***  HYDROLASE 14-JUN-24 8ZXG  ***
Job options:
ID = 24071808113545719
JOBID = HYDROLASE 14-JUN-24 8ZXG
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER HYDROLASE 14-JUN-24 8ZXG
TITLE CRYSTAL STRUCTURE OF PARAOXONASE FROM BACILLUS SP. STRAIN S3WAHI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARAOXONASE FROM BACILLUS SP. STRAIN S3WAHI;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP. (IN: FIRMICUTES);
SOURCE 3 ORGANISM_TAXID: 1409;
SOURCE 4 STRAIN: S3WAHI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS STRUCTURAL PROTEIN, HYDROLASE, METALLO-B-LACTAMASES, ENZYME
KEYWDS 2 PROMISCUITY, FUNCTION, METALLOHYDROLASE, PARAOXONASE,
KEYWDS 3 OGRANOPHOSPHATE-DEGRADING ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.AZMAN,N.D.MUHD NOOR,A.T.C.LEOW,S.A.MOHD NOOR,M.S.MOHAMAD ALI
JRNL AUTH A.A.AZMAN,N.D.MUHD NOOR,A.T.C.LEOW,S.A.MOHD NOOR,
JRNL AUTH 2 M.S.MOHAMAD ALI
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF PARAOXONASE FROM BACILLUS SP.
JRNL TITL 2 STRAIN S3WAHI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 67871
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4903
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2365
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 107
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66400
REMARK 3 B22 (A**2) : 0.66400
REMARK 3 B33 (A**2) : -1.32700
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.235
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2552 ; 0.024 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2429 ; 0.004 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3473 ; 1.997 ; 1.834
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5591 ; 0.759 ; 1.733
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 7.072 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 14 ;14.577 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 402 ;16.335 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2932 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 551 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 552 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 563 ; 0.728 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1230 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 84 ; 0.132 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 1.038 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1259 ;13.247 ; 3.510
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1259 ;13.235 ; 3.510
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1577 ;17.810 ; 6.329
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1578 ;17.809 ; 6.331
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1293 ;13.881 ; 3.841
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1288 ;13.835 ; 3.846
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1884 ;18.435 ; 6.920
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1879 ;18.426 ; 6.920
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4981 ; 5.735 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8ZXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-24
REMARK 200 TEMPERATURE (KELVIN) : 293.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.3
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67871
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.494
REMARK 200 RESOLUTION RANGE LOW (A) : 39.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 13.60
REMARK 200 R MERGE FOR SHELL (I) : 1.87100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: ALPHAFOLD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5 1.6 M
REMARK 280 MAGENSIUM SULFATE HEPTAHYDRATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 67.63300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.91150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.91150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.81650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.91150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.91150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 101.44950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.91150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.91150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.81650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.91150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.91150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 101.44950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.63300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -517.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 468 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 559 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 310
REMARK 465 TRP A 311
REMARK 465 ILE A 312
REMARK 465 TYR A 313
REMARK 465 TYR A 314
REMARK 465 ALA A 315
REMARK 465 LYS A 316
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 26 CG CD OE1 OE2
REMARK 470 LYS A 54 CE NZ
REMARK 470 ARG A 80 CD NE CZ NH1 NH2
REMARK 470 GLN A 98 CD OE1 NE2
REMARK 470 ILE A 100 CD1
REMARK 470 LYS A 101 CE NZ
REMARK 470 GLN A 105 CD OE1 NE2
REMARK 470 LEU A 108 CD2
REMARK 470 GLN A 113 CG CD OE1 NE2
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 173 CG CD OE1 OE2
REMARK 470 ILE A 188 CG1 CG2 CD1
REMARK 470 ILE A 202 CD1
REMARK 470 LEU A 209 CG CD1 CD2
REMARK 470 GLN A 246 CG CD OE1 NE2
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 GLN A 262 CG CD OE1 NE2
REMARK 470 LYS A 272 NZ
REMARK 470 GLU A 279 CB CG CD OE1 OE2
REMARK 470 LYS A 280 CG CD CE NZ
REMARK 470 ILE A 286 CD1
REMARK 470 SER A 287 CB OG
REMARK 470 LEU A 293 CG CD1 CD2
REMARK 470 TYR A 298 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 298 OH
REMARK 470 GLN A 301 CG CD OE1 NE2
REMARK 470 MET A 303 CG SD CE
REMARK 470 ILE A 304 CG1 CG2 CD1
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 O2 SO4 A 468 O3 SO4 A 468 7555 0.40
REMARK 500 O1 SO4 A 468 O4 SO4 A 468 7555 0.60
REMARK 500 C LEU A 42 CA LEU A 127 7555 0.74
REMARK 500 CA ALA A 43 CG LEU A 127 7555 0.79
REMARK 500 O LEU A 42 N LEU A 127 7555 0.82
REMARK 500 CB LEU A 42 N THR A 128 7555 0.93
REMARK 500 CB LEU A 42 C LEU A 127 7555 1.04
REMARK 500 N ALA A 43 CA LEU A 127 7555 1.10
REMARK 500 CG LEU A 42 CA THR A 128 7555 1.12
REMARK 500 CB ALA A 43 CG LEU A 127 7555 1.18
REMARK 500 CA ALA A 43 CB LEU A 127 7555 1.35
REMARK 500 N ALA A 43 CB LEU A 127 7555 1.36
REMARK 500 CA LEU A 42 C LEU A 127 7555 1.39
REMARK 500 O ALA A 43 CD1 LEU A 127 7555 1.39
REMARK 500 CD1 LEU A 42 CB THR A 128 7555 1.43
REMARK 500 CD1 LEU A 42 CA THR A 128 7555 1.44
REMARK 500 S SO4 A 468 O1 SO4 A 468 7555 1.44
REMARK 500 C LEU A 42 N LEU A 127 7555 1.45
REMARK 500 S SO4 A 468 O4 SO4 A 468 7555 1.45
REMARK 500 S SO4 A 468 O3 SO4 A 468 7555 1.47
REMARK 500 S SO4 A 468 O2 SO4 A 468 7555 1.51
REMARK 500 CB ALA A 43 CD2 LEU A 127 7555 1.55
REMARK 500 CB LEU A 42 O LEU A 127 7555 1.58
REMARK 500 O LEU A 42 CA LEU A 127 7555 1.60
REMARK 500 O LEU A 126 O HOH A 567 7555 1.62
REMARK 500 CB LEU A 42 CA THR A 128 7555 1.67
REMARK 500 O HOH A 513 O HOH A 579 4444 1.71
REMARK 500 C ALA A 43 CD1 LEU A 127 7555 1.73
REMARK 500 C LEU A 42 C LEU A 127 7555 1.78
REMARK 500 CD1 LEU A 42 OG1 THR A 128 7555 1.79
REMARK 500 CA ALA A 43 CD1 LEU A 127 7555 1.83
REMARK 500 CG LEU A 42 N THR A 128 7555 1.86
REMARK 500 CA LEU A 42 N THR A 128 7555 1.87
REMARK 500 C ALA A 43 CG LEU A 127 7555 1.90
REMARK 500 CA LEU A 42 CA LEU A 127 7555 1.93
REMARK 500 CD2 LEU A 42 CA THR A 128 7555 1.98
REMARK 500 O4 SO4 A 468 O4 SO4 A 468 7555 1.98
REMARK 500 CA LEU A 42 O LEU A 127 7555 2.01
REMARK 500 CB ALA A 43 CB LEU A 127 7555 2.02
REMARK 500 CD2 LEU A 42 C THR A 128 7555 2.04
REMARK 500 O LEU A 42 C LEU A 126 7555 2.10
REMARK 500 OE2 GLU A 45 CB ALA A 125 7555 2.11
REMARK 500 N LEU A 42 O LEU A 127 7555 2.11
REMARK 500 CD2 LEU A 42 N LYS A 129 7555 2.12
REMARK 500 O1 SO4 A 468 O3 SO4 A 468 7555 2.12
REMARK 500 CA ALA A 43 CA LEU A 127 7555 2.13
REMARK 500 CD2 LEU A 127 O HOH A 563 7555 2.14
REMARK 500 N ALA A 43 CG LEU A 127 7555 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 283 C PRO A 283 O 0.122
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 6 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU A 28 CB - CG - CD2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP A 69 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 126 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 PRO A 283 N - CA - CB ANGL. DEV. = -13.2 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 PRO A 12 37.10 -89.46
REMARK 500 GLU A 16 -42.20 74.26
REMARK 500 ASP A 32 159.83 72.77
REMARK 500 GLN A 123 -109.36 51.24
REMARK 500 ALA A 125 -174.99 -170.40
REMARK 500 LEU A 126 28.59 -155.04
REMARK 500 THR A 128 127.70 -177.91
REMARK 500 LYS A 129 -93.33 -84.48
REMARK 500 THR A 130 144.48 -176.73
REMARK 500 MET A 131 -10.85 68.03
REMARK 500 MET A 131 -10.85 68.03
REMARK 500 LEU A 284 -142.17 54.08
REMARK 500 THR A 285 -59.98 65.19
REMARK 500 ASP A 294 174.84 -54.18
REMARK 500 PHE A 295 -0.47 60.41
REMARK 500 MET A 303 -57.91 155.81
REMARK 500 ASP A 305 -48.13 142.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 125 LEU A 126 -144.33
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 144 0.20 SIDE CHAIN
REMARK 500 ARG A 204 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 579 DISTANCE = 6.52 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 412 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 45 O
REMARK 620 2 TYR A 53 O 114.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 415 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 63 O
REMARK 620 2 THR A 166 O 142.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 466 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 65 NE2
REMARK 620 2 HIS A 67 ND1 88.6
REMARK 620 3 HIS A 163 NE2 99.8 92.4
REMARK 620 4 ASP A 182 OD2 89.1 175.2 92.2
REMARK 620 5 GOL A 402 O3 168.4 103.0 79.3 79.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 467 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 69 OD2
REMARK 620 2 HIS A 70 NE2 87.3
REMARK 620 3 ASP A 182 OD2 168.5 92.8
REMARK 620 4 HIS A 230 NE2 85.9 103.9 105.2
REMARK 620 5 GOL A 402 O3 91.2 173.6 87.5 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 451 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 79 OE1
REMARK 620 2 GLY A 115 O 82.6
REMARK 620 3 THR A 265 OG1 82.3 5.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 421 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 92 O
REMARK 620 2 SER A 134 OG 124.4
REMARK 620 3 CYS A 135 O 125.2 100.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 428 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 113 O
