HEADER RIBOFLAVIN SYNTHASE 25-OCT-95 1RVV
TITLE SYNTHASE/RIBOFLAVIN SYNTHASE COMPLEX OF BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOFLAVIN SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, W, X, Y, Z, 1, 2, 3, 4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423
KEYWDS RIBOFLAVIN SYNTHASE, TRANSFERASE, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.RITSERT,R.HUBER,D.TURK,R.LADENSTEIN,K.SCHMIDT-BAESE,A.BACHER
REVDAT 4 14-FEB-24 1RVV 1 REMARK
REVDAT 3 13-JUL-11 1RVV 1 VERSN
REVDAT 2 24-FEB-09 1RVV 1 VERSN
REVDAT 1 07-DEC-96 1RVV 0
JRNL AUTH K.RITSERT,R.HUBER,D.TURK,R.LADENSTEIN,K.SCHMIDT-BASE,
JRNL AUTH 2 A.BACHER
JRNL TITL STUDIES ON THE LUMAZINE SYNTHASE/RIBOFLAVIN SYNTHASE COMPLEX
JRNL TITL 2 OF BACILLUS SUBTILIS: CRYSTAL STRUCTURE ANALYSIS OF
JRNL TITL 3 RECONSTITUTED, ICOSAHEDRAL BETA-SUBUNIT CAPSIDS WITH BOUND
JRNL TITL 4 SUBSTRATE ANALOGUE INHIBITOR AT 2.4 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 253 151 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7473709
JRNL DOI 10.1006/JMBI.1995.0542
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 34320
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 780
REMARK 3 SOLVENT ATOMS : 1050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176252.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 117.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 96.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 117.95000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 96.30000
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
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: 30-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, 1, 2, 3,
REMARK 350 AND CHAINS: 4
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 60-MERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 265510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 243120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1569.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, 1, 2, 3,
REMARK 350 AND CHAINS: 4
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 LYS A 14 CE NZ
REMARK 480 LYS A 70 CE NZ
REMARK 480 ILE A 76 O
REMARK 480 LYS A 98 CD CE NZ
REMARK 480 ARG A 151 CD NE CZ NH1 NH2
REMARK 480 GLU A 154 CB CG CD OE1 OE2
REMARK 480 LYS B 14 CE NZ
REMARK 480 LYS B 70 CE NZ
REMARK 480 ILE B 76 O
REMARK 480 LYS B 98 CD CE NZ
REMARK 480 ARG B 151 CD NE CZ NH1 NH2
REMARK 480 GLU B 154 CB CG CD OE1 OE2
REMARK 480 LYS C 14 CE NZ
REMARK 480 LYS C 70 CE NZ
REMARK 480 ILE C 76 O
REMARK 480 LYS C 98 CD CE NZ
REMARK 480 ARG C 151 CD NE CZ NH1 NH2
REMARK 480 GLU C 154 CB CG CD OE1 OE2
REMARK 480 LYS D 14 CE NZ
REMARK 480 LYS D 70 CE NZ
REMARK 480 ILE D 76 O
REMARK 480 LYS D 98 CD CE NZ
REMARK 480 ARG D 151 CD NE CZ NH1 NH2
REMARK 480 GLU D 154 CB CG CD OE1 OE2
REMARK 480 LYS E 14 CE NZ
REMARK 480 LYS E 70 CE NZ
REMARK 480 ILE E 76 O
REMARK 480 LYS E 98 CD CE NZ
REMARK 480 ARG E 151 CD NE CZ NH1 NH2
REMARK 480 GLU E 154 CB CG CD OE1 OE2
REMARK 480 LYS F 14 CE NZ
REMARK 480 LYS F 70 CE NZ
REMARK 480 ILE F 76 O
REMARK 480 LYS F 98 CD CE NZ
REMARK 480 ARG F 151 CD NE CZ NH1 NH2
REMARK 480 GLU F 154 CB CG CD OE1 OE2
REMARK 480 LYS G 14 CE NZ
REMARK 480 LYS G 70 CE NZ
REMARK 480 ILE G 76 O
REMARK 480 LYS G 98 CD CE NZ
REMARK 480 ARG G 151 CD NE CZ NH1 NH2
REMARK 480 GLU G 154 CB CG CD OE1 OE2
REMARK 480 LYS H 14 CE NZ
REMARK 480 LYS H 70 CE NZ
REMARK 480 ILE H 76 O
REMARK 480 LYS H 98 CD CE NZ
REMARK 480 ARG H 151 CD NE CZ NH1 NH2
REMARK 480 GLU H 154 CB CG CD OE1 OE2
REMARK 480 LYS I 14 CE NZ
REMARK 480 LYS I 70 CE NZ
REMARK 480 ILE I 76 O
REMARK 480 LYS I 98 CD CE NZ
REMARK 480 ARG I 151 CD NE CZ NH1 NH2
REMARK 480 GLU I 154 CB CG CD OE1 OE2
REMARK 480 LYS J 14 CE NZ
REMARK 480 LYS J 70 CE NZ
REMARK 480 ILE J 76 O
REMARK 480 LYS J 98 CD CE NZ
REMARK 480 ARG J 151 CD NE CZ NH1 NH2
REMARK 480 GLU J 154 CB CG CD OE1 OE2
REMARK 480 LYS K 14 CE NZ
REMARK 480 LYS K 70 CE NZ
REMARK 480 ILE K 76 O
REMARK 480 LYS K 98 CD CE NZ
REMARK 480 ARG K 151 CD NE CZ NH1 NH2
REMARK 480 GLU K 154 CB CG CD OE1 OE2
REMARK 480 LYS L 14 CE NZ
REMARK 480 LYS L 70 CE NZ
REMARK 480 ILE L 76 O
REMARK 480 LYS L 98 CD CE NZ
REMARK 480 ARG L 151 CD NE CZ NH1 NH2
REMARK 480 GLU L 154 CB CG CD OE1 OE2
REMARK 480 LYS M 14 CE NZ
REMARK 480 LYS M 70 CE NZ
REMARK 480 ILE M 76 O
REMARK 480 LYS M 98 CD CE NZ
REMARK 480 ARG M 151 CD NE CZ NH1 NH2
REMARK 480 GLU M 154 CB CG CD OE1 OE2
REMARK 480 LYS N 14 CE NZ
REMARK 480 LYS N 70 CE NZ
REMARK 480 ILE N 76 O
REMARK 480 LYS N 98 CD CE NZ
REMARK 480 ARG N 151 CD NE CZ NH1 NH2
REMARK 480 GLU N 154 CB CG CD OE1 OE2
REMARK 480 LYS O 14 CE NZ
REMARK 480 LYS O 70 CE NZ
REMARK 480 ILE O 76 O
REMARK 480 LYS O 98 CD CE NZ
REMARK 480 ARG O 151 CD NE CZ NH1 NH2
REMARK 480 GLU O 154 CB CG CD OE1 OE2
REMARK 480 LYS P 14 CE NZ
REMARK 480 LYS P 70 CE NZ
REMARK 480 ILE P 76 O
REMARK 480 LYS P 98 CD CE NZ
REMARK 480 ARG P 151 CD NE CZ NH1 NH2
REMARK 480 GLU P 154 CB CG CD OE1 OE2
REMARK 480 LYS Q 14 CE NZ
REMARK 480 LYS Q 70 CE NZ
REMARK 480 ILE Q 76 O
REMARK 480 LYS Q 98 CD CE NZ
REMARK 480 ARG Q 151 CD NE CZ NH1 NH2
REMARK 480 GLU Q 154 CB CG CD OE1 OE2
REMARK 480 LYS R 14 CE NZ
REMARK 480 LYS R 70 CE NZ
REMARK 480 ILE R 76 O
REMARK 480 LYS R 98 CD CE NZ
REMARK 480 ARG R 151 CD NE CZ NH1 NH2
REMARK 480 GLU R 154 CB CG CD OE1 OE2
REMARK 480 LYS S 14 CE NZ
REMARK 480 LYS S 70 CE NZ
REMARK 480 ILE S 76 O
REMARK 480 LYS S 98 CD CE NZ
REMARK 480 ARG S 151 CD NE CZ NH1 NH2
REMARK 480 GLU S 154 CB CG CD OE1 OE2
REMARK 480 LYS T 14 CE NZ
REMARK 480 LYS T 70 CE NZ
REMARK 480 ILE T 76 O
REMARK 480 LYS T 98 CD CE NZ
REMARK 480 ARG T 151 CD NE CZ NH1 NH2
REMARK 480 GLU T 154 CB CG CD OE1 OE2
REMARK 480 LYS U 14 CE NZ
REMARK 480 LYS U 70 CE NZ
REMARK 480 ILE U 76 O
REMARK 480 LYS U 98 CD CE NZ
REMARK 480 ARG U 151 CD NE CZ NH1 NH2
REMARK 480 GLU U 154 CB CG CD OE1 OE2
REMARK 480 LYS V 14 CE NZ
REMARK 480 LYS V 70 CE NZ
REMARK 480 ILE V 76 O
REMARK 480 LYS V 98 CD CE NZ
REMARK 480 ARG V 151 CD NE CZ NH1 NH2
REMARK 480 GLU V 154 CB CG CD OE1 OE2
REMARK 480 LYS W 14 CE NZ
REMARK 480 LYS W 70 CE NZ
REMARK 480 ILE W 76 O
REMARK 480 LYS W 98 CD CE NZ
REMARK 480 ARG W 151 CD NE CZ NH1 NH2
REMARK 480 GLU W 154 CB CG CD OE1 OE2
REMARK 480 LYS X 14 CE NZ
REMARK 480 LYS X 70 CE NZ
REMARK 480 ILE X 76 O
REMARK 480 LYS X 98 CD CE NZ
REMARK 480 ARG X 151 CD NE CZ NH1 NH2
REMARK 480 GLU X 154 CB CG CD OE1 OE2
REMARK 480 LYS Y 14 CE NZ
REMARK 480 LYS Y 70 CE NZ
REMARK 480 ILE Y 76 O
REMARK 480 LYS Y 98 CD CE NZ
REMARK 480 ARG Y 151 CD NE CZ NH1 NH2
REMARK 480 GLU Y 154 CB CG CD OE1 OE2
REMARK 480 LYS Z 14 CE NZ
REMARK 480 LYS Z 70 CE NZ
REMARK 480 ILE Z 76 O
REMARK 480 LYS Z 98 CD CE NZ
REMARK 480 ARG Z 151 CD NE CZ NH1 NH2
REMARK 480 GLU Z 154 CB CG CD OE1 OE2
REMARK 480 LYS 1 14 CE NZ
REMARK 480 LYS 1 70 CE NZ
REMARK 480 ILE 1 76 O
REMARK 480 LYS 1 98 CD CE NZ
REMARK 480 ARG 1 151 CD NE CZ NH1 NH2
REMARK 480 GLU 1 154 CB CG CD OE1 OE2
REMARK 480 LYS 2 14 CE NZ
REMARK 480 LYS 2 70 CE NZ
REMARK 480 ILE 2 76 O
REMARK 480 LYS 2 98 CD CE NZ
REMARK 480 ARG 2 151 CD NE CZ NH1 NH2
REMARK 480 GLU 2 154 CB CG CD OE1 OE2
REMARK 480 LYS 3 14 CE NZ
REMARK 480 LYS 3 70 CE NZ
REMARK 480 ILE 3 76 O
REMARK 480 LYS 3 98 CD CE NZ
REMARK 480 ARG 3 151 CD NE CZ NH1 NH2
REMARK 480 GLU 3 154 CB CG CD OE1 OE2
REMARK 480 LYS 4 14 CE NZ
REMARK 480 LYS 4 70 CE NZ
REMARK 480 ILE 4 76 O
REMARK 480 LYS 4 98 CD CE NZ
REMARK 480 ARG 4 151 CD NE CZ NH1 NH2
REMARK 480 GLU 4 154 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CD1 ILE 4 3 O HOH 4 888 1.25
REMARK 500 CD1 ILE M 3 O HOH M 468 1.33
REMARK 500 CD1 ILE X 3 O HOH X 853 1.35
REMARK 500 CD1 ILE 2 3 O HOH 2 993 1.40
REMARK 500 CD1 ILE V 3 O HOH V 538 1.40
REMARK 500 CD1 ILE K 3 O HOH K 398 1.44
REMARK 500 CD1 ILE I 3 O HOH I 328 1.45
REMARK 500 CD1 ILE P 3 O HOH P 573 1.48
REMARK 500 CD1 ILE Z 3 O HOH Z 923 1.49
REMARK 500 CG ASP Z 49 O HOH Z 1049 1.51
REMARK 500 CD1 ILE B 3 O HOH B 526 1.51
