HEADER HYDROLASE 07-JUN-00 1F4H
TITLE E. COLI (LACZ) BETA-GALACTOSIDASE (ORTHORHOMBIC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.1.23
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 OTHER_DETAILS: THE ENDOGENOUS BETA-GALACTOSIDASE WAS PURIFIED FROM
SOURCE 5 E. COLI STRAIN BL21
KEYWDS ALPHA/BETA BARREL, JELLY ROLL BARREL, FIBRONECTIN, BETA
KEYWDS 2 SUPERSANDWICH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.JUERS,R.H.JACOBSON,D.WIGLEY,X.J.ZHANG,R.E.HUBER,D.E.TRONRUD,
AUTHOR 2 B.W.MATTHEWS
REVDAT 4 07-FEB-24 1F4H 1 REMARK LINK
REVDAT 3 29-NOV-17 1F4H 1 REMARK
REVDAT 2 24-FEB-09 1F4H 1 VERSN
REVDAT 1 21-FEB-01 1F4H 0
JRNL AUTH D.H.JUERS,R.H.JACOBSON,D.WIGLEY,X.J.ZHANG,R.E.HUBER,
JRNL AUTH 2 D.E.TRONRUD,B.W.MATTHEWS
JRNL TITL HIGH RESOLUTION REFINEMENT OF BETA-GALACTOSIDASE IN A NEW
JRNL TITL 2 CRYSTAL FORM REVEALS MULTIPLE METAL-BINDING SITES AND
JRNL TITL 3 PROVIDES A STRUCTURAL BASIS FOR ALPHA-COMPLEMENTATION.
JRNL REF PROTEIN SCI. V. 9 1685 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11045615
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.H.JUERS,R.E.HUBER,B.W.MATTHEWS
REMARK 1 TITL STRUCTURAL COMPARISONS OF TIM BARREL PROTEINS SUGGEST
REMARK 1 TITL 2 FUNCTIONAL AND EVOLUTIONARY RELATIONSHIPS BETWEEN
REMARK 1 TITL 3 BETA-GALACTOSIDASE AND OTHER GLYCOHYDROLASES
REMARK 1 REF PROTEIN SCI. V. 8 122 1999
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.H.JACOBSON,X.J.ZHANG,R.F.DUBOSE,B.W.MATTHEWS
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF BETA-GALACTOSIDASE FROM E.
REMARK 1 TITL 2 COLI
REMARK 1 REF NATURE V. 369 761 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/369761A0
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.H.JACOBSON,B.W.MATTHEWS
REMARK 1 TITL CRYSTALLIZATION OF BETA-GALACTOSIDASE FROM ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 233 1177 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5E
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 116158
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM, WITHOUT PRECAUTIONS
REMARK 3 FOR THE NCS.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1614
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 845
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.800 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BABINET'S PRINCIPLE
REMARK 3 KSOL : 0.77
REMARK 3 BSOL : 367.0
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116158
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.09600
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0
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: NULL
REMARK 200 SOFTWARE USED: AMORE, MRCHK
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 2KMME, 100 MM BIS-TRIS, 200
REMARK 280 MM MGCL(2), 1 MM DTT, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 76.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER, WHICH IS THE
REMARK 300 ASYMMETRIC UNIT.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 137040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 49 CG CD OE1 NE2
REMARK 480 GLU A 117 CD OE1 OE2
REMARK 480 GLU A 131 CB CG CD OE1 OE2
REMARK 480 ARG A 178 NE CZ NH1 NH2
REMARK 480 GLU A 277 CG CD OE1 OE2
REMARK 480 LYS A 299 CD CE NZ
REMARK 480 GLN A 370 CG CD OE1 NE2
REMARK 480 GLU A 580 CB CG CD OE1 OE2
REMARK 480 GLU A 684 CG CD OE1 OE2
REMARK 480 GLU A 689 CB CG CD OE1 OE2
REMARK 480 ARG A 699 NE CZ NH1 NH2
REMARK 480 HIS A 735 CB CG ND1 CD2 CE1 NE2
REMARK 480 GLN A 761 CG CD OE1 NE2
REMARK 480 ASP A 772 CB CG OD1 OD2
REMARK 480 ARG A 800 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 819 CG CD OE1 OE2
REMARK 480 GLU A 893 CG CD OE1 OE2
REMARK 480 GLU A 980 CG CD OE1 OE2
REMARK 480 ARG A 1013 CB CG CD NE CZ NH1 NH2
REMARK 480 GLN B 49 CG CD OE1 NE2
REMARK 480 GLU B 117 CD OE1 OE2
REMARK 480 GLU B 131 CB CG CD OE1 OE2
REMARK 480 ARG B 178 NE CZ NH1 NH2
REMARK 480 GLU B 277 CG CD OE1 OE2
REMARK 480 LYS B 299 CD CE NZ
REMARK 480 GLN B 370 CG CD OE1 NE2
REMARK 480 GLU B 580 CB CG CD OE1 OE2
REMARK 480 GLU B 684 CG CD OE1 OE2
REMARK 480 GLU B 689 CB CG CD OE1 OE2
REMARK 480 ARG B 699 NE CZ NH1 NH2
REMARK 480 HIS B 735 CB CG ND1 CD2 CE1 NE2
REMARK 480 GLN B 761 CG CD OE1 NE2
REMARK 480 ASP B 772 CB CG OD1 OD2
REMARK 480 ARG B 800 CG CD NE CZ NH1 NH2
REMARK 480 GLU B 819 CG CD OE1 OE2
REMARK 480 GLU B 893 CG CD OE1 OE2
REMARK 480 GLU B 980 CG CD OE1 OE2
REMARK 480 ARG B 1013 CB CG CD NE CZ NH1 NH2
REMARK 480 GLN C 49 CG CD OE1 NE2
REMARK 480 GLU C 117 CD OE1 OE2
REMARK 480 GLU C 131 CB CG CD OE1 OE2
REMARK 480 ARG C 178 NE CZ NH1 NH2
REMARK 480 GLU C 277 CG CD OE1 OE2
REMARK 480 LYS C 299 CD CE NZ
REMARK 480 GLN C 370 CG CD OE1 NE2
REMARK 480 GLU C 580 CB CG CD OE1 OE2
REMARK 480 GLU C 684 CG CD OE1 OE2
REMARK 480 GLU C 689 CB CG CD OE1 OE2
REMARK 480 ARG C 699 NE CZ NH1 NH2
REMARK 480 HIS C 735 CB CG ND1 CD2 CE1 NE2
REMARK 480 GLN C 761 CG CD OE1 NE2
REMARK 480 ASP C 772 CB CG OD1 OD2
REMARK 480 ARG C 800 CG CD NE CZ NH1 NH2
REMARK 480 GLU C 819 CG CD OE1 OE2
REMARK 480 GLU C 893 CG CD OE1 OE2
REMARK 480 GLU C 980 CG CD OE1 OE2
REMARK 480 ARG C 1013 CB CG CD NE CZ NH1 NH2
REMARK 480 GLN D 49 CG CD OE1 NE2
REMARK 480 GLU D 117 CD OE1 OE2
REMARK 480 GLU D 131 CB CG CD OE1 OE2
REMARK 480 ARG D 178 NE CZ NH1 NH2
REMARK 480 GLU D 277 CG CD OE1 OE2
REMARK 480 LYS D 299 CD CE NZ
REMARK 480 GLN D 370 CG CD OE1 NE2
REMARK 480 GLU D 580 CB CG CD OE1 OE2
REMARK 480 GLU D 684 CG CD OE1 OE2
REMARK 480 GLU D 689 CB CG CD OE1 OE2
REMARK 480 ARG D 699 NE CZ NH1 NH2
REMARK 480 HIS D 735 CB CG ND1 CD2 CE1 NE2
REMARK 480 GLN D 761 CG CD OE1 NE2
REMARK 480 ASP D 772 CB CG OD1 OD2
REMARK 480 ARG D 800 CG CD NE CZ NH1 NH2
REMARK 480 GLU D 819 CG CD OE1 OE2
REMARK 480 GLU D 893 CG CD OE1 OE2
REMARK 480 GLU D 980 CG CD OE1 OE2
REMARK 480 ARG D 1013 CB CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 57 CD GLU A 57 OE2 0.067
REMARK 500 GLU A 75 CD GLU A 75 OE2 0.074
REMARK 500 GLU A 80 CD GLU A 80 OE2 0.070
REMARK 500 GLU A 198 CD GLU A 198 OE2 0.086
REMARK 500 GLU A 241 CD GLU A 241 OE2 0.080
REMARK 500 GLU A 249 CD GLU A 249 OE2 0.068
REMARK 500 GLU A 264 CD GLU A 264 OE2 0.068
REMARK 500 GLU A 281 CD GLU A 281 OE2 0.079
REMARK 500 GLU A 358 CD GLU A 358 OE2 0.086
REMARK 500 GLU A 438 CD GLU A 438 OE2 0.068
REMARK 500 GLU A 487 CD GLU A 487 OE2 0.085
REMARK 500 GLU A 508 CD GLU A 508 OE2 0.069
REMARK 500 GLU A 529 CD GLU A 529 OE2 0.072
REMARK 500 GLU A 681 CD GLU A 681 OE2 0.074
REMARK 500 GLU A 724 CD GLU A 724 OE2 0.067
REMARK 500 GLU A 744 CD GLU A 744 OE2 0.067
REMARK 500 GLU A 750 CD GLU A 750 OE2 0.078
REMARK 500 GLU A 871 CD GLU A 871 OE2 0.071
REMARK 500 GLU A 943 CD GLU A 943 OE2 0.074
REMARK 500 GLU A 969 CD GLU A 969 OE2 0.069
REMARK 500 GLU A 979 CD GLU A 979 OE2 0.074
REMARK 500 GLU A1006 CD GLU A1006 OE2 0.072
REMARK 500 GLU B 40 CD GLU B 40 OE2 0.078
REMARK 500 GLU B 57 CD GLU B 57 OE2 0.073
REMARK 500 GLU B 67 CD GLU B 67 OE2 0.077
REMARK 500 GLU B 75 CD GLU B 75 OE2 0.084
REMARK 500 GLU B 80 CD GLU B 80 OE2 0.068
REMARK 500 GLU B 136 CD GLU B 136 OE2 0.076
REMARK 500 GLU B 181 CD GLU B 181 OE2 0.080
REMARK 500 GLU B 241 CD GLU B 241 OE2 0.089
REMARK 500 GLU B 264 CD GLU B 264 OE2 0.077
REMARK 500 GLU B 281 CD GLU B 281 OE2 0.083
REMARK 500 GLU B 369 CD GLU B 369 OE2 0.072
REMARK 500 GLU B 416 CD GLU B 416 OE2 0.076
REMARK 500 GLU B 508 CD GLU B 508 OE2 0.080
REMARK 500 GLU B 537 CD GLU B 537 OE2 0.071
REMARK 500 GLU B 619 CD GLU B 619 OE2 0.071
REMARK 500 GLU B 641 CD GLU B 641 OE2 0.070
REMARK 500 GLU B 650 CD GLU B 650 OE2 0.079
REMARK 500 GLU B 667 CD GLU B 667 OE2 0.071
REMARK 500 GLU B 681 CD GLU B 681 OE2 0.069
REMARK 500 GLU B 710 CD GLU B 710 OE2 0.067