REMARK 620 2 SER A 307 O 100.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 416 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 152 O
REMARK 620 2 PHE A 155 O 82.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 409 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 154 O
REMARK 620 2 TYR A 171 O 81.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 459 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 188 O
REMARK 620 2 SER A 190 OG 120.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 432 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 193 O
REMARK 620 2 GLU A 195 OE2 95.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 443 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 213 O
REMARK 620 2 GLU A 213 OE1 103.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 445 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 218 O
REMARK 620 2 MET A 221 O 90.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 410 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 230 O
REMARK 620 2 GLU A 232 O 110.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 439 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 250 O
REMARK 620 2 ASN A 257 OD1 101.6
REMARK 620 N 1
DBREF 8ZXG A 1 316 PDB 8ZXG 8ZXG 1 316
SEQRES 1 A 316 MET THR VAL ILE HIS ARG MET GLU ILE PRO VAL PRO PHE
SEQRES 2 A 316 ALA VAL GLU THR VAL ASN VAL PHE LEU VAL GLU GLY GLU
SEQRES 3 A 316 THR LEU THR LEU ILE ASP THR GLY THR ASN THR LYS GLU
SEQRES 4 A 316 SER ARG LEU ALA LEU GLU LYS GLN LEU ALA ALA LEU GLY
SEQRES 5 A 316 TYR LYS VAL GLU ASP ILE GLU THR VAL VAL LEU THR HIS
SEQRES 6 A 316 HIS HIS ALA ASP HIS CYS GLY LEU LEU ASP ILE PHE SER
SEQRES 7 A 316 GLU ARG THR ASN ILE VAL GLY HIS PRO TRP ASN GLU PRO
SEQRES 8 A 316 TRP ILE THR GLN ASN PRO GLN PHE ILE LYS ARG TYR GLN
SEQRES 9 A 316 GLN PHE PHE LEU GLU ALA SER VAL GLN PHE GLY VAL PRO
SEQRES 10 A 316 GLU VAL LEU LEU PRO GLN GLY ALA LEU LEU THR LYS THR
SEQRES 11 A 316 MET ILE TYR SER CYS LYS ARG SER LEU THR HIS THR VAL
SEQRES 12 A 316 ARG GLU GLY ASP ARG ILE ALA SER LEU PRO GLU PHE THR
SEQRES 13 A 316 VAL ILE GLU THR PRO GLY HIS ALA SER THR HIS ILE SER
SEQRES 14 A 316 LEU TYR ARG GLU ARG ASP GLY VAL LEU ILE GLY GLY ASP
SEQRES 15 A 316 ALA LEU ILE GLY HIS ILE SER SER ASN PRO ILE LEU GLU
SEQRES 16 A 316 PRO PRO TYR GLU GLY GLU ILE GLU ARG ALA GLN PRO MET
SEQRES 17 A 316 LEU GLN TYR ASN GLU THR LEU LYS ARG LEU ALA ARG MET
SEQRES 18 A 316 ASN ILE SER ARG VAL LEU SER GLY HIS GLY GLU ASP VAL
SEQRES 19 A 316 LEU ASP VAL VAL GLY LEU VAL ASN GLU ARG LEU GLN LYS
SEQRES 20 A 316 GLN GLU ALA ARG ALA PHE LYS VAL LEU ASN LEU LEU LYS
SEQRES 21 A 316 ALA GLN PRO MET THR ALA PHE GLU VAL CYS VAL LYS LEU
SEQRES 22 A 316 PHE PRO THR LEU TYR GLU LYS GLN LEU PRO LEU THR ILE
SEQRES 23 A 316 SER GLU ASN VAL GLY GLN LEU ASP PHE LEU ALA TYR ASN
SEQRES 24 A 316 GLN GLN VAL MET ILE ASP LYS SER SER LYS GLN TRP ILE
SEQRES 25 A 316 TYR TYR ALA LYS
HET GOL A 401 6
HET GOL A 402 12
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 12
HET GOL A 406 6
HET GOL A 407 6
HET MG A 408 1
HET MG A 409 1
HET MG A 410 1
HET MG A 411 1
HET MG A 412 1
HET MG A 413 1
HET MG A 414 1
HET MG A 415 1
HET MG A 416 1
HET MG A 417 1
HET MG A 418 1
HET MG A 419 1
HET MG A 420 1
HET MG A 421 1
HET MG A 422 1
HET MG A 423 1
HET MG A 424 1
HET MG A 425 1
HET MG A 426 1
HET MG A 427 1
HET MG A 428 1
HET MG A 429 1
HET MG A 430 1
HET MG A 431 1
HET MG A 432 1
HET MG A 433 1
HET MG A 434 1
HET MG A 435 1
HET MG A 436 1
HET MG A 437 1
HET MG A 438 1
HET MG A 439 1
HET MG A 440 1
HET MG A 441 1
HET MG A 442 1
HET MG A 443 1
HET MG A 444 1
HET MG A 445 1
HET MG A 446 1
HET MG A 447 1
HET MG A 448 1
HET MG A 449 1
HET MG A 450 1
HET MG A 451 1
HET MG A 452 1
HET MG A 453 1
HET MG A 454 1
HET MG A 455 1
HET MG A 456 1
HET MG A 457 1
HET MG A 458 1
HET MG A 459 1
HET MG A 460 1
HET MG A 461 1
HET MG A 462 1
HET MG A 463 1
HET MG A 464 1
HET MG A 465 1
HET ZN A 466 1
HET ZN A 467 1
HET SO4 A 468 5
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 7(C3 H8 O3)
FORMUL 9 MG 58(MG 2+)
FORMUL 67 ZN 2(ZN 2+)
FORMUL 69 SO4 O4 S 2-
FORMUL 70 HOH *79(H2 O)
HELIX 1 1 THR A 37 LEU A 51 1 15
HELIX 2 2 LYS A 54 ILE A 58 1 5
HELIX 3 3 HIS A 67 PHE A 77 1 11
HELIX 4 4 TRP A 88 PHE A 114 1 27
HELIX 5 5 PRO A 117 LEU A 121 1 5
HELIX 6 6 GLN A 206 MET A 221 1 16
HELIX 7 7 ASP A 236 GLN A 262 1 27
HELIX 8 8 THR A 265 PHE A 274 1 10
HELIX 9 9 THR A 276 GLN A 281 1 6
HELIX 10 10 THR A 285 ALA A 297 1 13
SHEET 1 1 1 VAL A 3 PRO A 10 0
SHEET 2 2 1 THR A 17 GLU A 24 0
SHEET 3 3 1 LEU A 28 ILE A 31 0
SHEET 4 4 1 THR A 60 VAL A 62 0
SHEET 5 5 1 ASN A 82 GLY A 85 0
SHEET 6 6 1 HIS A 141 THR A 142 0
SHEET 7 7 1 PHE A 155 GLU A 159 0
SHEET 8 8 1 ILE A 168 ARG A 172 0
SHEET 9 9 1 VAL A 177 GLY A 181 0
SHEET 10 10 1 ARG A 225 SER A 228 0
LINK O ARG A 6 MG MG A 423 1555 1555 2.86
LINK O ARG A 6 MG MG A 424 1555 1555 2.78
LINK OD1 ASN A 36 MG MG A 414 1555 1555 2.97
LINK O GLU A 45 MG MG A 412 1555 1555 2.78
LINK OE1 GLN A 47 MG MG A 425 1555 1555 2.75
LINK O TYR A 53 MG MG A 412 1555 1555 2.85
LINK OE1 GLU A 56 MG MG A 440 1555 1555 2.82
LINK OE1 GLU A 59 MG MG A 417 1555 1555 2.72
LINK O LEU A 63 MG MG A 415 1555 1555 2.75
LINK NE2 HIS A 65 ZN ZN A 466 1555 1555 2.23
LINK ND1 HIS A 67 ZN ZN A 466 1555 1555 2.17
LINK OD2 ASP A 69 ZN ZN A 467 1555 1555 2.17
LINK NE2 HIS A 70 ZN ZN A 467 1555 1555 2.15
LINK OD2 ASP A 75 MG MG A 449 1555 1555 2.75
LINK OE1 GLU A 79 MG MG A 451 1555 6444 2.74
LINK O TRP A 92 MG MG A 421 1555 1555 2.61
LINK O GLN A 98 MG MG A 462 1555 1555 2.77
LINK O GLN A 113 MG MG A 428 1555 1555 2.73
LINK O GLY A 115 MG MG A 451 1555 1555 2.75
LINK OG1 THR A 130 MG MG A 441 1555 1555 2.54
LINK OG SER A 134 MG MG A 421 1555 1555 2.48
LINK O CYS A 135 MG MG A 421 1555 1555 2.60
LINK OE2 GLU A 145 MG MG A 420 1555 4444 2.68
LINK O LEU A 152 MG MG A 416 1555 1555 2.81
LINK O GLU A 154 MG MG A 409 1555 1555 2.97
LINK O PHE A 155 MG MG A 416 1555 1555 2.79
LINK OE1 GLU A 159 MG MG A 419 1555 4444 2.67
LINK NE2 HIS A 163 ZN ZN A 466 1555 1555 2.11
LINK O THR A 166 MG MG A 415 1555 1555 2.84
LINK O TYR A 171 MG MG A 409 1555 1555 3.00
LINK OD2 ASP A 182 ZN ZN A 466 1555 1555 2.33
LINK OD2 ASP A 182 ZN ZN A 467 1555 1555 2.09
LINK O ALA A 183 MG MG A 408 1555 1555 2.99
LINK O ILE A 188 MG MG A 459 1555 1555 2.80
LINK OG SER A 190 MG MG A 459 1555 1555 2.45
LINK O PRO A 192 MG MG A 446 1555 1555 2.93
LINK O ILE A 193 MG MG A 432 1555 1555 2.93
LINK O LEU A 194 MG MG A 431 1555 1555 2.77
LINK OE2 GLU A 195 MG MG A 432 1555 1555 2.66
LINK OH TYR A 211 MG MG A 460 1555 1555 2.47
LINK O GLU A 213 MG MG A 443 1555 1555 2.87
LINK OE1 GLU A 213 MG MG A 443 1555 1555 2.69
LINK O LEU A 218 MG MG A 445 1555 1555 2.77
LINK O MET A 221 MG MG A 445 1555 1555 2.55
LINK O HIS A 230 MG MG A 410 1555 1555 2.65
LINK NE2 HIS A 230 ZN ZN A 467 1555 1555 2.11
LINK O GLU A 232 MG MG A 410 1555 1555 2.70
LINK OE1 GLU A 232 MG MG A 448 1555 1555 2.72
LINK O ALA A 250 MG MG A 439 1555 8554 2.86
LINK OD1 ASN A 257 MG MG A 439 1555 1555 2.87
LINK OG1 THR A 265 MG MG A 451 1555 1555 2.76
LINK O GLU A 268 MG MG A 450 1555 1555 2.75
LINK OG1 THR A 276 MG MG A 454 1555 1555 2.17
LINK O SER A 307 MG MG A 428 1555 1555 2.73
LINK O3 BGOL A 402 ZN ZN A 466 1555 1555 2.29
LINK O3 AGOL A 402 ZN ZN A 467 1555 1555 2.17
CRYST1 77.823 77.823 135.266 90.00 90.00 90.00 P 41 21 2 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 0.012850 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007393 0.00000
ATOM 1 N MET A 1 -36.797 13.767 0.656 1.00 52.71 N
ANISOU 1 N MET A 1 6882 4660 8484 577 -472 373 N
ATOM 2 CA MET A 1 -37.357 12.519 0.093 1.00 48.08 C
ANISOU 2 CA MET A 1 7325 3462 7480 1015 -213 1097 C
ATOM 3 C MET A 1 -36.307 11.412 0.197 1.00 41.84 C
ANISOU 3 C MET A 1 6859 3976 5062 1487 509 52 C
ATOM 4 O MET A 1 -36.069 10.945 1.309 1.00 46.65 O
ANISOU 4 O MET A 1 8116 4641 4966 262 168 223 O
ATOM 5 CB MET A 1 -37.873 12.715 -1.331 1.00 53.62 C
ANISOU 5 CB MET A 1 7852 4930 7592 2027 -81 308 C
ATOM 6 CG MET A 1 -39.028 11.798 -1.691 1.00 58.73 C
ANISOU 6 CG MET A 1 7527 6061 8727 2047 585 -473 C
ATOM 7 SD MET A 1 -39.960 12.532 -3.052 1.00 78.93 S
ANISOU 7 SD MET A 1 9574 9541 10872 1084 -847 263 S
ATOM 8 CE MET A 1 -40.872 13.775 -2.136 1.00 59.47 C
ANISOU 8 CE MET A 1 3441 8116 11040 922 -2378 -760 C
ATOM 9 N THR A 2 -35.584 11.062 -0.889 1.00 36.29 N
ANISOU 9 N THR A 2 5290 3948 4549 594 214 257 N
ATOM 10 CA THR A 2 -34.793 9.843 -0.833 1.00 33.08 C
ANISOU 10 CA THR A 2 4496 3559 4515 134 -39 296 C
ATOM 11 C THR A 2 -33.445 10.125 -0.173 1.00 31.67 C
ANISOU 11 C THR A 2 5152 2483 4397 -163 -248 70 C
ATOM 12 O THR A 2 -32.868 11.223 -0.280 1.00 31.12 O
ANISOU 12 O THR A 2 4636 2878 4309 -99 -277 -189 O
ATOM 13 CB THR A 2 -34.585 9.178 -2.202 1.00 34.97 C
ANISOU 13 CB THR A 2 5062 3879 4346 579 -131 492 C
ATOM 14 OG1 THR A 2 -33.882 10.104 -3.028 1.00 35.01 O
ANISOU 14 OG1 THR A 2 5214 4309 3780 -457 -54 70 O
ATOM 15 CG2 THR A 2 -35.895 8.737 -2.829 1.00 40.41 C
ANISOU 15 CG2 THR A 2 5550 5176 4628 -142 -521 570 C
ATOM 16 N VAL A 3 -32.982 9.118 0.551 1.00 29.84 N
ANISOU 16 N VAL A 3 4464 2537 4336 222 -345 -170 N
ATOM 17 CA VAL A 3 -31.623 9.019 1.021 1.00 29.67 C
ANISOU 17 CA VAL A 3 4335 2548 4391 59 -438 -373 C
ATOM 18 C VAL A 3 -30.987 7.802 0.352 1.00 27.85 C
ANISOU 18 C VAL A 3 3796 2762 4023 360 -212 -237 C
ATOM 19 O VAL A 3 -31.600 6.748 0.316 1.00 28.60 O
ANISOU 19 O VAL A 3 3390 2701 4774 -168 10 -281 O
ATOM 20 CB VAL A 3 -31.539 8.889 2.553 1.00 36.65 C
ANISOU 20 CB VAL A 3 5308 4000 4616 763 -538 -1049 C
ATOM 21 CG1 VAL A 3 -30.090 8.931 2.993 1.00 38.06 C
ANISOU 21 CG1 VAL A 3 5320 4238 4902 291 -968 -1190 C
ATOM 22 CG2 VAL A 3 -32.344 9.967 3.265 1.00 39.74 C
ANISOU 22 CG2 VAL A 3 5527 4674 4898 291 -679 -1299 C
ATOM 23 N ILE A 4 -29.823 7.989 -0.268 1.00 28.52 N
ANISOU 23 N ILE A 4 3864 2456 4515 107 -120 -264 N
ATOM 24 CA ILE A 4 -29.115 6.897 -0.931 1.00 26.92 C
ANISOU 24 CA ILE A 4 3630 2602 3995 91 -238 -493 C
ATOM 25 C ILE A 4 -27.826 6.623 -0.182 1.00 25.45 C
ANISOU 25 C ILE A 4 3381 2723 3565 -153 -209 -510 C
ATOM 26 O ILE A 4 -27.090 7.543 0.176 1.00 27.66 O
ANISOU 26 O ILE A 4 3715 2503 4292 -379 -842 -41 O
ATOM 27 CB ILE A 4 -28.825 7.226 -2.399 1.00 29.27 C
ANISOU 27 CB ILE A 4 4091 3031 3999 41 -407 -356 C
ATOM 28 CG1 ILE A 4 -30.089 7.635 -3.112 1.00 30.30 C
ANISOU 28 CG1 ILE A 4 4360 2720 4435 -8 -765 -197 C
ATOM 29 CG2 ILE A 4 -28.122 6.070 -3.097 1.00 27.82 C
ANISOU 29 CG2 ILE A 4 3647 3227 3694 -180 -199 -46 C
ATOM 30 CD1 ILE A 4 -29.895 7.908 -4.579 1.00 33.36 C
ANISOU 30 CD1 ILE A 4 5107 3435 4134 824 -607 -50 C
ATOM 31 N HIS A 5 -27.581 5.333 0.053 1.00 25.69 N
ANISOU 31 N HIS A 5 3651 2458 3652 -259 -536 -241 N