REMARK 500 CD1 ILE O 3 O HOH O 511 1.52
REMARK 500 CD1 ILE H 3 O HOH H 293 1.52
REMARK 500 CG ASP 3 49 O HOH 3 979 1.53
REMARK 500 NE2 GLN R 5 NH2 ARG S 21 1.53
REMARK 500 CD1 ILE W 3 O HOH W 818 1.54
REMARK 500 CD1 ILE L 3 O HOH L 433 1.54
REMARK 500 CD1 ILE J 3 O HOH J 507 1.54
REMARK 500 CD1 ILE Y 3 O HOH Y 713 1.55
REMARK 500 CD1 ILE D 3 O HOH D 527 1.57
REMARK 500 CD1 ILE G 3 O HOH G 258 1.57
REMARK 500 CD1 ILE 1 3 O HOH 1 958 1.57
REMARK 500 CD1 ILE E 3 O HOH E 503 1.58
REMARK 500 CD1 ILE F 3 O HOH F 525 1.58
REMARK 500 CD1 ILE Q 3 O HOH Q 608 1.58
REMARK 500 CD1 ILE N 3 O HOH N 503 1.58
REMARK 500 CG ASP Y 49 O HOH Y 839 1.58
REMARK 500 CD1 ILE A 3 O HOH A 529 1.58
REMARK 500 CG ASP E 49 O HOH E 508 1.59
REMARK 500 CD1 ILE C 3 O HOH C 528 1.59
REMARK 500 CD1 ILE S 3 O HOH S 528 1.59
REMARK 500 CG ASP K 49 O HOH K 524 1.60
REMARK 500 CD1 ILE U 3 O HOH U 530 1.60
REMARK 500 CD1 ILE T 3 O HOH T 538 1.60
REMARK 500 CG ASP N 49 O HOH N 454 1.61
REMARK 500 CD1 ILE 3 3 O HOH 3 1028 1.61
REMARK 500 OD2 ASP Z 49 O HOH Z 1049 1.62
REMARK 500 NE2 GLN U 5 NH2 ARG V 21 1.64
REMARK 500 CG ASP F 49 O HOH F 530 1.64
REMARK 500 CG ASP W 49 O HOH W 769 1.64
REMARK 500 CG ASP V 49 O HOH V 508 1.65
REMARK 500 NE2 GLN 1 5 NH2 ARG 2 21 1.65
REMARK 500 CG ASP H 49 O HOH H 244 1.66
REMARK 500 CG1 ILE 4 3 O HOH 4 888 1.66
REMARK 500 CG ASP G 49 O HOH G 209 1.67
REMARK 500 NE2 GLN F 5 NH2 ARG G 21 1.67
REMARK 500 NH2 ARG K 21 NE2 GLN O 5 1.67
REMARK 500 NE2 GLN D 5 NH2 ARG E 21 1.67
REMARK 500 OD2 ASP Y 49 O HOH Y 839 1.67
REMARK 500 NE2 GLN S 5 NH2 ARG T 21 1.69
REMARK 500
REMARK 500 THIS ENTRY HAS 215 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
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 CA ASP O 44 O HOH 1 930 3555 1.02
REMARK 500 O HOH L 405 O HOH T 665 3454 1.30
REMARK 500 OE2 GLU A 154 O HOH 4 1035 4556 1.65
REMARK 500 N ASP O 44 O HOH 1 930 3555 1.70
REMARK 500 CG2 THR O 45 O HOH Z 928 3555 1.80
REMARK 500 O HOH G 230 O HOH O 517 4545 1.81
REMARK 500 CA ASP T 44 O HOH B 517 4546 1.85
REMARK 500 OE2 GLU Z 154 O HOH J 525 3445 2.17
REMARK 500 CB ASN G 46 OG SER N 152 4545 2.18
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 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU A 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR A 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU B 58 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR B 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG B 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU C 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR C 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG C 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU D 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR D 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG D 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG E 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU E 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR E 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG E 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG F 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU F 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR F 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG F 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG G 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU G 58 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR G 107 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG G 127 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG H 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU H 58 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR H 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG H 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG I 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU I 58 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR I 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG I 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG J 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU J 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR J 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG J 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG K 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU K 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR K 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG K 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG L 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU L 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 THR L 107 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG L 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG M 21 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU M 58 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 121 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 TYR A 89 -53.91 -25.14
REMARK 500 THR A 130 -144.84 -132.32
REMARK 500 LYS A 131 -54.59 -29.37
REMARK 500 TYR B 89 -53.90 -25.17
REMARK 500 THR B 130 -144.83 -132.36
REMARK 500 LYS B 131 -54.56 -29.38
REMARK 500 TYR C 89 -53.88 -25.16
REMARK 500 THR C 130 -144.84 -132.35
REMARK 500 LYS C 131 -54.60 -29.36
REMARK 500 TYR D 89 -53.94 -25.09
REMARK 500 THR D 130 -144.83 -132.31
REMARK 500 LYS D 131 -54.63 -29.33
REMARK 500 TYR E 89 -53.92 -25.19
REMARK 500 THR E 130 -144.81 -132.34
REMARK 500 LYS E 131 -54.58 -29.38
REMARK 500 TYR F 89 -53.94 -25.11
REMARK 500 THR F 130 -144.82 -132.30
REMARK 500 LYS F 131 -54.59 -29.38
REMARK 500 TYR G 89 -53.86 -25.20
REMARK 500 THR G 130 -144.84 -132.34
REMARK 500 LYS G 131 -54.54 -29.39
REMARK 500 TYR H 89 -53.89 -25.15
REMARK 500 THR H 130 -144.86 -132.30
REMARK 500 LYS H 131 -54.59 -29.36
REMARK 500 TYR I 89 -53.93 -25.13
REMARK 500 THR I 130 -144.85 -132.34
REMARK 500 LYS I 131 -54.68 -29.31
REMARK 500 TYR J 89 -53.93 -25.12
REMARK 500 THR J 130 -144.86 -132.32
REMARK 500 LYS J 131 -54.64 -29.31
REMARK 500 TYR K 89 -53.89 -25.10
REMARK 500 THR K 130 -144.82 -132.35
REMARK 500 LYS K 131 -54.56 -29.41
REMARK 500 TYR L 89 -53.88 -25.12
REMARK 500 THR L 130 -144.80 -132.30
REMARK 500 LYS L 131 -54.61 -29.33
REMARK 500 TYR M 89 -53.96 -25.09
REMARK 500 THR M 130 -144.82 -132.25
REMARK 500 LYS M 131 -54.67 -29.34
REMARK 500 TYR N 89 -53.90 -25.16
REMARK 500 THR N 130 -144.82 -132.35
REMARK 500 LYS N 131 -54.58 -29.37
REMARK 500 TYR O 89 -53.90 -25.14
REMARK 500 THR O 130 -144.84 -132.29
REMARK 500 LYS O 131 -54.65 -29.37
REMARK 500 TYR P 89 -53.89 -25.16
REMARK 500 THR P 130 -144.85 -132.31
REMARK 500 LYS P 131 -54.59 -29.33
REMARK 500 TYR Q 89 -53.89 -25.17
REMARK 500 THR Q 130 -144.83 -132.34
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 83 0.08 SIDE CHAIN
REMARK 500 TYR A 91 0.08 SIDE CHAIN
REMARK 500 ARG B 83 0.08 SIDE CHAIN
REMARK 500 TYR B 91 0.08 SIDE CHAIN
REMARK 500 ARG C 83 0.08 SIDE CHAIN
REMARK 500 TYR C 91 0.08 SIDE CHAIN
REMARK 500 ARG D 83 0.08 SIDE CHAIN
REMARK 500 TYR D 91 0.08 SIDE CHAIN
REMARK 500 ARG E 83 0.08 SIDE CHAIN
REMARK 500 TYR E 91 0.08 SIDE CHAIN
REMARK 500 ARG F 83 0.08 SIDE CHAIN
REMARK 500 TYR F 91 0.08 SIDE CHAIN
REMARK 500 ARG G 83 0.08 SIDE CHAIN
REMARK 500 TYR G 91 0.08 SIDE CHAIN
REMARK 500 ARG H 83 0.08 SIDE CHAIN
REMARK 500 TYR H 91 0.08 SIDE CHAIN
REMARK 500 ARG I 83 0.08 SIDE CHAIN
REMARK 500 TYR I 91 0.08 SIDE CHAIN
REMARK 500 ARG J 83 0.08 SIDE CHAIN
REMARK 500 TYR J 91 0.08 SIDE CHAIN
REMARK 500 ARG K 83 0.08 SIDE CHAIN
REMARK 500 TYR K 91 0.08 SIDE CHAIN
REMARK 500 ARG L 83 0.08 SIDE CHAIN
REMARK 500 TYR L 91 0.08 SIDE CHAIN
REMARK 500 ARG M 83 0.08 SIDE CHAIN
REMARK 500 TYR M 91 0.08 SIDE CHAIN
REMARK 500 ARG N 83 0.08 SIDE CHAIN
REMARK 500 TYR N 91 0.08 SIDE CHAIN
REMARK 500 ARG O 83 0.08 SIDE CHAIN
REMARK 500 TYR O 91 0.08 SIDE CHAIN
REMARK 500 ARG P 83 0.08 SIDE CHAIN
REMARK 500 TYR P 91 0.08 SIDE CHAIN
REMARK 500 ARG Q 83 0.08 SIDE CHAIN
REMARK 500 TYR Q 91 0.08 SIDE CHAIN