REMARK 500 GLU B 744 CD GLU B 744 OE2 0.073
REMARK 500 GLU B 797 CD GLU B 797 OE2 0.076
REMARK 500 GLU B 871 CD GLU B 871 OE2 0.070
REMARK 500 GLU B 969 CD GLU B 969 OE2 0.067
REMARK 500 GLU B 979 CD GLU B 979 OE2 0.069
REMARK 500 GLU C 57 CD GLU C 57 OE2 0.067
REMARK 500 GLU C 71 CD GLU C 71 OE2 0.066
REMARK 500 GLU C 75 CD GLU C 75 OE2 0.081
REMARK 500
REMARK 500 THIS ENTRY HAS 95 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 5 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 15 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 PRO A 19 C - N - CD ANGL. DEV. = -17.8 DEGREES
REMARK 500 ASN A 38 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 THR A 44 CA - CB - CG2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 PRO A 64 C - N - CD ANGL. DEV. = -14.3 DEGREES
REMARK 500 ASP A 77 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PRO A 79 C - N - CD ANGL. DEV. = -16.3 DEGREES
REMARK 500 ASP A 82 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 82 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 130 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 164 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 166 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A 172 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ALA A 175 CB - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 MET A 187 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 193 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 193 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 199 CB - CG - OD2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 233 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 233 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP A 234 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 GLU A 249 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 GLU A 249 CG - CD - OE2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 ASP A 252 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 252 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 287 CB - CG - OD1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP A 287 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ASP A 319 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 319 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 356 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 356 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 PRO A 361 C - N - CD ANGL. DEV. = -24.8 DEGREES
REMARK 500 ASP A 368 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 375 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASN A 385 CB - CA - C ANGL. DEV. = -21.2 DEGREES
REMARK 500 ASN A 385 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 ALA A 386 CB - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ALA A 386 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 CYS A 389 CA - CB - SG ANGL. DEV. = -10.9 DEGREES
REMARK 500 ASP A 403 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 444 ANGLE DEVIATIONS.
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 VAL A 10 -75.37 -51.92
REMARK 500 LEU A 11 -11.59 -49.58
REMARK 500 ASN A 25 34.60 74.23
REMARK 500 HIS A 30 163.00 179.46
REMARK 500 ASN A 102 -84.68 -78.30
REMARK 500 ASN A 110 60.16 -159.00
REMARK 500 PRO A 119 83.55 -40.14
REMARK 500 ASP A 164 96.94 80.03
REMARK 500 SER A 174 -58.20 -24.17
REMARK 500 ASP A 199 45.20 -97.62
REMARK 500 ASP A 201 84.41 -66.74
REMARK 500 ASP A 211 159.74 -47.49
REMARK 500 ASP A 252 -0.78 -52.88
REMARK 500 GLU A 281 -14.19 -49.38
REMARK 500 ASP A 319 30.88 -91.28
REMARK 500 GLU A 461 77.53 15.18
REMARK 500 ALA A 491 -11.49 73.87
REMARK 500 THR A 493 168.97 -44.92
REMARK 500 ALA A 514 -34.71 70.97
REMARK 500 THR A 530 5.30 -150.07
REMARK 500 ALA A 539 82.93 51.60
REMARK 500 HIS A 540 95.34 -60.38
REMARK 500 ALA A 541 13.00 -63.55
REMARK 500 LEU A 546 22.17 81.95
REMARK 500 GLN A 573 39.91 -83.35
REMARK 500 GLU A 580 10.53 -63.68
REMARK 500 ASN A 581 24.61 -155.22
REMARK 500 TYR A 588 -168.46 -127.30
REMARK 500 ARG A 599 -135.51 35.34
REMARK 500 ALA A 609 0.60 -62.54
REMARK 500 SER A 647 55.97 -54.52
REMARK 500 ASN A 649 53.67 -158.59
REMARK 500 ALA A 664 144.51 -177.40
REMARK 500 GLN A 675 4.74 59.37
REMARK 500 GLU A 684 118.47 -38.29
REMARK 500 SER A 690 150.40 -46.61
REMARK 500 THR A 706 -166.10 -124.71
REMARK 500 LEU A 722 -80.14 -90.87
REMARK 500 ALA A 733 73.19 -56.82
REMARK 500 SER A 734 120.77 8.97
REMARK 500 LEU A 751 119.84 -160.34
REMARK 500 GLN A 757 124.38 -174.64
REMARK 500 GLN A 761 -73.94 -72.68
REMARK 500 ALA A 820 172.14 -54.81
REMARK 500 CYS A 825 106.58 -163.73
REMARK 500 CYS A 886 166.67 179.96
REMARK 500 GLN A 890 150.87 -38.05
REMARK 500 ARG A 894 -166.57 -102.82
REMARK 500 PRO A 928 46.81 -73.70
REMARK 500 ASP A 996 -31.43 -39.26
REMARK 500
REMARK 500 THIS ENTRY HAS 237 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG C 352 10.05
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 A3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 15 O
REMARK 620 2 ASN A 18 O 108.3
REMARK 620 3 VAL A 21 O 126.8 83.3
REMARK 620 4 GLN A 163 NE2 88.4 158.6 97.7
REMARK 620 5 ASP A 193 OD1 124.4 80.1 108.6 79.3
REMARK 620 6 ASP A 193 OD2 79.5 85.3 153.5 84.6 45.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 102 ND2
REMARK 620 2 GLU A 416 OE1 152.4
REMARK 620 3 HIS A 418 ND1 105.5 81.4
REMARK 620 4 GLU A 461 OE2 151.3 56.3 69.9
REMARK 620 5 HOH A4008 O 116.1 70.4 134.6 64.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 15 O
REMARK 620 2 ASN B 18 O 87.2
REMARK 620 3 VAL B 21 O 108.0 87.5
REMARK 620 4 GLN B 163 OE1 125.9 146.6 86.1
REMARK 620 5 GLN B 163 NE2 81.0 168.1 97.1 45.1
REMARK 620 6 ASP B 193 OD1 129.5 114.4 117.6 43.3 73.2
REMARK 620 7 ASP B 193 OD2 91.1 91.6 160.8 84.2 87.7 46.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 102 ND2
REMARK 620 2 GLU B 416 OE1 119.9
REMARK 620 3 HIS B 418 ND1 110.8 57.4
REMARK 620 4 GLU B 461 OE2 172.9 53.0 65.9
REMARK 620 5 HOH B4014 O 109.8 50.3 107.3 66.6
REMARK 620 6 HOH B4156 O 66.6 54.0 69.4 106.4 75.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 15 O
REMARK 620 2 ASN C 18 O 90.9
REMARK 620 3 VAL C 21 O 96.3 106.0
REMARK 620 4 GLN C 163 NE2 82.5 172.0 79.2
REMARK 620 5 GLN C 163 OE1 123.3 134.6 99.3 48.4
REMARK 620 6 ASP C 193 OD2 87.2 77.7 174.8 97.5 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 418 ND1
REMARK 620 2 GLU C 461 OE2 91.7
REMARK 620 3 HOH C4014 O 102.7 64.7
REMARK 620 4 HOH C4156 O 59.3 115.3 67.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 15 O
REMARK 620 2 ASN D 18 O 90.1
REMARK 620 3 VAL D 21 O 88.5 64.4
REMARK 620 4 GLN D 163 OE1 127.1 139.3 97.3
REMARK 620 5 GLN D 163 NE2 78.2 157.2 95.4 49.0
REMARK 620 6 ASP D 193 OD2 96.5 109.4 172.2 84.5 91.5
REMARK 620 7 ASP D 193 OD1 144.6 95.6 125.4 64.5 105.3 48.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 416 OE1
REMARK 620 2 HIS D 418 ND1 61.5
REMARK 620 3 GLU D 461 OE2 69.1 81.6
REMARK 620 4 HOH D4014 O 85.5 146.6 81.7
REMARK 620 5 HOH D4156 O 70.4 66.8 137.1 108.9
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 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BGL RELATED DB: PDB
REMARK 900 BETA-GALACTOSIDASE (MONOCLINIC UNCONSTRAINED)
REMARK 900 RELATED ID: 1F49 RELATED DB: PDB
REMARK 900 BETA-GALACTOSIDASE (MONOCLINIC CONSTRAINED), CHAINS A-H
REMARK 900 RELATED ID: 1F4A RELATED DB: PDB
REMARK 900 BETA-GALACTOSIDASE (ORTHORHOMBIC CONSTRAINED)
REMARK 900 RELATED ID: 1DP0 RELATED DB: PDB
REMARK 900 BETA-GALACTOSIDASE (HIGH RESOLUTION, ORTHORHOMBIC)
REMARK 900 RELATED ID: 1GHO RELATED DB: PDB
REMARK 900 MONOCLINIC BETA-GALACTOSIDASE (CONSTRAINED NCS), CHAINS I-P