ATOM 32 CA HIS A 5 -26.395 4.889 0.772 1.00 26.84 C
ANISOU 32 CA HIS A 5 3867 2657 3676 36 -487 -582 C
ATOM 33 C HIS A 5 -25.633 3.905 -0.109 1.00 25.04 C
ANISOU 33 C HIS A 5 3457 3058 3000 -34 -468 -457 C
ATOM 34 O HIS A 5 -26.227 3.035 -0.726 1.00 26.37 O
ANISOU 34 O HIS A 5 3201 3094 3724 -152 -256 -673 O
ATOM 35 CB HIS A 5 -26.784 4.101 2.030 1.00 26.84 C
ANISOU 35 CB HIS A 5 3993 3111 3094 177 -483 -562 C
ATOM 36 CG HIS A 5 -27.676 4.834 2.922 1.00 31.82 C
ANISOU 36 CG HIS A 5 4743 4025 3321 395 -298 -519 C
ATOM 37 ND1 HIS A 5 -27.203 5.592 3.961 1.00 35.35 N
ANISOU 37 ND1 HIS A 5 5178 4356 3896 583 -521 -1021 N
ATOM 38 CD2 HIS A 5 -28.995 4.963 2.902 1.00 34.76 C
ANISOU 38 CD2 HIS A 5 4852 4803 3551 907 -498 -855 C
ATOM 39 CE1 HIS A 5 -28.251 6.171 4.539 1.00 42.65 C
ANISOU 39 CE1 HIS A 5 6271 6121 3813 874 -125 -1375 C
ATOM 40 NE2 HIS A 5 -29.352 5.781 3.926 1.00 41.93 N
ANISOU 40 NE2 HIS A 5 5915 5552 4466 1608 -24 -1217 N
ATOM 41 N ARG A 6 -24.317 4.065 -0.142 1.00 24.53 N
ANISOU 41 N ARG A 6 3295 2475 3548 -403 -315 -360 N
ATOM 42 CA ARG A 6 -23.425 3.124 -0.772 1.00 24.01 C
ANISOU 42 CA ARG A 6 3206 2664 3253 -91 -294 -461 C
ATOM 43 C ARG A 6 -22.975 2.088 0.243 1.00 26.13 C
ANISOU 43 C ARG A 6 3671 3305 2952 -264 -442 -418 C
ATOM 44 O ARG A 6 -22.469 2.477 1.298 1.00 25.97 O
ANISOU 44 O ARG A 6 3909 2750 3207 -161 -524 -294 O
ATOM 45 CB ARG A 6 -22.178 3.807 -1.334 1.00 27.41 C
ANISOU 45 CB ARG A 6 3900 2984 3529 -473 -219 -131 C
ATOM 46 CG ARG A 6 -21.169 2.908 -2.023 1.00 30.35 C
ANISOU 46 CG ARG A 6 4213 3307 4012 -169 78 -171 C
ATOM 47 CD ARG A 6 -20.066 3.893 -2.486 1.00 43.80 C
ANISOU 47 CD ARG A 6 4604 5655 6385 29 578 -714 C
ATOM 48 NE ARG A 6 -18.812 3.177 -2.596 1.00 54.28 N
ANISOU 48 NE ARG A 6 5521 7065 8038 -429 258 -201 N
ATOM 49 CZ ARG A 6 -17.699 3.662 -3.107 1.00 55.25 C
ANISOU 49 CZ ARG A 6 5560 7751 7683 -783 1226 -49 C
ATOM 50 NH1 ARG A 6 -17.548 4.958 -3.367 1.00 60.91 N
ANISOU 50 NH1 ARG A 6 5585 7936 9622 -346 1444 -770 N
ATOM 51 NH2 ARG A 6 -16.727 2.804 -3.325 1.00 47.31 N
ANISOU 51 NH2 ARG A 6 4358 8248 5369 -1149 -286 -135 N
ATOM 52 N MET A 7 -23.128 0.792 -0.094 1.00 23.30 N
ANISOU 52 N MET A 7 3107 2607 3139 -224 -572 57 N
ATOM 53 CA MET A 7 -22.577 -0.241 0.745 1.00 20.81 C
ANISOU 53 CA MET A 7 2677 2651 2580 -209 -275 -415 C
ATOM 54 C MET A 7 -21.543 -0.978 -0.105 1.00 21.11 C
ANISOU 54 C MET A 7 2498 2650 2874 -101 -195 -373 C
ATOM 55 O MET A 7 -21.804 -1.311 -1.238 1.00 24.54 O
ANISOU 55 O MET A 7 2875 3519 2928 -8 -428 -286 O
ATOM 56 CB MET A 7 -23.646 -1.201 1.291 1.00 23.22 C
ANISOU 56 CB MET A 7 2838 2905 3079 -272 34 -89 C
ATOM 57 CG MET A 7 -24.609 -0.508 2.243 1.00 25.67 C
ANISOU 57 CG MET A 7 3126 3704 2923 -487 -128 -232 C
ATOM 58 SD MET A 7 -25.900 -1.592 2.866 1.00 27.73 S
ANISOU 58 SD MET A 7 3584 3543 3410 -473 -102 -215 S
ATOM 59 CE MET A 7 -26.791 -1.916 1.370 1.00 26.11 C
ANISOU 59 CE MET A 7 3481 2968 3473 -177 -380 151 C
ATOM 60 N GLU A 8 -20.347 -1.159 0.440 1.00 23.91 N
ANISOU 60 N GLU A 8 3117 3187 2782 19 -423 -254 N
ATOM 61 CA GLU A 8 -19.272 -1.849 -0.261 1.00 22.78 C
ANISOU 61 CA GLU A 8 3029 2900 2728 -315 -161 -226 C
ATOM 62 C GLU A 8 -19.282 -3.307 0.195 1.00 24.05 C
ANISOU 62 C GLU A 8 3168 3202 2769 -317 -311 223 C
ATOM 63 O GLU A 8 -19.055 -3.590 1.366 1.00 25.05 O
ANISOU 63 O GLU A 8 3630 3135 2751 -345 -327 17 O
ATOM 64 CB GLU A 8 -17.929 -1.184 0.037 1.00 23.85 C
ANISOU 64 CB GLU A 8 2850 3026 3185 -119 -407 -80 C
ATOM 65 CG GLU A 8 -17.855 0.220 -0.517 1.00 28.16 C
ANISOU 65 CG GLU A 8 3374 3355 3969 -246 -721 106 C
ATOM 66 CD GLU A 8 -16.590 0.972 -0.244 1.00 37.77 C
ANISOU 66 CD GLU A 8 4142 4155 6052 -608 -1217 651 C
ATOM 67 OE1 GLU A 8 -16.635 2.161 -0.546 1.00 42.94 O
ANISOU 67 OE1 GLU A 8 5886 4269 6162 -1223 -1420 673 O
ATOM 68 OE2 GLU A 8 -15.626 0.405 0.275 1.00 45.40 O
ANISOU 68 OE2 GLU A 8 4839 4430 7982 -815 -2075 1240 O
ATOM 69 N ILE A 9 -19.567 -4.213 -0.742 1.00 22.19 N
ANISOU 69 N ILE A 9 2871 2860 2700 -139 -376 241 N
ATOM 70 CA ILE A 9 -19.724 -5.624 -0.436 1.00 22.81 C
ANISOU 70 CA ILE A 9 2745 2839 3082 -137 -291 152 C
ATOM 71 C ILE A 9 -18.535 -6.399 -0.987 1.00 21.31 C
ANISOU 71 C ILE A 9 2286 2719 3091 -391 -398 195 C
ATOM 72 O ILE A 9 -18.207 -6.307 -2.187 1.00 22.42 O
ANISOU 72 O ILE A 9 2715 2877 2928 -14 -261 236 O
ATOM 73 CB ILE A 9 -21.047 -6.160 -1.029 1.00 22.57 C
ANISOU 73 CB ILE A 9 2736 2915 2926 -118 -203 206 C
ATOM 74 CG1 ILE A 9 -22.255 -5.343 -0.572 1.00 24.34 C
ANISOU 74 CG1 ILE A 9 2706 3266 3278 89 -404 378 C
ATOM 75 CG2 ILE A 9 -21.221 -7.628 -0.700 1.00 24.16 C
ANISOU 75 CG2 ILE A 9 2942 2760 3478 -85 -330 288 C
ATOM 76 CD1 ILE A 9 -22.464 -5.205 0.921 1.00 24.33 C
ANISOU 76 CD1 ILE A 9 3125 3096 3024 16 -47 28 C
ATOM 77 N PRO A 10 -17.799 -7.137 -0.127 1.00 22.48 N
ANISOU 77 N PRO A 10 2605 2996 2939 -250 -414 203 N
ATOM 78 CA PRO A 10 -16.668 -7.930 -0.613 1.00 22.60 C
ANISOU 78 CA PRO A 10 2421 3048 3119 108 -453 249 C
ATOM 79 C PRO A 10 -17.096 -9.001 -1.624 1.00 22.17 C
ANISOU 79 C PRO A 10 2521 2883 3019 137 -612 512 C
ATOM 80 O PRO A 10 -18.141 -9.673 -1.446 1.00 24.00 O
ANISOU 80 O PRO A 10 2578 2928 3611 -170 -127 258 O
ATOM 81 CB PRO A 10 -16.093 -8.504 0.681 1.00 25.58 C
ANISOU 81 CB PRO A 10 2857 3297 3563 -60 -742 866 C
ATOM 82 CG PRO A 10 -17.208 -8.507 1.633 1.00 30.05 C
ANISOU 82 CG PRO A 10 3701 4092 3626 429 -271 745 C
ATOM 83 CD PRO A 10 -18.075 -7.352 1.298 1.00 24.84 C
ANISOU 83 CD PRO A 10 2776 3354 3309 93 -211 264 C
ATOM 84 N VAL A 11 -16.292 -9.132 -2.694 1.00 23.28 N
ANISOU 84 N VAL A 11 2615 3093 3137 -169 -335 255 N
ATOM 85 CA VAL A 11 -16.486 -10.168 -3.694 1.00 22.02 C
ANISOU 85 CA VAL A 11 2473 2562 3332 0 -227 359 C
ATOM 86 C VAL A 11 -15.169 -10.876 -3.913 1.00 23.35 C
ANISOU 86 C VAL A 11 2644 2780 3448 289 -409 135 C
ATOM 87 O VAL A 11 -14.108 -10.266 -3.706 1.00 28.00 O
ANISOU 87 O VAL A 11 2796 3125 4718 321 -426 116 O
ATOM 88 CB VAL A 11 -17.061 -9.603 -5.021 1.00 24.19 C
ANISOU 88 CB VAL A 11 2913 2843 3435 53 -375 451 C
ATOM 89 CG1 VAL A 11 -18.448 -9.016 -4.758 1.00 25.37 C
ANISOU 89 CG1 VAL A 11 3102 3062 3474 22 -704 226 C
ATOM 90 CG2 VAL A 11 -16.137 -8.560 -5.620 1.00 23.22 C
ANISOU 90 CG2 VAL A 11 2964 2567 3291 -305 -205 356 C
ATOM 91 N PRO A 12 -15.196 -12.153 -4.342 1.00 24.37 N
ANISOU 91 N PRO A 12 2760 2832 3666 184 64 413 N
ATOM 92 CA PRO A 12 -13.976 -12.955 -4.447 1.00 26.17 C
ANISOU 92 CA PRO A 12 2510 3089 4343 427 -2 429 C
ATOM 93 C PRO A 12 -13.312 -12.821 -5.805 1.00 30.55 C
ANISOU 93 C PRO A 12 3237 3840 4531 863 232 487 C
ATOM 94 O PRO A 12 -12.813 -13.789 -6.350 1.00 36.70 O
ANISOU 94 O PRO A 12 4452 4539 4955 1207 540 894 O
ATOM 95 CB PRO A 12 -14.531 -14.357 -4.257 1.00 28.20 C
ANISOU 95 CB PRO A 12 3444 2624 4648 745 -235 426 C
ATOM 96 CG PRO A 12 -15.864 -14.320 -4.924 1.00 30.40 C
ANISOU 96 CG PRO A 12 3845 3242 4465 687 197 250 C
ATOM 97 CD PRO A 12 -16.409 -12.981 -4.487 1.00 24.11 C
ANISOU 97 CD PRO A 12 2821 2526 3814 43 -25 438 C
ATOM 98 N PHE A 13 -13.366 -11.620 -6.339 1.00 30.52 N
ANISOU 98 N PHE A 13 3214 3750 4633 695 805 736 N
ATOM 99 CA PHE A 13 -12.827 -11.253 -7.629 1.00 29.26 C
ANISOU 99 CA PHE A 13 3257 3806 4054 608 -53 271 C
ATOM 100 C PHE A 13 -11.747 -10.196 -7.434 1.00 28.23 C
ANISOU 100 C PHE A 13 3014 3755 3956 99 -36 561 C
ATOM 101 O PHE A 13 -11.666 -9.587 -6.372 1.00 28.95 O
ANISOU 101 O PHE A 13 3153 3966 3881 -101 -35 650 O
ATOM 102 CB PHE A 13 -13.940 -10.688 -8.511 1.00 31.52 C
ANISOU 102 CB PHE A 13 3656 4250 4069 408 -69 634 C
ATOM 103 CG PHE A 13 -15.136 -11.607 -8.750 1.00 28.81 C
ANISOU 103 CG PHE A 13 3582 3269 4095 32 -228 412 C
ATOM 104 CD1 PHE A 13 -14.991 -12.963 -8.974 1.00 33.53 C
ANISOU 104 CD1 PHE A 13 4161 3539 5041 -217 194 130 C
ATOM 105 CD2 PHE A 13 -16.409 -11.089 -8.834 1.00 27.56 C
ANISOU 105 CD2 PHE A 13 3664 2680 4129 -20 17 178 C
ATOM 106 CE1 PHE A 13 -16.096 -13.775 -9.191 1.00 31.50 C
ANISOU 106 CE1 PHE A 13 3850 3415 4704 -71 -129 536 C
ATOM 107 CE2 PHE A 13 -17.514 -11.900 -9.078 1.00 29.00 C
ANISOU 107 CE2 PHE A 13 3652 3354 4010 86 159 166 C
ATOM 108 CZ PHE A 13 -17.361 -13.244 -9.253 1.00 30.14 C
ANISOU 108 CZ PHE A 13 4118 3197 4137 -18 15 263 C
ATOM 109 N ALA A 14 -10.980 -9.950 -8.500 1.00 30.93 N
ANISOU 109 N ALA A 14 3293 3861 4598 267 106 437 N
ATOM 110 CA ALA A 14 -9.858 -9.028 -8.413 1.00 32.68 C
ANISOU 110 CA ALA A 14 3268 4312 4835 -100 307 492 C
ATOM 111 C ALA A 14 -10.278 -7.625 -7.994 1.00 29.50 C
ANISOU 111 C ALA A 14 2714 3972 4524 -365 479 542 C
ATOM 112 O ALA A 14 -9.487 -6.926 -7.344 1.00 30.72 O
ANISOU 112 O ALA A 14 3048 4133 4492 -449 234 550 O
ATOM 113 CB ALA A 14 -9.103 -9.037 -9.715 1.00 35.01 C
ANISOU 113 CB ALA A 14 3824 4573 4905 -472 702 952 C
ATOM 114 N VAL A 15 -11.493 -7.214 -8.367 1.00 30.13 N
ANISOU 114 N VAL A 15 3004 4109 4336 -416 -23 546 N
ATOM 115 CA AVAL A 15 -12.009 -5.888 -8.058 0.50 26.84 C
ANISOU 115 CA AVAL A 15 2821 3212 4164 -146 -97 786 C
ATOM 116 CA BVAL A 15 -12.034 -5.887 -8.058 0.50 29.04 C
ANISOU 116 CA BVAL A 15 3154 3603 4275 -227 47 500 C
ATOM 117 C VAL A 15 -12.297 -5.717 -6.552 1.00 27.86 C
ANISOU 117 C VAL A 15 3018 3541 4028 -83 153 189 C
ATOM 118 O VAL A 15 -12.485 -4.586 -6.064 1.00 29.61 O
ANISOU 118 O VAL A 15 3545 3440 4267 -192 -38 307 O
ATOM 119 CB AVAL A 15 -13.260 -5.653 -8.927 0.50 26.91 C
ANISOU 119 CB AVAL A 15 2988 3132 4104 -140 -231 1055 C
ATOM 120 CB BVAL A 15 -13.332 -5.555 -8.829 0.50 33.04 C
ANISOU 120 CB BVAL A 15 3656 4472 4426 -307 -151 474 C
ATOM 121 CG1AVAL A 15 -14.481 -6.418 -8.411 0.50 25.28 C
ANISOU 121 CG1AVAL A 15 2308 2988 4308 160 -578 1206 C
ATOM 122 CG1BVAL A 15 -13.089 -5.315 -10.305 0.50 38.32 C
ANISOU 122 CG1BVAL A 15 4708 5046 4806 -416 -152 353 C
ATOM 123 CG2AVAL A 15 -13.564 -4.172 -9.028 0.50 24.43 C
ANISOU 123 CG2AVAL A 15 2692 2549 4043 -120 -159 1310 C
ATOM 124 CG2BVAL A 15 -14.428 -6.601 -8.611 0.50 30.84 C
ANISOU 124 CG2BVAL A 15 3299 4016 4402 -5 -44 616 C
ATOM 125 N GLU A 16 -12.351 -6.853 -5.818 1.00 26.62 N
ANISOU 125 N GLU A 16 2833 3360 3922 -137 10 406 N
ATOM 126 CA GLU A 16 -12.388 -6.909 -4.364 1.00 28.36 C
ANISOU 126 CA GLU A 16 2620 3627 4529 -19 -233 310 C
ATOM 127 C GLU A 16 -13.727 -6.515 -3.745 1.00 25.96 C
ANISOU 127 C GLU A 16 2960 3194 3710 -223 -450 133 C
ATOM 128 O GLU A 16 -14.147 -7.155 -2.771 1.00 25.44 O
ANISOU 128 O GLU A 16 2733 3250 3681 -73 -347 313 O
ATOM 129 CB GLU A 16 -11.274 -6.128 -3.659 1.00 32.53 C
ANISOU 129 CB GLU A 16 2987 4394 4980 -84 -471 597 C
ATOM 130 CG GLU A 16 -9.894 -6.659 -4.006 1.00 39.48 C
ANISOU 130 CG GLU A 16 3669 5950 5379 486 -741 147 C
ATOM 131 CD GLU A 16 -8.828 -5.987 -3.164 1.00 49.11 C
