 1 U 2 GLN F 128 ILE F 130 0
SHEET 2 U 2 LEU F 341 GLU F 343 -1 O LEU F 342 N VAL F 129
SHEET 1 V 8 ILE F 133 LEU F 135 0
SHEET 2 V 8 THR F 157 LYS F 161 1 O LYS F 159 N ILE F 133
SHEET 3 V 8 LYS F 185 ASP F 189 1 O LYS F 185 N LEU F 158
SHEET 4 V 8 ILE F 211 GLU F 215 1 O GLU F 215 N LEU F 188
SHEET 5 V 8 THR F 236 ALA F 239 1 O THR F 236 N VAL F 214
SHEET 6 V 8 VAL F 260 ILE F 263 1 O ASN F 262 N ALA F 239
SHEET 7 V 8 GLU F 287 ILE F 290 1 O MET F 289 N ILE F 263
SHEET 8 V 8 ILE F 314 ALA F 317 1 O ARG F 316 N ILE F 290
SHEET 1 W 2 THR F 331 GLY F 332 0
SHEET 2 W 2 ILE F 352 SER F 353 -1 O SER F 353 N THR F 331
SHEET 1 X 3 ILE G 3 ILE G 21 0
SHEET 2 X 3 GLY G 24 THR G 38 -1 O GLY G 24 N ILE G 21
SHEET 3 X 3 VAL G 43 GLY G 48 -1 O GLY G 46 N VAL G 34
SHEET 1 Y 2 GLN G 128 ILE G 130 0
SHEET 2 Y 2 LEU G 341 GLU G 343 -1 O LEU G 342 N VAL G 129
SHEET 1 Z 8 ILE G 133 LEU G 135 0
SHEET 2 Z 8 THR G 157 LYS G 161 1 O LYS G 159 N ILE G 133
SHEET 3 Z 8 LYS G 185 ASP G 189 1 O ARG G 187 N ILE G 160
SHEET 4 Z 8 ILE G 211 GLU G 215 1 O GLU G 215 N LEU G 188
SHEET 5 Z 8 THR G 236 ALA G 239 1 O MET G 238 N VAL G 214
SHEET 6 Z 8 VAL G 260 ILE G 263 1 O ASN G 262 N ALA G 239
SHEET 7 Z 8 GLU G 287 ILE G 290 1 O MET G 289 N ILE G 263
SHEET 8 Z 8 ILE G 314 ALA G 317 1 O ARG G 316 N ILE G 290
SHEET 1 AA 2 THR G 331 GLY G 332 0
SHEET 2 AA 2 ILE G 352 SER G 353 -1 O SER G 353 N THR G 331
SHEET 1 AB 3 ILE H 3 ILE H 21 0
SHEET 2 AB 3 GLY H 24 THR H 38 -1 O ALA H 29 N ILE H 13
SHEET 3 AB 3 VAL H 43 GLY H 48 -1 O GLY H 44 N ILE H 36
SHEET 1 AC 2 GLN H 128 ILE H 130 0
SHEET 2 AC 2 LEU H 341 GLU H 343 -1 O LEU H 342 N VAL H 129
SHEET 1 AD 8 ILE H 133 LEU H 135 0
SHEET 2 AD 8 THR H 157 LYS H 161 1 O LYS H 159 N LEU H 135
SHEET 3 AD 8 LYS H 185 ASP H 189 1 O ARG H 187 N ILE H 160
SHEET 4 AD 8 ILE H 211 GLU H 215 1 O LEU H 213 N LEU H 188
SHEET 5 AD 8 THR H 236 ALA H 239 1 O MET H 238 N VAL H 214
SHEET 6 AD 8 VAL H 260 ILE H 263 1 O ASN H 262 N ALA H 239
SHEET 7 AD 8 GLU H 287 ILE H 290 1 O MET H 289 N ILE H 263
SHEET 8 AD 8 ILE H 314 ALA H 317 1 O ARG H 316 N ILE H 290
SHEET 1 AE 2 THR H 331 GLY H 332 0
SHEET 2 AE 2 ILE H 352 SER H 353 -1 O SER H 353 N THR H 331
LINK C ILE A 355 N TYR A 356 1555 1555 1.33