REMARK 900 RELATED ID: 1HN1 RELATED DB: PDB
REMARK 900 E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC)
REMARK 900 RELATED ID: 1BGM RELATED DB: PDB
DBREF 1F4H A 3 1023 UNP P00722 BGAL_ECOLI 3 1023
DBREF 1F4H B 3 1023 UNP P00722 BGAL_ECOLI 3 1023
DBREF 1F4H C 3 1023 UNP P00722 BGAL_ECOLI 3 1023
DBREF 1F4H D 3 1023 UNP P00722 BGAL_ECOLI 3 1023
SEQRES 1 A 1021 ILE THR ASP SER LEU ALA VAL VAL LEU GLN ARG ARG ASP
SEQRES 2 A 1021 TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG LEU ALA
SEQRES 3 A 1021 ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER GLU GLU
SEQRES 4 A 1021 ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG SER LEU
SEQRES 5 A 1021 ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA PRO GLU
SEQRES 6 A 1021 ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU PRO GLU
SEQRES 7 A 1021 ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN MET HIS
SEQRES 8 A 1021 GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR TYR PRO
SEQRES 9 A 1021 ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU ASN PRO
SEQRES 10 A 1021 THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP GLU SER
SEQRES 11 A 1021 TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE ASP GLY
SEQRES 12 A 1021 VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY ARG TRP
SEQRES 13 A 1021 VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER GLU PHE
SEQRES 14 A 1021 ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN ARG LEU
SEQRES 15 A 1021 ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER TYR LEU
SEQRES 16 A 1021 GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE PHE ARG
SEQRES 17 A 1021 ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN ILE SER
SEQRES 18 A 1021 ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP PHE SER
SEQRES 19 A 1021 ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS GLY GLU
SEQRES 20 A 1021 LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU TRP GLN
SEQRES 21 A 1021 GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO PHE GLY
SEQRES 22 A 1021 GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA ASP ARG
SEQRES 23 A 1021 VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS LEU TRP
SEQRES 24 A 1021 SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL VAL GLU
SEQRES 25 A 1021 LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA GLU ALA
SEQRES 26 A 1021 CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU ASN GLY
SEQRES 27 A 1021 LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE ARG GLY
SEQRES 28 A 1021 VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY GLN VAL
SEQRES 29 A 1021 MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU LEU MET
SEQRES 30 A 1021 LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER HIS TYR
SEQRES 31 A 1021 PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP ARG TYR
SEQRES 32 A 1021 GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLU THR HIS
SEQRES 33 A 1021 GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP PRO ARG
SEQRES 34 A 1021 TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG MET VAL
SEQRES 35 A 1021 GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE TRP SER
SEQRES 36 A 1021 LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS ASP ALA
SEQRES 37 A 1021 LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER ARG PRO
SEQRES 38 A 1021 VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR ALA THR
SEQRES 39 A 1021 ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP GLU ASP
SEQRES 40 A 1021 GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE LYS LYS
SEQRES 41 A 1021 TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU ILE LEU
SEQRES 42 A 1021 CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU GLY GLY
SEQRES 43 A 1021 PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR PRO ARG
SEQRES 44 A 1021 LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP GLN SER
SEQRES 45 A 1021 LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP SER ALA
SEQRES 46 A 1021 TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP ARG GLN
SEQRES 47 A 1021 PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG THR PRO
SEQRES 48 A 1021 HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN GLN PHE
SEQRES 49 A 1021 PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU VAL THR
SEQRES 50 A 1021 SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU LEU LEU
SEQRES 51 A 1021 HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU ALA SER
SEQRES 52 A 1021 GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY LYS GLN
SEQRES 53 A 1021 LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU SER ALA
SEQRES 54 A 1021 GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN PRO ASN
SEQRES 55 A 1021 ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER ALA TRP
SEQRES 56 A 1021 GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL THR LEU
SEQRES 57 A 1021 PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR THR SER
SEQRES 58 A 1021 GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS ARG TRP
SEQRES 59 A 1021 GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN MET TRP
SEQRES 60 A 1021 ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU ARG ASP
SEQRES 61 A 1021 GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE GLY VAL
SEQRES 62 A 1021 SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP VAL GLU
SEQRES 63 A 1021 ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU ALA ALA
SEQRES 64 A 1021 LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP ALA VAL
SEQRES 65 A 1021 LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN GLY LYS
SEQRES 66 A 1021 THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE ASP GLY
SEQRES 67 A 1021 SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU VAL ALA
SEQRES 68 A 1021 SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU ASN CYS
SEQRES 69 A 1021 GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP LEU GLY
SEQRES 70 A 1021 LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU THR ALA
SEQRES 71 A 1021 ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER ASP MET
SEQRES 72 A 1021 TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY LEU ARG
SEQRES 73 A 1021 CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS GLN TRP
SEQRES 74 A 1021 ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR SER GLN
SEQRES 75 A 1021 GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU LEU HIS
SEQRES 76 A 1021 ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY PHE HIS
SEQRES 77 A 1021 MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO SER VAL
SEQRES 78 A 1021 SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR HIS TYR
SEQRES 79 A 1021 GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 B 1021 ILE THR ASP SER LEU ALA VAL VAL LEU GLN ARG ARG ASP
SEQRES 2 B 1021 TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG LEU ALA
SEQRES 3 B 1021 ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER GLU GLU
SEQRES 4 B 1021 ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG SER LEU
SEQRES 5 B 1021 ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA PRO GLU
SEQRES 6 B 1021 ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU PRO GLU
SEQRES 7 B 1021 ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN MET HIS
SEQRES 8 B 1021 GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR TYR PRO
SEQRES 9 B 1021 ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU ASN PRO
SEQRES 10 B 1021 THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP GLU SER
SEQRES 11 B 1021 TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE ASP GLY
SEQRES 12 B 1021 VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY ARG TRP