ANISOU 131 CD GLU A 16 4364 7146 7150 17 -1150 -643 C
ATOM 132 OE1 GLU A 16 -7.690 -6.393 -3.359 1.00 60.44 O
ANISOU 132 OE1 GLU A 16 5575 8226 9166 1224 -791 -463 O
ATOM 133 OE2 GLU A 16 -9.143 -5.117 -2.315 1.00 57.41 O
ANISOU 133 OE2 GLU A 16 6031 6496 9287 -200 -2590 -1310 O
ATOM 134 N THR A 17 -14.359 -5.453 -4.263 1.00 24.55 N
ANISOU 134 N THR A 17 2630 3155 3543 -193 -383 171 N
ATOM 135 CA THR A 17 -15.616 -4.954 -3.688 1.00 25.43 C
ANISOU 135 CA THR A 17 3319 3271 3071 -257 -731 84 C
ATOM 136 C THR A 17 -16.532 -4.598 -4.845 1.00 21.86 C
ANISOU 136 C THR A 17 2729 2509 3070 -232 -610 -165 C
ATOM 137 O THR A 17 -16.079 -4.191 -5.899 1.00 23.53 O
ANISOU 137 O THR A 17 2868 2971 3103 6 -582 289 O
ATOM 138 CB THR A 17 -15.477 -3.751 -2.761 1.00 30.87 C
ANISOU 138 CB THR A 17 4077 4305 3349 -219 -1319 57 C
ATOM 139 OG1 THR A 17 -15.019 -2.647 -3.483 1.00 34.60 O
ANISOU 139 OG1 THR A 17 4852 3319 4974 -595 -1194 148 O
ATOM 140 CG2 THR A 17 -14.508 -4.120 -1.672 1.00 35.11 C
ANISOU 140 CG2 THR A 17 5182 3810 4348 284 -2013 418 C
ATOM 141 N VAL A 18 -17.823 -4.726 -4.589 1.00 22.46 N
ANISOU 141 N VAL A 18 2727 2938 2871 -286 -496 321 N
ATOM 142 CA VAL A 18 -18.865 -4.197 -5.447 1.00 20.65 C
ANISOU 142 CA VAL A 18 2630 2494 2721 -205 -427 216 C
ATOM 143 C VAL A 18 -19.631 -3.152 -4.634 1.00 21.58 C
ANISOU 143 C VAL A 18 2645 2971 2585 -522 -452 55 C
ATOM 144 O VAL A 18 -19.823 -3.306 -3.411 1.00 22.50 O
ANISOU 144 O VAL A 18 2858 2783 2908 -166 -167 162 O
ATOM 145 CB VAL A 18 -19.817 -5.294 -5.986 1.00 20.65 C
ANISOU 145 CB VAL A 18 2927 2203 2716 -271 -472 162 C
ATOM 146 CG1 VAL A 18 -20.638 -5.977 -4.908 1.00 22.66 C
ANISOU 146 CG1 VAL A 18 3111 2525 2973 -61 -226 235 C
ATOM 147 CG2 VAL A 18 -20.744 -4.745 -7.064 1.00 20.54 C
ANISOU 147 CG2 VAL A 18 2854 2345 2606 -383 -345 214 C
ATOM 148 N ASN A 19 -20.044 -2.083 -5.317 1.00 21.11 N
ANISOU 148 N ASN A 19 2756 2482 2782 -57 -17 -132 N
ATOM 149 CA ASN A 19 -20.871 -1.073 -4.683 1.00 21.89 C
ANISOU 149 CA ASN A 19 2710 2607 2999 -259 -166 -114 C
ATOM 150 C ASN A 19 -22.327 -1.430 -4.911 1.00 22.14 C
ANISOU 150 C ASN A 19 3069 2493 2850 -122 -265 -111 C
ATOM 151 O ASN A 19 -22.725 -1.621 -6.064 1.00 23.79 O
ANISOU 151 O ASN A 19 2903 3204 2932 10 -406 -109 O
ATOM 152 CB ASN A 19 -20.631 0.301 -5.264 1.00 21.74 C
ANISOU 152 CB ASN A 19 3133 2239 2887 -179 182 -33 C
ATOM 153 CG ASN A 19 -19.224 0.791 -5.056 1.00 24.71 C
ANISOU 153 CG ASN A 19 3375 2863 3151 -597 -374 -129 C
ATOM 154 OD1 ASN A 19 -18.591 0.506 -4.013 1.00 27.15 O
ANISOU 154 OD1 ASN A 19 3613 3445 3259 -893 -589 308 O
ATOM 155 ND2 ASN A 19 -18.767 1.592 -6.033 1.00 28.30 N
ANISOU 155 ND2 ASN A 19 3870 3660 3222 -922 -367 298 N
ATOM 156 N VAL A 20 -23.101 -1.491 -3.809 1.00 21.92 N
ANISOU 156 N VAL A 20 2843 2687 2798 -218 -367 56 N
ATOM 157 CA VAL A 20 -24.528 -1.661 -3.911 1.00 21.50 C
ANISOU 157 CA VAL A 20 2812 2680 2679 -143 -112 -289 C
ATOM 158 C VAL A 20 -25.157 -0.419 -3.283 1.00 22.34 C
ANISOU 158 C VAL A 20 2886 2667 2934 -254 -383 -174 C
ATOM 159 O VAL A 20 -24.540 0.218 -2.420 1.00 23.57 O
ANISOU 159 O VAL A 20 2872 2858 3226 -89 -483 -497 O
ATOM 160 CB VAL A 20 -25.028 -2.965 -3.277 1.00 22.53 C
ANISOU 160 CB VAL A 20 2729 2579 3251 -169 -271 -84 C
ATOM 161 CG1 VAL A 20 -24.321 -4.172 -3.859 1.00 23.18 C
ANISOU 161 CG1 VAL A 20 2804 2675 3329 88 -603 -377 C
ATOM 162 CG2 VAL A 20 -24.948 -2.939 -1.769 1.00 23.34 C
ANISOU 162 CG2 VAL A 20 2743 2789 3334 -141 -323 -207 C
ATOM 163 N PHE A 21 -26.334 -0.038 -3.729 1.00 21.31 N
ANISOU 163 N PHE A 21 2895 2430 2771 -138 -341 -1 N
ATOM 164 CA PHE A 21 -26.920 1.234 -3.339 1.00 21.43 C
ANISOU 164 CA PHE A 21 3072 2571 2500 -9 -331 -442 C
ATOM 165 C PHE A 21 -28.291 1.012 -2.720 1.00 21.74 C
ANISOU 165 C PHE A 21 3055 2384 2820 54 -289 -35 C
ATOM 166 O PHE A 21 -29.152 0.411 -3.346 1.00 22.97 O
ANISOU 166 O PHE A 21 2852 2931 2944 -198 17 -491 O
ATOM 167 CB PHE A 21 -26.987 2.193 -4.538 1.00 22.66 C
ANISOU 167 CB PHE A 21 3190 2590 2829 -68 -479 -422 C
ATOM 168 CG PHE A 21 -25.618 2.543 -5.083 1.00 22.41 C
ANISOU 168 CG PHE A 21 3002 2577 2936 -9 -106 -160 C
ATOM 169 CD1 PHE A 21 -24.859 3.544 -4.477 1.00 22.32 C
ANISOU 169 CD1 PHE A 21 3149 2611 2722 210 -213 -387 C
ATOM 170 CD2 PHE A 21 -24.992 1.737 -6.020 1.00 21.66 C
ANISOU 170 CD2 PHE A 21 2938 2446 2845 9 -169 -192 C
ATOM 171 CE1 PHE A 21 -23.574 3.809 -4.891 1.00 24.52 C
ANISOU 171 CE1 PHE A 21 3523 2571 3221 -192 13 124 C
ATOM 172 CE2 PHE A 21 -23.697 2.046 -6.444 1.00 23.42 C
ANISOU 172 CE2 PHE A 21 3329 2657 2910 -188 168 -5 C
ATOM 173 CZ PHE A 21 -23.016 3.082 -5.897 1.00 24.90 C
ANISOU 173 CZ PHE A 21 3550 2914 2996 -291 208 49 C
ATOM 174 N LEU A 22 -28.454 1.451 -1.471 1.00 22.58 N
ANISOU 174 N LEU A 22 3000 2607 2972 -46 -332 -331 N
ATOM 175 CA LEU A 22 -29.715 1.336 -0.768 1.00 23.11 C
ANISOU 175 CA LEU A 22 3168 2524 3088 33 -85 -212 C
ATOM 176 C LEU A 22 -30.427 2.687 -0.828 1.00 23.96 C
ANISOU 176 C LEU A 22 3441 2515 3148 -106 -207 -343 C
ATOM 177 O LEU A 22 -29.882 3.697 -0.396 1.00 25.41 O
ANISOU 177 O LEU A 22 3615 2426 3614 -114 -515 -225 O
ATOM 178 CB LEU A 22 -29.483 0.968 0.695 1.00 23.06 C
ANISOU 178 CB LEU A 22 3130 2461 3172 81 -395 -300 C
ATOM 179 CG LEU A 22 -30.709 0.643 1.536 1.00 25.15 C
ANISOU 179 CG LEU A 22 3272 3091 3193 32 121 -427 C
ATOM 180 CD1 LEU A 22 -31.213 -0.714 1.119 1.00 24.68 C
ANISOU 180 CD1 LEU A 22 3104 3359 2915 -424 -17 22 C
ATOM 181 CD2 LEU A 22 -30.371 0.679 3.000 1.00 27.43 C
ANISOU 181 CD2 LEU A 22 4015 2946 3461 -453 -65 75 C
ATOM 182 N VAL A 23 -31.637 2.685 -1.372 1.00 23.69 N
ANISOU 182 N VAL A 23 3244 2480 3278 25 -356 -409 N
ATOM 183 CA VAL A 23 -32.422 3.880 -1.530 1.00 25.29 C
ANISOU 183 CA VAL A 23 3487 2697 3424 -33 -227 -82 C
ATOM 184 C VAL A 23 -33.545 3.846 -0.517 1.00 23.49 C
ANISOU 184 C VAL A 23 3255 2631 3040 -168 -304 -9 C
ATOM 185 O VAL A 23 -34.415 2.986 -0.579 1.00 24.39 O
ANISOU 185 O VAL A 23 3010 2841 3415 -150 -41 -300 O
ATOM 186 CB VAL A 23 -32.975 4.020 -2.959 1.00 24.73 C
ANISOU 186 CB VAL A 23 3466 2757 3172 183 -136 113 C
ATOM 187 CG1 VAL A 23 -33.749 5.330 -3.099 1.00 26.23 C
ANISOU 187 CG1 VAL A 23 3816 2823 3327 437 -196 -226 C
ATOM 188 CG2 VAL A 23 -31.840 3.917 -3.985 1.00 25.66 C
ANISOU 188 CG2 VAL A 23 3258 2904 3587 -347 -336 97 C
ATOM 189 N GLU A 24 -33.489 4.762 0.438 1.00 25.44 N
ANISOU 189 N GLU A 24 3380 2886 3400 57 -164 -424 N
ATOM 190 CA GLU A 24 -34.558 4.899 1.410 1.00 26.03 C
ANISOU 190 CA GLU A 24 3496 2819 3575 -102 -69 -191 C
ATOM 191 C GLU A 24 -35.573 5.896 0.859 1.00 27.32 C
ANISOU 191 C GLU A 24 3540 3110 3731 25 299 -57 C
ATOM 192 O GLU A 24 -35.356 7.106 0.900 1.00 31.79 O
ANISOU 192 O GLU A 24 4949 3065 4066 -84 -15 -24 O
ATOM 193 CB GLU A 24 -33.986 5.461 2.699 1.00 30.41 C
ANISOU 193 CB GLU A 24 4519 3410 3623 228 86 -915 C
ATOM 194 CG GLU A 24 -32.946 4.613 3.383 1.00 31.88 C
ANISOU 194 CG GLU A 24 5110 3508 3495 233 -225 -411 C
ATOM 195 CD GLU A 24 -32.493 5.322 4.652 1.00 34.67 C
ANISOU 195 CD GLU A 24 5539 3711 3924 3 -359 -701 C
ATOM 196 OE1 GLU A 24 -31.846 6.366 4.586 1.00 37.51 O
ANISOU 196 OE1 GLU A 24 5927 4009 4316 186 -696 -1036 O
ATOM 197 OE2 GLU A 24 -32.790 4.854 5.707 1.00 43.49 O
ANISOU 197 OE2 GLU A 24 7851 4447 4227 -836 -385 -329 O
ATOM 198 N GLY A 25 -36.660 5.372 0.342 1.00 29.98 N
ANISOU 198 N GLY A 25 3859 3466 4067 609 138 -388 N
ATOM 199 CA GLY A 25 -37.748 6.154 -0.204 1.00 32.37 C
ANISOU 199 CA GLY A 25 4199 3955 4144 790 -78 -183 C
ATOM 200 C GLY A 25 -39.038 5.804 0.554 1.00 31.89 C
ANISOU 200 C GLY A 25 3773 4089 4255 799 538 -458 C
ATOM 201 O GLY A 25 -39.006 5.432 1.741 1.00 32.94 O
ANISOU 201 O GLY A 25 3832 4335 4349 473 227 -611 O
ATOM 202 N GLU A 26 -40.165 5.874 -0.161 1.00 32.60 N
ANISOU 202 N GLU A 26 3994 3897 4497 869 317 -347 N
ATOM 203 CA GLU A 26 -41.433 5.464 0.417 1.00 30.71 C
ANISOU 203 CA GLU A 26 3617 4235 3815 637 516 -428 C
ATOM 204 C GLU A 26 -41.335 3.986 0.805 1.00 31.35 C
ANISOU 204 C GLU A 26 3804 4083 4023 353 611 -133 C
ATOM 205 O GLU A 26 -41.913 3.580 1.817 1.00 33.76 O
ANISOU 205 O GLU A 26 4092 4583 4151 828 1257 -93 O
ATOM 206 CB GLU A 26 -42.626 5.777 -0.486 1.00 34.96 C
ANISOU 206 CB GLU A 26 4960 4601 3720 1216 336 -851 C
ATOM 207 N THR A 27 -40.595 3.223 -0.008 1.00 29.80 N
ANISOU 207 N THR A 27 3329 3845 4150 653 412 89 N
ATOM 208 CA THR A 27 -40.196 1.849 0.297 1.00 29.03 C
ANISOU 208 CA THR A 27 3323 3771 3937 419 276 49 C
ATOM 209 C THR A 27 -38.680 1.779 0.132 1.00 25.57 C
ANISOU 209 C THR A 27 3386 3390 2940 277 246 -40 C
ATOM 210 O THR A 27 -38.071 2.745 -0.336 1.00 26.94 O
ANISOU 210 O THR A 27 3264 3553 3418 316 498 -204 O
ATOM 211 CB THR A 27 -40.871 0.850 -0.645 1.00 30.83 C
ANISOU 211 CB THR A 27 3221 3743 4750 -40 134 -169 C
ATOM 212 OG1 THR A 27 -40.448 1.073 -1.990 1.00 30.54 O
ANISOU 212 OG1 THR A 27 3592 4191 3822 352 -172 -98 O
ATOM 213 CG2 THR A 27 -42.384 0.944 -0.611 1.00 37.87 C
ANISOU 213 CG2 THR A 27 4185 4820 5384 336 755 -544 C
ATOM 214 N LEU A 28 -38.111 0.658 0.557 1.00 24.28 N
ANISOU 214 N LEU A 28 3324 2771 3129 121 -118 -118 N
ATOM 215 CA LEU A 28 -36.672 0.457 0.547 1.00 24.57 C
ANISOU 215 CA LEU A 28 3073 2969 3292 142 -82 -158 C
ATOM 216 C LEU A 28 -36.265 -0.337 -0.691 1.00 24.93 C
ANISOU 216 C LEU A 28 3052 2893 3526 157 -34 -377 C
ATOM 217 O LEU A 28 -36.820 -1.424 -0.924 1.00 23.57 O
ANISOU 217 O LEU A 28 2815 2928 3210 -3 195 -212 O
ATOM 218 CB LEU A 28 -36.318 -0.345 1.785 1.00 29.40 C
ANISOU 218 CB LEU A 28 4987 3087 3096 -193 -45 84 C
ATOM 219 CG LEU A 28 -35.249 0.099 2.724 1.00 36.22 C
ANISOU 219 CG LEU A 28 5384 3719 4660 -557 -878 422 C
ATOM 220 CD1 LEU A 28 -34.712 -1.157 3.436 1.00 28.82 C
ANISOU 220 CD1 LEU A 28 4666 2872 3414 -534 -397 104 C
ATOM 221 CD2 LEU A 28 -34.259 1.155 2.441 1.00 28.43 C
ANISOU 221 CD2 LEU A 28 3918 2536 4348 -760 -413 -74 C
ATOM 222 N THR A 29 -35.372 0.242 -1.516 1.00 22.77 N
ANISOU 222 N THR A 29 2617 2780 3253 85 -254 -350 N
ATOM 223 CA THR A 29 -34.877 -0.416 -2.718 1.00 22.09 C
ANISOU 223 CA THR A 29 2709 2768 2916 109 81 -285 C
ATOM 224 C THR A 29 -33.377 -0.661 -2.578 1.00 21.92 C
ANISOU 224 C THR A 29 2907 2455 2965 0 -218 -437 C
ATOM 225 O THR A 29 -32.641 0.178 -2.052 1.00 24.40 O
ANISOU 225 O THR A 29 2993 2454 3824 -79 -69 -728 O
ATOM 226 CB THR A 29 -35.154 0.457 -3.924 1.00 24.06 C
ANISOU 226 CB THR A 29 3046 3103 2994 218 -39 -323 C
ATOM 227 OG1 THR A 29 -36.556 0.701 -3.996 1.00 24.67 O
ANISOU 227 OG1 THR A 29 2885 3130 3358 292 48 -298 O
ATOM 228 CG2 THR A 29 -34.627 -0.141 -5.218 1.00 23.98 C
ANISOU 228 CG2 THR A 29 2814 2834 3463 288 -140 44 C
ATOM 229 N LEU A 30 -32.914 -1.829 -3.015 1.00 21.15 N
ANISOU 229 N LEU A 30 2595 2556 2884 64 35 -385 N
