HEADER OXIDOREDUCTASE 05-OCT-07 2RGZ
TITLE ENSEMBLE REFINEMENT OF THE PROTEIN CRYSTAL STRUCTURE OF HUMAN HEME
TITLE 2 OXYGENASE-2 C127A (HO-2) WITH BOUND HEME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME OXYGENASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HO-2;
COMPND 5 EC: 1.14.99.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HMOX2, HO2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T-2
KEYWDS ENSEMBLE REFINEMENT, REFINEMENT METHODOLOGY DEVELOPMENT, STRUCTURAL
KEYWDS 2 GENOMICS MEDICAL RELEVANCE, STRUCTURAL GENOMICS COMMUNITY REQUEST,
KEYWDS 3 HO-2, HEME OXYGENASE, ENDOPLASMIC RETICULUM, IRON, METAL-BINDING,
KEYWDS 4 MICROSOME, OXIDOREDUCTASE, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 5 INITIATIVE, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG
EXPDTA X-RAY DIFFRACTION
NUMMDL 16
AUTHOR C.M.BIANCHETTI,C.A.BINGMAN,E.BITTO,G.E.WESENBERG,G.N.PHILLIPS JR.,
AUTHOR 2 CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 7 30-AUG-23 2RGZ 1 REMARK
REVDAT 6 20-OCT-21 2RGZ 1 REMARK SEQADV
REVDAT 5 25-OCT-17 2RGZ 1 REMARK
REVDAT 4 10-AUG-11 2RGZ 1 REMARK
REVDAT 3 24-FEB-09 2RGZ 1 VERSN
REVDAT 2 22-JAN-08 2RGZ 1 JRNL
REVDAT 1 23-OCT-07 2RGZ 0
JRNL AUTH C.M.BIANCHETTI,L.YI,S.W.RAGSDALE,G.N.PHILLIPS JR.
JRNL TITL COMPARISON OF APO- AND HEME-BOUND CRYSTAL STRUCTURES OF A
JRNL TITL 2 TRUNCATED HUMAN HEME OXYGENASE-2.
JRNL REF J.BIOL.CHEM. V. 282 37624 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17965015
JRNL DOI 10.1074/JBC.M707396200
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD USING AMPLITUDES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1772722.500
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 19515
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1005
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2977
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 154
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3552
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.020 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.660 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.200 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 53.31
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : HEMEFE+3.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS PDB ENTRY IS A RE-REFINEMENT USING AN ENSEMBLE MODEL OF THE
REMARK 3 PREVIOUSLY
REMARK 3 DEPOSITED SINGLE-CONFORMER STRUCTURE 2QPP AND
REMARK 3 THE FIRST DATA SET IN THE DEPOSITED STRUCTURE FACTOR FILE
REMARK 3 FOR 2QPP ALONG WITH THE R-FREE SET DEFINED THEREIN. THE COORDINATES
REMARK 3 WERE GENERATED BY AN AUTOMATED PROTOCOL FROM AN INITIAL MODEL
REMARK 3 CONSISTING
REMARK 3 OF 16 IDENTICAL COPIES OF THE PROTEIN AND NON-WATER
REMARK 3 HETERO-ATOMS ASSIGNED FRACTIONAL OCCUPANCIES ADDING UP TO ONE, AND
REMARK 3 A
REMARK 3 SINGLE COPY OF THE SOLVENT MOLECULES. REFINEMENT WAS CARRIED OUT
REMARK 3 WITH
REMARK 3 ALL THE CONFORMERS PRESENT SIMULTANEOUSLY AND WITH THE POTENTIAL
REMARK 3 ENERGY
REMARK 3 TERMS CORRESPONDING TO INTERACTIONS BETWEEN THE DIFFERENT
REMARK 3 CONFORMERS
REMARK 3 EXCLUDED. THE HELIX AND SHEET RECORDS WERE CALCULATED USING
REMARK 3 COORDINATES
REMARK 3 FROM THE FIRST CONFORMER ONLY. THE STRUCTURE VISUALIZATION PROGRAM
REMARK 3 PYMOL IS WELL-SUITED FOR DIRECTLY VIEWING THE ENSEMBLE MODEL
REMARK 3 PRESENTED IN THIS PDB FILE.
REMARK 4
REMARK 4 2RGZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : ADJUSTABLE FOCUS K-B PAIR SI
REMARK 200 PLUS PT, RH COATINGS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24030
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320
REMARK 200 RESOLUTION RANGE LOW (A) : 42.413
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.6
REMARK 200 DATA REDUNDANCY : 11.60
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2680
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 27.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.71500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.776
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTI-CONFORMER RE
REMARK 200 -REFINEMENT
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 2QPP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (5 MG/ML PROTEIN, 1:1
REMARK 280 RATIO HEME, 2% DMSO, 0.050 M POTASSIUM CHLORIDE, 0.050 M TRIS-
REMARK 280 HCL PH 7.5) MIXED IN A 1.5:1 RATIO WITH THE WELL SOLUTION (33%
REMARK 280 PEG DME 500, 0.020 M MAGNESIUM CHLORIDE, 0.10 M HEPES PH 7.5).
REMARK 280 CRYOPROTECTED WITH WELL SOLUTION, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 37.48850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.92300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.54700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.92300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.48850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.54700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 1 MET A 1
REMARK 465 1 SER A 2
REMARK 465 1 ALA A 3
REMARK 465 1 GLU A 4
REMARK 465 1 VAL A 5
REMARK 465 1 GLU A 6
REMARK 465 1 THR A 7
REMARK 465 1 SER A 8
REMARK 465 1 GLU A 9
REMARK 465 1 GLY A 10
REMARK 465 1 VAL A 11
REMARK 465 1 ASP A 12
REMARK 465 1 GLU A 13
REMARK 465 1 SER A 14
REMARK 465 1 GLU A 15
REMARK 465 1 LYS A 16
REMARK 465 1 LYS A 17
REMARK 465 1 ASN A 18
REMARK 465 1 SER A 19
REMARK 465 1 GLY A 20
REMARK 465 1 ALA A 21
REMARK 465 1 LEU A 22
REMARK 465 1 GLU A 23
REMARK 465 1 LYS A 24
REMARK 465 1 GLU A 25
REMARK 465 1 ASN A 26
REMARK 465 1 GLN A 27
REMARK 465 1 MET A 28
REMARK 465 1 THR A 243
REMARK 465 1 LEU A 244
REMARK 465 1 ALA A 245
REMARK 465 1 ARG A 246
REMARK 465 1 GLU A 247
REMARK 465 1 THR A 248
REMARK 465 1 LEU A 249
REMARK 465 1 GLU A 250
REMARK 465 1 ASP A 251
REMARK 465 1 GLY A 252
REMARK 465 1 PHE A 253
REMARK 465 1 PRO A 254
REMARK 465 1 VAL A 255
REMARK 465 1 HIS A 256
REMARK 465 1 ASP A 257
REMARK 465 1 GLY A 258
REMARK 465 1 LYS A 259
REMARK 465 1 GLY A 260
REMARK 465 1 ASP A 261
REMARK 465 1 MET A 262
REMARK 465 1 ARG A 263
REMARK 465 1 LYS A 264
REMARK 465 1 MET B 1
REMARK 465 1 SER B 2