SEQRES 13 B 1021 VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER GLU PHE
SEQRES 14 B 1021 ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN ARG LEU
SEQRES 15 B 1021 ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER TYR LEU
SEQRES 16 B 1021 GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE PHE ARG
SEQRES 17 B 1021 ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN ILE SER
SEQRES 18 B 1021 ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP PHE SER
SEQRES 19 B 1021 ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS GLY GLU
SEQRES 20 B 1021 LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU TRP GLN
SEQRES 21 B 1021 GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO PHE GLY
SEQRES 22 B 1021 GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA ASP ARG
SEQRES 23 B 1021 VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS LEU TRP
SEQRES 24 B 1021 SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL VAL GLU
SEQRES 25 B 1021 LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA GLU ALA
SEQRES 26 B 1021 CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU ASN GLY
SEQRES 27 B 1021 LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE ARG GLY
SEQRES 28 B 1021 VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY GLN VAL
SEQRES 29 B 1021 MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU LEU MET
SEQRES 30 B 1021 LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER HIS TYR
SEQRES 31 B 1021 PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP ARG TYR
SEQRES 32 B 1021 GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLU THR HIS
SEQRES 33 B 1021 GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP PRO ARG
SEQRES 34 B 1021 TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG MET VAL
SEQRES 35 B 1021 GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE TRP SER
SEQRES 36 B 1021 LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS ASP ALA
SEQRES 37 B 1021 LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER ARG PRO
SEQRES 38 B 1021 VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR ALA THR
SEQRES 39 B 1021 ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP GLU ASP
SEQRES 40 B 1021 GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE LYS LYS
SEQRES 41 B 1021 TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU ILE LEU
SEQRES 42 B 1021 CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU GLY GLY
SEQRES 43 B 1021 PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR PRO ARG
SEQRES 44 B 1021 LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP GLN SER
SEQRES 45 B 1021 LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP SER ALA
SEQRES 46 B 1021 TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP ARG GLN
SEQRES 47 B 1021 PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG THR PRO
SEQRES 48 B 1021 HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN GLN PHE
SEQRES 49 B 1021 PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU VAL THR
SEQRES 50 B 1021 SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU LEU LEU
SEQRES 51 B 1021 HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU ALA SER
SEQRES 52 B 1021 GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY LYS GLN
SEQRES 53 B 1021 LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU SER ALA
SEQRES 54 B 1021 GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN PRO ASN
SEQRES 55 B 1021 ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER ALA TRP
SEQRES 56 B 1021 GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL THR LEU
SEQRES 57 B 1021 PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR THR SER
SEQRES 58 B 1021 GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS ARG TRP
SEQRES 59 B 1021 GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN MET TRP
SEQRES 60 B 1021 ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU ARG ASP
SEQRES 61 B 1021 GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE GLY VAL
SEQRES 62 B 1021 SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP VAL GLU
SEQRES 63 B 1021 ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU ALA ALA
SEQRES 64 B 1021 LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP ALA VAL
SEQRES 65 B 1021 LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN GLY LYS
SEQRES 66 B 1021 THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE ASP GLY
SEQRES 67 B 1021 SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU VAL ALA
SEQRES 68 B 1021 SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU ASN CYS
SEQRES 69 B 1021 GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP LEU GLY
SEQRES 70 B 1021 LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU THR ALA
SEQRES 71 B 1021 ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER ASP MET
SEQRES 72 B 1021 TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY LEU ARG
SEQRES 73 B 1021 CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS GLN TRP
SEQRES 74 B 1021 ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR SER GLN
SEQRES 75 B 1021 GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU LEU HIS
SEQRES 76 B 1021 ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY PHE HIS
SEQRES 77 B 1021 MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO SER VAL
SEQRES 78 B 1021 SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR HIS TYR
SEQRES 79 B 1021 GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 C 1021 ILE THR ASP SER LEU ALA VAL VAL LEU GLN ARG ARG ASP
SEQRES 2 C 1021 TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG LEU ALA
SEQRES 3 C 1021 ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER GLU GLU
SEQRES 4 C 1021 ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG SER LEU
SEQRES 5 C 1021 ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA PRO GLU
SEQRES 6 C 1021 ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU PRO GLU
SEQRES 7 C 1021 ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN MET HIS
SEQRES 8 C 1021 GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR TYR PRO
SEQRES 9 C 1021 ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU ASN PRO
SEQRES 10 C 1021 THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP GLU SER
SEQRES 11 C 1021 TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE ASP GLY
SEQRES 12 C 1021 VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY ARG TRP
SEQRES 13 C 1021 VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER GLU PHE
SEQRES 14 C 1021 ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN ARG LEU
SEQRES 15 C 1021 ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER TYR LEU
SEQRES 16 C 1021 GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE PHE ARG
SEQRES 17 C 1021 ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN ILE SER
SEQRES 18 C 1021 ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP PHE SER
SEQRES 19 C 1021 ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS GLY GLU
SEQRES 20 C 1021 LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU TRP GLN
SEQRES 21 C 1021 GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO PHE GLY
SEQRES 22 C 1021 GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA ASP ARG
SEQRES 23 C 1021 VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS LEU TRP
SEQRES 24 C 1021 SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL VAL GLU
SEQRES 25 C 1021 LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA GLU ALA
SEQRES 26 C 1021 CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU ASN GLY
SEQRES 27 C 1021 LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE ARG GLY