ATOM 230 CA LEU A 30 -31.501 -2.102 -3.132 1.00 20.86 C
ANISOU 230 CA LEU A 30 2502 2657 2767 -177 -119 -69 C
ATOM 231 C LEU A 30 -31.152 -2.221 -4.615 1.00 19.81 C
ANISOU 231 C LEU A 30 2663 2176 2688 37 -193 -165 C
ATOM 232 O LEU A 30 -31.795 -2.986 -5.323 1.00 21.80 O
ANISOU 232 O LEU A 30 3017 2625 2641 -182 34 -376 O
ATOM 233 CB LEU A 30 -31.154 -3.406 -2.424 1.00 20.29 C
ANISOU 233 CB LEU A 30 2621 2346 2743 -295 -90 -120 C
ATOM 234 CG LEU A 30 -29.685 -3.796 -2.380 1.00 22.53 C
ANISOU 234 CG LEU A 30 2940 2489 3133 -131 -31 103 C
ATOM 235 CD1 LEU A 30 -28.877 -2.772 -1.576 1.00 24.72 C
ANISOU 235 CD1 LEU A 30 2671 2854 3868 -267 -186 163 C
ATOM 236 CD2 LEU A 30 -29.487 -5.207 -1.809 1.00 23.82 C
ANISOU 236 CD2 LEU A 30 3093 2672 3286 -313 -295 204 C
ATOM 237 N ILE A 31 -30.061 -1.564 -5.044 1.00 19.76 N
ANISOU 237 N ILE A 31 2460 2377 2671 -197 -71 -381 N
ATOM 238 CA ILE A 31 -29.550 -1.723 -6.391 1.00 20.04 C
ANISOU 238 CA ILE A 31 2361 2448 2806 -153 -248 -44 C
ATOM 239 C ILE A 31 -28.270 -2.552 -6.311 1.00 20.27 C
ANISOU 239 C ILE A 31 2473 2231 3000 -44 -226 52 C
ATOM 240 O ILE A 31 -27.271 -2.104 -5.739 1.00 20.95 O
ANISOU 240 O ILE A 31 2530 2488 2940 -178 -308 -78 O
ATOM 241 CB ILE A 31 -29.338 -0.363 -7.062 1.00 22.38 C
ANISOU 241 CB ILE A 31 2733 2712 3058 27 -330 -12 C
ATOM 242 CG1 ILE A 31 -30.672 0.386 -7.151 1.00 27.12 C
ANISOU 242 CG1 ILE A 31 3373 3101 3829 246 -87 157 C
ATOM 243 CG2 ILE A 31 -28.727 -0.572 -8.433 1.00 23.13 C
ANISOU 243 CG2 ILE A 31 2693 2805 3291 90 -179 174 C
ATOM 244 CD1 ILE A 31 -30.605 1.782 -6.695 1.00 34.95 C
ANISOU 244 CD1 ILE A 31 3988 4339 4953 60 -895 -983 C
ATOM 245 N ASP A 32 -28.318 -3.758 -6.880 1.00 20.79 N
ANISOU 245 N ASP A 32 2716 2370 2811 -151 -280 152 N
ATOM 246 CA ASP A 32 -27.235 -4.739 -6.904 1.00 19.33 C
ANISOU 246 CA ASP A 32 2429 2467 2448 261 -515 -20 C
ATOM 247 C ASP A 32 -27.032 -5.381 -5.527 1.00 19.12 C
ANISOU 247 C ASP A 32 2622 2344 2300 -8 -105 -45 C
ATOM 248 O ASP A 32 -27.496 -4.850 -4.517 1.00 20.42 O
ANISOU 248 O ASP A 32 2470 2488 2799 37 -159 2 O
ATOM 249 CB ASP A 32 -26.003 -4.166 -7.581 1.00 20.76 C
ANISOU 249 CB ASP A 32 2763 2280 2843 12 -320 63 C
ATOM 250 CG ASP A 32 -26.179 -3.867 -9.053 1.00 20.33 C
ANISOU 250 CG ASP A 32 2583 2163 2980 409 -311 -140 C
ATOM 251 OD1 ASP A 32 -27.184 -4.416 -9.646 1.00 20.72 O
ANISOU 251 OD1 ASP A 32 2753 2683 2436 86 -148 67 O
ATOM 252 OD2 ASP A 32 -25.329 -3.166 -9.631 1.00 21.61 O
ANISOU 252 OD2 ASP A 32 2706 2678 2827 -97 -216 70 O
ATOM 253 N THR A 33 -26.373 -6.580 -5.497 1.00 20.09 N
ANISOU 253 N THR A 33 2599 2194 2840 231 -226 -12 N
ATOM 254 CA THR A 33 -26.434 -7.370 -4.288 1.00 20.29 C
ANISOU 254 CA THR A 33 2684 2461 2564 221 -125 268 C
ATOM 255 C THR A 33 -25.102 -7.842 -3.701 1.00 21.07 C
ANISOU 255 C THR A 33 2871 2370 2763 -34 -198 -34 C
ATOM 256 O THR A 33 -25.072 -8.131 -2.503 1.00 22.97 O
ANISOU 256 O THR A 33 2953 2993 2781 196 -95 90 O
ATOM 257 CB THR A 33 -27.314 -8.597 -4.486 1.00 22.02 C
ANISOU 257 CB THR A 33 2523 2662 3183 39 84 96 C
ATOM 258 OG1 THR A 33 -26.646 -9.533 -5.332 1.00 21.70 O
ANISOU 258 OG1 THR A 33 2797 2467 2981 206 -57 135 O
ATOM 259 CG2 THR A 33 -28.656 -8.276 -5.063 1.00 22.02 C
ANISOU 259 CG2 THR A 33 2459 2505 3402 -236 -102 62 C
ATOM 260 N GLY A 34 -24.100 -8.073 -4.541 1.00 20.26 N
ANISOU 260 N GLY A 34 2557 2320 2821 69 -281 159 N
ATOM 261 CA GLY A 34 -22.973 -8.889 -4.137 1.00 20.04 C
ANISOU 261 CA GLY A 34 2495 2477 2643 -49 -260 77 C
ATOM 262 C GLY A 34 -23.058 -10.319 -4.658 1.00 20.20 C
ANISOU 262 C GLY A 34 2408 2614 2654 -62 -222 62 C
ATOM 263 O GLY A 34 -24.109 -10.770 -5.078 1.00 21.12 O
ANISOU 263 O GLY A 34 2552 2634 2838 123 -401 154 O
ATOM 264 N THR A 35 -21.932 -11.026 -4.644 1.00 20.52 N
ANISOU 264 N THR A 35 2177 2621 2998 -47 -238 74 N
ATOM 265 CA THR A 35 -21.877 -12.420 -5.045 1.00 20.45 C
ANISOU 265 CA THR A 35 2582 2740 2447 61 -311 173 C
ATOM 266 C THR A 35 -22.634 -13.339 -4.072 1.00 19.54 C
ANISOU 266 C THR A 35 2279 2643 2502 263 -324 130 C
ATOM 267 O THR A 35 -22.839 -13.001 -2.908 1.00 21.60 O
ANISOU 267 O THR A 35 2707 2542 2959 337 -150 126 O
ATOM 268 CB THR A 35 -20.410 -12.843 -5.117 1.00 21.50 C
ANISOU 268 CB THR A 35 2623 2687 2860 418 -161 196 C
ATOM 269 OG1 THR A 35 -19.702 -12.355 -3.970 1.00 22.60 O
ANISOU 269 OG1 THR A 35 2674 3036 2878 205 -373 86 O
ATOM 270 CG2 THR A 35 -19.705 -12.396 -6.380 1.00 21.16 C
ANISOU 270 CG2 THR A 35 2484 2851 2705 106 -371 151 C
ATOM 271 N ASN A 36 -22.943 -14.543 -4.551 1.00 21.25 N
ANISOU 271 N ASN A 36 3096 2518 2459 217 -374 308 N
ATOM 272 CA ASN A 36 -23.526 -15.580 -3.723 1.00 20.18 C
ANISOU 272 CA ASN A 36 2682 2456 2529 -6 -398 207 C
ATOM 273 C ASN A 36 -22.417 -16.213 -2.878 1.00 21.80 C
ANISOU 273 C ASN A 36 2779 2436 3067 172 -423 254 C
ATOM 274 O ASN A 36 -21.936 -17.303 -3.219 1.00 23.01 O
ANISOU 274 O ASN A 36 2980 2594 3170 184 -507 233 O
ATOM 275 CB ASN A 36 -24.213 -16.625 -4.570 1.00 21.37 C
ANISOU 275 CB ASN A 36 2260 2668 3190 161 -592 84 C
ATOM 276 CG ASN A 36 -25.075 -17.545 -3.764 1.00 24.11 C
ANISOU 276 CG ASN A 36 2873 2790 3497 -145 -153 145 C
ATOM 277 OD1 ASN A 36 -25.145 -17.482 -2.535 1.00 25.24 O
ANISOU 277 OD1 ASN A 36 3212 2975 3404 -415 -318 -11 O
ATOM 278 ND2 ASN A 36 -25.763 -18.412 -4.486 1.00 29.96 N
ANISOU 278 ND2 ASN A 36 4302 3663 3418 -672 -504 -141 N
ATOM 279 N THR A 37 -22.037 -15.522 -1.825 1.00 20.95 N
ANISOU 279 N THR A 37 2999 2345 2616 293 -439 204 N
ATOM 280 CA THR A 37 -21.051 -16.005 -0.873 1.00 19.79 C
ANISOU 280 CA THR A 37 2439 2351 2730 227 -409 228 C
ATOM 281 C THR A 37 -21.513 -15.684 0.536 1.00 20.75 C
ANISOU 281 C THR A 37 2676 2592 2616 158 -447 -67 C
ATOM 282 O THR A 37 -22.255 -14.729 0.739 1.00 21.78 O
ANISOU 282 O THR A 37 2711 2595 2969 383 -329 128 O
ATOM 283 CB THR A 37 -19.666 -15.413 -1.116 1.00 22.88 C
ANISOU 283 CB THR A 37 2720 2730 3244 321 -285 545 C
ATOM 284 OG1 THR A 37 -19.692 -14.023 -0.800 1.00 23.72 O
ANISOU 284 OG1 THR A 37 3103 2564 3347 471 94 -41 O
ATOM 285 CG2 THR A 37 -19.142 -15.721 -2.507 1.00 22.12 C
ANISOU 285 CG2 THR A 37 2638 2608 3159 379 -153 336 C
ATOM 286 N LYS A 38 -21.090 -16.506 1.503 1.00 22.22 N
ANISOU 286 N LYS A 38 3045 2367 3030 28 -621 359 N
ATOM 287 CA LYS A 38 -21.354 -16.213 2.914 1.00 21.67 C
ANISOU 287 CA LYS A 38 2912 2358 2965 93 -374 318 C
ATOM 288 C LYS A 38 -20.765 -14.850 3.271 1.00 21.15 C
ANISOU 288 C LYS A 38 2803 2642 2591 37 -415 402 C
ATOM 289 O LYS A 38 -21.373 -14.082 4.001 1.00 23.07 O
ANISOU 289 O LYS A 38 3090 2647 3030 18 -160 -92 O
ATOM 290 CB LYS A 38 -20.759 -17.334 3.766 1.00 23.92 C
ANISOU 290 CB LYS A 38 2907 2938 3245 -200 -410 583 C
ATOM 291 CG LYS A 38 -21.309 -18.727 3.440 1.00 24.67 C
ANISOU 291 CG LYS A 38 3549 2607 3216 -105 -719 602 C
ATOM 292 CD LYS A 38 -20.333 -19.848 3.957 1.00 30.42 C
ANISOU 292 CD LYS A 38 4351 3046 4161 -464 -983 725 C
ATOM 293 CE LYS A 38 -20.744 -21.139 3.439 1.00 31.72 C
ANISOU 293 CE LYS A 38 4818 3301 3932 411 -958 612 C
ATOM 294 NZ LYS A 38 -19.962 -22.329 3.743 1.00 32.36 N
ANISOU 294 NZ LYS A 38 3139 4526 4629 -277 -496 146 N
ATOM 295 N GLU A 39 -19.553 -14.568 2.766 1.00 22.26 N
ANISOU 295 N GLU A 39 2993 2524 2941 72 -295 -66 N
ATOM 296 CA GLU A 39 -18.870 -13.311 3.087 1.00 21.55 C
ANISOU 296 CA GLU A 39 2764 2508 2914 3 -347 305 C
ATOM 297 C GLU A 39 -19.683 -12.109 2.589 1.00 20.43 C
ANISOU 297 C GLU A 39 2401 2494 2868 8 -10 278 C
ATOM 298 O GLU A 39 -19.853 -11.168 3.342 1.00 22.83 O
ANISOU 298 O GLU A 39 3153 2681 2838 186 -387 -16 O
ATOM 299 CB GLU A 39 -17.495 -13.334 2.437 1.00 23.00 C
ANISOU 299 CB GLU A 39 2600 2569 3569 159 -549 1 C
ATOM 300 CG GLU A 39 -16.669 -12.084 2.671 1.00 23.89 C
ANISOU 300 CG GLU A 39 3053 2343 3682 114 -482 202 C
ATOM 301 CD GLU A 39 -15.358 -12.008 1.905 1.00 27.77 C
ANISOU 301 CD GLU A 39 3247 3213 4091 -200 -613 -252 C
ATOM 302 OE1 GLU A 39 -14.482 -11.251 2.362 1.00 27.37 O
ANISOU 302 OE1 GLU A 39 2926 3683 3791 -373 -619 199 O
ATOM 303 OE2 GLU A 39 -15.258 -12.607 0.803 1.00 28.86 O
ANISOU 303 OE2 GLU A 39 2975 2852 5137 -387 252 -243 O
ATOM 304 N SER A 40 -20.191 -12.175 1.350 1.00 20.29 N
ANISOU 304 N SER A 40 2571 2564 2576 279 -169 27 N
ATOM 305 CA SER A 40 -20.997 -11.083 0.838 1.00 19.48 C
ANISOU 305 CA SER A 40 2445 2227 2730 249 -266 284 C
ATOM 306 C SER A 40 -22.252 -10.914 1.693 1.00 20.89 C
ANISOU 306 C SER A 40 3169 2262 2504 15 -163 104 C
ATOM 307 O SER A 40 -22.652 -9.797 2.000 1.00 21.11 O
ANISOU 307 O SER A 40 3016 2097 2909 101 -357 -17 O
ATOM 308 CB SER A 40 -21.342 -11.268 -0.648 1.00 21.20 C
ANISOU 308 CB SER A 40 3112 2436 2508 218 -426 98 C
ATOM 309 OG SER A 40 -20.213 -11.303 -1.496 1.00 22.65 O
ANISOU 309 OG SER A 40 2813 2952 2840 -23 12 -11 O
ATOM 310 N ARG A 41 -22.940 -12.040 1.968 1.00 20.18 N
ANISOU 310 N ARG A 41 2535 2470 2663 112 -130 -37 N
ATOM 311 CA ARG A 41 -24.182 -11.981 2.704 1.00 20.42 C
ANISOU 311 CA ARG A 41 2712 2314 2731 -55 -185 131 C
ATOM 312 C ARG A 41 -23.979 -11.363 4.084 1.00 22.37 C
ANISOU 312 C ARG A 41 2885 2729 2885 -47 -288 271 C
ATOM 313 O ARG A 41 -24.740 -10.508 4.517 1.00 23.06 O
ANISOU 313 O ARG A 41 3080 2830 2852 140 -403 -163 O
ATOM 314 CB ARG A 41 -24.799 -13.380 2.792 1.00 21.04 C
ANISOU 314 CB ARG A 41 2758 2483 2752 -152 -177 36 C
ATOM 315 CG ARG A 41 -26.095 -13.348 3.560 1.00 23.10 C
ANISOU 315 CG ARG A 41 2901 2947 2930 37 -11 -20 C
ATOM 316 CD ARG A 41 -26.803 -14.673 3.508 1.00 26.88 C
ANISOU 316 CD ARG A 41 3472 3277 3465 -260 223 3 C
ATOM 317 NE ARG A 41 -28.077 -14.635 4.207 1.00 30.27 N
ANISOU 317 NE ARG A 41 4005 3462 4034 -71 522 265 N
ATOM 318 CZ ARG A 41 -28.980 -15.606 4.179 1.00 37.56 C
ANISOU 318 CZ ARG A 41 4443 4030 5800 -789 965 -78 C
ATOM 319 NH1 ARG A 41 -28.672 -16.769 3.615 1.00 39.18 N
ANISOU 319 NH1 ARG A 41 4700 4388 5797 -433 892 -59 N
ATOM 320 NH2 ARG A 41 -30.138 -15.437 4.811 1.00 40.90 N
ANISOU 320 NH2 ARG A 41 4672 4347 6522 -598 1831 11 N
ATOM 321 N LEU A 42 -22.944 -11.849 4.793 1.00 21.19 N
ANISOU 321 N LEU A 42 2599 2934 2520 24 -420 44 N
ATOM 322 CA LEU A 42 -22.674 -11.351 6.137 1.00 22.01 C
ANISOU 322 CA LEU A 42 2725 2957 2680 158 -307 271 C
ATOM 323 C LEU A 42 -22.398 -9.824 6.113 1.00 22.07 C
ANISOU 323 C LEU A 42 2698 2810 2875 72 -417 156 C
ATOM 324 O LEU A 42 -22.862 -9.052 6.983 1.00 24.30 O
ANISOU 324 O LEU A 42 3337 3113 2785 116 -97 117 O
ATOM 325 CB LEU A 42 -21.511 -12.146 6.754 1.00 22.53 C
ANISOU 325 CB LEU A 42 3212 2793 2554 216 -542 152 C
ATOM 326 CG LEU A 42 -21.922 -13.571 7.179 1.00 30.15 C
ANISOU 326 CG LEU A 42 4648 3095 3710 471 480 543 C
ATOM 327 CD1 LEU A 42 -20.715 -14.465 7.683 1.00 31.26 C
ANISOU 327 CD1 LEU A 42 5076 3531 3271 650 -247 602 C