LINK C ILE B 355 N TYR B 356 1555 1555 1.33
LINK C ILE C 355 N TYR C 356 1555 1555 1.33
LINK C ILE D 355 N TYR D 356 1555 1555 1.33
LINK C ILE E 355 N TYR E 356 1555 1555 1.33
LINK C ILE F 355 N TYR F 356 1555 1555 1.33
LINK C ILE G 355 N TYR G 356 1555 1555 1.33
LINK C ILE H 355 N TYR H 356 1555 1555 1.33
LINK OD2 ASP A 189 MG MG A 358 1555 1555 2.32
LINK OE2 GLU A 215 MG MG A 358 1555 1555 2.33
LINK OD2 ASP A 240 MG MG A 358 1555 1555 2.34
LINK OXT TYR A 356 MG MG A 358 1555 1555 2.34
LINK O TYR A 356 MG MG A 358 1555 1555 2.76
LINK MG MG A 358 O HOH A 360 1555 1555 2.43
LINK OD2 ASP B 189 MG MG B 358 1555 1555 2.30
LINK OE2 GLU B 215 MG MG B 358 1555 1555 2.28
LINK OD2 ASP B 240 MG MG B 358 1555 1555 2.32
LINK OXT TYR B 356 MG MG B 358 1555 1555 2.30
LINK O TYR B 356 MG MG B 358 1555 1555 2.72
LINK MG MG B 358 O HOH B 359 1555 1555 2.41
LINK OD2 ASP C 189 MG MG C 358 1555 1555 2.32
LINK OE2 GLU C 215 MG MG C 358 1555 1555 2.24
LINK OD2 ASP C 240 MG MG C 358 1555 1555 2.31
LINK OXT TYR C 356 MG MG C 358 1555 1555 2.51
LINK O TYR C 356 MG MG C 358 1555 1555 2.78
LINK MG MG C 358 O HOH C 363 1555 1555 2.40
LINK OD2 ASP D 189 MG MG D 358 1555 1555 2.36
LINK OE2 GLU D 215 MG MG D 358 1555 1555 2.09
LINK OD2 ASP D 240 MG MG D 358 1555 1555 2.32
LINK OXT TYR D 356 MG MG D 358 1555 1555 2.51
LINK O TYR D 356 MG MG D 358 1555 1555 2.79
LINK MG MG D 358 O HOH D 925 1555 1555 2.44
LINK OD2 ASP E 189 MG MG E 358 1555 1555 2.44
LINK OE2 GLU E 215 MG MG E 358 1555 1555 2.22
LINK OD2 ASP E 240 MG MG E 358 1555 1555 2.27
LINK OXT TYR E 356 MG MG E 358 1555 1555 2.30
LINK O TYR E 356 MG MG E 358 1555 1555 2.68
LINK MG MG E 358 O HOH E 368 1555 1555 2.30
LINK OD2 ASP F 189 MG MG F 358 1555 1555 2.40
LINK OE2 GLU F 215 MG MG F 358 1555 1555 2.22
LINK OD2 ASP F 240 MG MG F 358 1555 1555 2.21
LINK OXT TYR F 356 MG MG F 358 1555 1555 2.41
LINK O TYR F 356 MG MG F 358 1555 1555 2.77
LINK MG MG F 358 O HOH F 393 1555 1555 2.22
LINK OD2 ASP G 189 MG MG G 358 1555 1555 2.44
LINK OE2 GLU G 215 MG MG G 358 1555 1555 2.21
LINK OD2 ASP G 240 MG MG G 358 1555 1555 2.19
LINK OXT TYR G 356 MG MG G 358 1555 1555 2.40
LINK O TYR G 356 MG MG G 358 1555 1555 2.82
LINK MG MG G 358 O HOH G 384 1555 1555 2.28