SEQRES 28 C 1021 VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY GLN VAL
SEQRES 29 C 1021 MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU LEU MET
SEQRES 30 C 1021 LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER HIS TYR
SEQRES 31 C 1021 PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP ARG TYR
SEQRES 32 C 1021 GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLU THR HIS
SEQRES 33 C 1021 GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP PRO ARG
SEQRES 34 C 1021 TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG MET VAL
SEQRES 35 C 1021 GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE TRP SER
SEQRES 36 C 1021 LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS ASP ALA
SEQRES 37 C 1021 LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER ARG PRO
SEQRES 38 C 1021 VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR ALA THR
SEQRES 39 C 1021 ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP GLU ASP
SEQRES 40 C 1021 GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE LYS LYS
SEQRES 41 C 1021 TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU ILE LEU
SEQRES 42 C 1021 CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU GLY GLY
SEQRES 43 C 1021 PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR PRO ARG
SEQRES 44 C 1021 LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP GLN SER
SEQRES 45 C 1021 LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP SER ALA
SEQRES 46 C 1021 TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP ARG GLN
SEQRES 47 C 1021 PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG THR PRO
SEQRES 48 C 1021 HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN GLN PHE
SEQRES 49 C 1021 PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU VAL THR
SEQRES 50 C 1021 SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU LEU LEU
SEQRES 51 C 1021 HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU ALA SER
SEQRES 52 C 1021 GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY LYS GLN
SEQRES 53 C 1021 LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU SER ALA
SEQRES 54 C 1021 GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN PRO ASN
SEQRES 55 C 1021 ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER ALA TRP
SEQRES 56 C 1021 GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL THR LEU
SEQRES 57 C 1021 PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR THR SER
SEQRES 58 C 1021 GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS ARG TRP
SEQRES 59 C 1021 GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN MET TRP
SEQRES 60 C 1021 ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU ARG ASP
SEQRES 61 C 1021 GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE GLY VAL
SEQRES 62 C 1021 SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP VAL GLU
SEQRES 63 C 1021 ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU ALA ALA
SEQRES 64 C 1021 LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP ALA VAL
SEQRES 65 C 1021 LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN GLY LYS
SEQRES 66 C 1021 THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE ASP GLY
SEQRES 67 C 1021 SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU VAL ALA
SEQRES 68 C 1021 SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU ASN CYS
SEQRES 69 C 1021 GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP LEU GLY
SEQRES 70 C 1021 LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU THR ALA
SEQRES 71 C 1021 ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER ASP MET
SEQRES 72 C 1021 TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY LEU ARG
SEQRES 73 C 1021 CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS GLN TRP
SEQRES 74 C 1021 ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR SER GLN
SEQRES 75 C 1021 GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU LEU HIS
SEQRES 76 C 1021 ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY PHE HIS
SEQRES 77 C 1021 MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO SER VAL
SEQRES 78 C 1021 SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR HIS TYR
SEQRES 79 C 1021 GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 D 1021 ILE THR ASP SER LEU ALA VAL VAL LEU GLN ARG ARG ASP
SEQRES 2 D 1021 TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG LEU ALA
SEQRES 3 D 1021 ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER GLU GLU
SEQRES 4 D 1021 ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG SER LEU
SEQRES 5 D 1021 ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA PRO GLU
SEQRES 6 D 1021 ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU PRO GLU
SEQRES 7 D 1021 ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN MET HIS
SEQRES 8 D 1021 GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR TYR PRO
SEQRES 9 D 1021 ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU ASN PRO
SEQRES 10 D 1021 THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP GLU SER
SEQRES 11 D 1021 TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE ASP GLY
SEQRES 12 D 1021 VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY ARG TRP
SEQRES 13 D 1021 VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER GLU PHE
SEQRES 14 D 1021 ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN ARG LEU
SEQRES 15 D 1021 ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER TYR LEU
SEQRES 16 D 1021 GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE PHE ARG
SEQRES 17 D 1021 ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN ILE SER
SEQRES 18 D 1021 ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP PHE SER
SEQRES 19 D 1021 ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS GLY GLU
SEQRES 20 D 1021 LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU TRP GLN
SEQRES 21 D 1021 GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO PHE GLY
SEQRES 22 D 1021 GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA ASP ARG
SEQRES 23 D 1021 VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS LEU TRP
SEQRES 24 D 1021 SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL VAL GLU
SEQRES 25 D 1021 LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA GLU ALA
SEQRES 26 D 1021 CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU ASN GLY
SEQRES 27 D 1021 LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE ARG GLY
SEQRES 28 D 1021 VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY GLN VAL
SEQRES 29 D 1021 MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU LEU MET
SEQRES 30 D 1021 LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER HIS TYR
SEQRES 31 D 1021 PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP ARG TYR
SEQRES 32 D 1021 GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLU THR HIS
SEQRES 33 D 1021 GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP PRO ARG
SEQRES 34 D 1021 TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG MET VAL
SEQRES 35 D 1021 GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE TRP SER
SEQRES 36 D 1021 LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS ASP ALA
SEQRES 37 D 1021 LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER ARG PRO
SEQRES 38 D 1021 VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR ALA THR
SEQRES 39 D 1021 ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP GLU ASP
SEQRES 40 D 1021 GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE LYS LYS
SEQRES 41 D 1021 TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU ILE LEU
SEQRES 42 D 1021 CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU GLY GLY
SEQRES 43 D 1021 PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR PRO ARG