REMARK 465 1 ALA B 3
REMARK 465 1 GLU B 4
REMARK 465 1 VAL B 5
REMARK 465 1 GLU B 6
REMARK 465 1 THR B 7
REMARK 465 1 SER B 8
REMARK 465 1 GLU B 9
REMARK 465 1 GLY B 10
REMARK 465 1 VAL B 11
REMARK 465 1 ASP B 12
REMARK 465 1 GLU B 13
REMARK 465 1 SER B 14
REMARK 465 1 GLU B 15
REMARK 465 1 LYS B 16
REMARK 465 1 LYS B 17
REMARK 465 1 ASN B 18
REMARK 465 1 SER B 19
REMARK 465 1 GLY B 20
REMARK 465 1 ALA B 21
REMARK 465 1 LEU B 22
REMARK 465 1 GLU B 23
REMARK 465 1 LYS B 24
REMARK 465 1 GLU B 25
REMARK 465 1 ASN B 26
REMARK 465 1 GLN B 27
REMARK 465 1 MET B 28
REMARK 465 1 ARG B 29
REMARK 465 1 LEU B 249
REMARK 465 1 GLU B 250
REMARK 465 1 ASP B 251
REMARK 465 1 GLY B 252
REMARK 465 1 PHE B 253
REMARK 465 1 PRO B 254
REMARK 465 1 VAL B 255
REMARK 465 1 HIS B 256
REMARK 465 1 ASP B 257
REMARK 465 1 GLY B 258
REMARK 465 1 LYS B 259
REMARK 465 1 GLY B 260
REMARK 465 1 ASP B 261
REMARK 465 1 MET B 262
REMARK 465 1 ARG B 263
REMARK 465 1 LYS B 264
REMARK 465 2 MET A 1
REMARK 465 2 SER A 2
REMARK 465 2 ALA A 3
REMARK 465 2 GLU A 4
REMARK 465 2 VAL A 5
REMARK 465 2 GLU A 6
REMARK 465 2 THR A 7
REMARK 465 2 SER A 8
REMARK 465 2 GLU A 9
REMARK 465 2 GLY A 10
REMARK 465 2 VAL A 11
REMARK 465 2 ASP A 12
REMARK 465 2 GLU A 13
REMARK 465 2 SER A 14
REMARK 465 2 GLU A 15
REMARK 465 2 LYS A 16
REMARK 465 2 LYS A 17
REMARK 465 2 ASN A 18
REMARK 465 2 SER A 19
REMARK 465 2 GLY A 20
REMARK 465 2 ALA A 21
REMARK 465 2 LEU A 22
REMARK 465 2 GLU A 23
REMARK 465 2 LYS A 24
REMARK 465 2 GLU A 25
REMARK 465 2 ASN A 26
REMARK 465 2 GLN A 27
REMARK 465 2 MET A 28
REMARK 465 2 THR A 243
REMARK 465 2 LEU A 244
REMARK 465 2 ALA A 245
REMARK 465 2 ARG A 246
REMARK 465 2 GLU A 247
REMARK 465 2 THR A 248
REMARK 465 2 LEU A 249
REMARK 465 2 GLU A 250
REMARK 465 2 ASP A 251
REMARK 465 2 GLY A 252
REMARK 465 2 PHE A 253
REMARK 465 2 PRO A 254
REMARK 465 2 VAL A 255
REMARK 465 2 HIS A 256
REMARK 465 2 ASP A 257
REMARK 465 2 GLY A 258
REMARK 465 2 LYS A 259
REMARK 465 2 GLY A 260
REMARK 465 2 ASP A 261
REMARK 465 2 MET A 262
REMARK 465 2 ARG A 263
REMARK 465 2 LYS A 264
REMARK 465 2 MET B 1
REMARK 465 2 SER B 2
REMARK 465 2 ALA B 3
REMARK 465 2 GLU B 4
REMARK 465 2 VAL B 5
REMARK 465 2 GLU B 6
REMARK 465 2 THR B 7
REMARK 465 2 SER B 8
REMARK 465 2 GLU B 9
REMARK 465 2 GLY B 10
REMARK 465 2 VAL B 11
REMARK 465 2 ASP B 12
REMARK 465 2 GLU B 13
REMARK 465 2 SER B 14
REMARK 465 2 GLU B 15
REMARK 465 2 LYS B 16
REMARK 465 2 LYS B 17
REMARK 465 2 ASN B 18
REMARK 465 2 SER B 19
REMARK 465 2 GLY B 20
REMARK 465 2 ALA B 21
REMARK 465 2 LEU B 22
REMARK 465 2 GLU B 23
REMARK 465 2 LYS B 24
REMARK 465 2 GLU B 25
REMARK 465 2 ASN B 26
REMARK 465 2 GLN B 27
REMARK 465 2 MET B 28
REMARK 465 2 ARG B 29
REMARK 465 2 LEU B 249
REMARK 465 2 GLU B 250
REMARK 465 2 ASP B 251
REMARK 465 2 GLY B 252
REMARK 465 2 PHE B 253
REMARK 465 2 PRO B 254
REMARK 465 2 VAL B 255
REMARK 465 2 HIS B 256
REMARK 465 2 ASP B 257
REMARK 465 2 GLY B 258
REMARK 465 2 LYS B 259
REMARK 465 2 GLY B 260
REMARK 465 2 ASP B 261
REMARK 465 2 MET B 262
REMARK 465 2 ARG B 263
REMARK 465 2 LYS B 264
REMARK 465 3 MET A 1
REMARK 465 3 SER A 2
REMARK 465 3 ALA A 3
REMARK 465 3 GLU A 4
REMARK 465 3 VAL A 5
REMARK 465 3 GLU A 6
REMARK 465 3 THR A 7
REMARK 465 3 SER A 8
REMARK 465 3 GLU A 9
REMARK 465 3 GLY A 10
REMARK 465 3 VAL A 11
REMARK 465 3 ASP A 12
REMARK 465 3 GLU A 13
REMARK 465 3 SER A 14
REMARK 465 3 GLU A 15
REMARK 465 3 LYS A 16
REMARK 465 3 LYS A 17
REMARK 465 3 ASN A 18
REMARK 465 3 SER A 19
REMARK 465 3 GLY A 20
REMARK 465 3 ALA A 21
REMARK 465 3 LEU A 22
REMARK 465 3 GLU A 23
REMARK 465 3 LYS A 24
REMARK 465 3 GLU A 25
REMARK 465 3 ASN A 26
REMARK 465 3 GLN A 27
REMARK 465 3 MET A 28
REMARK 465 3 THR A 243
REMARK 465 3 LEU A 244
REMARK 465 3 ALA A 245
REMARK 465 3 ARG A 246
REMARK 465 3 GLU A 247
REMARK 465 3 THR A 248
REMARK 465 3 LEU A 249
REMARK 465 3 GLU A 250
REMARK 465 3 ASP A 251
REMARK 465 3 GLY A 252
REMARK 465 3 PHE A 253
REMARK 465 3 PRO A 254
REMARK 465 3 VAL A 255
REMARK 465 3 HIS A 256
REMARK 465 3 ASP A 257
REMARK 465 3 GLY A 258
REMARK 465 3 LYS A 259
REMARK 465 3 GLY A 260
REMARK 465 3 ASP A 261
REMARK 465 3 MET A 262
REMARK 465 3 ARG A 263
REMARK 465 3 LYS A 264
REMARK 465 3 MET B 1
REMARK 465 3 SER B 2
REMARK 465 3 ALA B 3
REMARK 465 3 GLU B 4
REMARK 465 3 VAL B 5
REMARK 465 3 GLU B 6
REMARK 465 3 THR B 7
REMARK 465 3 SER B 8
REMARK 465 3 GLU B 9
REMARK 465 3 GLY B 10
REMARK 465 3 VAL B 11
REMARK 465 3 ASP B 12
REMARK 465 3 GLU B 13
REMARK 465 3 SER B 14
REMARK 465 3 GLU B 15
REMARK 465 3 LYS B 16
REMARK 465 3 LYS B 17
REMARK 465 3 ASN B 18
REMARK 465 3 SER B 19
REMARK 465 3 GLY B 20
REMARK 465 3 ALA B 21
REMARK 465 3 LEU B 22
REMARK 465 3 GLU B 23
REMARK 465 3 LYS B 24
REMARK 465 3 GLU B 25
REMARK 465 3 ASN B 26
REMARK 465 3 GLN B 27
REMARK 465 3 MET B 28
REMARK 465 3 ARG B 29
REMARK 465 3 LEU B 249
REMARK 465 3 GLU B 250
REMARK 465 3 ASP B 251
REMARK 465 3 GLY B 252
REMARK 465 3 PHE B 253
REMARK 465 3 PRO B 254
REMARK 465 3 VAL B 255
REMARK 465 3 HIS B 256
REMARK 465 3 ASP B 257
REMARK 465 3 GLY B 258
REMARK 465 3 LYS B 259
REMARK 465 3 GLY B 260
REMARK 465 3 ASP B 261
REMARK 465 3 MET B 262
REMARK 465 3 ARG B 263
REMARK 465 3 LYS B 264
REMARK 465 4 MET A 1
REMARK 465 4 SER A 2
REMARK 465 4 ALA A 3
REMARK 465 4 GLU A 4
REMARK 465 4 VAL A 5
REMARK 465 4 GLU A 6
REMARK 465 4 THR A 7
REMARK 465 4 SER A 8
REMARK 465 4 GLU A 9
REMARK 465 4 GLY A 10
REMARK 465 4 VAL A 11
REMARK 465 4 ASP A 12
REMARK 465 4 GLU A 13
REMARK 465 4 SER A 14
REMARK 465 4 GLU A 15
REMARK 465 4 LYS A 16
REMARK 465 4 LYS A 17
REMARK 465 4 ASN A 18
REMARK 465 4 SER A 19
REMARK 465 4 GLY A 20
REMARK 465 4 ALA A 21
REMARK 465 4 LEU A 22
REMARK 465 4 GLU A 23
REMARK 465 4 LYS A 24
REMARK 465 4 GLU A 25
REMARK 465 4 ASN A 26
REMARK 465 4 GLN A 27
REMARK 465 4 MET A 28
REMARK 465 4 THR A 243
REMARK 465 4 LEU A 244
REMARK 465 4 ALA A 245
REMARK 465 4 ARG A 246
REMARK 465 4 GLU A 247
REMARK 465 4 THR A 248
REMARK 465 4 LEU A 249
REMARK 465 4 GLU A 250
REMARK 465 4 ASP A 251
REMARK 465 4 GLY A 252