LINK OD2 ASP H 189 MG MG H 358 1555 1555 2.40
LINK OE2 GLU H 215 MG MG H 358 1555 1555 2.24
LINK OD2 ASP H 240 MG MG H 358 1555 1555 2.26
LINK OXT TYR H 356 MG MG H 358 1555 1555 2.33
LINK O TYR H 356 MG MG H 358 1555 1555 2.67
LINK MG MG H 358 O HOH H 359 1555 1555 2.30
SITE 1 AC1 7 PHE A 19 THR A 134 LYS A 161 CYS A 292
SITE 2 AC1 7 ASP A 318 ASP A 320 TYR A 356
SITE 1 AC2 15 ILE A 21 ILE A 26 PHE A 53 LYS A 159
SITE 2 AC2 15 LYS A 161 ASP A 189 ASN A 191 ASP A 240
SITE 3 AC2 15 LYS A 264 CYS A 292 ALA A 294 GLU A 295
SITE 4 AC2 15 ILE A 355 MG A 358 HOH A 369
SITE 1 AC3 9 LEU A 15 PHE A 19 ASP A 320 ALA A 321
SITE 2 AC3 9 PHE A 323 GLY A 324 HOH A 449 HOH A1068
SITE 3 AC3 9 HOH A1258
SITE 1 AC4 6 LYS A 159 ASP A 189 GLU A 215 ASP A 240
SITE 2 AC4 6 TYR A 356 HOH A 360
SITE 1 AC5 8 PHE B 19 THR B 134 LYS B 159 LYS B 161
SITE 2 AC5 8 CYS B 292 ASP B 318 ASP B 320 TYR B 356
SITE 1 AC6 15 ILE B 21 ILE B 26 PHE B 53 LYS B 159
SITE 2 AC6 15 LYS B 161 ASP B 189 ASN B 191 ASP B 240
SITE 3 AC6 15 LYS B 264 CYS B 292 ALA B 294 GLU B 295
SITE 4 AC6 15 ILE B 355 MG B 358 HOH B 369
SITE 1 AC7 8 LEU B 15 PHE B 19 ASP B 320 ALA B 321
SITE 2 AC7 8 GLY B 324 HOH B 644 HOH B1030 HOH B1082
SITE 1 AC8 6 LYS B 159 ASP B 189 GLU B 215 ASP B 240
SITE 2 AC8 6 TYR B 356 HOH B 359
SITE 1 AC9 7 PHE C 19 THR C 134 LYS C 161 CYS C 292
SITE 2 AC9 7 ASP C 318 ASP C 320 TYR C 356
SITE 1 BC1 14 ILE C 21 PHE C 53 LYS C 159 LYS C 161
SITE 2 BC1 14 ASP C 189 ASN C 191 ASP C 240 LYS C 264
SITE 3 BC1 14 CYS C 292 ALA C 294 GLU C 295 ILE C 355
SITE 4 BC1 14 MG C 358 HOH C 364
SITE 1 BC2 7 LEU C 15 PHE C 19 ASP C 320 ALA C 321
SITE 2 BC2 7 PHE C 323 GLY C 324 HOH C 864
SITE 1 BC3 6 LYS C 159 ASP C 189 GLU C 215 ASP C 240
SITE 2 BC3 6 TYR C 356 HOH C 363
SITE 1 BC4 6 THR D 134 LYS D 161 CYS D 292 ASP D 318
SITE 2 BC4 6 ASP D 320 TYR D 356
SITE 1 BC5 15 ILE D 21 ILE D 26 PHE D 53 LYS D 159
SITE 2 BC5 15 LYS D 161 ASP D 189 ASN D 191 ASP D 240
SITE 3 BC5 15 LYS D 264 CYS D 292 ALA D 294 GLU D 295
SITE 4 BC5 15 ILE D 355 MG D 358 HOH D 397
SITE 1 BC6 7 LEU D 15 PHE D 19 THR D 134 ASP D 320
SITE 2 BC6 7 ALA D 321 GLY D 324 HOH D 519
SITE 1 BC7 6 LYS D 159 ASP D 189 GLU D 215 ASP D 240
SITE 2 BC7 6 TYR D 356 HOH D 925
SITE 1 BC8 7 THR E 134 LYS E 159 LYS E 161 CYS E 292