SEQRES 44 D 1021 LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP GLN SER
SEQRES 45 D 1021 LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP SER ALA
SEQRES 46 D 1021 TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP ARG GLN
SEQRES 47 D 1021 PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG THR PRO
SEQRES 48 D 1021 HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN GLN PHE
SEQRES 49 D 1021 PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU VAL THR
SEQRES 50 D 1021 SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU LEU LEU
SEQRES 51 D 1021 HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU ALA SER
SEQRES 52 D 1021 GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY LYS GLN
SEQRES 53 D 1021 LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU SER ALA
SEQRES 54 D 1021 GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN PRO ASN
SEQRES 55 D 1021 ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER ALA TRP
SEQRES 56 D 1021 GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL THR LEU
SEQRES 57 D 1021 PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR THR SER
SEQRES 58 D 1021 GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS ARG TRP
SEQRES 59 D 1021 GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN MET TRP
SEQRES 60 D 1021 ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU ARG ASP
SEQRES 61 D 1021 GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE GLY VAL
SEQRES 62 D 1021 SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP VAL GLU
SEQRES 63 D 1021 ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU ALA ALA
SEQRES 64 D 1021 LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP ALA VAL
SEQRES 65 D 1021 LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN GLY LYS
SEQRES 66 D 1021 THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE ASP GLY
SEQRES 67 D 1021 SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU VAL ALA
SEQRES 68 D 1021 SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU ASN CYS
SEQRES 69 D 1021 GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP LEU GLY
SEQRES 70 D 1021 LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU THR ALA
SEQRES 71 D 1021 ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER ASP MET
SEQRES 72 D 1021 TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY LEU ARG
SEQRES 73 D 1021 CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS GLN TRP
SEQRES 74 D 1021 ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR SER GLN
SEQRES 75 D 1021 GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU LEU HIS
SEQRES 76 D 1021 ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY PHE HIS
SEQRES 77 D 1021 MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO SER VAL
SEQRES 78 D 1021 SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR HIS TYR
SEQRES 79 D 1021 GLN LEU VAL TRP CYS GLN LYS
HET MG A3001 1
HET MG A3002 1
HET MG B3001 1
HET MG B3002 1
HET MG C3001 1
HET MG C3002 1
HET MG D3001 1
HET MG D3002 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 8(MG 2+)
FORMUL 13 HOH *845(H2 O)
HELIX 1 1 SER A 6 LEU A 11 1 6
HELIX 2 2 ARG A 14 ASN A 18 5 5
HELIX 3 3 ASN A 38 THR A 44 1 7
HELIX 4 4 ALA A 65 VAL A 69 5 5
HELIX 5 5 PRO A 70 GLU A 75 5 6
HELIX 6 6 ASN A 89 GLY A 94 5 6
HELIX 7 7 GLU A 131 GLU A 136 1 6
HELIX 8 8 SER A 192 LEU A 197 5 6
HELIX 9 9 ASP A 368 ASN A 382 1 15
HELIX 10 10 PRO A 396 GLY A 406 1 11
HELIX 11 11 ASP A 429 ARG A 431 5 3
HELIX 12 12 TRP A 432 ARG A 448 1 17
HELIX 13 13 GLY A 465 ASP A 479 1 15
HELIX 14 14 SER A 519 LEU A 524 1 6
HELIX 15 15 GLY A 548 TYR A 559 1 12
HELIX 16 16 ASP A 598 MET A 603 5 6
HELIX 17 17 PRO A 615 GLN A 624 1 10
HELIX 18 18 LEU A 789 GLY A 794 1 6
HELIX 19 19 ALA A 805 GLY A 814 1 10
HELIX 20 20 HIS A 815 ALA A 818 5 4
HELIX 21 21 SER A 923 TYR A 926 5 4
HELIX 22 22 SER A 963 THR A 970 1 8
HELIX 23 23 HIS A 972 LEU A 976 5 5
HELIX 24 24 SER A 1004 GLN A 1008 5 5
HELIX 25 25 SER B 6 LEU B 11 1 6
HELIX 26 26 GLN B 12 ARG B 13 5 2
HELIX 27 27 ARG B 14 ASN B 18 5 5
HELIX 28 28 ASN B 38 ASP B 45 1 8
HELIX 29 29 ALA B 65 VAL B 69 5 5
HELIX 30 30 PRO B 70 GLU B 75 5 6
HELIX 31 31 GLN B 91 GLY B 94 5 4
HELIX 32 32 GLU B 131 GLU B 136 1 6
HELIX 33 33 ASP B 193 GLU B 198 1 6
HELIX 34 34 ASP B 368 ASN B 382 1 15
HELIX 35 35 PRO B 396 GLY B 406 1 11
HELIX 36 36 ASP B 429 ARG B 431 5 3
HELIX 37 37 TRP B 432 ARG B 448 1 17
HELIX 38 38 GLY B 465 ASP B 479 1 15
HELIX 39 39 SER B 519 LEU B 524 1 6
HELIX 40 40 GLY B 548 TYR B 559 1 12
HELIX 41 41 ASP B 598 MET B 603 5 6
HELIX 42 42 PRO B 615 GLN B 624 1 10
HELIX 43 43 LEU B 789 GLY B 794 1 6
HELIX 44 44 ALA B 805 ALA B 812 1 8
HELIX 45 45 SER B 923 TYR B 926 5 4
HELIX 46 46 SER B 963 THR B 970 1 8
HELIX 47 47 HIS B 972 LEU B 976 5 5
HELIX 48 48 SER B 1004 GLN B 1008 5 5
HELIX 49 49 SER C 6 ARG C 13 1 8
HELIX 50 50 ARG C 14 ASN C 18 5 5
HELIX 51 51 ASN C 38 THR C 44 1 7
HELIX 52 52 ALA C 65 VAL C 69 5 5
HELIX 53 53 PRO C 70 GLU C 75 5 6
HELIX 54 54 GLU C 131 GLU C 136 1 6
HELIX 55 55 SER C 192 TYR C 196 5 5
HELIX 56 56 ASP C 368 ASN C 382 1 15
HELIX 57 57 HIS C 395 GLY C 406 1 12
HELIX 58 58 PRO C 422 LEU C 426 5 5
HELIX 59 59 TRP C 432 ARG C 448 1 17
HELIX 60 60 GLY C 465 ASP C 479 1 15
HELIX 61 61 GLU C 487 ALA C 491 5 5
HELIX 62 62 SER C 519 SER C 525 1 7
HELIX 63 63 GLY C 548 TYR C 559 1 12
HELIX 64 64 ASP C 598 MET C 603 5 6
HELIX 65 65 PRO C 615 GLN C 624 1 10
HELIX 66 66 LEU C 789 GLY C 794 1 6
HELIX 67 67 ALA C 805 ALA C 812 1 8
HELIX 68 68 SER C 923 MET C 925 5 3
HELIX 69 69 SER C 963 THR C 970 1 8
HELIX 70 70 HIS C 972 LEU C 976 5 5
HELIX 71 71 SER C 1004 GLN C 1008 5 5
HELIX 72 72 SER D 6 ARG D 13 1 8
HELIX 73 73 ARG D 14 ASN D 18 5 5
HELIX 74 74 ASN D 38 THR D 44 1 7
HELIX 75 75 ALA D 65 VAL D 69 5 5
HELIX 76 76 PRO D 70 PRO D 70 5 1
HELIX 77 77 GLU D 71 CYS D 76 1 6
HELIX 78 78 GLN D 91 HIS D 93 5 3
HELIX 79 79 ASP D 130 GLU D 136 1 7
HELIX 80 80 SER D 192 LEU D 197 5 6
HELIX 81 81 ASP D 368 ASN D 382 1 15
HELIX 82 82 HIS D 395 GLY D 406 1 12
HELIX 83 83 PRO D 422 LEU D 426 5 5
HELIX 84 84 ASP D 429 ARG D 431 5 3
HELIX 85 85 TRP D 432 ARG D 448 1 17
HELIX 86 86 GLY D 465 ASP D 479 1 15
HELIX 87 87 GLU D 487 ALA D 491 5 5
HELIX 88 88 SER D 519 SER D 525 1 7
HELIX 89 89 GLY D 548 TYR D 559 1 12
HELIX 90 90 ASP D 598 MET D 603 5 6
HELIX 91 91 PRO D 615 GLN D 624 1 10
HELIX 92 92 LEU D 789 GLY D 794 1 6
HELIX 93 93 ALA D 805 GLY D 814 1 10
HELIX 94 94 HIS D 815 ALA D 818 5 4
HELIX 95 95 SER D 923 TYR D 926 5 4
HELIX 96 96 SER D 963 THR D 970 1 8
HELIX 97 97 HIS D 972 LEU D 976 5 5
HELIX 98 98 SER D 1004 GLN D 1008 5 5
SHEET 1 A 7 GLN A 23 LEU A 24 0
SHEET 2 A 7 ARG A 157 GLY A 162 -1 O TYR A 161 N LEU A 24
SHEET 3 A 7 ALA A 149 CYS A 154 -1 N PHE A 150 O GLY A 162
SHEET 4 A 7 GLY A 180 LEU A 189 -1 N ALA A 185 O TRP A 153
SHEET 5 A 7 THR A 120 VAL A 129 -1 N GLY A 121 O VAL A 188
SHEET 6 A 7 GLY A 56 PHE A 63 -1 N ARG A 59 O SER A 124
SHEET 7 A 7 ASP A 82 VAL A 86 -1 O ASP A 82 N PHE A 60
SHEET 1 B 4 LEU A 51 SER A 53 0
SHEET 2 B 4 VAL A 212 LYS A 217 -1 N LEU A 214 O ARG A 52
SHEET 3 B 4 GLN A 138 PHE A 143 -1 N GLN A 138 O LYS A 217
SHEET 4 B 4 SER A 169 ASP A 172 -1 O SER A 169 N PHE A 143
SHEET 1 C 2 ILE A 99 THR A 101 0
SHEET 2 C 2 MET A 202 ARG A 204 -1 N MET A 202 O THR A 101
SHEET 1 D 3 GLN A 221 PHE A 231 0
SHEET 2 D 3 ARG A 237 CYS A 247 -1 N VAL A 239 O ARG A 230
SHEET 3 D 3 ARG A 288 GLU A 296 -1 O VAL A 289 N VAL A 244
SHEET 1 E 4 THR A 265 ALA A 272 0
SHEET 2 E 4 LEU A 254 GLN A 262 -1 O VAL A 256 N ALA A 272
SHEET 3 E 4 LEU A 308 THR A 317 -1 O ARG A 310 N TRP A 261
SHEET 4 E 4 LEU A 322 GLY A 331 -1 N ILE A 323 O LEU A 315