REMARK 500 ARG R 83 0.08 SIDE CHAIN
REMARK 500 TYR R 91 0.08 SIDE CHAIN
REMARK 500 ARG S 83 0.08 SIDE CHAIN
REMARK 500 TYR S 91 0.08 SIDE CHAIN
REMARK 500 ARG T 83 0.08 SIDE CHAIN
REMARK 500 TYR T 91 0.08 SIDE CHAIN
REMARK 500 ARG U 83 0.08 SIDE CHAIN
REMARK 500 TYR U 91 0.08 SIDE CHAIN
REMARK 500 ARG V 83 0.08 SIDE CHAIN
REMARK 500 TYR V 91 0.08 SIDE CHAIN
REMARK 500 ARG W 83 0.08 SIDE CHAIN
REMARK 500 TYR W 91 0.08 SIDE CHAIN
REMARK 500 ARG X 83 0.08 SIDE CHAIN
REMARK 500 TYR X 91 0.08 SIDE CHAIN
REMARK 500 ARG Y 83 0.08 SIDE CHAIN
REMARK 500 TYR Y 91 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 I 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 J 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 K 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 L 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 M 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 N 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 O 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Q 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 S 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 T 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 U 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 V 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 W 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 X 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Y 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Z 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 1 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 2 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 3 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 4 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI E 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI F 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI G 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI H 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI I 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI J 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI K 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI L 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI M 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI N 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI O 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI P 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI Q 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI R 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI S 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI T 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI U 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI V 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI W 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI X 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI Y 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI Z 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI 1 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI 2 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI 3 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INI 4 200
DBREF 1RVV A 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV B 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV C 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV D 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV E 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV F 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV G 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV H 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV I 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV J 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV K 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV L 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV M 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV N 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV O 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV P 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV Q 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV R 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV S 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV T 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV U 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV V 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV W 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV X 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV Y 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV Z 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV 1 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV 2 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV 3 1 154 UNP P11998 RISB_BACSU 1 154
DBREF 1RVV 4 1 154 UNP P11998 RISB_BACSU 1 154
SEQRES 1 A 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 A 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 A 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 A 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 A 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 A 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 A 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 A 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 A 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 A 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 A 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 A 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 B 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 B 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 B 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 B 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 B 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 B 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 B 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 B 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 B 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 B 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 B 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 B 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 C 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 C 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 C 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 C 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 C 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 C 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 C 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 C 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 C 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 C 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 C 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 C 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 D 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 D 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 D 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 D 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 D 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 D 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 D 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 D 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 D 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 D 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 D 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 D 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 E 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 E 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 E 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 E 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 E 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 E 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 E 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 