REMARK 465 4 PHE A 253
REMARK 465 4 PRO A 254
REMARK 465 4 VAL A 255
REMARK 465 4 HIS A 256
REMARK 465 4 ASP A 257
REMARK 465 4 GLY A 258
REMARK 465 4 LYS A 259
REMARK 465 4 GLY A 260
REMARK 465 4 ASP A 261
REMARK 465 4 MET A 262
REMARK 465 4 ARG A 263
REMARK 465 4 LYS A 264
REMARK 465 4 MET B 1
REMARK 465 4 SER B 2
REMARK 465 4 ALA B 3
REMARK 465 4 GLU B 4
REMARK 465 4 VAL B 5
REMARK 465 4 GLU B 6
REMARK 465 4 THR B 7
REMARK 465 4 SER B 8
REMARK 465 4 GLU B 9
REMARK 465 4 GLY B 10
REMARK 465 4 VAL B 11
REMARK 465 4 ASP B 12
REMARK 465 4 GLU B 13
REMARK 465 4 SER B 14
REMARK 465 4 GLU B 15
REMARK 465 4 LYS B 16
REMARK 465 4 LYS B 17
REMARK 465 4 ASN B 18
REMARK 465 4 SER B 19
REMARK 465 4 GLY B 20
REMARK 465 4 ALA B 21
REMARK 465 4 LEU B 22
REMARK 465 4 GLU B 23
REMARK 465 4 LYS B 24
REMARK 465 4 GLU B 25
REMARK 465 4 ASN B 26
REMARK 465 4 GLN B 27
REMARK 465 4 MET B 28
REMARK 465 4 ARG B 29
REMARK 465 4 LEU B 249
REMARK 465 4 GLU B 250
REMARK 465 4 ASP B 251
REMARK 465 4 GLY B 252
REMARK 465 4 PHE B 253
REMARK 465 4 PRO B 254
REMARK 465 4 VAL B 255
REMARK 465 4 HIS B 256
REMARK 465 4 ASP B 257
REMARK 465 4 GLY B 258
REMARK 465 4 LYS B 259
REMARK 465 4 GLY B 260
REMARK 465 4 ASP B 261
REMARK 465 4 MET B 262
REMARK 465 4 ARG B 263
REMARK 465 4 LYS B 264
REMARK 465 5 MET A 1
REMARK 465 5 SER A 2
REMARK 465 5 ALA A 3
REMARK 465 5 GLU A 4
REMARK 465 5 VAL A 5
REMARK 465 5 GLU A 6
REMARK 465 5 THR A 7
REMARK 465 5 SER A 8
REMARK 465 5 GLU A 9
REMARK 465 5 GLY A 10
REMARK 465 5 VAL A 11
REMARK 465 5 ASP A 12
REMARK 465 5 GLU A 13
REMARK 465 5 SER A 14
REMARK 465 5 GLU A 15
REMARK 465 5 LYS A 16
REMARK 465 5 LYS A 17
REMARK 465 5 ASN A 18
REMARK 465 5 SER A 19
REMARK 465 5 GLY A 20
REMARK 465 5 ALA A 21
REMARK 465 5 LEU A 22
REMARK 465 5 GLU A 23
REMARK 465 5 LYS A 24
REMARK 465 5 GLU A 25
REMARK 465 5 ASN A 26
REMARK 465 5 GLN A 27
REMARK 465 5 MET A 28
REMARK 465 5 THR A 243
REMARK 465 5 LEU A 244
REMARK 465 5 ALA A 245
REMARK 465 5 ARG A 246
REMARK 465 5 GLU A 247
REMARK 465 5 THR A 248
REMARK 465 5 LEU A 249
REMARK 465 5 GLU A 250
REMARK 465 5 ASP A 251
REMARK 465 5 GLY A 252
REMARK 465 5 PHE A 253
REMARK 465 5 PRO A 254
REMARK 465 5 VAL A 255
REMARK 465 5 HIS A 256
REMARK 465 5 ASP A 257
REMARK 465 5 GLY A 258
REMARK 465 5 LYS A 259
REMARK 465 5 GLY A 260
REMARK 465 5 ASP A 261
REMARK 465 5 MET A 262
REMARK 465 5 ARG A 263
REMARK 465 5 LYS A 264
REMARK 465 5 MET B 1
REMARK 465 5 SER B 2
REMARK 465 5 ALA B 3
REMARK 465 5 GLU B 4
REMARK 465 5 VAL B 5
REMARK 465 5 GLU B 6
REMARK 465 5 THR B 7
REMARK 465 5 SER B 8
REMARK 465 5 GLU B 9
REMARK 465 5 GLY B 10
REMARK 465 5 VAL B 11
REMARK 465 5 ASP B 12
REMARK 465 5 GLU B 13
REMARK 465 5 SER B 14
REMARK 465 5 GLU B 15
REMARK 465 5 LYS B 16
REMARK 465 5 LYS B 17
REMARK 465 5 ASN B 18
REMARK 465 5 SER B 19
REMARK 465 5 GLY B 20
REMARK 465 5 ALA B 21
REMARK 465 5 LEU B 22
REMARK 465 5 GLU B 23
REMARK 465 5 LYS B 24
REMARK 465 5 GLU B 25
REMARK 465 5 ASN B 26
REMARK 465 5 GLN B 27
REMARK 465 5 MET B 28
REMARK 465 5 ARG B 29
REMARK 465 5 LEU B 249
REMARK 465 5 GLU B 250
REMARK 465 5 ASP B 251
REMARK 465 5 GLY B 252
REMARK 465 5 PHE B 253
REMARK 465 5 PRO B 254
REMARK 465 5 VAL B 255
REMARK 465 5 HIS B 256
REMARK 465 5 ASP B 257
REMARK 465 5 GLY B 258
REMARK 465 5 LYS B 259
REMARK 465 5 GLY B 260
REMARK 465 5 ASP B 261
REMARK 465 5 MET B 262
REMARK 465 5 ARG B 263
REMARK 465 5 LYS B 264
REMARK 465 6 MET A 1
REMARK 465 6 SER A 2
REMARK 465 6 ALA A 3
REMARK 465 6 GLU A 4
REMARK 465 6 VAL A 5
REMARK 465 6 GLU A 6
REMARK 465 6 THR A 7
REMARK 465 6 SER A 8
REMARK 465 6 GLU A 9
REMARK 465 6 GLY A 10
REMARK 465 6 VAL A 11
REMARK 465 6 ASP A 12
REMARK 465 6 GLU A 13
REMARK 465 6 SER A 14
REMARK 465 6 GLU A 15
REMARK 465 6 LYS A 16
REMARK 465 6 LYS A 17
REMARK 465 6 ASN A 18
REMARK 465 6 SER A 19
REMARK 465 6 GLY A 20
REMARK 465 6 ALA A 21
REMARK 465 6 LEU A 22
REMARK 465 6 GLU A 23
REMARK 465 6 LYS A 24
REMARK 465 6 GLU A 25
REMARK 465 6 ASN A 26
REMARK 465 6 GLN A 27
REMARK 465 6 MET A 28
REMARK 465 6 THR A 243
REMARK 465 6 LEU A 244
REMARK 465 6 ALA A 245
REMARK 465 6 ARG A 246
REMARK 465 6 GLU A 247
REMARK 465 6 THR A 248
REMARK 465 6 LEU A 249
REMARK 465 6 GLU A 250
REMARK 465 6 ASP A 251
REMARK 465 6 GLY A 252
REMARK 465 6 PHE A 253
REMARK 465 6 PRO A 254
REMARK 465 6 VAL A 255
REMARK 465 6 HIS A 256
REMARK 465 6 ASP A 257
REMARK 465 6 GLY A 258
REMARK 465 6 LYS A 259
REMARK 465 6 GLY A 260
REMARK 465 6 ASP A 261
REMARK 465 6 MET A 262
REMARK 465 6 ARG A 263
REMARK 465 6 LYS A 264
REMARK 465 6 MET B 1
REMARK 465 6 SER B 2
REMARK 465 6 ALA B 3
REMARK 465 6 GLU B 4
REMARK 465 6 VAL B 5
REMARK 465 6 GLU B 6
REMARK 465 6 THR B 7
REMARK 465 6 SER B 8
REMARK 465 6 GLU B 9
REMARK 465 6 GLY B 10
REMARK 465 6 VAL B 11
REMARK 465 6 ASP B 12
REMARK 465 6 GLU B 13
REMARK 465 6 SER B 14
REMARK 465 6 GLU B 15
REMARK 465 6 LYS B 16
REMARK 465 6 LYS B 17
REMARK 465 6 ASN B 18
REMARK 465 6 SER B 19
REMARK 465 6 GLY B 20
REMARK 465 6 ALA B 21
REMARK 465 6 LEU B 22
REMARK 465 6 GLU B 23
REMARK 465 6 LYS B 24
REMARK 465 6 GLU B 25
REMARK 465 6 ASN B 26
REMARK 465 6 GLN B 27
REMARK 465 6 MET B 28
REMARK 465 6 ARG B 29
REMARK 465 6 LEU B 249
REMARK 465 6 GLU B 250
REMARK 465 6 ASP B 251
REMARK 465 6 GLY B 252
REMARK 465 6 PHE B 253
REMARK 465 6 PRO B 254
REMARK 465 6 VAL B 255
REMARK 465 6 HIS B 256
REMARK 465 6 ASP B 257
REMARK 465 6 GLY B 258
REMARK 465 6 LYS B 259
REMARK 465 6 GLY B 260
REMARK 465 6 ASP B 261
REMARK 465 6 MET B 262
REMARK 465 6 ARG B 263
REMARK 465 6 LYS B 264
REMARK 465 7 MET A 1
REMARK 465 7 SER A 2
REMARK 465 7 ALA A 3
REMARK 465 7 GLU A 4
REMARK 465 7 VAL A 5
REMARK 465 7 GLU A 6
REMARK 465 7 THR A 7
REMARK 465 7 SER A 8
REMARK 465 7 GLU A 9
REMARK 465 7 GLY A 10
REMARK 465 7 VAL A 11
REMARK 465 7 ASP A 12
REMARK 465 7 GLU A 13
REMARK 465 7 SER A 14
REMARK 465 7 GLU A 15
REMARK 465 7 LYS A 16
REMARK 465 7 LYS A 17
REMARK 465 7 ASN A 18
REMARK 465 7 SER A 19
REMARK 465 7 GLY A 20
REMARK 465 7 ALA A 21
REMARK 465 7 LEU A 22
REMARK 465 7 GLU A 23
REMARK 465 7 LYS A 24
REMARK 465 7 GLU A 25