ATOM 328 CD2 LEU A 42 -23.256 -13.492 8.074 1.00 38.69 C
ANISOU 328 CD2 LEU A 42 5793 3953 4956 528 611 415 C
ATOM 329 N ALA A 43 -21.651 -9.385 5.086 1.00 22.58 N
ANISOU 329 N ALA A 43 3099 2649 2831 4 -172 208 N
ATOM 330 CA ALA A 43 -21.320 -7.959 4.978 1.00 21.77 C
ANISOU 330 CA ALA A 43 2999 2450 2821 -164 -401 -57 C
ATOM 331 C ALA A 43 -22.602 -7.143 4.706 1.00 22.65 C
ANISOU 331 C ALA A 43 2762 2936 2909 -115 -137 3 C
ATOM 332 O ALA A 43 -22.795 -6.053 5.297 1.00 24.18 O
ANISOU 332 O ALA A 43 3378 2769 3038 -151 -476 -208 O
ATOM 333 CB ALA A 43 -20.260 -7.801 3.848 1.00 25.25 C
ANISOU 333 CB ALA A 43 3387 2930 3278 -181 -242 -1 C
ATOM 334 N LEU A 44 -23.450 -7.652 3.784 1.00 21.48 N
ANISOU 334 N LEU A 44 2935 2367 2860 -4 -378 -67 N
ATOM 335 CA LEU A 44 -24.682 -6.922 3.495 1.00 21.52 C
ANISOU 335 CA LEU A 44 2788 2644 2744 -18 -411 -131 C
ATOM 336 C LEU A 44 -25.539 -6.816 4.754 1.00 21.37 C
ANISOU 336 C LEU A 44 2867 2601 2651 -171 -406 -73 C
ATOM 337 O LEU A 44 -26.124 -5.781 5.056 1.00 23.06 O
ANISOU 337 O LEU A 44 3416 2564 2780 42 -277 -89 O
ATOM 338 CB LEU A 44 -25.389 -7.614 2.354 1.00 20.42 C
ANISOU 338 CB LEU A 44 2566 2482 2708 -278 -206 -127 C
ATOM 339 CG LEU A 44 -26.705 -7.004 1.925 1.00 22.15 C
ANISOU 339 CG LEU A 44 2553 2696 3168 -47 -363 42 C
ATOM 340 CD1 LEU A 44 -26.525 -5.615 1.392 1.00 24.24 C
ANISOU 340 CD1 LEU A 44 2862 2610 3739 104 -524 73 C
ATOM 341 CD2 LEU A 44 -27.389 -7.893 0.861 1.00 23.23 C
ANISOU 341 CD2 LEU A 44 2604 2977 3245 120 -491 -159 C
ATOM 342 N GLU A 45 -25.661 -7.938 5.452 1.00 22.08 N
ANISOU 342 N GLU A 45 2850 2742 2795 52 -243 132 N
ATOM 343 CA GLU A 45 -26.522 -7.958 6.631 1.00 22.45 C
ANISOU 343 CA GLU A 45 2878 2754 2898 208 96 -79 C
ATOM 344 C GLU A 45 -25.973 -6.991 7.680 1.00 22.13 C
ANISOU 344 C GLU A 45 2997 2828 2583 -317 -364 63 C
ATOM 345 O GLU A 45 -26.731 -6.295 8.340 1.00 25.20 O
ANISOU 345 O GLU A 45 3252 3077 3247 120 -33 -569 O
ATOM 346 CB GLU A 45 -26.693 -9.353 7.194 1.00 22.44 C
ANISOU 346 CB GLU A 45 2805 2722 3000 282 117 -96 C
ATOM 347 CG GLU A 45 -27.508 -10.256 6.273 1.00 25.79 C
ANISOU 347 CG GLU A 45 3547 2981 3274 -158 -76 26 C
ATOM 348 CD GLU A 45 -27.617 -11.716 6.695 1.00 29.62 C
ANISOU 348 CD GLU A 45 3959 3672 3623 -181 -650 299 C
ATOM 349 OE1 GLU A 45 -28.454 -12.450 6.151 1.00 34.36 O
ANISOU 349 OE1 GLU A 45 3877 3919 5257 -766 322 -906 O
ATOM 350 OE2 GLU A 45 -26.750 -12.172 7.461 1.00 37.27 O
ANISOU 350 OE2 GLU A 45 5988 3711 4461 102 -589 638 O
ATOM 351 N LYS A 46 -24.658 -6.999 7.862 1.00 23.64 N
ANISOU 351 N LYS A 46 3514 2751 2719 -117 -248 -134 N
ATOM 352 CA LYS A 46 -24.059 -6.140 8.892 1.00 25.00 C
ANISOU 352 CA LYS A 46 3349 3267 2884 -139 -359 -272 C
ATOM 353 C LYS A 46 -24.252 -4.664 8.558 1.00 24.24 C
ANISOU 353 C LYS A 46 2982 2918 3309 73 -295 -97 C
ATOM 354 O LYS A 46 -24.623 -3.878 9.435 1.00 26.65 O
ANISOU 354 O LYS A 46 3690 3185 3250 284 -228 -336 O
ATOM 355 CB LYS A 46 -22.565 -6.415 8.989 1.00 26.53 C
ANISOU 355 CB LYS A 46 3302 3200 3578 -235 -166 -594 C
ATOM 356 CG LYS A 46 -21.779 -5.568 9.999 1.00 34.43 C
ANISOU 356 CG LYS A 46 4210 4544 4328 -615 -793 -1071 C
ATOM 357 CD LYS A 46 -20.275 -5.859 10.033 1.00 38.89 C
ANISOU 357 CD LYS A 46 4447 5606 4725 168 -917 -1381 C
ATOM 358 CE LYS A 46 -19.577 -5.242 11.234 1.00 52.35 C
ANISOU 358 CE LYS A 46 5770 7217 6901 -884 -1521 -1978 C
ATOM 359 NZ LYS A 46 -18.175 -5.022 10.925 1.00 61.84 N
ANISOU 359 NZ LYS A 46 5807 9068 8622 -333 -1954 -1425 N
ATOM 360 N GLN A 47 -24.049 -4.319 7.287 1.00 23.16 N
ANISOU 360 N GLN A 47 3176 2578 3044 -115 -263 -327 N
ATOM 361 CA GLN A 47 -24.175 -2.911 6.881 1.00 22.84 C
ANISOU 361 CA GLN A 47 3018 2334 3328 -151 -402 -193 C
ATOM 362 C GLN A 47 -25.637 -2.456 6.901 1.00 26.21 C
ANISOU 362 C GLN A 47 3421 3127 3412 -110 -398 -298 C
ATOM 363 O GLN A 47 -25.955 -1.345 7.335 1.00 26.95 O
ANISOU 363 O GLN A 47 3630 2695 3913 -329 -601 -478 O
ATOM 364 CB GLN A 47 -23.482 -2.693 5.536 1.00 25.18 C
ANISOU 364 CB GLN A 47 3369 2852 3344 -471 -218 -371 C
ATOM 365 CG GLN A 47 -21.975 -2.842 5.623 1.00 27.19 C
ANISOU 365 CG GLN A 47 3360 3177 3793 -745 -486 138 C
ATOM 366 CD GLN A 47 -21.226 -2.558 4.338 1.00 27.85 C
ANISOU 366 CD GLN A 47 3331 3521 3728 -1190 -703 326 C
ATOM 367 OE1 GLN A 47 -21.429 -1.527 3.680 1.00 32.44 O
ANISOU 367 OE1 GLN A 47 4029 4426 3872 -854 -1211 928 O
ATOM 368 NE2 GLN A 47 -20.394 -3.491 3.916 1.00 29.57 N
ANISOU 368 NE2 GLN A 47 4157 3771 3306 -730 -123 -80 N
ATOM 369 N LEU A 48 -26.547 -3.350 6.512 1.00 23.56 N
ANISOU 369 N LEU A 48 3416 2642 2892 22 -177 -463 N
ATOM 370 CA LEU A 48 -27.961 -3.022 6.630 1.00 23.56 C
ANISOU 370 CA LEU A 48 3249 2766 2935 168 -383 -515 C
ATOM 371 C LEU A 48 -28.330 -2.802 8.102 1.00 24.15 C
ANISOU 371 C LEU A 48 3555 3032 2589 178 -402 -406 C
ATOM 372 O LEU A 48 -29.108 -1.900 8.432 1.00 26.37 O
ANISOU 372 O LEU A 48 3692 2846 3479 -41 -129 -702 O
ATOM 373 CB LEU A 48 -28.813 -4.142 6.054 1.00 23.74 C
ANISOU 373 CB LEU A 48 3055 2719 3244 61 -410 -717 C
ATOM 374 CG LEU A 48 -28.899 -4.162 4.513 1.00 23.07 C
ANISOU 374 CG LEU A 48 2959 2909 2897 25 -598 -639 C
ATOM 375 CD1 LEU A 48 -29.596 -5.434 4.114 1.00 23.63 C
ANISOU 375 CD1 LEU A 48 2946 2743 3288 184 -388 -295 C
ATOM 376 CD2 LEU A 48 -29.582 -2.954 3.972 1.00 24.44 C
ANISOU 376 CD2 LEU A 48 2628 3579 3079 93 -431 -144 C
ATOM 377 N ALA A 49 -27.831 -3.684 8.974 1.00 24.25 N
ANISOU 377 N ALA A 49 3375 2799 3040 233 -259 -545 N
ATOM 378 CA ALA A 49 -28.172 -3.577 10.397 1.00 26.36 C
ANISOU 378 CA ALA A 49 3453 3258 3306 137 -309 -539 C
ATOM 379 C ALA A 49 -27.729 -2.241 10.982 1.00 27.15 C
ANISOU 379 C ALA A 49 4019 3104 3192 269 -159 -648 C
ATOM 380 O ALA A 49 -28.415 -1.645 11.848 1.00 30.52 O
ANISOU 380 O ALA A 49 4344 3396 3858 -12 187 -1081 O
ATOM 381 CB ALA A 49 -27.596 -4.731 11.168 1.00 28.94 C
ANISOU 381 CB ALA A 49 4485 3751 2761 82 -232 -617 C
ATOM 382 N ALA A 50 -26.568 -1.770 10.553 1.00 26.11 N
ANISOU 382 N ALA A 50 3705 2961 3255 311 -400 -766 N
ATOM 383 CA ALA A 50 -26.097 -0.504 11.063 1.00 28.33 C
ANISOU 383 CA ALA A 50 4267 2959 3539 375 -531 -1126 C
ATOM 384 C ALA A 50 -27.015 0.649 10.643 1.00 28.24 C
ANISOU 384 C ALA A 50 3946 2883 3901 -8 -263 -631 C
ATOM 385 O ALA A 50 -27.003 1.700 11.315 1.00 30.46 O
ANISOU 385 O ALA A 50 4045 3318 4212 45 -450 -1164 O
ATOM 386 CB ALA A 50 -24.670 -0.280 10.642 1.00 31.04 C
ANISOU 386 CB ALA A 50 3697 3642 4456 741 -536 -1380 C
ATOM 387 N LEU A 51 -27.719 0.460 9.524 1.00 29.04 N
ANISOU 387 N LEU A 51 4290 3147 3595 212 -538 -1181 N
ATOM 388 CA LEU A 51 -28.692 1.421 9.014 1.00 29.23 C
ANISOU 388 CA LEU A 51 4121 3161 3824 171 -436 -752 C
ATOM 389 C LEU A 51 -30.085 1.177 9.608 1.00 28.93 C
ANISOU 389 C LEU A 51 4149 3670 3174 102 -613 -1023 C
ATOM 390 O LEU A 51 -31.029 1.928 9.304 1.00 31.79 O
ANISOU 390 O LEU A 51 3814 4789 3478 570 -585 -1200 O
ATOM 391 CB LEU A 51 -28.719 1.398 7.486 1.00 28.22 C
ANISOU 391 CB LEU A 51 3843 2908 3969 238 -373 -648 C
ATOM 392 CG LEU A 51 -27.433 1.850 6.764 1.00 30.50 C
ANISOU 392 CG LEU A 51 3646 3320 4622 597 -457 -537 C
ATOM 393 CD1 LEU A 51 -27.330 1.513 5.273 1.00 33.39 C
ANISOU 393 CD1 LEU A 51 4289 3718 4678 616 -438 174 C
ATOM 394 CD2 LEU A 51 -27.278 3.360 6.922 1.00 39.30 C
ANISOU 394 CD2 LEU A 51 4974 3861 6098 96 18 -674 C
ATOM 395 N GLY A 52 -30.206 0.154 10.452 1.00 27.30 N
ANISOU 395 N GLY A 52 3750 2979 3645 97 22 -1004 N
ATOM 396 CA GLY A 52 -31.439 -0.178 11.131 1.00 29.09 C
ANISOU 396 CA GLY A 52 3973 3294 3787 -107 203 -828 C
ATOM 397 C GLY A 52 -32.377 -1.077 10.354 1.00 27.05 C
ANISOU 397 C GLY A 52 3457 3831 2990 170 -16 -747 C
ATOM 398 O GLY A 52 -33.565 -1.144 10.695 1.00 27.63 O
ANISOU 398 O GLY A 52 3675 3358 3465 -304 119 -892 O
ATOM 399 N TYR A 53 -31.821 -1.812 9.366 1.00 23.87 N
ANISOU 399 N TYR A 53 3107 3088 2875 268 19 -472 N
ATOM 400 CA TYR A 53 -32.645 -2.630 8.499 1.00 23.83 C
ANISOU 400 CA TYR A 53 3163 3250 2642 -40 -118 -118 C
ATOM 401 C TYR A 53 -32.204 -4.081 8.501 1.00 24.65 C
ANISOU 401 C TYR A 53 3254 3382 2729 15 -206 119 C
ATOM 402 O TYR A 53 -31.045 -4.411 8.826 1.00 26.14 O
ANISOU 402 O TYR A 53 3743 2957 3231 39 -509 -259 O
ATOM 403 CB TYR A 53 -32.572 -2.154 7.041 1.00 26.33 C
ANISOU 403 CB TYR A 53 3749 3284 2973 24 -145 -302 C
ATOM 404 CG TYR A 53 -33.071 -0.742 6.832 1.00 24.73 C
ANISOU 404 CG TYR A 53 3499 3082 2814 -125 -338 -388 C
ATOM 405 CD1 TYR A 53 -34.391 -0.423 7.052 1.00 25.98 C
ANISOU 405 CD1 TYR A 53 3331 3311 3230 -340 -145 -505 C
ATOM 406 CD2 TYR A 53 -32.219 0.259 6.401 1.00 26.49 C
ANISOU 406 CD2 TYR A 53 3709 3282 3074 -82 -30 -276 C
ATOM 407 CE1 TYR A 53 -34.868 0.847 6.795 1.00 29.28 C
ANISOU 407 CE1 TYR A 53 4076 3623 3428 -156 -180 -107 C
ATOM 408 CE2 TYR A 53 -32.680 1.522 6.179 1.00 28.82 C
ANISOU 408 CE2 TYR A 53 4379 3159 3411 -322 -284 -368 C
ATOM 409 CZ TYR A 53 -34.003 1.822 6.366 1.00 27.31 C
ANISOU 409 CZ TYR A 53 3955 3620 2800 6 -51 -316 C
ATOM 410 OH TYR A 53 -34.431 3.098 6.150 1.00 32.32 O
ANISOU 410 OH TYR A 53 5234 3238 3807 542 -840 -244 O
ATOM 411 N LYS A 54 -33.150 -4.947 8.170 1.00 25.05 N
ANISOU 411 N LYS A 54 3379 3157 2982 73 -106 -386 N
ATOM 412 CA LYS A 54 -32.872 -6.349 7.910 1.00 26.16 C
ANISOU 412 CA LYS A 54 4050 2882 3006 -201 -188 -182 C
ATOM 413 C LYS A 54 -33.108 -6.576 6.415 1.00 24.79 C
ANISOU 413 C LYS A 54 3690 2738 2989 -251 126 -129 C
ATOM 414 O LYS A 54 -33.815 -5.791 5.768 1.00 24.26 O
ANISOU 414 O LYS A 54 3433 2854 2931 -147 -70 -336 O
ATOM 415 CB LYS A 54 -33.808 -7.242 8.725 1.00 28.36 C
ANISOU 415 CB LYS A 54 4694 3345 2735 -292 106 -247 C
ATOM 416 CG LYS A 54 -33.650 -7.221 10.255 1.00 33.85 C
ANISOU 416 CG LYS A 54 5561 4159 3143 -898 735 -267 C
ATOM 417 CD LYS A 54 -34.724 -8.097 10.912 1.00 42.07 C
ANISOU 417 CD LYS A 54 6387 5104 4493 -1389 881 67 C
ATOM 418 N VAL A 55 -32.532 -7.658 5.881 1.00 25.54 N
ANISOU 418 N VAL A 55 3955 2768 2979 -137 10 -116 N
ATOM 419 CA VAL A 55 -32.777 -8.038 4.499 1.00 24.89 C
ANISOU 419 CA VAL A 55 3824 2773 2859 -284 239 -202 C
ATOM 420 C VAL A 55 -34.276 -8.031 4.168 1.00 24.44 C
ANISOU 420 C VAL A 55 3697 2561 3028 -255 189 -365 C
ATOM 421 O VAL A 55 -34.663 -7.592 3.086 1.00 24.79 O
ANISOU 421 O VAL A 55 3457 3056 2906 -367 104 -169 O
ATOM 422 CB VAL A 55 -32.098 -9.373 4.185 1.00 26.70 C
ANISOU 422 CB VAL A 55 4290 2752 3101 -330 -60 -421 C
ATOM 423 CG1 VAL A 55 -32.606 -9.982 2.876 1.00 27.76 C
ANISOU 423 CG1 VAL A 55 4473 2918 3155 111 -190 -292 C
ATOM 424 CG2 VAL A 55 -30.583 -9.221 4.117 1.00 28.46 C
ANISOU 424 CG2 VAL A 55 3999 3174 3639 -143 -91 -479 C
ATOM 425 N GLU A 56 -35.116 -8.557 5.069 1.00 25.68 N
ANISOU 425 N GLU A 56 3673 3040 3046 -528 54 -207 N