E 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 E 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 E 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 E 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 E 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 F 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 F 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 F 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 F 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 F 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 F 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 F 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 F 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 F 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 F 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 F 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 F 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 G 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 G 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 G 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 G 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 G 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 G 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 G 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 G 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 G 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 G 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 G 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 G 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 H 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 H 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 H 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 H 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 H 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 H 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 H 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 H 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 H 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 H 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 H 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 H 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 I 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 I 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 I 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 I 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 I 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 I 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 I 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 I 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 I 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 I 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 I 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 I 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 J 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 J 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 J 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 J 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 J 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 J 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 J 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 J 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 J 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 J 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 J 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 J 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 K 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 K 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 K 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 K 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 K 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 K 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 K 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 K 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 K 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 K 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 K 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 K 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 L 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 L 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 L 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 L 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 L 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 L 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 L 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 L 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 L 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 L 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 L 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 L 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 M 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 M 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 M 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 M 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 M 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 M 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 M 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 M 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 M 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 M 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 M 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 M 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 N 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 N 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 N 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 N 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 N 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 N 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 N 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 N 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 N 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 N 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 N 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 N 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 O 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 O 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 O 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 O 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 O 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 O 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 O 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 O 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 O 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 O 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 O 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 O 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 P 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 P 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 P 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 P 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 P 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 P 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 P 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 P 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 P 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 P 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 P 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 P 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 Q 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 Q 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 Q 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 Q 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 Q 