REMARK 465 7 ASN A 26
REMARK 465 7 GLN A 27
REMARK 465 7 MET A 28
REMARK 465 7 THR A 243
REMARK 465 7 LEU A 244
REMARK 465 7 ALA A 245
REMARK 465 7 ARG A 246
REMARK 465 7 GLU A 247
REMARK 465 7 THR A 248
REMARK 465 7 LEU A 249
REMARK 465 7 GLU A 250
REMARK 465 7 ASP A 251
REMARK 465 7 GLY A 252
REMARK 465 7 PHE A 253
REMARK 465 7 PRO A 254
REMARK 465 7 VAL A 255
REMARK 465 7 HIS A 256
REMARK 465 7 ASP A 257
REMARK 465 7 GLY A 258
REMARK 465 7 LYS A 259
REMARK 465 7 GLY A 260
REMARK 465 7 ASP A 261
REMARK 465 7 MET A 262
REMARK 465 7 ARG A 263
REMARK 465 7 LYS A 264
REMARK 465 7 MET B 1
REMARK 465 7 SER B 2
REMARK 465 7 ALA B 3
REMARK 465 7 GLU B 4
REMARK 465 7 VAL B 5
REMARK 465 7 GLU B 6
REMARK 465 7 THR B 7
REMARK 465 7 SER B 8
REMARK 465 7 GLU B 9
REMARK 465 7 GLY B 10
REMARK 465 7 VAL B 11
REMARK 465 7 ASP B 12
REMARK 465 7 GLU B 13
REMARK 465 7 SER B 14
REMARK 465 7 GLU B 15
REMARK 465 7 LYS B 16
REMARK 465 7 LYS B 17
REMARK 465 7 ASN B 18
REMARK 465 7 SER B 19
REMARK 465 7 GLY B 20
REMARK 465 7 ALA B 21
REMARK 465 7 LEU B 22
REMARK 465 7 GLU B 23
REMARK 465 7 LYS B 24
REMARK 465 7 GLU B 25
REMARK 465 7 ASN B 26
REMARK 465 7 GLN B 27
REMARK 465 7 MET B 28
REMARK 465 7 ARG B 29
REMARK 465 7 LEU B 249
REMARK 465 7 GLU B 250
REMARK 465 7 ASP B 251
REMARK 465 7 GLY B 252
REMARK 465 7 PHE B 253
REMARK 465 7 PRO B 254
REMARK 465 7 VAL B 255
REMARK 465 7 HIS B 256
REMARK 465 7 ASP B 257
REMARK 465 7 GLY B 258
REMARK 465 7 LYS B 259
REMARK 465 7 GLY B 260
REMARK 465 7 ASP B 261
REMARK 465 7 MET B 262
REMARK 465 7 ARG B 263
REMARK 465 7 LYS B 264
REMARK 465 8 MET A 1
REMARK 465 8 SER A 2
REMARK 465 8 ALA A 3
REMARK 465 8 GLU A 4
REMARK 465 8 VAL A 5
REMARK 465 8 GLU A 6
REMARK 465 8 THR A 7
REMARK 465 8 SER A 8
REMARK 465 8 GLU A 9
REMARK 465 8 GLY A 10
REMARK 465 8 VAL A 11
REMARK 465 8 ASP A 12
REMARK 465 8 GLU A 13
REMARK 465 8 SER A 14
REMARK 465 8 GLU A 15
REMARK 465 8 LYS A 16
REMARK 465 8 LYS A 17
REMARK 465 8 ASN A 18
REMARK 465 8 SER A 19
REMARK 465 8 GLY A 20
REMARK 465 8 ALA A 21
REMARK 465 8 LEU A 22
REMARK 465 8 GLU A 23
REMARK 465 8 LYS A 24
REMARK 465 8 GLU A 25
REMARK 465 8 ASN A 26
REMARK 465 8 GLN A 27
REMARK 465 8 MET A 28
REMARK 465 8 THR A 243
REMARK 465 8 LEU A 244
REMARK 465 8 ALA A 245
REMARK 465 8 ARG A 246
REMARK 465 8 GLU A 247
REMARK 465 8 THR A 248
REMARK 465 8 LEU A 249
REMARK 465 8 GLU A 250
REMARK 465 8 ASP A 251
REMARK 465 8 GLY A 252
REMARK 465 8 PHE A 253
REMARK 465 8 PRO A 254
REMARK 465 8 VAL A 255
REMARK 465 8 HIS A 256
REMARK 465 8 ASP A 257
REMARK 465 8 GLY A 258
REMARK 465 8 LYS A 259
REMARK 465 8 GLY A 260
REMARK 465 8 ASP A 261
REMARK 465 8 MET A 262
REMARK 465 8 ARG A 263
REMARK 465 8 LYS A 264
REMARK 465 8 MET B 1
REMARK 465 8 SER B 2
REMARK 465 8 ALA B 3
REMARK 465 8 GLU B 4
REMARK 465 8 VAL B 5
REMARK 465 8 GLU B 6
REMARK 465 8 THR B 7
REMARK 465 8 SER B 8
REMARK 465 8 GLU B 9
REMARK 465 8 GLY B 10
REMARK 465 8 VAL B 11
REMARK 465 8 ASP B 12
REMARK 465 8 GLU B 13
REMARK 465 8 SER B 14
REMARK 465 8 GLU B 15
REMARK 465 8 LYS B 16
REMARK 465 8 LYS B 17
REMARK 465 8 ASN B 18
REMARK 465 8 SER B 19
REMARK 465 8 GLY B 20
REMARK 465 8 ALA B 21
REMARK 465 8 LEU B 22
REMARK 465 8 GLU B 23
REMARK 465 8 LYS B 24
REMARK 465 8 GLU B 25
REMARK 465 8 ASN B 26
REMARK 465 8 GLN B 27
REMARK 465 8 MET B 28
REMARK 465 8 ARG B 29
REMARK 465 8 LEU B 249
REMARK 465 8 GLU B 250
REMARK 465 8 ASP B 251
REMARK 465 8 GLY B 252
REMARK 465 8 PHE B 253
REMARK 465 8 PRO B 254
REMARK 465 8 VAL B 255
REMARK 465 8 HIS B 256
REMARK 465 8 ASP B 257
REMARK 465 8 GLY B 258
REMARK 465 8 LYS B 259
REMARK 465 8 GLY B 260
REMARK 465 8 ASP B 261
REMARK 465 8 MET B 262
REMARK 465 8 ARG B 263
REMARK 465 8 LYS B 264
REMARK 465 9 MET A 1
REMARK 465 9 SER A 2
REMARK 465 9 ALA A 3
REMARK 465 9 GLU A 4
REMARK 465 9 VAL A 5
REMARK 465 9 GLU A 6
REMARK 465 9 THR A 7
REMARK 465 9 SER A 8
REMARK 465 9 GLU A 9
REMARK 465 9 GLY A 10
REMARK 465 9 VAL A 11
REMARK 465 9 ASP A 12
REMARK 465 9 GLU A 13
REMARK 465 9 SER A 14
REMARK 465 9 GLU A 15
REMARK 465 9 LYS A 16
REMARK 465 9 LYS A 17
REMARK 465 9 ASN A 18
REMARK 465 9 SER A 19
REMARK 465 9 GLY A 20
REMARK 465 9 ALA A 21
REMARK 465 9 LEU A 22
REMARK 465 9 GLU A 23
REMARK 465 9 LYS A 24
REMARK 465 9 GLU A 25
REMARK 465 9 ASN A 26
REMARK 465 9 GLN A 27
REMARK 465 9 MET A 28
REMARK 465 9 THR A 243
REMARK 465 9 LEU A 244
REMARK 465 9 ALA A 245
REMARK 465 9 ARG A 246
REMARK 465 9 GLU A 247
REMARK 465 9 THR A 248
REMARK 465 9 LEU A 249
REMARK 465 9 GLU A 250
REMARK 465 9 ASP A 251
REMARK 465 9 GLY A 252
REMARK 465 9 PHE A 253
REMARK 465 9 PRO A 254
REMARK 465 9 VAL A 255
REMARK 465 9 HIS A 256
REMARK 465 9 ASP A 257
REMARK 465 9 GLY A 258
REMARK 465 9 LYS A 259
REMARK 465 9 GLY A 260
REMARK 465 9 ASP A 261
REMARK 465 9 MET A 262
REMARK 465 9 ARG A 263
REMARK 465 9 LYS A 264
REMARK 465 9 MET B 1
REMARK 465 9 SER B 2
REMARK 465 9 ALA B 3
REMARK 465 9 GLU B 4
REMARK 465 9 VAL B 5
REMARK 465 9 GLU B 6
REMARK 465 9 THR B 7
REMARK 465 9 SER B 8
REMARK 465 9 GLU B 9
REMARK 465 9 GLY B 10
REMARK 465 9 VAL B 11
REMARK 465 9 ASP B 12
REMARK 465 9 GLU B 13
REMARK 465 9 SER B 14
REMARK 465 9 GLU B 15
REMARK 465 9 LYS B 16
REMARK 465 9 LYS B 17
REMARK 465 9 ASN B 18
REMARK 465 9 SER B 19
REMARK 465 9 GLY B 20
REMARK 465 9 ALA B 21
REMARK 465 9 LEU B 22
REMARK 465 9 GLU B 23
REMARK 465 9 LYS B 24
REMARK 465 9 GLU B 25
REMARK 465 9 ASN B 26
REMARK 465 9 GLN B 27
REMARK 465 9 MET B 28
REMARK 465 9 ARG B 29
REMARK 465 9 LEU B 249
REMARK 465 9 GLU B 250
REMARK 465 9 ASP B 251
REMARK 465 9 GLY B 252
REMARK 465 9 PHE B 253
REMARK 465 9 PRO B 254
REMARK 465 9 VAL B 255
REMARK 465 9 HIS B 256
REMARK 465 9 ASP B 257
REMARK 465 9 GLY B 258
REMARK 465 9 LYS B 259
REMARK 465 9 GLY B 260
REMARK 465 9 ASP B 261
REMARK 465 9 MET B 262
REMARK 465 9 ARG B 263
REMARK 465 9 LYS B 264
REMARK 465 10 MET A 1
REMARK 465 10 SER A 2
REMARK 465 10 ALA A 3
REMARK 465 10 GLU A 4
REMARK 465 10 VAL A 5
REMARK 465 10 GLU A 6
REMARK 465 10 THR A 7
REMARK 465 10 SER A 8
REMARK 465 10 GLU A 9
REMARK 465 10 GLY A 10