ATOM 426 CA GLU A 56 -36.550 -8.686 4.818 1.00 25.62 C
ANISOU 426 CA GLU A 56 3340 3489 2906 -166 0 -51 C
ATOM 427 C GLU A 56 -37.240 -7.322 4.650 1.00 26.11 C
ANISOU 427 C GLU A 56 3784 3494 2643 -356 175 -181 C
ATOM 428 O GLU A 56 -38.372 -7.260 4.150 1.00 29.76 O
ANISOU 428 O GLU A 56 3873 3947 3488 -955 -208 54 O
ATOM 429 CB GLU A 56 -37.217 -9.502 5.915 1.00 31.99 C
ANISOU 429 CB GLU A 56 3702 4770 3683 -717 242 165 C
ATOM 430 CG GLU A 56 -37.138 -8.884 7.299 1.00 39.24 C
ANISOU 430 CG GLU A 56 5198 5535 4175 -718 1131 331 C
ATOM 431 CD GLU A 56 -37.432 -9.806 8.486 1.00 53.62 C
ANISOU 431 CD GLU A 56 7306 7080 5988 3 1255 1762 C
ATOM 432 OE1 GLU A 56 -36.609 -10.641 8.952 1.00 62.94 O
ANISOU 432 OE1 GLU A 56 9172 8331 6410 -74 1519 2797 O
ATOM 433 OE2 GLU A 56 -38.553 -9.640 8.945 1.00 58.12 O
ANISOU 433 OE2 GLU A 56 6306 8698 7077 -892 2385 3979 O
ATOM 434 N ASP A 57 -36.581 -6.223 5.039 1.00 25.15 N
ANISOU 434 N ASP A 57 3292 3464 2800 -559 88 -257 N
ATOM 435 CA ASP A 57 -37.174 -4.890 4.883 1.00 24.39 C
ANISOU 435 CA ASP A 57 3183 3365 2720 -232 303 -130 C
ATOM 436 C ASP A 57 -37.084 -4.373 3.441 1.00 23.97 C
ANISOU 436 C ASP A 57 3249 2993 2867 -343 -207 -245 C
ATOM 437 O ASP A 57 -37.778 -3.432 3.079 1.00 25.26 O
ANISOU 437 O ASP A 57 3202 3458 2937 2 56 -127 O
ATOM 438 CB ASP A 57 -36.501 -3.886 5.800 1.00 25.87 C
ANISOU 438 CB ASP A 57 3270 3728 2831 -260 26 -256 C
ATOM 439 CG ASP A 57 -36.665 -4.159 7.295 1.00 25.60 C
ANISOU 439 CG ASP A 57 3295 3307 3125 -104 49 -191 C
ATOM 440 OD1 ASP A 57 -37.754 -4.623 7.693 1.00 31.11 O
ANISOU 440 OD1 ASP A 57 3685 4720 3417 -786 433 -507 O
ATOM 441 OD2 ASP A 57 -35.743 -3.845 8.068 1.00 28.42 O
ANISOU 441 OD2 ASP A 57 3659 3980 3157 455 -317 -607 O
ATOM 442 N ILE A 58 -36.204 -4.969 2.627 1.00 23.36 N
ANISOU 442 N ILE A 58 3036 3004 2836 -264 -247 -133 N
ATOM 443 CA ILE A 58 -36.017 -4.519 1.258 1.00 23.06 C
ANISOU 443 CA ILE A 58 2690 3299 2775 -330 4 -297 C
ATOM 444 C ILE A 58 -37.224 -4.998 0.441 1.00 23.37 C
ANISOU 444 C ILE A 58 3031 3270 2580 -155 -8 -293 C
ATOM 445 O ILE A 58 -37.479 -6.188 0.348 1.00 24.54 O
ANISOU 445 O ILE A 58 3135 3066 3122 -189 30 -247 O
ATOM 446 CB ILE A 58 -34.674 -5.024 0.706 1.00 24.11 C
ANISOU 446 CB ILE A 58 2878 3481 2802 -247 -16 -209 C
ATOM 447 CG1 ILE A 58 -33.510 -4.343 1.509 1.00 25.03 C
ANISOU 447 CG1 ILE A 58 3203 3616 2689 67 -299 209 C
ATOM 448 CG2 ILE A 58 -34.581 -4.735 -0.789 1.00 23.69 C
ANISOU 448 CG2 ILE A 58 2782 3513 2705 -573 -40 8 C
ATOM 449 CD1 ILE A 58 -32.158 -4.946 1.288 1.00 25.06 C
ANISOU 449 CD1 ILE A 58 3361 3197 2964 182 -273 -226 C
ATOM 450 N GLU A 59 -37.914 -4.055 -0.214 1.00 23.85 N
ANISOU 450 N GLU A 59 3073 3153 2837 121 56 -31 N
ATOM 451 CA GLU A 59 -39.116 -4.362 -0.962 1.00 24.77 C
ANISOU 451 CA GLU A 59 3162 3657 2594 80 158 -343 C
ATOM 452 C GLU A 59 -38.871 -4.470 -2.458 1.00 23.53 C
ANISOU 452 C GLU A 59 2790 3210 2940 208 262 -232 C
ATOM 453 O GLU A 59 -39.718 -5.054 -3.154 1.00 24.26 O
ANISOU 453 O GLU A 59 2821 3228 3167 73 94 -294 O
ATOM 454 CB GLU A 59 -40.095 -3.246 -0.619 1.00 28.23 C
ANISOU 454 CB GLU A 59 3812 4179 2735 622 100 -151 C
ATOM 455 CG GLU A 59 -41.381 -3.173 -1.423 1.00 36.55 C
ANISOU 455 CG GLU A 59 4291 6096 3498 764 201 -394 C
ATOM 456 CD GLU A 59 -41.337 -2.303 -2.684 1.00 41.38 C
ANISOU 456 CD GLU A 59 5348 6179 4194 507 -114 182 C
ATOM 457 OE1 GLU A 59 -42.398 -2.434 -3.383 1.00 44.10 O
ANISOU 457 OE1 GLU A 59 4456 7273 5027 133 -241 384 O
ATOM 458 OE2 GLU A 59 -40.322 -1.531 -3.005 1.00 43.70 O
ANISOU 458 OE2 GLU A 59 7480 4611 4513 1795 1686 651 O
ATOM 459 N THR A 60 -37.792 -3.842 -2.971 1.00 22.49 N
ANISOU 459 N THR A 60 2732 3162 2650 -20 54 -261 N
ATOM 460 CA THR A 60 -37.448 -3.951 -4.381 1.00 22.58 C
ANISOU 460 CA THR A 60 2276 3113 3189 -3 68 -48 C
ATOM 461 C THR A 60 -35.937 -4.132 -4.473 1.00 22.79 C
ANISOU 461 C THR A 60 2625 3291 2743 -70 105 52 C
ATOM 462 O THR A 60 -35.180 -3.421 -3.804 1.00 22.41 O
ANISOU 462 O THR A 60 2790 3003 2720 -116 -20 -241 O
ATOM 463 CB THR A 60 -37.911 -2.719 -5.174 1.00 25.02 C
ANISOU 463 CB THR A 60 3104 3557 2846 -225 38 108 C
ATOM 464 OG1 THR A 60 -39.324 -2.621 -5.178 1.00 25.85 O
ANISOU 464 OG1 THR A 60 2807 3465 3549 240 183 159 O
ATOM 465 CG2 THR A 60 -37.388 -2.691 -6.607 1.00 24.57 C
ANISOU 465 CG2 THR A 60 2976 3213 3146 -219 -93 54 C
ATOM 466 N VAL A 61 -35.516 -5.040 -5.345 1.00 22.06 N
ANISOU 466 N VAL A 61 2470 3094 2817 -237 -93 -199 N
ATOM 467 CA VAL A 61 -34.115 -5.171 -5.740 1.00 20.20 C
ANISOU 467 CA VAL A 61 2612 2635 2426 23 -107 4 C
ATOM 468 C VAL A 61 -34.069 -4.888 -7.241 1.00 21.72 C
ANISOU 468 C VAL A 61 2453 2821 2977 138 58 -140 C
ATOM 469 O VAL A 61 -34.807 -5.498 -8.003 1.00 22.41 O
ANISOU 469 O VAL A 61 2791 2988 2735 -67 -248 -118 O
ATOM 470 CB VAL A 61 -33.494 -6.532 -5.404 1.00 21.50 C
ANISOU 470 CB VAL A 61 2665 2528 2978 -169 -131 -111 C
ATOM 471 CG1 VAL A 61 -32.069 -6.669 -5.945 1.00 23.31 C
ANISOU 471 CG1 VAL A 61 2706 2997 3155 138 -321 -127 C
ATOM 472 CG2 VAL A 61 -33.520 -6.756 -3.913 1.00 21.63 C
ANISOU 472 CG2 VAL A 61 2758 2653 2809 -134 -283 72 C
ATOM 473 N VAL A 62 -33.174 -3.991 -7.651 1.00 20.54 N
ANISOU 473 N VAL A 62 2327 2667 2810 -135 -34 -221 N
ATOM 474 CA VAL A 62 -32.909 -3.688 -9.053 1.00 20.27 C
ANISOU 474 CA VAL A 62 2277 2649 2776 174 -12 -237 C
ATOM 475 C VAL A 62 -31.524 -4.241 -9.420 1.00 20.28 C
ANISOU 475 C VAL A 62 2363 2757 2584 139 105 58 C
ATOM 476 O VAL A 62 -30.574 -4.015 -8.663 1.00 21.27 O
ANISOU 476 O VAL A 62 2546 2785 2751 -51 39 -170 O
ATOM 477 CB VAL A 62 -32.964 -2.186 -9.339 1.00 21.58 C
ANISOU 477 CB VAL A 62 2584 2881 2736 -6 -97 -151 C
ATOM 478 CG1 VAL A 62 -32.719 -1.898 -10.824 1.00 23.74 C
ANISOU 478 CG1 VAL A 62 2866 2952 3200 15 -9 67 C
ATOM 479 CG2 VAL A 62 -34.289 -1.582 -8.861 1.00 23.51 C
ANISOU 479 CG2 VAL A 62 2874 3308 2749 134 211 6 C
ATOM 480 N LEU A 63 -31.420 -4.921 -10.564 1.00 19.64 N
ANISOU 480 N LEU A 63 2283 2672 2508 -23 -82 87 N
ATOM 481 CA LEU A 63 -30.147 -5.408 -11.053 1.00 20.17 C
ANISOU 481 CA LEU A 63 2352 2503 2807 98 -159 -51 C
ATOM 482 C LEU A 63 -29.688 -4.510 -12.199 1.00 20.82 C
ANISOU 482 C LEU A 63 2471 2676 2765 126 -154 -119 C
ATOM 483 O LEU A 63 -30.419 -4.345 -13.186 1.00 21.21 O
ANISOU 483 O LEU A 63 2374 2958 2727 -123 -281 59 O
ATOM 484 CB LEU A 63 -30.320 -6.806 -11.635 1.00 24.20 C
ANISOU 484 CB LEU A 63 2750 2964 3481 91 -485 -142 C
ATOM 485 CG LEU A 63 -30.826 -7.903 -10.738 1.00 26.15 C
ANISOU 485 CG LEU A 63 3692 2550 3693 87 -235 61 C
ATOM 486 CD1 LEU A 63 -30.816 -9.140 -11.644 1.00 27.73 C
ANISOU 486 CD1 LEU A 63 3518 3008 4009 24 -761 -34 C
ATOM 487 CD2 LEU A 63 -29.911 -8.019 -9.524 1.00 28.50 C
ANISOU 487 CD2 LEU A 63 3588 3115 4126 -175 -680 602 C
ATOM 488 N THR A 64 -28.465 -3.975 -12.108 1.00 21.21 N
ANISOU 488 N THR A 64 2661 2675 2722 27 -566 48 N
ATOM 489 CA THR A 64 -27.892 -3.306 -13.248 1.00 20.29 C
ANISOU 489 CA THR A 64 2401 2389 2918 -14 -76 218 C
ATOM 490 C THR A 64 -27.546 -4.285 -14.358 1.00 19.05 C
ANISOU 490 C THR A 64 2111 2311 2815 161 -349 249 C
ATOM 491 O THR A 64 -27.606 -3.920 -15.539 1.00 20.60 O
ANISOU 491 O THR A 64 2455 2540 2831 162 -264 187 O
ATOM 492 CB THR A 64 -26.672 -2.447 -12.892 1.00 20.31 C
ANISOU 492 CB THR A 64 2394 2334 2990 88 -196 35 C
ATOM 493 OG1 THR A 64 -25.636 -3.287 -12.339 1.00 20.56 O
ANISOU 493 OG1 THR A 64 2402 2593 2818 -181 -116 150 O
ATOM 494 CG2 THR A 64 -27.023 -1.327 -11.937 1.00 21.96 C
ANISOU 494 CG2 THR A 64 2889 2509 2944 75 -124 31 C
ATOM 495 N HIS A 65 -27.149 -5.506 -13.988 1.00 19.03 N
ANISOU 495 N HIS A 65 2357 2404 2470 276 -327 95 N
ATOM 496 CA HIS A 65 -26.816 -6.541 -14.956 1.00 19.75 C
ANISOU 496 CA HIS A 65 2588 2314 2601 163 -156 240 C
ATOM 497 C HIS A 65 -26.654 -7.901 -14.260 1.00 19.02 C
ANISOU 497 C HIS A 65 2449 2296 2481 154 -72 257 C
ATOM 498 O HIS A 65 -26.728 -7.985 -13.052 1.00 20.41 O
ANISOU 498 O HIS A 65 2657 2495 2601 41 -91 -47 O
ATOM 499 CB HIS A 65 -25.574 -6.141 -15.775 1.00 19.77 C
ANISOU 499 CB HIS A 65 2513 2301 2699 34 -218 196 C
ATOM 500 CG HIS A 65 -24.289 -5.990 -15.037 1.00 20.11 C
ANISOU 500 CG HIS A 65 2389 2565 2687 78 -127 222 C
ATOM 501 ND1 HIS A 65 -24.098 -5.100 -14.002 1.00 21.24 N
ANISOU 501 ND1 HIS A 65 2706 2787 2576 -52 -373 78 N
ATOM 502 CD2 HIS A 65 -23.084 -6.582 -15.271 1.00 20.76 C
ANISOU 502 CD2 HIS A 65 2764 2594 2529 402 -283 127 C
ATOM 503 CE1 HIS A 65 -22.823 -5.117 -13.662 1.00 21.96 C
ANISOU 503 CE1 HIS A 65 2657 2678 3007 -31 -183 -169 C
ATOM 504 NE2 HIS A 65 -22.187 -6.005 -14.416 1.00 21.39 N
ANISOU 504 NE2 HIS A 65 2294 2965 2869 201 -541 -45 N
ATOM 505 N HIS A 66 -26.429 -8.953 -15.069 1.00 19.30 N
ANISOU 505 N HIS A 66 2149 2568 2615 221 -58 -72 N
ATOM 506 CA HIS A 66 -26.497 -10.330 -14.583 1.00 19.38 C
ANISOU 506 CA HIS A 66 2296 2443 2623 9 -5 -103 C
ATOM 507 C HIS A 66 -25.191 -10.849 -13.968 1.00 19.26 C
ANISOU 507 C HIS A 66 2326 2380 2612 -49 -404 -182 C
ATOM 508 O HIS A 66 -25.161 -11.957 -13.466 1.00 21.18 O
ANISOU 508 O HIS A 66 2691 2479 2875 13 -220 -79 O
ATOM 509 CB HIS A 66 -26.847 -11.258 -15.733 1.00 20.71 C
ANISOU 509 CB HIS A 66 2556 2639 2674 116 -453 8 C
ATOM 510 CG HIS A 66 -25.759 -11.435 -16.750 1.00 20.35 C
ANISOU 510 CG HIS A 66 2297 2764 2671 33 -140 -251 C
ATOM 511 ND1 HIS A 66 -25.653 -10.666 -17.876 1.00 21.70 N
ANISOU 511 ND1 HIS A 66 2871 2696 2677 92 -408 -88 N
ATOM 512 CD2 HIS A 66 -24.766 -12.355 -16.826 1.00 22.12 C
ANISOU 512 CD2 HIS A 66 2726 2578 3100 118 -435 -144 C
ATOM 513 CE1 HIS A 66 -24.627 -11.060 -18.594 1.00 22.05 C
ANISOU 513 CE1 HIS A 66 3089 2196 3091 58 -312 21 C
ATOM 514 NE2 HIS A 66 -24.063 -12.084 -17.964 1.00 21.89 N
ANISOU 514 NE2 HIS A 66 2938 2831 2547 -17 -82 -89 N
ATOM 515 N HIS A 67 -24.115 -10.038 -14.021 1.00 19.49 N
ANISOU 515 N HIS A 67 2549 2520 2335 55 -253 191 N
ATOM 516 CA HIS A 67 -22.855 -10.530 -13.484 1.00 19.21 C
ANISOU 516 CA HIS A 67 2370 2334 2595 104 -183 185 C
ATOM 517 C HIS A 67 -23.038 -10.871 -11.992 1.00 19.58 C
ANISOU 517 C HIS A 67 2367 2641 2430 -140 -110 190 C
ATOM 518 O HIS A 67 -23.784 -10.229 -11.289 1.00 20.55 O
ANISOU 518 O HIS A 67 2555 2964 2289 -113 -309 66 O
ATOM 519 CB HIS A 67 -21.746 -9.518 -13.693 1.00 19.36 C
ANISOU 519 CB HIS A 67 2015 2720 2621 25 -150 147 C
ATOM 520 CG HIS A 67 -21.354 -9.312 -15.118 1.00 20.45 C
ANISOU 520 CG HIS A 67 2490 2567 2713 155 -32 180 C
ATOM 521 ND1 HIS A 67 -20.530 -8.322 -15.569 1.00 21.22 N
ANISOU 521 ND1 HIS A 67 2255 2822 2985 -177 -269 117 N
ATOM 522 CD2 HIS A 67 -21.667 -10.068 -16.211 1.00 21.57 C
ANISOU 522 CD2 HIS A 67 2226 3131 2838 38 -85 227 C
ATOM 523 CE1 HIS A 67 -20.344 -8.479 -16.871 1.00 22.34 C
ANISOU 523 CE1 HIS A 67 2650 2834 3005 -100 135 53 C