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 Q 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 Q 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 Q 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 Q 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 Q 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 Q 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 Q 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 R 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 R 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 R 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 R 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 R 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 R 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 R 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 R 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 R 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 R 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 R 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 R 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 S 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 S 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 S 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 S 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 S 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 S 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 S 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 S 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 S 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 S 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 S 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 S 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 T 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 T 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 T 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 T 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 T 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 T 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 T 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 T 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 T 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 T 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 T 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 T 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 U 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 U 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 U 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 U 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 U 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 U 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 U 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 U 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 U 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 U 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 U 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 U 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 V 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 V 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 V 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 V 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 V 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 V 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 V 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 V 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 V 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 V 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 V 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 V 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 W 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 W 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 W 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 W 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 W 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 W 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 W 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 W 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 W 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 W 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 W 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 W 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 X 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 X 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 X 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 X 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 X 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 X 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 X 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 X 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 X 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 X 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 X 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 X 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 Y 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 Y 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 Y 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 Y 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 Y 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 Y 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 Y 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 Y 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 Y 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 Y 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 Y 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 Y 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 Z 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 Z 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 Z 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 Z 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 Z 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 Z 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 Z 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 Z 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 Z 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 Z 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 Z 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 Z 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 1 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 1 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 1 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 1 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 1 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 1 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 1 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 1 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 1 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 1 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 1 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 1 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 2 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 2 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 2 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 2 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 2 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 2 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 2 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 2 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 2 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 2 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 2 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 2 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 3 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 3 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 3 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 3 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 3 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 3 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 3 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 3 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 3 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 3 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 3 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 3 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