REMARK 465 10 VAL A 11
REMARK 465 10 ASP A 12
REMARK 465 10 GLU A 13
REMARK 465 10 SER A 14
REMARK 465 10 GLU A 15
REMARK 465 10 LYS A 16
REMARK 465 10 LYS A 17
REMARK 465 10 ASN A 18
REMARK 465 10 SER A 19
REMARK 465 10 GLY A 20
REMARK 465 10 ALA A 21
REMARK 465 10 LEU A 22
REMARK 465 10 GLU A 23
REMARK 465 10 LYS A 24
REMARK 465 10 GLU A 25
REMARK 465 10 ASN A 26
REMARK 465 10 GLN A 27
REMARK 465 10 MET A 28
REMARK 465 10 THR A 243
REMARK 465 10 LEU A 244
REMARK 465 10 ALA A 245
REMARK 465 10 ARG A 246
REMARK 465 10 GLU A 247
REMARK 465 10 THR A 248
REMARK 465 10 LEU A 249
REMARK 465 10 GLU A 250
REMARK 465 10 ASP A 251
REMARK 465 10 GLY A 252
REMARK 465 10 PHE A 253
REMARK 465 10 PRO A 254
REMARK 465 10 VAL A 255
REMARK 465 10 HIS A 256
REMARK 465 10 ASP A 257
REMARK 465 10 GLY A 258
REMARK 465 10 LYS A 259
REMARK 465 10 GLY A 260
REMARK 465 10 ASP A 261
REMARK 465 10 MET A 262
REMARK 465 10 ARG A 263
REMARK 465 10 LYS A 264
REMARK 465 10 MET B 1
REMARK 465 10 SER B 2
REMARK 465 10 ALA B 3
REMARK 465 10 GLU B 4
REMARK 465 10 VAL B 5
REMARK 465 10 GLU B 6
REMARK 465 10 THR B 7
REMARK 465 10 SER B 8
REMARK 465 10 GLU B 9
REMARK 465 10 GLY B 10
REMARK 465 10 VAL B 11
REMARK 465 10 ASP B 12
REMARK 465 10 GLU B 13
REMARK 465 10 SER B 14
REMARK 465 10 GLU B 15
REMARK 465 10 LYS B 16
REMARK 465 10 LYS B 17
REMARK 465 10 ASN B 18
REMARK 465 10 SER B 19
REMARK 465 10 GLY B 20
REMARK 465 10 ALA B 21
REMARK 465 10 LEU B 22
REMARK 465 10 GLU B 23
REMARK 465 10 LYS B 24
REMARK 465 10 GLU B 25
REMARK 465 10 ASN B 26
REMARK 465 10 GLN B 27
REMARK 465 10 MET B 28
REMARK 465 10 ARG B 29
REMARK 465 10 LEU B 249
REMARK 465 10 GLU B 250
REMARK 465 10 ASP B 251
REMARK 465 10 GLY B 252
REMARK 465 10 PHE B 253
REMARK 465 10 PRO B 254
REMARK 465 10 VAL B 255
REMARK 465 10 HIS B 256
REMARK 465 10 ASP B 257
REMARK 465 10 GLY B 258
REMARK 465 10 LYS B 259
REMARK 465 10 GLY B 260
REMARK 465 10 ASP B 261
REMARK 465 10 MET B 262
REMARK 465 10 ARG B 263
REMARK 465 10 LYS B 264
REMARK 465 11 MET A 1
REMARK 465 11 SER A 2
REMARK 465 11 ALA A 3
REMARK 465 11 GLU A 4
REMARK 465 11 VAL A 5
REMARK 465 11 GLU A 6
REMARK 465 11 THR A 7
REMARK 465 11 SER A 8
REMARK 465 11 GLU A 9
REMARK 465 11 GLY A 10
REMARK 465 11 VAL A 11
REMARK 465 11 ASP A 12
REMARK 465 11 GLU A 13
REMARK 465 11 SER A 14
REMARK 465 11 GLU A 15
REMARK 465 11 LYS A 16
REMARK 465 11 LYS A 17
REMARK 465 11 ASN A 18
REMARK 465 11 SER A 19
REMARK 465 11 GLY A 20
REMARK 465 11 ALA A 21
REMARK 465 11 LEU A 22
REMARK 465 11 GLU A 23
REMARK 465 11 LYS A 24
REMARK 465 11 GLU A 25
REMARK 465 11 ASN A 26
REMARK 465 11 GLN A 27
REMARK 465 11 MET A 28
REMARK 465 11 THR A 243
REMARK 465 11 LEU A 244
REMARK 465 11 ALA A 245
REMARK 465 11 ARG A 246
REMARK 465 11 GLU A 247
REMARK 465 11 THR A 248
REMARK 465 11 LEU A 249
REMARK 465 11 GLU A 250
REMARK 465 11 ASP A 251
REMARK 465 11 GLY A 252
REMARK 465 11 PHE A 253
REMARK 465 11 PRO A 254
REMARK 465 11 VAL A 255
REMARK 465 11 HIS A 256
REMARK 465 11 ASP A 257
REMARK 465 11 GLY A 258
REMARK 465 11 LYS A 259
REMARK 465 11 GLY A 260
REMARK 465 11 ASP A 261
REMARK 465 11 MET A 262
REMARK 465 11 ARG A 263
REMARK 465 11 LYS A 264
REMARK 465 11 MET B 1
REMARK 465 11 SER B 2
REMARK 465 11 ALA B 3
REMARK 465 11 GLU B 4
REMARK 465 11 VAL B 5
REMARK 465 11 GLU B 6
REMARK 465 11 THR B 7
REMARK 465 11 SER B 8
REMARK 465 11 GLU B 9
REMARK 465 11 GLY B 10
REMARK 465 11 VAL B 11
REMARK 465 11 ASP B 12
REMARK 465 11 GLU B 13
REMARK 465 11 SER B 14
REMARK 465 11 GLU B 15
REMARK 465 11 LYS B 16
REMARK 465 11 LYS B 17
REMARK 465 11 ASN B 18
REMARK 465 11 SER B 19
REMARK 465 11 GLY B 20
REMARK 465 11 ALA B 21
REMARK 465 11 LEU B 22
REMARK 465 11 GLU B 23
REMARK 465 11 LYS B 24
REMARK 465 11 GLU B 25
REMARK 465 11 ASN B 26
REMARK 465 11 GLN B 27
REMARK 465 11 MET B 28
REMARK 465 11 ARG B 29
REMARK 465 11 LEU B 249
REMARK 465 11 GLU B 250
REMARK 465 11 ASP B 251
REMARK 465 11 GLY B 252
REMARK 465 11 PHE B 253
REMARK 465 11 PRO B 254
REMARK 465 11 VAL B 255
REMARK 465 11 HIS B 256
REMARK 465 11 ASP B 257
REMARK 465 11 GLY B 258
REMARK 465 11 LYS B 259
REMARK 465 11 GLY B 260
REMARK 465 11 ASP B 261
REMARK 465 11 MET B 262
REMARK 465 11 ARG B 263
REMARK 465 11 LYS B 264
REMARK 465 12 MET A 1
REMARK 465 12 SER A 2
REMARK 465 12 ALA A 3
REMARK 465 12 GLU A 4
REMARK 465 12 VAL A 5
REMARK 465 12 GLU A 6
REMARK 465 12 THR A 7
REMARK 465 12 SER A 8
REMARK 465 12 GLU A 9
REMARK 465 12 GLY A 10
REMARK 465 12 VAL A 11
REMARK 465 12 ASP A 12
REMARK 465 12 GLU A 13
REMARK 465 12 SER A 14
REMARK 465 12 GLU A 15
REMARK 465 12 LYS A 16
REMARK 465 12 LYS A 17
REMARK 465 12 ASN A 18
REMARK 465 12 SER A 19
REMARK 465 12 GLY A 20
REMARK 465 12 ALA A 21
REMARK 465 12 LEU A 22
REMARK 465 12 GLU A 23
REMARK 465 12 LYS A 24
REMARK 465 12 GLU A 25
REMARK 465 12 ASN A 26
REMARK 465 12 GLN A 27
REMARK 465 12 MET A 28
REMARK 465 12 THR A 243
REMARK 465 12 LEU A 244
REMARK 465 12 ALA A 245
REMARK 465 12 ARG A 246
REMARK 465 12 GLU A 247
REMARK 465 12 THR A 248
REMARK 465 12 LEU A 249
REMARK 465 12 GLU A 250
REMARK 465 12 ASP A 251
REMARK 465 12 GLY A 252
REMARK 465 12 PHE A 253
REMARK 465 12 PRO A 254
REMARK 465 12 VAL A 255
REMARK 465 12 HIS A 256
REMARK 465 12 ASP A 257
REMARK 465 12 GLY A 258
REMARK 465 12 LYS A 259
REMARK 465 12 GLY A 260
REMARK 465 12 ASP A 261
REMARK 465 12 MET A 262
REMARK 465 12 ARG A 263
REMARK 465 12 LYS A 264
REMARK 465 12 MET B 1
REMARK 465 12 SER B 2
REMARK 465 12 ALA B 3
REMARK 465 12 GLU B 4
REMARK 465 12 VAL B 5
REMARK 465 12 GLU B 6
REMARK 465 12 THR B 7
REMARK 465 12 SER B 8
REMARK 465 12 GLU B 9
REMARK 465 12 GLY B 10
REMARK 465 12 VAL B 11
REMARK 465 12 ASP B 12
REMARK 465 12 GLU B 13
REMARK 465 12 SER B 14
REMARK 465 12 GLU B 15
REMARK 465 12 LYS B 16
REMARK 465 12 LYS B 17
REMARK 465 12 ASN B 18
REMARK 465 12 SER B 19
REMARK 465 12 GLY B 20
REMARK 465 12 ALA B 21
REMARK 465 12 LEU B 22
REMARK 465 12 GLU B 23
REMARK 465 12 LYS B 24
REMARK 465 12 GLU B 25
REMARK 465 12 ASN B 26
REMARK 465 12 GLN B 27
REMARK 465 12 MET B 28
REMARK 465 12 ARG B 29