SHEET 1 F 3 VAL A 335 GLU A 338 0
SHEET 2 F 3 LEU A 341 LEU A 344 -1 O LEU A 341 N GLU A 338
SHEET 3 F 3 LYS A 347 PRO A 348 -1 O LYS A 347 N LEU A 344
SHEET 1 G 7 VAL A 484 GLN A 485 0
SHEET 2 G 7 VAL A 453 SER A 457 1 O TRP A 456 N GLN A 485
SHEET 3 G 7 TYR A 408 GLU A 412 1 O VAL A 409 N ILE A 454
SHEET 4 G 7 ALA A 386 ARG A 388 1 N VAL A 387 O TYR A 408
SHEET 5 G 7 ILE A 351 ASN A 355 1 O ARG A 352 N ALA A 386
SHEET 6 G 7 LEU A 562 VAL A 567 1 O GLN A 563 N ILE A 351
SHEET 7 G 7 LEU A 533 TYR A 538 1 O LEU A 533 N GLN A 563
SHEET 1 H 2 LEU A 575 TYR A 578 0
SHEET 2 H 2 PRO A 584 ALA A 587 -1 O TRP A 585 N LYS A 577
SHEET 1 I 3 PHE A 627 SER A 632 0
SHEET 2 I 3 THR A 635 SER A 640 -1 O THR A 635 N SER A 632
SHEET 3 I 3 LYS A 677 GLU A 681 -1 O GLN A 678 N VAL A 638
SHEET 1 J 4 LYS A 661 PRO A 669 0
SHEET 2 J 4 LEU A 651 LEU A 658 -1 N LEU A 652 O VAL A 668
SHEET 3 J 4 LEU A 694 GLN A 702 -1 N TRP A 695 O ALA A 657
SHEET 4 J 4 HIS A 713 ARG A 721 -1 O HIS A 713 N GLN A 702
SHEET 1 K 5 HIS A 739 THR A 742 0
SHEET 2 K 5 ASP A 746 LEU A 751 -1 N CYS A 748 O THR A 741
SHEET 3 K 5 LYS A 754 ASN A 759 -1 O LYS A 754 N LEU A 751
SHEET 4 K 5 LEU A 765 ILE A 770 -1 N SER A 766 O GLN A 757
SHEET 5 K 5 LYS A 773 LYS A 774 -1 O LYS A 773 N ILE A 770
SHEET 1 L 6 GLN B 23 LEU B 24 0
SHEET 2 L 6 ARG B 157 GLN B 163 -1 O TYR B 161 N LEU B 24
SHEET 3 L 6 ALA B 149 CYS B 154 -1 O PHE B 150 N GLY B 162
SHEET 4 L 6 GLY B 180 LEU B 189 -1 O ALA B 185 N TRP B 153
SHEET 5 L 6 THR B 120 VAL B 129 -1 O GLY B 121 N VAL B 188
SHEET 6 L 6 TRP B 62 PHE B 63 -1 O PHE B 63 N THR B 120
SHEET 1 M 4 LEU B 51 SER B 53 0
SHEET 2 M 4 VAL B 212 LYS B 217 -1 O LEU B 214 N ARG B 52
SHEET 3 M 4 GLN B 138 PHE B 143 -1 O GLN B 138 N LYS B 217
SHEET 4 M 4 SER B 169 ASP B 172 -1 N SER B 169 O PHE B 143
SHEET 1 N 2 GLY B 56 PHE B 60 0
SHEET 2 N 2 ASP B 82 VAL B 86 -1 N ASP B 82 O PHE B 60
SHEET 1 O 2 SER B 88 ASN B 89 0
SHEET 2 O 2 GLY B 207 ILE B 208 -1 O ILE B 208 N SER B 88
SHEET 1 P 2 ILE B 99 THR B 101 0
SHEET 2 P 2 MET B 202 ARG B 204 -1 N MET B 202 O THR B 101
SHEET 1 Q 3 GLN B 221 PHE B 231 0
SHEET 2 Q 3 ARG B 237 CYS B 247 -1 N VAL B 239 O ARG B 230
SHEET 3 Q 3 ARG B 288 GLU B 296 -1 O VAL B 289 N VAL B 244
SHEET 1 R 4 THR B 265 PRO B 273 0
SHEET 2 R 4 LEU B 254 GLN B 262 -1 O VAL B 256 N ALA B 272
SHEET 3 R 4 LEU B 308 THR B 317 -1 N ARG B 310 O TRP B 261
SHEET 4 R 4 LEU B 322 GLY B 331 -1 N ILE B 323 O LEU B 315
SHEET 1 S 3 VAL B 335 GLU B 338 0
SHEET 2 S 3 LEU B 341 LEU B 344 -1 O LEU B 341 N GLU B 338
SHEET 3 S 3 LYS B 347 PRO B 348 -1 O LYS B 347 N LEU B 344
SHEET 1 T 7 VAL B 484 GLN B 485 0
SHEET 2 T 7 VAL B 453 SER B 457 1 O TRP B 456 N GLN B 485
SHEET 3 T 7 TYR B 408 GLU B 412 1 O VAL B 409 N ILE B 454
SHEET 4 T 7 ALA B 386 ARG B 388 1 N VAL B 387 O TYR B 408
SHEET 5 T 7 ILE B 351 ASN B 355 1 O ARG B 352 N ALA B 386
SHEET 6 T 7 LEU B 562 TRP B 568 1 O GLN B 563 N ILE B 351
SHEET 7 T 7 LEU B 533 HIS B 540 1 O LEU B 533 N GLN B 563
SHEET 1 U 2 LEU B 575 TYR B 578 0
SHEET 2 U 2 PRO B 584 ALA B 587 -1 O TRP B 585 N LYS B 577
SHEET 1 V 3 PHE B 627 SER B 632 0
SHEET 2 V 3 THR B 635 SER B 640 -1 O THR B 635 N SER B 632
SHEET 3 V 3 LYS B 677 GLU B 681 -1 O GLN B 678 N VAL B 638
SHEET 1 W 4 LYS B 661 PRO B 669 0
SHEET 2 W 4 LEU B 651 LEU B 658 -1 N LEU B 652 O VAL B 668
SHEET 3 W 4 GLY B 692 GLN B 702 -1 O TRP B 695 N ALA B 657
SHEET 4 W 4 HIS B 713 ASN B 725 -1 O HIS B 713 N GLN B 702
SHEET 1 X 5 HIS B 739 THR B 741 0
SHEET 2 X 5 ASP B 746 LEU B 751 -1 N CYS B 748 O THR B 741
SHEET 3 X 5 LYS B 754 ASN B 759 -1 O LYS B 754 N LEU B 751
SHEET 4 X 5 GLN B 767 ILE B 770 -1 O GLN B 767 N GLN B 757
SHEET 5 X 5 LYS B 773 LYS B 774 -1 O LYS B 773 N ILE B 770
SHEET 1 Y 9 LEU B 822 THR B 829 0
SHEET 2 Y 9 ALA B 833 GLN B 843 -1 N LEU B 835 O ASP B 828
SHEET 3 Y 9 THR B 848 ASP B 859 -1 N LEU B 849 O TRP B 842
SHEET 4 Y 9 GLN B 863 VAL B 872 -1 O GLN B 863 N ASP B 859
SHEET 5 Y 9 ARG B1013 CYS B1021 -1 N TYR B1014 O VAL B 870
SHEET 6 Y 9 HIS B 949 SER B 960 -1 O GLN B 950 N CYS B1021
SHEET 7 Y 9 ARG B 938 TYR B 946 -1 N ARG B 938 O PHE B 957
SHEET 8 Y 9 ARG B 894 GLY B 901 -1 O ASN B 896 N ASN B 945
SHEET 9 Y 9 CYS B 914 PRO B 921 -1 N CYS B 914 O GLY B 901
SHEET 1 Z 9 LEU B 822 THR B 829 0
SHEET 2 Z 9 ALA B 833 GLN B 843 -1 N LEU B 835 O ASP B 828
SHEET 3 Z 9 THR B 848 ASP B 859 -1 N LEU B 849 O TRP B 842
SHEET 4 Z 9 GLN B 863 VAL B 872 -1 O GLN B 863 N ASP B 859
SHEET 5 Z 9 ARG B1013 CYS B1021 -1 N TYR B1014 O VAL B 870
SHEET 6 Z 9 HIS B 949 SER B 960 -1 O GLN B 950 N CYS B1021
SHEET 7 Z 9 THR B 982 HIS B 990 -1 O TRP B 983 N SER B 960
SHEET 8 Z 9 ARG B 881 LEU B 888 -1 N ILE B 882 O PHE B 989
SHEET 9 Z 9 ARG B 781 GLN B 783 -1 N ARG B 781 O ASN B 885
SHEET 1 AA 7 GLN C 23 LEU C 24 0
SHEET 2 AA 7 ARG C 157 GLN C 163 -1 O TYR C 161 N LEU C 24
SHEET 3 AA 7 ALA C 149 CYS C 154 -1 O PHE C 150 N GLY C 162
SHEET 4 AA 7 GLY C 180 LEU C 189 -1 N ALA C 185 O TRP C 153
SHEET 5 AA 7 THR C 120 VAL C 129 -1 N GLY C 121 O VAL C 188
SHEET 6 AA 7 GLY C 56 PHE C 63 -1 N ARG C 59 O SER C 124
SHEET 7 AA 7 ASP C 82 VAL C 86 -1 O ASP C 82 N PHE C 60
SHEET 1 AB 4 LEU C 51 SER C 53 0
SHEET 2 AB 4 VAL C 212 LYS C 217 -1 N LEU C 214 O ARG C 52
SHEET 3 AB 4 GLN C 138 PHE C 143 -1 O GLN C 138 N LYS C 217
SHEET 4 AB 4 SER C 169 ASP C 172 -1 N SER C 169 O PHE C 143
SHEET 1 AC 2 ILE C 99 THR C 101 0
SHEET 2 AC 2 MET C 202 ARG C 204 -1 N MET C 202 O THR C 101
SHEET 1 AD 2 VAL C 146 ASN C 147 0
SHEET 2 AD 2 GLY C 207 ILE C 208 -1 N GLY C 207 O ASN C 147
SHEET 1 AE 3 ARG C 288 GLU C 296 0
SHEET 2 AE 3 ARG C 237 CYS C 247 -1 O ALA C 238 N VAL C 295
SHEET 3 AE 3 GLN C 221 HIS C 226 -1 N GLN C 221 O CYS C 247
SHEET 1 AF 3 ARG C 288 GLU C 296 0
SHEET 2 AF 3 ARG C 237 CYS C 247 -1 O ALA C 238 N VAL C 295
SHEET 3 AF 3 THR C 229 PHE C 231 -1 O ARG C 230 N VAL C 239
SHEET 1 AG 4 THR C 265 PRO C 273 0
SHEET 2 AG 4 LEU C 254 GLN C 262 -1 O VAL C 256 N ALA C 272
SHEET 3 AG 4 TYR C 309 THR C 317 -1 O ARG C 310 N TRP C 261
SHEET 4 AG 4 LEU C 322 VAL C 330 -1 N ILE C 323 O LEU C 315
SHEET 1 AH 3 VAL C 335 GLU C 338 0
SHEET 2 AH 3 LEU C 341 LEU C 344 -1 O LEU C 341 N GLU C 338
SHEET 3 AH 3 LYS C 347 PRO C 348 -1 O LYS C 347 N LEU C 344
SHEET 1 AI 7 VAL C 484 GLN C 485 0
SHEET 2 AI 7 VAL C 453 SER C 457 1 O TRP C 456 N GLN C 485
SHEET 3 AI 7 TYR C 408 GLU C 412 1 O VAL C 409 N ILE C 454
SHEET 4 AI 7 ALA C 386 ARG C 388 1 O VAL C 387 N VAL C 410
SHEET 5 AI 7 ILE C 351 ASN C 355 1 O ARG C 352 N ALA C 386
SHEET 6 AI 7 LEU C 562 VAL C 567 1 O GLN C 563 N ILE C 351
SHEET 7 AI 7 LEU C 533 TYR C 538 1 O LEU C 533 N GLN C 563
SHEET 1 AJ 2 LEU C 575 TYR C 578 0
SHEET 2 AJ 2 PRO C 584 ALA C 587 -1 O TRP C 585 N LYS C 577
SHEET 1 AK 3 PHE C 627 SER C 632 0
SHEET 2 AK 3 THR C 635 SER C 640 -1 O THR C 635 N SER C 632
SHEET 3 AK 3 LYS C 677 GLU C 681 -1 O GLN C 678 N VAL C 638
SHEET 1 AL 4 LYS C 661 PRO C 669 0
SHEET 2 AL 4 LEU C 651 LEU C 658 -1 O LEU C 652 N VAL C 668
SHEET 3 AL 4 GLY C 692 GLN C 702 -1 N TRP C 695 O ALA C 657
SHEET 4 AL 4 HIS C 713 ASN C 725 -1 O HIS C 713 N GLN C 702
SHEET 1 AM 5 HIS C 739 THR C 741 0
SHEET 2 AM 5 PHE C 747 LEU C 751 -1 O CYS C 748 N THR C 741
SHEET 3 AM 5 LYS C 754 PHE C 758 -1 O LYS C 754 N LEU C 751
SHEET 4 AM 5 LEU C 765 ILE C 770 -1 N SER C 766 O GLN C 757
SHEET 5 AM 5 LYS C 773 LYS C 774 -1 O LYS C 773 N ILE C 770
SHEET 1 AN 7 GLN D 23 LEU D 24 0
SHEET 2 AN 7 ARG D 157 GLY D 162 -1 O TYR D 161 N LEU D 24
SHEET 3 AN 7 ALA D 149 CYS D 154 -1 O PHE D 150 N GLY D 162
SHEET 4 AN 7 GLY D 180 LEU D 189 -1 N ALA D 185 O TRP D 153
SHEET 5 AN 7 THR D 120 VAL D 129 -1 N GLY D 121 O VAL D 188
SHEET 6 AN 7 GLY D 56 PHE D 63 -1 N ARG D 59 O SER D 124