SEQRES 1 4 154 MET ASN ILE ILE GLN GLY ASN LEU VAL GLY THR GLY LEU
SEQRES 2 4 154 LYS ILE GLY ILE VAL VAL GLY ARG PHE ASN ASP PHE ILE
SEQRES 3 4 154 THR SER LYS LEU LEU SER GLY ALA GLU ASP ALA LEU LEU
SEQRES 4 4 154 ARG HIS GLY VAL ASP THR ASN ASP ILE ASP VAL ALA TRP
SEQRES 5 4 154 VAL PRO GLY ALA PHE GLU ILE PRO PHE ALA ALA LYS LYS
SEQRES 6 4 154 MET ALA GLU THR LYS LYS TYR ASP ALA ILE ILE THR LEU
SEQRES 7 4 154 GLY THR VAL ILE ARG GLY ALA THR THR HIS TYR ASP TYR
SEQRES 8 4 154 VAL CYS ASN GLU ALA ALA LYS GLY ILE ALA GLN ALA ALA
SEQRES 9 4 154 ASN THR THR GLY VAL PRO VAL ILE PHE GLY ILE VAL THR
SEQRES 10 4 154 THR GLU ASN ILE GLU GLN ALA ILE GLU ARG ALA GLY THR
SEQRES 11 4 154 LYS ALA GLY ASN LYS GLY VAL ASP CYS ALA VAL SER ALA
SEQRES 12 4 154 ILE GLU MET ALA ASN LEU ASN ARG SER PHE GLU
HET PO4 A 500 5
HET INI A 200 21
HET PO4 B 500 5
HET INI B 200 21
HET PO4 C 500 5
HET INI C 200 21
HET PO4 D 500 5
HET INI D 200 21
HET PO4 E 500 5
HET INI E 200 21
HET PO4 F 500 5
HET INI F 200 21
HET PO4 G 500 5
HET INI G 200 21
HET PO4 H 500 5
HET INI H 200 21
HET PO4 I 500 5
HET INI I 200 21
HET PO4 J 500 5
HET INI J 200 21
HET PO4 K 500 5
HET INI K 200 21
HET PO4 L 500 5
HET INI L 200 21
HET PO4 M 500 5
HET INI M 200 21
HET PO4 N 500 5
HET INI N 200 21
HET PO4 O 500 5
HET INI O 200 21
HET PO4 P 500 5
HET INI P 200 21
HET PO4 Q 500 5
HET INI Q 200 21
HET PO4 R 500 5
HET INI R 200 21
HET PO4 S 500 5
HET INI S 200 21
HET PO4 T 500 5
HET INI T 200 21
HET PO4 U 500 5
HET INI U 200 21
HET PO4 V 500 5
HET INI V 200 21
HET PO4 W 500 5
HET INI W 200 21
HET PO4 X 500 5
HET INI X 200 21
HET PO4 Y 500 5
HET INI Y 200 21
HET PO4 Z 500 5
HET INI Z 200 21
HET PO4 1 500 5
HET INI 1 200 21
HET PO4 2 500 5
HET INI 2 200 21
HET PO4 3 500 5
HET INI 3 200 21
HET PO4 4 500 5
HET INI 4 200 21
HETNAM PO4 PHOSPHATE ION
HETNAM INI 5-NITRO-6-RIBITYL-AMINO-2,4(1H,3H)-PYRIMIDINEDIONE
FORMUL 31 PO4 30(O4 P 3-)
FORMUL 32 INI 30(C9 H14 N4 O8)
FORMUL 91 HOH *1050(H2 O)
HELIX 1 1 ASP A 24 ARG A 40 1 17
HELIX 2 2 THR A 45 ASP A 47 5 3
HELIX 3 3 ALA A 56 THR A 69 1 14
HELIX 4 4 HIS A 88 THR A 107 1 20
HELIX 5 5 ILE A 121 ARG A 127 1 7
HELIX 6 6 LYS A 135 PHE A 153 1 19
HELIX 7 7 ASP B 24 ARG B 40 1 17
HELIX 8 8 THR B 45 ASP B 47 5 3
HELIX 9 9 ALA B 56 THR B 69 1 14
HELIX 10 10 HIS B 88 THR B 107 1 20
HELIX 11 11 ILE B 121 ARG B 127 1 7
HELIX 12 12 LYS B 135 PHE B 153 1 19
HELIX 13 13 ASP C 24 ARG C 40 1 17
HELIX 14 14 THR C 45 ASP C 47 5 3
HELIX 15 15 ALA C 56 THR C 69 1 14
HELIX 16 16 HIS C 88 THR C 107 1 20
HELIX 17 17 ILE C 121 ARG C 127 1 7
HELIX 18 18 LYS C 135 PHE C 153 1 19
HELIX 19 19 ASP D 24 ARG D 40 1 17
HELIX 20 20 THR D 45 ASP D 47 5 3
HELIX 21 21 ALA D 56 THR D 69 1 14
HELIX 22 22 HIS D 88 THR D 107 1 20
HELIX 23 23 ILE D 121 ARG D 127 1 7
HELIX 24 24 LYS D 135 PHE D 153 1 19
HELIX 25 25 ASP E 24 ARG E 40 1 17
HELIX 26 26 THR E 45 ASP E 47 5 3
HELIX 27 27 ALA E 56 THR E 69 1 14
HELIX 28 28 HIS E 88 THR E 107 1 20
HELIX 29 29 ILE E 121 ARG E 127 1 7
HELIX 30 30 LYS E 135 PHE E 153 1 19
HELIX 31 31 ASP F 24 ARG F 40 1 17
HELIX 32 32 THR F 45 ASP F 47 5 3
HELIX 33 33 ALA F 56 THR F 69 1 14
HELIX 34 34 HIS F 88 THR F 107 1 20
HELIX 35 35 ILE F 121 ARG F 127 1 7
HELIX 36 36 LYS F 135 PHE F 153 1 19
HELIX 37 37 ASP G 24 ARG G 40 1 17
HELIX 38 38 THR G 45 ASP G 47 5 3
HELIX 39 39 ALA G 56 THR G 69 1 14
HELIX 40 40 HIS G 88 THR G 107 1 20
HELIX 41 41 ILE G 121 ARG G 127 1 7
HELIX 42 42 LYS G 135 PHE G 153 1 19
HELIX 43 43 ASP H 24 ARG H 40 1 17
HELIX 44 44 THR H 45 ASP H 47 5 3
HELIX 45 45 ALA H 56 THR H 69 1 14
HELIX 46 46 HIS H 88 THR H 107 1 20
HELIX 47 47 ILE H 121 ARG H 127 1 7
HELIX 48 48 LYS H 135 PHE H 153 1 19
HELIX 49 49 ASP I 24 ARG I 40 1 17
HELIX 50 50 THR I 45 ASP I 47 5 3
HELIX 51 51 ALA I 56 THR I 69 1 14
HELIX 52 52 HIS I 88 THR I 107 1 20
HELIX 53 53 ILE I 121 ARG I 127 1 7
HELIX 54 54 LYS I 135 PHE I 153 1 19
HELIX 55 55 ASP J 24 ARG J 40 1 17
HELIX 56 56 THR J 45 ASP J 47 5 3
HELIX 57 57 ALA J 56 THR J 69 1 14
HELIX 58 58 HIS J 88 THR J 107 1 20
HELIX 59 59 ILE J 121 ARG J 127 1 7
HELIX 60 60 LYS J 135 PHE J 153 1 19
HELIX 61 61 ASP K 24 ARG K 40 1 17
HELIX 62 62 THR K 45 ASP K 47 5 3
HELIX 63 63 ALA K 56 THR K 69 1 14
HELIX 64 64 HIS K 88 THR K 107 1 20
HELIX 65 65 ILE K 121 ARG K 127 1 7
HELIX 66 66 LYS K 135 PHE K 153 1 19
HELIX 67 67 ASP L 24 ARG L 40 1 17
HELIX 68 68 THR L 45 ASP L 47 5 3
HELIX 69 69 ALA L 56 THR L 69 1 14
HELIX 70 70 HIS L 88 THR L 107 1 20
HELIX 71 71 ILE L 121 ARG L 127 1 7
HELIX 72 72 LYS L 135 PHE L 153 1 19
HELIX 73 73 ASP M 24 ARG M 40 1 17
HELIX 74 74 THR M 45 ASP M 47 5 3
HELIX 75 75 ALA M 56 THR M 69 1 14
HELIX 76 76 HIS M 88 THR M 107 1 20
HELIX 77 77 ILE M 121 ARG M 127 1 7
HELIX 78 78 LYS M 135 PHE M 153 1 19
HELIX 79 79 ASP N 24 ARG N 40 1 17
HELIX 80 80 THR N 45 ASP N 47 5 3
HELIX 81 81 ALA N 56 THR N 69 1 14
HELIX 82 82 HIS N 88 THR N 107 1 20
HELIX 83 83 ILE N 121 ARG N 127 1 7
HELIX 84 84 LYS N 135 PHE N 153 1 19
HELIX 85 85 ASP O 24 ARG O 40 1 17
HELIX 86 86 THR O 45 ASP O 47 5 3
HELIX 87 87 ALA O 56 THR O 69 1 14
HELIX 88 88 HIS O 88 THR O 107 1 20
HELIX 89 89 ILE O 121 ARG O 127 1 7
HELIX 90 90 LYS O 135 PHE O 153 1 19
HELIX 91 91 ASP P 24 ARG P 40 1 17
HELIX 92 92 THR P 45 ASP P 47 5 3
HELIX 93 93 ALA P 56 THR P 69 1 14
HELIX 94 94 HIS P 88 THR P 107 1 20
HELIX 95 95 ILE P 121 ARG P 127 1 7
HELIX 96 96 LYS P 135 PHE P 153 1 19
HELIX 97 97 ASP Q 24 ARG Q 40 1 17
HELIX 98 98 THR Q 45 ASP Q 47 5 3
HELIX 99 99 ALA Q 56 THR Q 69 1 14
HELIX 100 100 HIS Q 88 THR Q 107 1 20
HELIX 101 101 ILE Q 121 ARG Q 127 1 7
HELIX 102 102 LYS Q 135 PHE Q 153 1 19
HELIX 103 103 ASP R 24 ARG R 40 1 17
HELIX 104 104 THR R 45 ASP R 47 5 3
HELIX 105 105 ALA R 56 THR R 69 1 14
HELIX 106 106 HIS R 88 THR R 107 1 20
HELIX 107 107 ILE R 121 ARG R 127 1 7
HELIX 108 108 LYS R 135 PHE R 153 1 19
HELIX 109 109 ASP S 24 ARG S 40 1 17
HELIX 110 110 THR S 45 ASP S 47 5 3
HELIX 111 111 ALA S 56 THR S 69 1 14
HELIX 112 112 HIS S 88 THR S 107 1 20
HELIX 113 113 ILE S 121 ARG S 127 1 7
HELIX 114 114 LYS S 135 PHE S 153 1 19
HELIX 115 115 ASP T 24 ARG T 40 1 17
HELIX 116 116 THR T 45 ASP T 47 5 3
HELIX 117 117 ALA T 56 THR T 69 1 14
HELIX 118 118 HIS T 88 THR T 107 1 20
HELIX 119 119 ILE T 121 ARG T 127 1 7
HELIX 120 120 LYS T 135 PHE T 153 1 19
HELIX 121 121 ASP U 24 ARG U 40 1 17
HELIX 122 122 THR U 45 ASP U 47 5 3
HELIX 123 123 ALA U 56 THR U 69 1 14
HELIX 124 124 HIS U 88 THR U 107 1 20
HELIX 125 125 ILE U 121 ARG U 127 1 7
HELIX 126 126 LYS U 135 PHE U 153 1 19
HELIX 127 127 ASP V 24 ARG V 40 1 17
HELIX 128 128 THR V 45 ASP V 47 5 3
HELIX 129 129 ALA V 56 THR V 69 1 14
HELIX 130 130 HIS V 88 THR V 107 1 20
HELIX 131 131 ILE V 121 ARG V 127 1 7
HELIX 132 132 LYS V 135 PHE V 153 1 19
HELIX 133 133 ASP W 24 ARG W 40 1 17
HELIX 134 134 THR W 45 ASP W 47 5 3
HELIX 135 135 ALA W 56 THR W 69 1 14
HELIX 136 136 HIS W 88 THR W 107 1 20
HELIX 137 137 ILE W 121 ARG W 127 1 7
HELIX 138 138 LYS W 135 PHE W 153 1 19
HELIX 139 139 ASP X 24 ARG X 40 1 17
HELIX 140 140 THR X 45 ASP X 47 5 3
HELIX 141 141 ALA X 56 THR X 69 1 14
HELIX 142 142 HIS X 88 THR X 107 1 20
HELIX 143 143 ILE X 121 ARG X 127 1 7
HELIX 144 144 LYS X 135 PHE X 153 1 19
HELIX 145 145 ASP Y 24 ARG Y 40 1 17
HELIX 146 146 THR Y 45 ASP Y 47 5 3
HELIX 147 147 ALA Y 56 THR Y 69 1 14
HELIX 148 148 HIS Y 88 THR Y 107 1 20
HELIX 149 149 ILE Y 121 ARG Y 127 1 7