REMARK 465 12 LEU B 249
REMARK 465 12 GLU B 250
REMARK 465 12 ASP B 251
REMARK 465 12 GLY B 252
REMARK 465 12 PHE B 253
REMARK 465 12 PRO B 254
REMARK 465 12 VAL B 255
REMARK 465 12 HIS B 256
REMARK 465 12 ASP B 257
REMARK 465 12 GLY B 258
REMARK 465 12 LYS B 259
REMARK 465 12 GLY B 260
REMARK 465 12 ASP B 261
REMARK 465 12 MET B 262
REMARK 465 12 ARG B 263
REMARK 465 12 LYS B 264
REMARK 465 13 MET A 1
REMARK 465 13 SER A 2
REMARK 465 13 ALA A 3
REMARK 465 13 GLU A 4
REMARK 465 13 VAL A 5
REMARK 465 13 GLU A 6
REMARK 465 13 THR A 7
REMARK 465 13 SER A 8
REMARK 465 13 GLU A 9
REMARK 465 13 GLY A 10
REMARK 465 13 VAL A 11
REMARK 465 13 ASP A 12
REMARK 465 13 GLU A 13
REMARK 465 13 SER A 14
REMARK 465 13 GLU A 15
REMARK 465 13 LYS A 16
REMARK 465 13 LYS A 17
REMARK 465 13 ASN A 18
REMARK 465 13 SER A 19
REMARK 465 13 GLY A 20
REMARK 465 13 ALA A 21
REMARK 465 13 LEU A 22
REMARK 465 13 GLU A 23
REMARK 465 13 LYS A 24
REMARK 465 13 GLU A 25
REMARK 465 13 ASN A 26
REMARK 465 13 GLN A 27
REMARK 465 13 MET A 28
REMARK 465 13 THR A 243
REMARK 465 13 LEU A 244
REMARK 465 13 ALA A 245
REMARK 465 13 ARG A 246
REMARK 465 13 GLU A 247
REMARK 465 13 THR A 248
REMARK 465 13 LEU A 249
REMARK 465 13 GLU A 250
REMARK 465 13 ASP A 251
REMARK 465 13 GLY A 252
REMARK 465 13 PHE A 253
REMARK 465 13 PRO A 254
REMARK 465 13 VAL A 255
REMARK 465 13 HIS A 256
REMARK 465 13 ASP A 257
REMARK 465 13 GLY A 258
REMARK 465 13 LYS A 259
REMARK 465 13 GLY A 260
REMARK 465 13 ASP A 261
REMARK 465 13 MET A 262
REMARK 465 13 ARG A 263
REMARK 465 13 LYS A 264
REMARK 465 13 MET B 1
REMARK 465 13 SER B 2
REMARK 465 13 ALA B 3
REMARK 465 13 GLU B 4
REMARK 465 13 VAL B 5
REMARK 465 13 GLU B 6
REMARK 465 13 THR B 7
REMARK 465 13 SER B 8
REMARK 465 13 GLU B 9
REMARK 465 13 GLY B 10
REMARK 465 13 VAL B 11
REMARK 465 13 ASP B 12
REMARK 465 13 GLU B 13
REMARK 465 13 SER B 14
REMARK 465 13 GLU B 15
REMARK 465 13 LYS B 16
REMARK 465 13 LYS B 17
REMARK 465 13 ASN B 18
REMARK 465 13 SER B 19
REMARK 465 13 GLY B 20
REMARK 465 13 ALA B 21
REMARK 465 13 LEU B 22
REMARK 465 13 GLU B 23
REMARK 465 13 LYS B 24
REMARK 465 13 GLU B 25
REMARK 465 13 ASN B 26
REMARK 465 13 GLN B 27
REMARK 465 13 MET B 28
REMARK 465 13 ARG B 29
REMARK 465 13 LEU B 249
REMARK 465 13 GLU B 250
REMARK 465 13 ASP B 251
REMARK 465 13 GLY B 252
REMARK 465 13 PHE B 253
REMARK 465 13 PRO B 254
REMARK 465 13 VAL B 255
REMARK 465 13 HIS B 256
REMARK 465 13 ASP B 257
REMARK 465 13 GLY B 258
REMARK 465 13 LYS B 259
REMARK 465 13 GLY B 260
REMARK 465 13 ASP B 261
REMARK 465 13 MET B 262
REMARK 465 13 ARG B 263
REMARK 465 13 LYS B 264
REMARK 465 14 MET A 1
REMARK 465 14 SER A 2
REMARK 465 14 ALA A 3
REMARK 465 14 GLU A 4
REMARK 465 14 VAL A 5
REMARK 465 14 GLU A 6
REMARK 465 14 THR A 7
REMARK 465 14 SER A 8
REMARK 465 14 GLU A 9
REMARK 465 14 GLY A 10
REMARK 465 14 VAL A 11
REMARK 465 14 ASP A 12
REMARK 465 14 GLU A 13
REMARK 465 14 SER A 14
REMARK 465 14 GLU A 15
REMARK 465 14 LYS A 16
REMARK 465 14 LYS A 17
REMARK 465 14 ASN A 18
REMARK 465 14 SER A 19
REMARK 465 14 GLY A 20
REMARK 465 14 ALA A 21
REMARK 465 14 LEU A 22
REMARK 465 14 GLU A 23
REMARK 465 14 LYS A 24
REMARK 465 14 GLU A 25
REMARK 465 14 ASN A 26
REMARK 465 14 GLN A 27
REMARK 465 14 MET A 28
REMARK 465 14 THR A 243
REMARK 465 14 LEU A 244
REMARK 465 14 ALA A 245
REMARK 465 14 ARG A 246
REMARK 465 14 GLU A 247
REMARK 465 14 THR A 248
REMARK 465 14 LEU A 249
REMARK 465 14 GLU A 250
REMARK 465 14 ASP A 251
REMARK 465 14 GLY A 252
REMARK 465 14 PHE A 253
REMARK 465 14 PRO A 254
REMARK 465 14 VAL A 255
REMARK 465 14 HIS A 256
REMARK 465 14 ASP A 257
REMARK 465 14 GLY A 258
REMARK 465 14 LYS A 259
REMARK 465 14 GLY A 260
REMARK 465 14 ASP A 261
REMARK 465 14 MET A 262
REMARK 465 14 ARG A 263
REMARK 465 14 LYS A 264
REMARK 465 14 MET B 1
REMARK 465 14 SER B 2
REMARK 465 14 ALA B 3
REMARK 465 14 GLU B 4
REMARK 465 14 VAL B 5
REMARK 465 14 GLU B 6
REMARK 465 14 THR B 7
REMARK 465 14 SER B 8
REMARK 465 14 GLU B 9
REMARK 465 14 GLY B 10
REMARK 465 14 VAL B 11
REMARK 465 14 ASP B 12
REMARK 465 14 GLU B 13
REMARK 465 14 SER B 14
REMARK 465 14 GLU B 15
REMARK 465 14 LYS B 16
REMARK 465 14 LYS B 17
REMARK 465 14 ASN B 18
REMARK 465 14 SER B 19
REMARK 465 14 GLY B 20
REMARK 465 14 ALA B 21
REMARK 465 14 LEU B 22
REMARK 465 14 GLU B 23
REMARK 465 14 LYS B 24
REMARK 465 14 GLU B 25
REMARK 465 14 ASN B 26
REMARK 465 14 GLN B 27
REMARK 465 14 MET B 28
REMARK 465 14 ARG B 29
REMARK 465 14 LEU B 249
REMARK 465 14 GLU B 250
REMARK 465 14 ASP B 251
REMARK 465 14 GLY B 252
REMARK 465 14 PHE B 253
REMARK 465 14 PRO B 254
REMARK 465 14 VAL B 255
REMARK 465 14 HIS B 256
REMARK 465 14 ASP B 257
REMARK 465 14 GLY B 258
REMARK 465 14 LYS B 259
REMARK 465 14 GLY B 260
REMARK 465 14 ASP B 261
REMARK 465 14 MET B 262
REMARK 465 14 ARG B 263
REMARK 465 14 LYS B 264
REMARK 465 15 MET A 1
REMARK 465 15 SER A 2
REMARK 465 15 ALA A 3
REMARK 465 15 GLU A 4
REMARK 465 15 VAL A 5
REMARK 465 15 GLU A 6
REMARK 465 15 THR A 7
REMARK 465 15 SER A 8
REMARK 465 15 GLU A 9
REMARK 465 15 GLY A 10
REMARK 465 15 VAL A 11
REMARK 465 15 ASP A 12
REMARK 465 15 GLU A 13
REMARK 465 15 SER A 14
REMARK 465 15 GLU A 15
REMARK 465 15 LYS A 16
REMARK 465 15 LYS A 17
REMARK 465 15 ASN A 18
REMARK 465 15 SER A 19
REMARK 465 15 GLY A 20
REMARK 465 15 ALA A 21
REMARK 465 15 LEU A 22
REMARK 465 15 GLU A 23
REMARK 465 15 LYS A 24
REMARK 465 15 GLU A 25
REMARK 465 15 ASN A 26
REMARK 465 15 GLN A 27
REMARK 465 15 MET A 28
REMARK 465 15 THR A 243
REMARK 465 15 LEU A 244
REMARK 465 15 ALA A 245
REMARK 465 15 ARG A 246
REMARK 465 15 GLU A 247
REMARK 465 15 THR A 248
REMARK 465 15 LEU A 249
REMARK 465 15 GLU A 250
REMARK 465 15 ASP A 251
REMARK 465 15 GLY A 252
REMARK 465 15 PHE A 253
REMARK 465 15 PRO A 254
REMARK 465 15 VAL A 255
REMARK 465 15 HIS A 256
REMARK 465 15 ASP A 257
REMARK 465 15 GLY A 258
REMARK 465 15 LYS A 259
REMARK 465 15 GLY A 260
REMARK 465 15 ASP A 261
REMARK 465 15 MET A 262
REMARK 465 15 ARG A 263
REMARK 465 15 LYS A 264
REMARK 465 15 MET B 1
REMARK 465 15 SER B 2
REMARK 465 15 ALA B 3