SITE 2 BC8 7 ASP E 318 ASP E 320 TYR E 356
SITE 1 BC9 15 ILE E 26 PHE E 53 LYS E 159 LYS E 161
SITE 2 BC9 15 ASP E 189 ASN E 191 GLU E 215 ASP E 240
SITE 3 BC9 15 LYS E 264 CYS E 292 ALA E 294 GLU E 295
SITE 4 BC9 15 ILE E 355 MG E 358 HOH E 387
SITE 1 CC1 7 LEU E 15 PHE E 19 ASP E 320 ALA E 321
SITE 2 CC1 7 GLY E 324 HOH E 414 HOH E 459
SITE 1 CC2 6 LYS E 159 ASP E 189 GLU E 215 ASP E 240
SITE 2 CC2 6 TYR E 356 HOH E 368
SITE 1 CC3 7 THR F 134 LYS F 159 LYS F 161 CYS F 292
SITE 2 CC3 7 ASP F 318 ASP F 320 TYR F 356
SITE 1 CC4 15 ILE F 21 PHE F 53 LYS F 159 LYS F 161
SITE 2 CC4 15 ASP F 189 ASN F 191 GLU F 215 ASP F 240
SITE 3 CC4 15 LYS F 264 CYS F 292 ALA F 294 GLU F 295
SITE 4 CC4 15 ILE F 355 MG F 358 HOH F 390
SITE 1 CC5 9 LEU F 15 PHE F 19 ASP F 320 ALA F 321
SITE 2 CC5 9 PHE F 323 GLY F 324 HOH F 808 HOH F1032
SITE 3 CC5 9 HOH F2157
SITE 1 CC6 5 ASP F 189 GLU F 215 ASP F 240 TYR F 356
SITE 2 CC6 5 HOH F 393
SITE 1 CC7 7 THR G 134 LYS G 159 LYS G 161 CYS G 292
SITE 2 CC7 7 ASP G 318 ASP G 320 TYR G 356
SITE 1 CC8 15 ILE G 21 ILE G 26 PHE G 53 LYS G 159
SITE 2 CC8 15 LYS G 161 ASP G 189 ASN G 191 ASP G 240
SITE 3 CC8 15 LYS G 264 CYS G 292 ALA G 294 GLU G 295
SITE 4 CC8 15 ILE G 355 MG G 358 HOH G 406
SITE 1 CC9 8 LEU G 15 PHE G 19 ASP G 320 ALA G 321
SITE 2 CC9 8 GLY G 324 HOH G 719 HOH G1047 HOH G2223
SITE 1 DC1 5 ASP G 189 GLU G 215 ASP G 240 TYR G 356
SITE 2 DC1 5 HOH G 384
SITE 1 DC2 7 THR H 134 LYS H 159 LYS H 161 CYS H 292
SITE 2 DC2 7 ASP H 318 ASP H 320 TYR H 356
SITE 1 DC3 15 ILE H 26 PHE H 53 LYS H 159 LYS H 161
SITE 2 DC3 15 ASP H 189 ASN H 191 GLU H 215 ASP H 240
SITE 3 DC3 15 LYS H 264 CYS H 292 ALA H 294 GLU H 295
SITE 4 DC3 15 ILE H 355 MG H 358 HOH H 417
SITE 1 DC4 9 LEU H 15 PHE H 19 ASP H 320 ALA H 321
SITE 2 DC4 9 PHE H 323 GLY H 324 HOH H 406 HOH H 788
SITE 3 DC4 9 HOH H 797
SITE 1 DC5 6 LYS H 159 ASP H 189 GLU H 215 ASP H 240
SITE 2 DC5 6 TYR H 356 HOH H 359
CRYST1 194.918 187.442 91.894 90.00 89.99 90.00 C 1 2 1 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 0.005130 0.000000 -0.000001 0.00000
SCALE2 0.000000 0.005335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010882 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