HELIX 150 150 LYS Y 135 PHE Y 153 1 19
HELIX 151 151 ASP Z 24 ARG Z 40 1 17
HELIX 152 152 THR Z 45 ASP Z 47 5 3
HELIX 153 153 ALA Z 56 THR Z 69 1 14
HELIX 154 154 HIS Z 88 THR Z 107 1 20
HELIX 155 155 ILE Z 121 ARG Z 127 1 7
HELIX 156 156 LYS Z 135 PHE Z 153 1 19
HELIX 157 157 ASP 1 24 ARG 1 40 1 17
HELIX 158 158 THR 1 45 ASP 1 47 5 3
HELIX 159 159 ALA 1 56 THR 1 69 1 14
HELIX 160 160 HIS 1 88 THR 1 107 1 20
HELIX 161 161 ILE 1 121 ARG 1 127 1 7
HELIX 162 162 LYS 1 135 PHE 1 153 1 19
HELIX 163 163 ASP 2 24 ARG 2 40 1 17
HELIX 164 164 THR 2 45 ASP 2 47 5 3
HELIX 165 165 ALA 2 56 THR 2 69 1 14
HELIX 166 166 HIS 2 88 THR 2 107 1 20
HELIX 167 167 ILE 2 121 ARG 2 127 1 7
HELIX 168 168 LYS 2 135 PHE 2 153 1 19
HELIX 169 169 ASP 3 24 ARG 3 40 1 17
HELIX 170 170 THR 3 45 ASP 3 47 5 3
HELIX 171 171 ALA 3 56 THR 3 69 1 14
HELIX 172 172 HIS 3 88 THR 3 107 1 20
HELIX 173 173 ILE 3 121 ARG 3 127 1 7
HELIX 174 174 LYS 3 135 PHE 3 153 1 19
HELIX 175 175 ASP 4 24 ARG 4 40 1 17
HELIX 176 176 THR 4 45 ASP 4 47 5 3
HELIX 177 177 ALA 4 56 THR 4 69 1 14
HELIX 178 178 HIS 4 88 THR 4 107 1 20
HELIX 179 179 ILE 4 121 ARG 4 127 1 7
HELIX 180 180 LYS 4 135 SER 4 152 1 18
SHEET 1 A 5 ASN A 2 ILE A 4 0
SHEET 2 A 5 ILE B 48 VAL B 53 1 N VAL B 50 O ASN A 2
SHEET 3 A 5 ILE B 15 GLY B 20 1 N ILE B 15 O ASP B 49
SHEET 4 A 5 ALA B 74 ILE B 82 1 N ALA B 74 O GLY B 16
SHEET 5 A 5 PRO B 110 THR B 118 1 N PRO B 110 O ILE B 75
SHEET 1 B 5 PRO A 110 THR A 118 0
SHEET 2 B 5 ALA A 74 ILE A 82 1 N ILE A 75 O PRO A 110
SHEET 3 B 5 ILE A 15 GLY A 20 1 N GLY A 16 O ALA A 74
SHEET 4 B 5 ILE A 48 VAL A 53 1 N ASP A 49 O ILE A 15
SHEET 5 B 5 ASN E 2 ILE E 4 1 N ASN E 2 O VAL A 50
SHEET 1 C 5 ASN B 2 ILE B 4 0
SHEET 2 C 5 ILE C 48 VAL C 53 1 N VAL C 50 O ASN B 2
SHEET 3 C 5 ILE C 15 GLY C 20 1 N ILE C 15 O ASP C 49
SHEET 4 C 5 ALA C 74 ILE C 82 1 N ALA C 74 O GLY C 16
SHEET 5 C 5 PRO C 110 THR C 118 1 N PRO C 110 O ILE C 75
SHEET 1 D 5 ASN C 2 ILE C 4 0
SHEET 2 D 5 ILE D 48 VAL D 53 1 N VAL D 50 O ASN C 2
SHEET 3 D 5 ILE D 15 GLY D 20 1 N ILE D 15 O ASP D 49
SHEET 4 D 5 ALA D 74 ILE D 82 1 N ALA D 74 O GLY D 16
SHEET 5 D 5 PRO D 110 THR D 118 1 N PRO D 110 O ILE D 75
SHEET 1 E 5 ASN D 2 ILE D 4 0
SHEET 2 E 5 ILE E 48 VAL E 53 1 N VAL E 50 O ASN D 2
SHEET 3 E 5 ILE E 15 GLY E 20 1 N ILE E 15 O ASP E 49
SHEET 4 E 5 ALA E 74 ILE E 82 1 N ALA E 74 O GLY E 16
SHEET 5 E 5 PRO E 110 THR E 118 1 N PRO E 110 O ILE E 75
SHEET 1 F 5 ASN F 2 ILE F 4 0
SHEET 2 F 5 ILE G 48 VAL G 53 1 N VAL G 50 O ASN F 2
SHEET 3 F 5 ILE G 15 GLY G 20 1 N ILE G 15 O ASP G 49
SHEET 4 F 5 ALA G 74 ILE G 82 1 N ALA G 74 O GLY G 16
SHEET 5 F 5 PRO G 110 THR G 118 1 N PRO G 110 O ILE G 75
SHEET 1 G 5 PRO F 110 THR F 118 0
SHEET 2 G 5 ALA F 74 ILE F 82 1 N ILE F 75 O PRO F 110
SHEET 3 G 5 ILE F 15 GLY F 20 1 N GLY F 16 O ALA F 74
SHEET 4 G 5 ILE F 48 VAL F 53 1 N ASP F 49 O ILE F 15
SHEET 5 G 5 ASN J 2 ILE J 4 1 N ASN J 2 O VAL F 50
SHEET 1 H 5 ASN G 2 ILE G 4 0
SHEET 2 H 5 ILE H 48 VAL H 53 1 N VAL H 50 O ASN G 2
SHEET 3 H 5 ILE H 15 GLY H 20 1 N ILE H 15 O ASP H 49
SHEET 4 H 5 ALA H 74 ILE H 82 1 N ALA H 74 O GLY H 16
SHEET 5 H 5 PRO H 110 THR H 118 1 N PRO H 110 O ILE H 75
SHEET 1 I 5 ASN H 2 ILE H 4 0
SHEET 2 I 5 ILE I 48 VAL I 53 1 N VAL I 50 O ASN H 2
SHEET 3 I 5 ILE I 15 GLY I 20 1 N ILE I 15 O ASP I 49
SHEET 4 I 5 ALA I 74 ILE I 82 1 N ALA I 74 O GLY I 16
SHEET 5 I 5 PRO I 110 THR I 118 1 N PRO I 110 O ILE I 75
SHEET 1 J 5 ASN I 2 ILE I 4 0
SHEET 2 J 5 ILE J 48 VAL J 53 1 N VAL J 50 O ASN I 2
SHEET 3 J 5 ILE J 15 GLY J 20 1 N ILE J 15 O ASP J 49
SHEET 4 J 5 ALA J 74 ILE J 82 1 N ALA J 74 O GLY J 16
SHEET 5 J 5 PRO J 110 THR J 118 1 N PRO J 110 O ILE J 75
SHEET 1 K 5 ASN K 2 ILE K 4 0
SHEET 2 K 5 ILE L 48 VAL L 53 1 N VAL L 50 O ASN K 2
SHEET 3 K 5 ILE L 15 GLY L 20 1 N ILE L 15 O ASP L 49
SHEET 4 K 5 ALA L 74 ILE L 82 1 N ALA L 74 O GLY L 16
SHEET 5 K 5 PRO L 110 THR L 118 1 N PRO L 110 O ILE L 75
SHEET 1 L 5 PRO K 110 THR K 118 0
SHEET 2 L 5 ALA K 74 ILE K 82 1 N ILE K 75 O PRO K 110
SHEET 3 L 5 ILE K 15 GLY K 20 1 N GLY K 16 O ALA K 74
SHEET 4 L 5 ILE K 48 VAL K 53 1 N ASP K 49 O ILE K 15
SHEET 5 L 5 ASN O 2 ILE O 4 1 N ASN O 2 O VAL K 50
SHEET 1 M 5 ASN L 2 ILE L 4 0
SHEET 2 M 5 ILE M 48 VAL M 53 1 N VAL M 50 O ASN L 2
SHEET 3 M 5 ILE M 15 GLY M 20 1 N ILE M 15 O ASP M 49
SHEET 4 M 5 ALA M 74 ILE M 82 1 N ALA M 74 O GLY M 16
SHEET 5 M 5 PRO M 110 THR M 118 1 N PRO M 110 O ILE M 75
SHEET 1 N 5 ASN M 2 ILE M 4 0
SHEET 2 N 5 ILE N 48 VAL N 53 1 N VAL N 50 O ASN M 2
SHEET 3 N 5 ILE N 15 GLY N 20 1 N ILE N 15 O ASP N 49
SHEET 4 N 5 ALA N 74 ILE N 82 1 N ALA N 74 O GLY N 16
SHEET 5 N 5 PRO N 110 THR N 118 1 N PRO N 110 O ILE N 75
SHEET 1 O 5 ASN N 2 ILE N 4 0
SHEET 2 O 5 ILE O 48 VAL O 53 1 N VAL O 50 O ASN N 2
SHEET 3 O 5 ILE O 15 GLY O 20 1 N ILE O 15 O ASP O 49
SHEET 4 O 5 ALA O 74 ILE O 82 1 N ALA O 74 O GLY O 16
SHEET 5 O 5 PRO O 110 THR O 118 1 N PRO O 110 O ILE O 75
SHEET 1 P 5 ASN P 2 ILE P 4 0
SHEET 2 P 5 ILE Q 48 VAL Q 53 1 N VAL Q 50 O ASN P 2
SHEET 3 P 5 ILE Q 15 GLY Q 20 1 N ILE Q 15 O ASP Q 49
SHEET 4 P 5 ALA Q 74 ILE Q 82 1 N ALA Q 74 O GLY Q 16
SHEET 5 P 5 PRO Q 110 THR Q 118 1 N PRO Q 110 O ILE Q 75
SHEET 1 Q 5 PRO P 110 THR P 118 0
SHEET 2 Q 5 ALA P 74 ILE P 82 1 N ILE P 75 O PRO P 110
SHEET 3 Q 5 ILE P 15 GLY P 20 1 N GLY P 16 O ALA P 74
SHEET 4 Q 5 ILE P 48 VAL P 53 1 N ASP P 49 O ILE P 15
SHEET 5 Q 5 ASN T 2 ILE T 4 1 N ASN T 2 O VAL P 50
SHEET 1 R 5 ASN Q 2 ILE Q 4 0
SHEET 2 R 5 ILE R 48 VAL R 53 1 N VAL R 50 O ASN Q 2
SHEET 3 R 5 ILE R 15 GLY R 20 1 N ILE R 15 O ASP R 49
SHEET 4 R 5 ALA R 74 ILE R 82 1 N ALA R 74 O GLY R 16
SHEET 5 R 5 PRO R 110 THR R 118 1 N PRO R 110 O ILE R 75
SHEET 1 S 5 ASN R 2 ILE R 4 0
SHEET 2 S 5 ILE S 48 VAL S 53 1 N VAL S 50 O ASN R 2
SHEET 3 S 5 ILE S 15 GLY S 20 1 N ILE S 15 O ASP S 49
SHEET 4 S 5 ALA S 74 ILE S 82 1 N ALA S 74 O GLY S 16
SHEET 5 S 5 PRO S 110 THR S 118 1 N PRO S 110 O ILE S 75
SHEET 1 T 5 ASN S 2 ILE S 4 0
SHEET 2 T 5 ILE T 48 VAL T 53 1 N VAL T 50 O ASN S 2
SHEET 3 T 5 ILE T 15 GLY T 20 1 N ILE T 15 O ASP T 49
SHEET 4 T 5 ALA T 74 ILE T 82 1 N ALA T 74 O GLY T 16
SHEET 5 T 5 PRO T 110 THR T 118 1 N PRO T 110 O ILE T 75
SHEET 1 U 5 ASN U 2 ILE U 4 0
SHEET 2 U 5 ILE V 48 VAL V 53 1 N VAL V 50 O ASN U 2
SHEET 3 U 5 ILE V 15 GLY V 20 1 N ILE V 15 O ASP V 49
SHEET 4 U 5 ALA V 74 ILE V 82 1 N ALA V 74 O GLY V 16
SHEET 5 U 5 PRO V 110 THR V 118 1 N PRO V 110 O ILE V 75
SHEET 1 V 5 PRO U 110 THR U 118 0
SHEET 2 V 5 ALA U 74 ILE U 82 1 N ILE U 75 O PRO U 110
SHEET 3 V 5 ILE U 15 GLY U 20 1 N GLY U 16 O ALA U 74
SHEET 4 V 5 ILE U 48 VAL U 53 1 N ASP U 49 O ILE U 15
SHEET 5 V 5 ASN Y 2 ILE Y 4 1 N ASN Y 2 O VAL U 50
SHEET 1 W 5 ASN V 2 ILE V 4 0
SHEET 2 W 5 ILE W 48 VAL W 53 1 N VAL W 50 O ASN V 2
SHEET 3 W 5 ILE W 15 GLY W 20 1 N ILE W 15 O ASP W 49
SHEET 4 W 5 ALA W 74 ILE W 82 1 N ALA W 74 O GLY W 16
SHEET 5 W 5 PRO W 110 THR W 118 1 N PRO W 110 O ILE W 75
SHEET 1 X 5 ASN W 2 ILE W 4 0
SHEET 2 X 5 ILE X 48 VAL X 53 1 N VAL X 50 O ASN W 2
SHEET 3 X 5 ILE X 15 GLY X 20 1 N ILE X 15 O ASP X 49
SHEET 4 X 5 ALA X 74 ILE X 82 1 N ALA X 74 O GLY X 16
SHEET 5 X 5 PRO X 110 THR X 118 1 N PRO X 110 O ILE X 75
SHEET 1 Y 5 ASN X 2 ILE X 4 0
SHEET 2 Y 5 ILE Y 48 VAL Y 53 1 N VAL Y 50 O ASN X 2
SHEET 3 Y 5 ILE Y 15 GLY Y 20 1 N ILE Y 15 O ASP Y 49
SHEET 4 Y 5 ALA Y 74 ILE Y 82 1 N ALA Y 74 O GLY Y 16
SHEET 5 Y 5 PRO Y 110 THR Y 118 1 N PRO Y 110 O ILE Y 75
SHEET 1 Z 5 ASN Z 2 ILE Z 4 0
SHEET 2 Z 5 ILE 1 48 VAL 1 53 1 N VAL 1 50 O ASN Z 2
SHEET 3 Z 5 ILE 1 15 GLY 1 20 1 N ILE 1 15 O ASP 1 49
SHEET 4 Z 5 ALA 1 74 ILE 1 82 1 N ALA 1 74 O GLY 1 16
SHEET 5 Z 5 PRO 1 110 THR 1 118 1 N PRO 1 110 O ILE 1 75
SHEET 1 AA 5 PRO Z 110 THR Z 118 0
SHEET 2 AA 5 ALA Z 74 ILE Z 82 1 N ILE Z 75 O PRO Z 110
SHEET 3 AA 5 ILE Z 15 GLY Z 20 1 N GLY Z 16 O ALA Z 74
SHEET 4 AA 5 ILE Z 48 VAL Z 53 1 N ASP Z 49 O ILE Z 15
SHEET 5 AA 5 ASN 4 2 ILE 4 4 1 N ASN 4 2 O VAL Z 50
SHEET 1 BB 5 ASN 1 2 ILE 1 4 0