REMARK 465 15 GLU B 4
REMARK 465 15 VAL B 5
REMARK 465 15 GLU B 6
REMARK 465 15 THR B 7
REMARK 465 15 SER B 8
REMARK 465 15 GLU B 9
REMARK 465 15 GLY B 10
REMARK 465 15 VAL B 11
REMARK 465 15 ASP B 12
REMARK 465 15 GLU B 13
REMARK 465 15 SER B 14
REMARK 465 15 GLU B 15
REMARK 465 15 LYS B 16
REMARK 465 15 LYS B 17
REMARK 465 15 ASN B 18
REMARK 465 15 SER B 19
REMARK 465 15 GLY B 20
REMARK 465 15 ALA B 21
REMARK 465 15 LEU B 22
REMARK 465 15 GLU B 23
REMARK 465 15 LYS B 24
REMARK 465 15 GLU B 25
REMARK 465 15 ASN B 26
REMARK 465 15 GLN B 27
REMARK 465 15 MET B 28
REMARK 465 15 ARG B 29
REMARK 465 15 LEU B 249
REMARK 465 15 GLU B 250
REMARK 465 15 ASP B 251
REMARK 465 15 GLY B 252
REMARK 465 15 PHE B 253
REMARK 465 15 PRO B 254
REMARK 465 15 VAL B 255
REMARK 465 15 HIS B 256
REMARK 465 15 ASP B 257
REMARK 465 15 GLY B 258
REMARK 465 15 LYS B 259
REMARK 465 15 GLY B 260
REMARK 465 15 ASP B 261
REMARK 465 15 MET B 262
REMARK 465 15 ARG B 263
REMARK 465 15 LYS B 264
REMARK 465 16 MET A 1
REMARK 465 16 SER A 2
REMARK 465 16 ALA A 3
REMARK 465 16 GLU A 4
REMARK 465 16 VAL A 5
REMARK 465 16 GLU A 6
REMARK 465 16 THR A 7
REMARK 465 16 SER A 8
REMARK 465 16 GLU A 9
REMARK 465 16 GLY A 10
REMARK 465 16 VAL A 11
REMARK 465 16 ASP A 12
REMARK 465 16 GLU A 13
REMARK 465 16 SER A 14
REMARK 465 16 GLU A 15
REMARK 465 16 LYS A 16
REMARK 465 16 LYS A 17
REMARK 465 16 ASN A 18
REMARK 465 16 SER A 19
REMARK 465 16 GLY A 20
REMARK 465 16 ALA A 21
REMARK 465 16 LEU A 22
REMARK 465 16 GLU A 23
REMARK 465 16 LYS A 24
REMARK 465 16 GLU A 25
REMARK 465 16 ASN A 26
REMARK 465 16 GLN A 27
REMARK 465 16 MET A 28
REMARK 465 16 THR A 243
REMARK 465 16 LEU A 244
REMARK 465 16 ALA A 245
REMARK 465 16 ARG A 246
REMARK 465 16 GLU A 247
REMARK 465 16 THR A 248
REMARK 465 16 LEU A 249
REMARK 465 16 GLU A 250
REMARK 465 16 ASP A 251
REMARK 465 16 GLY A 252
REMARK 465 16 PHE A 253
REMARK 465 16 PRO A 254
REMARK 465 16 VAL A 255
REMARK 465 16 HIS A 256
REMARK 465 16 ASP A 257
REMARK 465 16 GLY A 258
REMARK 465 16 LYS A 259
REMARK 465 16 GLY A 260
REMARK 465 16 ASP A 261
REMARK 465 16 MET A 262
REMARK 465 16 ARG A 263
REMARK 465 16 LYS A 264
REMARK 465 16 MET B 1
REMARK 465 16 SER B 2
REMARK 465 16 ALA B 3
REMARK 465 16 GLU B 4
REMARK 465 16 VAL B 5
REMARK 465 16 GLU B 6
REMARK 465 16 THR B 7
REMARK 465 16 SER B 8
REMARK 465 16 GLU B 9
REMARK 465 16 GLY B 10
REMARK 465 16 VAL B 11
REMARK 465 16 ASP B 12
REMARK 465 16 GLU B 13
REMARK 465 16 SER B 14
REMARK 465 16 GLU B 15
REMARK 465 16 LYS B 16
REMARK 465 16 LYS B 17
REMARK 465 16 ASN B 18
REMARK 465 16 SER B 19
REMARK 465 16 GLY B 20
REMARK 465 16 ALA B 21
REMARK 465 16 LEU B 22
REMARK 465 16 GLU B 23
REMARK 465 16 LYS B 24
REMARK 465 16 GLU B 25
REMARK 465 16 ASN B 26
REMARK 465 16 GLN B 27
REMARK 465 16 MET B 28
REMARK 465 16 ARG B 29
REMARK 465 16 LEU B 249
REMARK 465 16 GLU B 250
REMARK 465 16 ASP B 251
REMARK 465 16 GLY B 252
REMARK 465 16 PHE B 253
REMARK 465 16 PRO B 254
REMARK 465 16 VAL B 255
REMARK 465 16 HIS B 256
REMARK 465 16 ASP B 257
REMARK 465 16 GLY B 258
REMARK 465 16 LYS B 259
REMARK 465 16 GLY B 260
REMARK 465 16 ASP B 261
REMARK 465 16 MET B 262
REMARK 465 16 ARG B 263
REMARK 465 16 LYS B 264
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 13 PRO A 128 C - N - CA ANGL. DEV. = 9.1 DEGREES
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 1 MET A 30 22.05 -76.95
REMARK 500 1 LYS A 63 -167.72 -79.69
REMARK 500 1 TYR A 75 -70.82 -45.54
REMARK 500 1 PHE A 76 -79.02 -37.87
REMARK 500 1 LYS A 89 -19.29 -46.28
REMARK 500 1 PHE A 94 -19.72 -150.01
REMARK 500 1 PHE A 99 46.51 -155.46
REMARK 500 1 HIS A 104 130.22 -23.07
REMARK 500 1 TRP A 121 -47.76 -28.39
REMARK 500 1 GLU A 123 30.34 -75.33
REMARK 500 1 GLN A 124 -34.14 -138.67
REMARK 500 1 VAL A 125 153.43 -35.48
REMARK 500 1 GLN A 126 112.77 -169.14
REMARK 500 1 LYS A 129 -38.81 -37.49
REMARK 500 1 GLN A 143 5.50 -158.78
REMARK 500 1 PRO A 146 -29.34 -38.37
REMARK 500 1 GLN A 185 -2.85 -58.81
REMARK 500 1 ASN A 194 84.05 -158.36
REMARK 500 1 GLN A 196 -79.22 -38.21
REMARK 500 1 LYS B 42 -66.51 -24.29
REMARK 500 1 GLN B 52 -52.42 -19.33
REMARK 500 1 LYS B 59 -87.48 -88.50
REMARK 500 1 LYS B 64 -57.07 -12.36
REMARK 500 1 LYS B 106 -73.74 -49.45
REMARK 500 1 PHE B 116 -71.54 -80.35
REMARK 500 1 ASN B 120 30.82 -75.07
REMARK 500 1 GLU B 136 -36.61 -39.07
REMARK 500 1 ARG B 156 -64.77 -96.79
REMARK 500 1 LYS B 168 -76.12 -51.28
REMARK 500 1 GLU B 182 127.54 -39.80
REMARK 500 1 GLN B 185 2.71 -61.57
REMARK 500 1 GLU B 190 24.34 -68.79
REMARK 500 1 ASP B 193 -93.62 -67.96
REMARK 500 1 ASN B 212 -166.26 -79.57
REMARK 500 1 PHE B 234 -73.41 -61.68
REMARK 500 1 ARG B 246 -14.72 -49.60
REMARK 500 2 MET A 30 -72.79 -65.78
REMARK 500 2 LYS A 63 -168.40 -112.57
REMARK 500 2 LYS A 64 -86.54 -36.20
REMARK 500 2 ALA A 93 31.78 -98.30
REMARK 500 2 PHE A 94 -21.21 -173.58
REMARK 500 2 ASN A 144 -13.50 -151.56
REMARK 500 2 GLU A 145 56.07 -153.44
REMARK 500 2 TYR A 154 -79.59 -56.07
REMARK 500 2 THR A 155 -32.70 -31.59
REMARK 500 2 ARG A 156 -92.06 -87.18
REMARK 500 2 LEU A 161 28.88 -72.58
REMARK 500 2 SER A 162 -36.61 -143.53
REMARK 500 2 GLN A 185 -3.03 -58.96
REMARK 500 2 ASN A 194 74.49 -169.50
REMARK 500
REMARK 500 THIS ENTRY HAS 562 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 300 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 45 NE2
REMARK 620 2 HEM A 300 NA 95.7
REMARK 620 3 HEM A 300 NB 95.2 89.4
REMARK 620 4 HEM A 300 NC 87.3 177.0 90.3
REMARK 620 5 HEM A 300 ND 88.8 90.5 176.0 89.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 265 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 45 NE2
REMARK 620 2 HEM B 265 NA 95.0
REMARK 620 3 HEM B 265 NB 97.2 89.3
REMARK 620 4 HEM B 265 NC 92.0 173.0 89.8
REMARK 620 5 HEM B 265 ND 93.6 89.7 169.2 89.9
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 HEM A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.91265 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2QPP RELATED DB: PDB
REMARK 900 ORIGINAL REFINEMENT BASED ON SAME DATA AND R-FREE SET.