SHEET 7 AN 7 ASP D 82 VAL D 86 -1 O ASP D 82 N PHE D 60
SHEET 1 AO 4 LEU D 51 SER D 53 0
SHEET 2 AO 4 VAL D 212 LYS D 217 -1 N LEU D 214 O ARG D 52
SHEET 3 AO 4 GLN D 138 PHE D 143 -1 N GLN D 138 O LYS D 217
SHEET 4 AO 4 SER D 169 ASP D 172 -1 O SER D 169 N PHE D 143
SHEET 1 AP 3 SER D 88 ASN D 89 0
SHEET 2 AP 3 GLY D 207 ILE D 208 -1 O ILE D 208 N SER D 88
SHEET 3 AP 3 VAL D 146 ASN D 147 -1 O ASN D 147 N GLY D 207
SHEET 1 AQ 2 ILE D 99 THR D 101 0
SHEET 2 AQ 2 MET D 202 ARG D 204 -1 N MET D 202 O THR D 101
SHEET 1 AR 3 GLN D 221 PHE D 231 0
SHEET 2 AR 3 ARG D 237 CYS D 247 -1 N VAL D 239 O ARG D 230
SHEET 3 AR 3 ARG D 288 GLU D 296 -1 O VAL D 289 N VAL D 244
SHEET 1 AS 4 THR D 265 PRO D 273 0
SHEET 2 AS 4 LEU D 254 GLN D 262 -1 N VAL D 256 O ALA D 272
SHEET 3 AS 4 TYR D 309 THR D 317 -1 O ARG D 310 N TRP D 261
SHEET 4 AS 4 LEU D 322 VAL D 330 -1 N ILE D 323 O LEU D 315
SHEET 1 AT 3 VAL D 335 GLU D 338 0
SHEET 2 AT 3 LEU D 341 LEU D 344 -1 O LEU D 341 N GLU D 338
SHEET 3 AT 3 LYS D 347 PRO D 348 -1 O LYS D 347 N LEU D 344
SHEET 1 AU 7 VAL D 484 GLN D 485 0
SHEET 2 AU 7 VAL D 453 SER D 457 1 O TRP D 456 N GLN D 485
SHEET 3 AU 7 TYR D 408 GLU D 412 1 O VAL D 409 N ILE D 454
SHEET 4 AU 7 ALA D 386 ARG D 388 1 N VAL D 387 O TYR D 408
SHEET 5 AU 7 ILE D 351 ASN D 355 1 O ARG D 352 N ALA D 386
SHEET 6 AU 7 LEU D 562 VAL D 567 1 O GLN D 563 N ILE D 351
SHEET 7 AU 7 LEU D 533 LEU D 535 1 O LEU D 533 N GLN D 563
SHEET 1 AV 2 LEU D 575 TYR D 578 0
SHEET 2 AV 2 PRO D 584 ALA D 587 -1 O TRP D 585 N LYS D 577
SHEET 1 AW 3 PHE D 627 SER D 632 0
SHEET 2 AW 3 THR D 635 SER D 640 -1 N THR D 635 O SER D 632
SHEET 3 AW 3 LYS D 677 GLU D 681 -1 O GLN D 678 N VAL D 638
SHEET 1 AX 4 HIS D 713 ASN D 725 0
SHEET 2 AX 4 GLY D 692 GLN D 702 -1 O GLY D 692 N ASN D 725
SHEET 3 AX 4 LEU D 651 LEU D 658 -1 O LEU D 651 N VAL D 701
SHEET 4 AX 4 LYS D 661 ALA D 664 -1 O LYS D 661 N LEU D 658
SHEET 1 AY 4 HIS D 713 ASN D 725 0
SHEET 2 AY 4 GLY D 692 GLN D 702 -1 O GLY D 692 N ASN D 725
SHEET 3 AY 4 LEU D 651 LEU D 658 -1 O LEU D 651 N VAL D 701
SHEET 4 AY 4 VAL D 668 PRO D 669 -1 O VAL D 668 N LEU D 652
SHEET 1 AZ 5 HIS D 739 THR D 741 0
SHEET 2 AZ 5 ASP D 746 LEU D 751 -1 O CYS D 748 N THR D 741
SHEET 3 AZ 5 LYS D 754 ASN D 759 -1 O LYS D 754 N LEU D 751
SHEET 4 AZ 5 LEU D 765 ILE D 770 -1 N SER D 766 O GLN D 757
SHEET 5 AZ 5 LYS D 773 LYS D 774 -1 O LYS D 773 N ILE D 770
SHEET 1 BA 9 GLU D 819 THR D 829 0
SHEET 2 BA 9 ALA D 833 HIS D 844 -1 N LEU D 835 O ASP D 828
SHEET 3 BA 9 LYS D 847 ASP D 859 -1 O LYS D 847 N HIS D 844
SHEET 4 BA 9 GLN D 863 VAL D 872 -1 O GLN D 863 N ASP D 859
SHEET 5 BA 9 ARG D1013 GLN D1022 -1 O TYR D1014 N VAL D 870
SHEET 6 BA 9 HIS D 949 SER D 960 -1 N GLN D 950 O CYS D1021
SHEET 7 BA 9 ARG D 938 TYR D 946 -1 N ARG D 938 O PHE D 957
SHEET 8 BA 9 ARG D 894 GLY D 901 -1 O ASN D 896 N ASN D 945
SHEET 9 BA 9 CYS D 914 PRO D 921 -1 N CYS D 914 O GLY D 901
SHEET 1 BB 9 GLU D 819 THR D 829 0
SHEET 2 BB 9 ALA D 833 HIS D 844 -1 N LEU D 835 O ASP D 828
SHEET 3 BB 9 LYS D 847 ASP D 859 -1 O LYS D 847 N HIS D 844
SHEET 4 BB 9 GLN D 863 VAL D 872 -1 O GLN D 863 N ASP D 859
SHEET 5 BB 9 ARG D1013 GLN D1022 -1 O TYR D1014 N VAL D 870
SHEET 6 BB 9 HIS D 949 SER D 960 -1 N GLN D 950 O CYS D1021
SHEET 7 BB 9 THR D 982 HIS D 990 -1 N TRP D 983 O SER D 960
SHEET 8 BB 9 ARG D 881 LEU D 888 -1 N ILE D 882 O PHE D 989
SHEET 9 BB 9 LEU D 776 GLN D 783 -1 N LEU D 777 O GLN D 887
LINK O ASP A 15 MG MG A3002 1555 1555 2.32
LINK O ASN A 18 MG MG A3002 1555 1555 2.28
LINK O VAL A 21 MG MG A3002 1555 1555 2.10
LINK ND2 ASN A 102 MG MG A3001 1555 1555 3.12
LINK NE2 GLN A 163 MG MG A3002 1555 1555 2.24
LINK OD1 ASP A 193 MG MG A3002 1555 1555 3.09
LINK OD2 ASP A 193 MG MG A3002 1555 1555 2.32
LINK OE1 GLU A 416 MG MG A3001 1555 1555 2.56
LINK ND1 HIS A 418 MG MG A3001 1555 1555 2.48
LINK OE2 GLU A 461 MG MG A3001 1555 1555 2.27
LINK MG MG A3001 O HOH A4008 1555 1555 2.43
LINK O ASP B 15 MG MG B3002 1555 1555 2.44
LINK O ASN B 18 MG MG B3002 1555 1555 2.03
LINK O VAL B 21 MG MG B3002 1555 1555 2.11
LINK ND2 ASN B 102 MG MG B3001 1555 1555 2.80
LINK OE1 GLN B 163 MG MG B3002 1555 1555 3.11
LINK NE2 GLN B 163 MG MG B3002 1555 1555 2.58
LINK OD1 ASP B 193 MG MG B3002 1555 1555 3.12
LINK OD2 ASP B 193 MG MG B3002 1555 1555 2.20
LINK OE1 GLU B 416 MG MG B3001 1555 1555 2.98
LINK ND1 HIS B 418 MG MG B3001 1555 1555 2.30
LINK OE2 GLU B 461 MG MG B3001 1555 1555 2.49
LINK MG MG B3001 O HOH B4014 1555 1555 2.04
LINK MG MG B3001 O HOH B4156 1555 1555 2.23
LINK O ASP C 15 MG MG C3002 1555 1555 2.56
LINK O ASN C 18 MG MG C3002 1555 1555 2.16
LINK O VAL C 21 MG MG C3002 1555 1555 2.54
LINK NE2 GLN C 163 MG MG C3002 1555 1555 2.36
LINK OE1 GLN C 163 MG MG C3002 1555 1555 2.92
LINK OD2 ASP C 193 MG MG C3002 1555 1555 2.32
LINK ND1 HIS C 418 MG MG C3001 1555 1555 2.50
LINK OE2 GLU C 461 MG MG C3001 1555 1555 2.57
LINK MG MG C3001 O HOH C4014 1555 1555 2.50
LINK MG MG C3001 O HOH C4156 1555 1555 2.25
LINK O ASP D 15 MG MG D3002 1555 1555 2.63
LINK O ASN D 18 MG MG D3002 1555 1555 2.14
LINK O VAL D 21 MG MG D3002 1555 1555 2.45
LINK OE1 GLN D 163 MG MG D3002 1555 1555 2.99
LINK NE2 GLN D 163 MG MG D3002 1555 1555 2.23
LINK OD2 ASP D 193 MG MG D3002 1555 1555 1.97
LINK OD1 ASP D 193 MG MG D3002 1555 1555 2.91
LINK OE1 GLU D 416 MG MG D3001 1555 1555 2.76
LINK ND1 HIS D 418 MG MG D3001 1555 1555 2.76
LINK OE2 GLU D 461 MG MG D3001 1555 1555 1.60
LINK MG MG D3001 O HOH D4014 1555 1555 1.95
LINK MG MG D3001 O HOH D4156 1555 1555 1.96
CISPEP 1 VAL A 86 PRO A 87 0 5.07
CISPEP 2 PRO A 111 PRO A 112 0 5.71
CISPEP 3 ASN A 147 SER A 148 0 -0.13
CISPEP 4 SER A 390 HIS A 391 0 0.44
CISPEP 5 VAL A 421 PRO A 422 0 -4.04
CISPEP 6 TRP A 568 ASP A 569 0 1.69
CISPEP 7 THR A 595 PRO A 596 0 1.35
CISPEP 8 GLY A 901 PRO A 902 0 4.74
CISPEP 9 VAL B 86 PRO B 87 0 6.37
CISPEP 10 PRO B 111 PRO B 112 0 2.28
CISPEP 11 ASN B 147 SER B 148 0 2.01
CISPEP 12 SER B 390 HIS B 391 0 1.44
CISPEP 13 VAL B 421 PRO B 422 0 -3.06
CISPEP 14 TRP B 568 ASP B 569 0 -7.33
CISPEP 15 THR B 595 PRO B 596 0 -0.04
CISPEP 16 GLY B 901 PRO B 902 0 2.23
CISPEP 17 VAL C 86 PRO C 87 0 5.04
CISPEP 18 PRO C 111 PRO C 112 0 2.08
CISPEP 19 ASN C 147 SER C 148 0 0.34
CISPEP 20 SER C 390 HIS C 391 0 -4.61
CISPEP 21 VAL C 421 PRO C 422 0 0.34
CISPEP 22 TRP C 568 ASP C 569 0 -12.57
CISPEP 23 THR C 595 PRO C 596 0 -0.49
CISPEP 24 GLY C 901 PRO C 902 0 2.80
CISPEP 25 VAL D 86 PRO D 87 0 5.78
CISPEP 26 PRO D 111 PRO D 112 0 2.23
CISPEP 27 ASN D 147 SER D 148 0 2.95
CISPEP 28 SER D 390 HIS D 391 0 -7.30
CISPEP 29 VAL D 421 PRO D 422 0 -12.14
CISPEP 30 TRP D 568 ASP D 569 0 -8.58
CISPEP 31 THR D 595 PRO D 596 0 -1.39
CISPEP 32 GLY D 901 PRO D 902 0 4.46
SITE 1 AC1 5 ASN A 102 GLU A 416 HIS A 418 GLU A 461
SITE 2 AC1 5 HOH A4008
SITE 1 AC2 5 ASP A 15 ASN A 18 VAL A 21 GLN A 163
SITE 2 AC2 5 ASP A 193
SITE 1 AC3 6 ASN B 102 GLU B 416 HIS B 418 GLU B 461
SITE 2 AC3 6 HOH B4014 HOH B4156
SITE 1 AC4 6 ASP B 15 ASN B 18 PRO B 19 VAL B 21
SITE 2 AC4 6 GLN B 163 ASP B 193
SITE 1 AC5 6 ASN C 102 GLU C 416 HIS C 418 GLU C 461
SITE 2 AC5 6 HOH C4014 HOH C4156
SITE 1 AC6 5 ASP C 15 ASN C 18 VAL C 21 GLN C 163
SITE 2 AC6 5 ASP C 193
SITE 1 AC7 6 ASN D 102 GLU D 416 HIS D 418 GLU D 461
SITE 2 AC7 6 HOH D4014 HOH D4156
SITE 1 AC8 6 ASP D 15 ASN D 18 PRO D 19 VAL D 21
SITE 2 AC8 6 GLN D 163 ASP D 193
CRYST1 153.400 173.400 204.400 90.00 90.00 90.00 P 21 21 21 16
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 0.006519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005767 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004892 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