SHEET 2 BB 5 ILE 2 48 VAL 2 53 1 N VAL 2 50 O ASN 1 2
SHEET 3 BB 5 ILE 2 15 GLY 2 20 1 N ILE 2 15 O ASP 2 49
SHEET 4 BB 5 ALA 2 74 ILE 2 82 1 N ALA 2 74 O GLY 2 16
SHEET 5 BB 5 PRO 2 110 THR 2 118 1 N PRO 2 110 O ILE 2 75
SHEET 1 CC 5 ASN 2 2 ILE 2 4 0
SHEET 2 CC 5 ILE 3 48 VAL 3 53 1 N VAL 3 50 O ASN 2 2
SHEET 3 CC 5 ILE 3 15 GLY 3 20 1 N ILE 3 15 O ASP 3 49
SHEET 4 CC 5 ALA 3 74 ILE 3 82 1 N ALA 3 74 O GLY 3 16
SHEET 5 CC 5 PRO 3 110 THR 3 118 1 N PRO 3 110 O ILE 3 75
SHEET 1 DD 5 ASN 3 2 ILE 3 4 0
SHEET 2 DD 5 ILE 4 48 VAL 4 53 1 N VAL 4 50 O ASN 3 2
SHEET 3 DD 5 ILE 4 15 GLY 4 20 1 N ILE 4 15 O ASP 4 49
SHEET 4 DD 5 ALA 4 74 ILE 4 82 1 N ALA 4 74 O GLY 4 16
SHEET 5 DD 5 PRO 4 110 THR 4 118 1 N PRO 4 110 O ILE 4 75
SITE 1 AC1 5 GLY A 84 ALA A 85 THR A 86 HIS A 88
SITE 2 AC1 5 ARG E 127
SITE 1 AC2 5 ARG A 127 GLY B 84 ALA B 85 THR B 86
SITE 2 AC2 5 HIS B 88
SITE 1 AC3 5 ARG B 127 GLY C 84 ALA C 85 THR C 86
SITE 2 AC3 5 HIS C 88
SITE 1 AC4 5 ARG C 127 GLY D 84 ALA D 85 THR D 86
SITE 2 AC4 5 HIS D 88
SITE 1 AC5 5 ARG D 127 GLY E 84 ALA E 85 THR E 86
SITE 2 AC5 5 HIS E 88
SITE 1 AC6 5 GLY F 84 ALA F 85 THR F 86 HIS F 88
SITE 2 AC6 5 ARG J 127
SITE 1 AC7 5 ARG F 127 GLY G 84 ALA G 85 THR G 86
SITE 2 AC7 5 HIS G 88
SITE 1 AC8 5 ARG G 127 GLY H 84 ALA H 85 THR H 86
SITE 2 AC8 5 HIS H 88
SITE 1 AC9 5 ARG H 127 GLY I 84 ALA I 85 THR I 86
SITE 2 AC9 5 HIS I 88
SITE 1 BC1 5 ARG I 127 GLY J 84 ALA J 85 THR J 86
SITE 2 BC1 5 HIS J 88
SITE 1 BC2 5 GLY K 84 ALA K 85 THR K 86 HIS K 88
SITE 2 BC2 5 ARG O 127
SITE 1 BC3 5 ARG K 127 GLY L 84 ALA L 85 THR L 86
SITE 2 BC3 5 HIS L 88
SITE 1 BC4 5 ARG L 127 GLY M 84 ALA M 85 THR M 86
SITE 2 BC4 5 HIS M 88
SITE 1 BC5 5 ARG M 127 GLY N 84 ALA N 85 THR N 86
SITE 2 BC5 5 HIS N 88
SITE 1 BC6 5 ARG N 127 GLY O 84 ALA O 85 THR O 86
SITE 2 BC6 5 HIS O 88
SITE 1 BC7 5 GLY P 84 ALA P 85 THR P 86 HIS P 88
SITE 2 BC7 5 ARG T 127
SITE 1 BC8 5 ARG P 127 GLY Q 84 ALA Q 85 THR Q 86
SITE 2 BC8 5 HIS Q 88
SITE 1 BC9 5 ARG Q 127 GLY R 84 ALA R 85 THR R 86
SITE 2 BC9 5 HIS R 88
SITE 1 CC1 5 ARG R 127 GLY S 84 ALA S 85 THR S 86
SITE 2 CC1 5 HIS S 88
SITE 1 CC2 5 ARG S 127 GLY T 84 ALA T 85 THR T 86
SITE 2 CC2 5 HIS T 88
SITE 1 CC3 5 GLY U 84 ALA U 85 THR U 86 HIS U 88
SITE 2 CC3 5 ARG Y 127
SITE 1 CC4 5 ARG U 127 GLY V 84 ALA V 85 THR V 86
SITE 2 CC4 5 HIS V 88
SITE 1 CC5 5 ARG V 127 GLY W 84 ALA W 85 THR W 86
SITE 2 CC5 5 HIS W 88
SITE 1 CC6 5 ARG W 127 GLY X 84 ALA X 85 THR X 86
SITE 2 CC6 5 HIS X 88
SITE 1 CC7 5 ARG X 127 GLY Y 84 ALA Y 85 THR Y 86
SITE 2 CC7 5 HIS Y 88
SITE 1 CC8 5 ARG 4 127 GLY Z 84 ALA Z 85 THR Z 86
SITE 2 CC8 5 HIS Z 88
SITE 1 CC9 5 GLY 1 84 ALA 1 85 THR 1 86 HIS 1 88
SITE 2 CC9 5 ARG Z 127
SITE 1 DC1 5 ARG 1 127 GLY 2 84 ALA 2 85 THR 2 86
SITE 2 DC1 5 HIS 2 88
SITE 1 DC2 5 ARG 2 127 GLY 3 84 ALA 3 85 THR 3 86
SITE 2 DC2 5 HIS 3 88
SITE 1 DC3 5 ARG 3 127 GLY 4 84 ALA 4 85 THR 4 86
SITE 2 DC3 5 HIS 4 88
SITE 1 DC4 12 PHE A 22 ASN A 23 GLY A 55 ALA A 56
SITE 2 DC4 12 PHE A 57 GLU A 58 THR A 80 VAL A 81
SITE 3 DC4 12 ILE A 82 HOH A 531 ILE E 112 PHE E 113
SITE 1 DC5 11 PHE A 113 PHE B 22 ASN B 23 GLY B 55
SITE 2 DC5 11 ALA B 56 PHE B 57 GLU B 58 THR B 80
SITE 3 DC5 11 VAL B 81 ILE B 82 HOH B 501
SITE 1 DC6 13 ILE B 112 PHE B 113 LYS B 135 PHE C 22
SITE 2 DC6 13 ASN C 23 GLY C 55 ALA C 56 PHE C 57
SITE 3 DC6 13 GLU C 58 THR C 80 VAL C 81 ILE C 82
SITE 4 DC6 13 HOH C 501
SITE 1 DC7 11 PHE C 113 PHE D 22 ASN D 23 GLY D 55
SITE 2 DC7 11 ALA D 56 PHE D 57 GLU D 58 THR D 80
SITE 3 DC7 11 VAL D 81 ILE D 82 HOH D 501
SITE 1 DC8 12 ILE D 112 PHE D 113 PHE E 22 ASN E 23
SITE 2 DC8 12 GLY E 55 ALA E 56 PHE E 57 GLU E 58
SITE 3 DC8 12 THR E 80 VAL E 81 ILE E 82 HOH E 505
SITE 1 DC9 12 PHE F 22 ASN F 23 GLY F 55 ALA F 56
SITE 2 DC9 12 PHE F 57 GLU F 58 THR F 80 VAL F 81
SITE 3 DC9 12 ILE F 82 HOH F 527 ILE J 112 PHE J 113
SITE 1 EC1 12 ILE F 112 PHE F 113 PHE G 22 ASN G 23
SITE 2 EC1 12 GLY G 55 ALA G 56 PHE G 57 GLU G 58
SITE 3 EC1 12 THR G 80 VAL G 81 ILE G 82 HOH G 202
SITE 1 EC2 12 ILE G 112 PHE G 113 PHE H 22 ASN H 23
SITE 2 EC2 12 GLY H 55 ALA H 56 PHE H 57 GLU H 58
SITE 3 EC2 12 THR H 80 VAL H 81 ILE H 82 HOH H 237
SITE 1 EC3 12 ILE H 112 PHE H 113 PHE I 22 ASN I 23
SITE 2 EC3 12 GLY I 55 ALA I 56 PHE I 57 GLU I 58
SITE 3 EC3 12 THR I 80 VAL I 81 ILE I 82 HOH I 272
SITE 1 EC4 13 ILE I 112 PHE I 113 LYS I 135 PHE J 22
SITE 2 EC4 13 ASN J 23 GLY J 55 ALA J 56 PHE J 57
SITE 3 EC4 13 GLU J 58 THR J 80 VAL J 81 ILE J 82
SITE 4 EC4 13 HOH J 509
SITE 1 EC5 12 PHE K 22 ASN K 23 GLY K 55 ALA K 56
SITE 2 EC5 12 PHE K 57 GLU K 58 THR K 80 VAL K 81
SITE 3 EC5 12 ILE K 82 HOH K 517 ILE O 112 PHE O 113
SITE 1 EC6 12 ILE K 112 PHE K 113 PHE L 22 ASN L 23
SITE 2 EC6 12 GLY L 55 ALA L 56 PHE L 57 GLU L 58
SITE 3 EC6 12 THR L 80 VAL L 81 ILE L 82 HOH L 377
SITE 1 EC7 13 ILE L 112 PHE L 113 LYS L 135 PHE M 22
SITE 2 EC7 13 ASN M 23 GLY M 55 ALA M 56 PHE M 57
SITE 3 EC7 13 GLU M 58 THR M 80 VAL M 81 ILE M 82
SITE 4 EC7 13 HOH M 412
SITE 1 EC8 13 ILE M 112 PHE M 113 LYS M 135 PHE N 22
SITE 2 EC8 13 ASN N 23 GLY N 55 ALA N 56 PHE N 57
SITE 3 EC8 13 GLU N 58 THR N 80 VAL N 81 ILE N 82
SITE 4 EC8 13 HOH N 447
SITE 1 EC9 12 ILE N 112 PHE N 113 PHE O 22 ASN O 23
SITE 2 EC9 12 GLY O 55 ALA O 56 PHE O 57 GLU O 58
SITE 3 EC9 12 THR O 80 VAL O 81 ILE O 82 HOH O 513
SITE 1 FC1 12 PHE P 22 ASN P 23 GLY P 55 ALA P 56
SITE 2 FC1 12 PHE P 57 GLU P 58 THR P 80 VAL P 81
SITE 3 FC1 12 ILE P 82 HOH P 692 ILE T 112 PHE T 113
SITE 1 FC2 13 ILE P 112 PHE P 113 LYS P 135 PHE Q 22
SITE 2 FC2 13 ASN Q 23 GLY Q 55 ALA Q 56 PHE Q 57
SITE 3 FC2 13 GLU Q 58 THR Q 80 VAL Q 81 ILE Q 82
SITE 4 FC2 13 HOH Q 552
SITE 1 FC3 12 ILE Q 112 PHE Q 113 PHE R 22 ASN R 23
SITE 2 FC3 12 GLY R 55 ALA R 56 PHE R 57 GLU R 58
SITE 3 FC3 12 THR R 80 VAL R 81 ILE R 82 HOH R 507
SITE 1 FC4 12 ILE R 112 PHE R 113 PHE S 22 ASN S 23
SITE 2 FC4 12 GLY S 55 ALA S 56 PHE S 57 GLU S 58
SITE 3 FC4 12 THR S 80 VAL S 81 ILE S 82 HOH S 504
SITE 1 FC5 12 ILE S 112 PHE S 113 PHE T 22 ASN T 23
SITE 2 FC5 12 GLY T 55 ALA T 56 PHE T 57 GLU T 58
SITE 3 FC5 12 THR T 80 VAL T 81 ILE T 82 HOH T 657
SITE 1 FC6 12 PHE U 22 ASN U 23 GLY U 55 ALA U 56
SITE 2 FC6 12 PHE U 57 GLU U 58 THR U 80 VAL U 81
SITE 3 FC6 12 ILE U 82 HOH U 532 ILE Y 112 PHE Y 113
SITE 1 FC7 12 ILE U 112 PHE U 113 PHE V 22 ASN V 23
SITE 2 FC7 12 GLY V 55 ALA V 56 PHE V 57 GLU V 58
SITE 3 FC7 12 THR V 80 VAL V 81 ILE V 82 HOH V 505
SITE 1 FC8 12 ILE V 112 PHE V 113 PHE W 22 ASN W 23
SITE 2 FC8 12 GLY W 55 ALA W 56 PHE W 57 GLU W 58
SITE 3 FC8 12 THR W 80 VAL W 81 ILE W 82 HOH W 762
SITE 1 FC9 12 ILE W 112 PHE W 113 PHE X 22 ASN X 23
SITE 2 FC9 12 GLY X 55 ALA X 56 PHE X 57 GLU X 58
SITE 3 FC9 12 THR X 80 VAL X 81 ILE X 82 HOH X 797
SITE 1 GC1 13 ILE X 112 PHE X 113 LYS X 135 PHE Y 22
SITE 2 GC1 13 ASN Y 23 GLY Y 55 ALA Y 56 PHE Y 57
SITE 3 GC1 13 GLU Y 58 THR Y 80 VAL Y 81 ILE Y 82
SITE 4 GC1 13 HOH Y 832
SITE 1 GC2 13 ILE 4 112 PHE 4 113 LYS 4 135 PHE Z 22
SITE 2 GC2 13 ASN Z 23 GLY Z 55 ALA Z 56 PHE Z 57
SITE 3 GC2 13 GLU Z 58 THR Z 80 VAL Z 81 ILE Z 82
SITE 4 GC2 13 HOH Z1042
SITE 1 GC3 11 PHE 1 22 ASN 1 23 GLY 1 55 ALA 1 56
SITE 2 GC3 11 PHE 1 57 GLU 1 58 THR 1 80 VAL 1 81
SITE 3 GC3 11 ILE 1 82 HOH 1 902 PHE Z 113
SITE 1 GC4 12 ILE 1 112 PHE 1 113 PHE 2 22 ASN 2 23
SITE 2 GC4 12 GLY 2 55 ALA 2 56 PHE 2 57 GLU 2 58
SITE 3 GC4 12 THR 2 80 VAL 2 81 ILE 2 82 HOH 2 937
SITE 1 GC5 13 ILE 2 112 PHE 2 113 LYS 2 135 PHE 3 22
SITE 2 GC5 13 ASN 3 23 GLY 3 55 ALA 3 56 PHE 3 57
SITE 3 GC5 13 GLU 3 58 THR 3 80 VAL 3 81 ILE 3 82
SITE 4 GC5 13 HOH 3 972
SITE 1 GC6 12 ILE 3 112 PHE 3 113 PHE 4 22 ASN 4 23
SITE 2 GC6 12 GLY 4 55 ALA 4 56 PHE 4 57 GLU 4 58
SITE 3 GC6 12 THR 4 80 VAL 4 81 ILE 4 82 HOH 41007
CRYST1 235.900 192.600 168.600 90.00 134.90 90.00 C 1 2 1 120
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 0.004239 0.000000 0.004224 0.00000
SCALE2 0.000000 0.005192 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008373 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