REMARK 900 RELATED ID: 2Q32 RELATED DB: PDB
REMARK 900 HUMAN HEME OXYGENASE-2 C127A (HO-2) WITHOUT BOUND HEME.
DBREF 2RGZ A 1 264 UNP P30519 HMOX2_HUMAN 1 264
DBREF 2RGZ B 1 264 UNP P30519 HMOX2_HUMAN 1 264
SEQADV 2RGZ ALA A 127 UNP P30519 CYS 127 ENGINEERED MUTATION
SEQADV 2RGZ ALA B 127 UNP P30519 CYS 127 ENGINEERED MUTATION
SEQRES 1 A 264 MET SER ALA GLU VAL GLU THR SER GLU GLY VAL ASP GLU
SEQRES 2 A 264 SER GLU LYS LYS ASN SER GLY ALA LEU GLU LYS GLU ASN
SEQRES 3 A 264 GLN MET ARG MET ALA ASP LEU SER GLU LEU LEU LYS GLU
SEQRES 4 A 264 GLY THR LYS GLU ALA HIS ASP ARG ALA GLU ASN THR GLN
SEQRES 5 A 264 PHE VAL LYS ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU
SEQRES 6 A 264 LEU PHE LYS LEU ALA THR THR ALA LEU TYR PHE THR TYR
SEQRES 7 A 264 SER ALA LEU GLU GLU GLU MET GLU ARG ASN LYS ASP HIS
SEQRES 8 A 264 PRO ALA PHE ALA PRO LEU TYR PHE PRO MET GLU LEU HIS
SEQRES 9 A 264 ARG LYS GLU ALA LEU THR LYS ASP MET GLU TYR PHE PHE
SEQRES 10 A 264 GLY GLU ASN TRP GLU GLU GLN VAL GLN ALA PRO LYS ALA
SEQRES 11 A 264 ALA GLN LYS TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN
SEQRES 12 A 264 ASN GLU PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG
SEQRES 13 A 264 TYR MET GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS
SEQRES 14 A 264 VAL ALA GLN ARG ALA LEU LYS LEU PRO SER THR GLY GLU
SEQRES 15 A 264 GLY THR GLN PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA
SEQRES 16 A 264 GLN GLN PHE LYS GLN LEU TYR ARG ALA ARG MET ASN ALA
SEQRES 17 A 264 LEU ASP LEU ASN MET LYS THR LYS GLU ARG ILE VAL GLU
SEQRES 18 A 264 GLU ALA ASN LYS ALA PHE GLU TYR ASN MET GLN ILE PHE
SEQRES 19 A 264 ASN GLU LEU ASP GLN ALA GLY SER THR LEU ALA ARG GLU
SEQRES 20 A 264 THR LEU GLU ASP GLY PHE PRO VAL HIS ASP GLY LYS GLY
SEQRES 21 A 264 ASP MET ARG LYS
SEQRES 1 B 264 MET SER ALA GLU VAL GLU THR SER GLU GLY VAL ASP GLU
SEQRES 2 B 264 SER GLU LYS LYS ASN SER GLY ALA LEU GLU LYS GLU ASN
SEQRES 3 B 264 GLN MET ARG MET ALA ASP LEU SER GLU LEU LEU LYS GLU
SEQRES 4 B 264 GLY THR LYS GLU ALA HIS ASP ARG ALA GLU ASN THR GLN
SEQRES 5 B 264 PHE VAL LYS ASP PHE LEU LYS GLY ASN ILE LYS LYS GLU
SEQRES 6 B 264 LEU PHE LYS LEU ALA THR THR ALA LEU TYR PHE THR TYR
SEQRES 7 B 264 SER ALA LEU GLU GLU GLU MET GLU ARG ASN LYS ASP HIS
SEQRES 8 B 264 PRO ALA PHE ALA PRO LEU TYR PHE PRO MET GLU LEU HIS
SEQRES 9 B 264 ARG LYS GLU ALA LEU THR LYS ASP MET GLU TYR PHE PHE
SEQRES 10 B 264 GLY GLU ASN TRP GLU GLU GLN VAL GLN ALA PRO LYS ALA
SEQRES 11 B 264 ALA GLN LYS TYR VAL GLU ARG ILE HIS TYR ILE GLY GLN
SEQRES 12 B 264 ASN GLU PRO GLU LEU LEU VAL ALA HIS ALA TYR THR ARG
SEQRES 13 B 264 TYR MET GLY ASP LEU SER GLY GLY GLN VAL LEU LYS LYS
SEQRES 14 B 264 VAL ALA GLN ARG ALA LEU LYS LEU PRO SER THR GLY GLU
SEQRES 15 B 264 GLY THR GLN PHE TYR LEU PHE GLU ASN VAL ASP ASN ALA
SEQRES 16 B 264 GLN GLN PHE LYS GLN LEU TYR ARG ALA ARG MET ASN ALA
SEQRES 17 B 264 LEU ASP LEU ASN MET LYS THR LYS GLU ARG ILE VAL GLU
SEQRES 18 B 264 GLU ALA ASN LYS ALA PHE GLU TYR ASN MET GLN ILE PHE
SEQRES 19 B 264 ASN GLU LEU ASP GLN ALA GLY SER THR LEU ALA ARG GLU
SEQRES 20 B 264 THR LEU GLU ASP GLY PHE PRO VAL HIS ASP GLY LYS GLY
SEQRES 21 B 264 ASP MET ARG LYS
HET HEM A 300 43
HET HEM B 265 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *83(H2 O)
HELIX 1 1 ASP A 32 THR A 41 1 10
HELIX 2 2 THR A 41 THR A 51 1 11
HELIX 3 3 THR A 51 LYS A 59 1 9
HELIX 4 4 LYS A 64 ASN A 88 1 25
HELIX 5 5 PHE A 94 TYR A 98 5 5
HELIX 6 6 ARG A 105 PHE A 117 1 13
HELIX 7 7 GLY A 118 GLN A 124 5 7
HELIX 8 8 PRO A 128 ILE A 141 1 14
HELIX 9 9 GLU A 145 LEU A 148 5 4
HELIX 10 10 LEU A 149 LEU A 175 1 27
HELIX 11 11 ASN A 194 LEU A 209 1 16
HELIX 12 12 ASN A 212 ALA A 240 1 29
HELIX 13 13 ASP B 32 THR B 41 1 10
HELIX 14 14 THR B 41 ARG B 47 1 7
HELIX 15 15 THR B 51 LYS B 59 1 9
HELIX 16 16 LYS B 63 ASN B 88 1 26
HELIX 17 17 PHE B 94 TYR B 98 5 5
HELIX 18 18 PHE B 99 HIS B 104 1 6
HELIX 19 19 ARG B 105 GLY B 118 1 14
HELIX 20 20 GLU B 119 GLN B 124 5 6
HELIX 21 21 PRO B 128 GLU B 145 1 18
HELIX 22 22 LEU B 148 LEU B 161 1 14
HELIX 23 23 GLY B 163 LEU B 175 1 13
HELIX 24 24 THR B 184 LEU B 188 5 5
HELIX 25 25 ASN B 194 ALA B 208 1 15
HELIX 26 26 MET B 213 THR B 243 1 31
LINK NE2 HIS A 45 FE HEM A 300 1555 1555 2.09
LINK NE2 HIS B 45 FE HEM B 265 1555 1555 2.13
SITE 1 AC1 16 HIS A 45 ALA A 48 GLU A 49 VAL A 54
SITE 2 AC1 16 LEU A 58 TYR A 154 THR A 155 ARG A 156
SITE 3 AC1 16 GLY A 159 SER A 162 LYS A 199 ARG A 203
SITE 4 AC1 16 PHE A 227 ASN A 230 PHE A 234 HOH A 319
SITE 1 AC2 12 HIS B 45 VAL B 54 LEU B 58 TYR B 154
SITE 2 AC2 12 THR B 155 ARG B 156 MET B 158 GLY B 159
SITE 3 AC2 12 SER B 162 ARG B 203 PHE B 227 PHE B 234
CRYST1 74.977 85.094 97.846 90.00 90.00 90.00 P 21 21 21 8
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 0.013337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010220 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