ATOM 524 NE2 HIS A 67 -21.042 -9.543 -17.305 1.00 21.40 N
ANISOU 524 NE2 HIS A 67 2394 2698 3039 257 33 318 N
ATOM 525 N ALA A 68 -22.360 -11.933 -11.559 1.00 20.05 N
ANISOU 525 N ALA A 68 2384 2364 2868 273 -189 59 N
ATOM 526 CA ALA A 68 -22.594 -12.520 -10.248 1.00 20.88 C
ANISOU 526 CA ALA A 68 2618 2420 2895 105 -53 204 C
ATOM 527 C ALA A 68 -22.389 -11.567 -9.072 1.00 18.66 C
ANISOU 527 C ALA A 68 2246 2008 2835 122 -253 52 C
ATOM 528 O ALA A 68 -23.056 -11.705 -8.029 1.00 21.33 O
ANISOU 528 O ALA A 68 2505 2741 2859 -20 -229 71 O
ATOM 529 CB ALA A 68 -21.713 -13.739 -10.060 1.00 21.92 C
ANISOU 529 CB ALA A 68 2974 2178 3175 65 -242 -46 C
ATOM 530 N ASP A 69 -21.459 -10.598 -9.249 1.00 19.76 N
ANISOU 530 N ASP A 69 2354 2657 2498 -58 -71 113 N
ATOM 531 CA ASP A 69 -21.247 -9.614 -8.206 1.00 19.21 C
ANISOU 531 CA ASP A 69 2323 2460 2516 60 -172 -22 C
ATOM 532 C ASP A 69 -22.447 -8.668 -7.989 1.00 19.52 C
ANISOU 532 C ASP A 69 2367 2185 2866 85 -92 120 C
ATOM 533 O ASP A 69 -22.531 -8.023 -6.943 1.00 20.87 O
ANISOU 533 O ASP A 69 2482 2580 2868 -155 -392 62 O
ATOM 534 CB ASP A 69 -19.934 -8.873 -8.401 1.00 19.58 C
ANISOU 534 CB ASP A 69 2483 2543 2412 -297 -188 -103 C
ATOM 535 CG ASP A 69 -19.607 -8.377 -9.818 1.00 20.72 C
ANISOU 535 CG ASP A 69 2273 2869 2732 268 -163 740 C
ATOM 536 OD1 ASP A 69 -19.887 -8.958 -10.944 1.00 23.44 O
ANISOU 536 OD1 ASP A 69 2840 3135 2929 -27 -136 -169 O
ATOM 537 OD2 ASP A 69 -19.054 -7.226 -9.904 1.00 22.82 O
ANISOU 537 OD2 ASP A 69 2704 2504 3461 -164 -373 257 O
ATOM 538 N HIS A 70 -23.350 -8.620 -8.966 1.00 19.37 N
ANISOU 538 N HIS A 70 2650 2282 2430 -272 -37 -27 N
ATOM 539 CA HIS A 70 -24.501 -7.737 -8.912 1.00 19.82 C
ANISOU 539 CA HIS A 70 2598 2361 2571 33 -182 118 C
ATOM 540 C HIS A 70 -25.817 -8.445 -8.571 1.00 19.41 C
ANISOU 540 C HIS A 70 2447 2633 2296 -89 -172 265 C
ATOM 541 O HIS A 70 -26.726 -7.793 -8.089 1.00 21.71 O
ANISOU 541 O HIS A 70 2579 2771 2899 144 213 -107 O
ATOM 542 CB HIS A 70 -24.570 -6.901 -10.181 1.00 19.46 C
ANISOU 542 CB HIS A 70 2233 2435 2725 -118 -142 274 C
ATOM 543 CG HIS A 70 -23.327 -6.113 -10.422 1.00 20.85 C
ANISOU 543 CG HIS A 70 2498 2446 2977 28 -56 306 C
ATOM 544 ND1 HIS A 70 -23.192 -4.792 -10.092 1.00 20.73 N
ANISOU 544 ND1 HIS A 70 2548 2568 2760 -249 2 239 N
ATOM 545 CD2 HIS A 70 -22.131 -6.521 -10.854 1.00 19.81 C
ANISOU 545 CD2 HIS A 70 2605 2298 2625 -66 48 308 C
ATOM 546 CE1 HIS A 70 -21.940 -4.410 -10.329 1.00 20.02 C
ANISOU 546 CE1 HIS A 70 2341 2248 3016 -278 -164 16 C
ATOM 547 NE2 HIS A 70 -21.279 -5.448 -10.798 1.00 20.78 N
ANISOU 547 NE2 HIS A 70 2551 2440 2906 34 -101 155 N
ATOM 548 N CYS A 71 -25.932 -9.743 -8.884 1.00 20.79 N
ANISOU 548 N CYS A 71 2435 2524 2942 313 -244 279 N
ATOM 549 CA CYS A 71 -27.177 -10.473 -8.667 1.00 20.61 C
ANISOU 549 CA CYS A 71 2400 2337 3092 -249 -403 167 C
ATOM 550 C CYS A 71 -27.049 -11.656 -7.702 1.00 19.63 C
ANISOU 550 C CYS A 71 2419 2435 2604 82 -352 -43 C
ATOM 551 O CYS A 71 -28.027 -12.353 -7.497 1.00 21.95 O
ANISOU 551 O CYS A 71 2504 2734 3101 -110 -232 288 O
ATOM 552 CB CYS A 71 -27.723 -10.975 -10.010 1.00 23.66 C
ANISOU 552 CB CYS A 71 2474 2629 3887 -409 -706 93 C
ATOM 553 SG CYS A 71 -26.744 -12.346 -10.681 1.00 27.26 S
ANISOU 553 SG CYS A 71 2918 4121 3318 -576 -124 -625 S
ATOM 554 N GLY A 72 -25.824 -11.963 -7.234 1.00 19.85 N
ANISOU 554 N GLY A 72 2472 2297 2772 -150 -207 343 N
ATOM 555 CA GLY A 72 -25.604 -13.264 -6.620 1.00 20.62 C
ANISOU 555 CA GLY A 72 2670 2320 2846 -82 -95 79 C
ATOM 556 C GLY A 72 -26.420 -13.577 -5.373 1.00 21.25 C
ANISOU 556 C GLY A 72 2563 2806 2705 -35 -42 80 C
ATOM 557 O GLY A 72 -26.652 -14.764 -5.124 1.00 22.54 O
ANISOU 557 O GLY A 72 2696 2474 3395 -156 36 145 O
ATOM 558 N LEU A 73 -26.823 -12.561 -4.605 1.00 20.89 N
ANISOU 558 N LEU A 73 2761 2517 2658 8 -239 11 N
ATOM 559 CA LEU A 73 -27.559 -12.815 -3.355 1.00 20.71 C
ANISOU 559 CA LEU A 73 2761 2777 2330 199 -206 311 C
ATOM 560 C LEU A 73 -29.079 -12.722 -3.554 1.00 22.49 C
ANISOU 560 C LEU A 73 2919 2781 2844 69 -314 74 C
ATOM 561 O LEU A 73 -29.811 -12.661 -2.582 1.00 22.20 O
ANISOU 561 O LEU A 73 2870 2773 2793 -144 -173 53 O
ATOM 562 CB LEU A 73 -27.091 -11.847 -2.275 1.00 21.46 C
ANISOU 562 CB LEU A 73 2893 2441 2820 181 -216 105 C
ATOM 563 CG LEU A 73 -25.714 -12.114 -1.688 1.00 22.12 C
ANISOU 563 CG LEU A 73 2803 2691 2909 7 -123 -60 C
ATOM 564 CD1 LEU A 73 -25.369 -11.021 -0.749 1.00 22.79 C
ANISOU 564 CD1 LEU A 73 3025 2546 3089 -86 -565 7 C
ATOM 565 CD2 LEU A 73 -25.635 -13.466 -1.037 1.00 22.30 C
ANISOU 565 CD2 LEU A 73 2992 2758 2721 88 -72 -39 C
ATOM 566 N LEU A 74 -29.562 -12.744 -4.814 1.00 22.14 N
ANISOU 566 N LEU A 74 2919 2743 2750 -12 52 90 N
ATOM 567 CA LEU A 74 -30.998 -12.583 -5.052 1.00 23.11 C
ANISOU 567 CA LEU A 74 2810 3056 2914 -177 -253 -21 C
ATOM 568 C LEU A 74 -31.865 -13.549 -4.255 1.00 22.32 C
ANISOU 568 C LEU A 74 2942 2825 2712 -102 -251 53 C
ATOM 569 O LEU A 74 -32.975 -13.201 -3.881 1.00 25.10 O
ANISOU 569 O LEU A 74 2742 3297 3496 -222 -19 -240 O
ATOM 570 CB LEU A 74 -31.303 -12.676 -6.536 1.00 25.24 C
ANISOU 570 CB LEU A 74 3149 3528 2912 -399 -162 96 C
ATOM 571 CG LEU A 74 -31.179 -11.393 -7.337 1.00 27.53 C
ANISOU 571 CG LEU A 74 3778 3484 3197 -22 -395 90 C
ATOM 572 CD1 LEU A 74 -31.698 -11.653 -8.745 1.00 26.21 C
ANISOU 572 CD1 LEU A 74 3342 3291 3325 667 -451 79 C
ATOM 573 CD2 LEU A 74 -31.860 -10.207 -6.693 1.00 25.77 C
ANISOU 573 CD2 LEU A 74 2988 3079 3726 -324 -475 36 C
ATOM 574 N ASP A 75 -31.368 -14.759 -3.988 1.00 21.91 N
ANISOU 574 N ASP A 75 2756 2872 2697 -280 -72 -94 N
ATOM 575 CA ASP A 75 -32.176 -15.776 -3.302 1.00 23.56 C
ANISOU 575 CA ASP A 75 2948 2948 3057 -724 -166 -209 C
ATOM 576 C ASP A 75 -32.549 -15.382 -1.867 1.00 22.66 C
ANISOU 576 C ASP A 75 2692 2896 3021 -441 62 -185 C
ATOM 577 O ASP A 75 -33.552 -15.905 -1.349 1.00 25.73 O
ANISOU 577 O ASP A 75 3111 3270 3396 -381 278 83 O
ATOM 578 CB ASP A 75 -31.478 -17.133 -3.317 1.00 25.16 C
ANISOU 578 CB ASP A 75 3716 2619 3224 -614 -33 -152 C
ATOM 579 CG ASP A 75 -31.028 -17.639 -4.697 1.00 33.25 C
ANISOU 579 CG ASP A 75 4652 3429 4552 -16 -66 -404 C
ATOM 580 OD1 ASP A 75 -31.829 -17.542 -5.620 1.00 39.11 O
ANISOU 580 OD1 ASP A 75 6065 4041 4753 565 210 -342 O
ATOM 581 OD2 ASP A 75 -29.855 -18.182 -4.869 1.00 39.13 O
ANISOU 581 OD2 ASP A 75 5308 4694 4867 2 -738 -921 O
ATOM 582 N ILE A 76 -31.782 -14.465 -1.247 1.00 22.44 N
ANISOU 582 N ILE A 76 2955 2785 2787 -449 -108 -35 N
ATOM 583 CA ILE A 76 -31.971 -14.183 0.176 1.00 22.55 C
ANISOU 583 CA ILE A 76 3152 2583 2832 -576 21 -169 C
ATOM 584 C ILE A 76 -33.180 -13.291 0.458 1.00 23.21 C
ANISOU 584 C ILE A 76 3215 2860 2742 -337 -348 26 C
ATOM 585 O ILE A 76 -33.672 -13.243 1.617 1.00 23.37 O
ANISOU 585 O ILE A 76 2973 2833 3073 -107 242 14 O
ATOM 586 CB ILE A 76 -30.715 -13.645 0.843 1.00 23.73 C
ANISOU 586 CB ILE A 76 3069 3167 2780 -401 -177 -108 C
ATOM 587 CG1 ILE A 76 -30.455 -12.182 0.517 1.00 23.87 C
ANISOU 587 CG1 ILE A 76 2762 3520 2787 -199 -154 -58 C
ATOM 588 CG2 ILE A 76 -29.494 -14.557 0.595 1.00 25.10 C
ANISOU 588 CG2 ILE A 76 3227 3315 2993 -210 -288 -284 C
ATOM 589 CD1 ILE A 76 -29.279 -11.599 1.286 1.00 26.66 C
ANISOU 589 CD1 ILE A 76 3180 3976 2973 -750 -11 -180 C
ATOM 590 N PHE A 77 -33.645 -12.571 -0.571 1.00 22.01 N
ANISOU 590 N PHE A 77 2960 2768 2634 -420 -202 -155 N
ATOM 591 CA PHE A 77 -34.666 -11.574 -0.344 1.00 22.81 C
ANISOU 591 CA PHE A 77 3121 2696 2852 -256 -190 -27 C
ATOM 592 C PHE A 77 -36.020 -12.242 -0.114 1.00 22.78 C
ANISOU 592 C PHE A 77 2729 2956 2969 82 44 51 C
ATOM 593 O PHE A 77 -36.271 -13.351 -0.583 1.00 24.11 O
ANISOU 593 O PHE A 77 3013 2876 3270 -259 113 -32 O
ATOM 594 CB PHE A 77 -34.688 -10.565 -1.487 1.00 23.11 C
ANISOU 594 CB PHE A 77 2809 3058 2913 -194 -226 49 C
ATOM 595 CG PHE A 77 -33.366 -9.829 -1.585 1.00 21.90 C
ANISOU 595 CG PHE A 77 2567 2861 2893 -235 -243 210 C
ATOM 596 CD1 PHE A 77 -33.093 -8.787 -0.739 1.00 24.60 C
ANISOU 596 CD1 PHE A 77 3206 3026 3117 -542 65 150 C
ATOM 597 CD2 PHE A 77 -32.383 -10.242 -2.461 1.00 24.36 C
ANISOU 597 CD2 PHE A 77 3083 2767 3404 -298 250 112 C
ATOM 598 CE1 PHE A 77 -31.857 -8.156 -0.773 1.00 24.81 C
ANISOU 598 CE1 PHE A 77 3370 2827 3231 -931 16 -181 C
ATOM 599 CE2 PHE A 77 -31.126 -9.628 -2.452 1.00 23.21 C
ANISOU 599 CE2 PHE A 77 2747 2899 3173 -340 238 150 C
ATOM 600 CZ PHE A 77 -30.868 -8.590 -1.603 1.00 24.11 C
ANISOU 600 CZ PHE A 77 3136 3213 2812 -599 67 191 C
ATOM 601 N SER A 78 -36.927 -11.507 0.548 1.00 23.80 N
ANISOU 601 N SER A 78 2928 3035 3082 -272 119 -191 N
ATOM 602 CA SER A 78 -38.218 -12.047 0.926 1.00 25.09 C
ANISOU 602 CA SER A 78 2650 3485 3397 -308 127 -159 C
ATOM 603 C SER A 78 -39.011 -12.393 -0.332 1.00 23.63 C
ANISOU 603 C SER A 78 2511 2863 3604 -401 147 -318 C
ATOM 604 O SER A 78 -38.801 -11.819 -1.411 1.00 24.67 O
ANISOU 604 O SER A 78 2968 3055 3351 -630 76 -347 O
ATOM 605 CB SER A 78 -39.000 -11.039 1.723 1.00 29.11 C
ANISOU 605 CB SER A 78 3712 3883 3467 -416 521 -306 C
ATOM 606 OG SER A 78 -39.611 -10.096 0.850 1.00 33.59 O
ANISOU 606 OG SER A 78 4032 4308 4424 331 -36 -400 O
ATOM 607 N GLU A 79 -39.986 -13.284 -0.156 1.00 29.88 N
ANISOU 607 N GLU A 79 3169 3530 4656 -1110 6 315 N
ATOM 608 CA GLU A 79 -40.818 -13.685 -1.264 1.00 31.68 C
ANISOU 608 CA GLU A 79 3483 3698 4854 -604 -797 80 C
ATOM 609 C GLU A 79 -41.701 -12.549 -1.785 1.00 29.67 C
ANISOU 609 C GLU A 79 3440 3304 4528 -472 -15 288 C
ATOM 610 O GLU A 79 -42.151 -12.664 -2.921 1.00 31.69 O
ANISOU 610 O GLU A 79 3865 3942 4232 -382 -526 -213 O
ATOM 611 CB GLU A 79 -41.597 -14.934 -0.856 1.00 42.82 C
ANISOU 611 CB GLU A 79 4627 4649 6993 -902 -683 374 C
ATOM 612 CG GLU A 79 -40.728 -16.197 -0.849 1.00 52.87 C
ANISOU 612 CG GLU A 79 5877 5516 8697 -399 -644 785 C
ATOM 613 CD GLU A 79 -39.880 -16.464 -2.112 1.00 62.19 C
ANISOU 613 CD GLU A 79 6141 7528 9962 436 -1168 14 C
ATOM 614 OE1 GLU A 79 -40.470 -16.439 -3.234 1.00 70.17 O
ANISOU 614 OE1 GLU A 79 6706 8323 11630 -622 -3174 -29 O
ATOM 615 OE2 GLU A 79 -38.624 -16.676 -2.013 1.00 62.57 O
ANISOU 615 OE2 GLU A 79 5953 5871 11951 438 -2796 -371 O
ATOM 616 N ARG A 80 -41.866 -11.444 -1.020 1.00 28.30 N
ANISOU 616 N ARG A 80 2825 3969 3959 -785 44 307 N
ATOM 617 CA AARG A 80 -42.658 -10.296 -1.449 0.50 31.78 C
ANISOU 617 CA AARG A 80 3242 4239 4596 -550 474 375 C
ATOM 618 CA BARG A 80 -42.658 -10.296 -1.449 0.50 31.78 C
ANISOU 618 CA BARG A 80 3242 4239 4596 -549 475 375 C
ATOM 619 C ARG A 80 -41.857 -9.295 -2.280 1.00 30.73 C
ANISOU 619 C ARG A 80 3028 4042 4606 -480 364 365 C
ATOM 620 O ARG A 80 -42.423 -8.349 -2.858 1.00 32.59 O
ANISOU 620 O ARG A 80 2955 4366 5063 68 387 522 O
ATOM 621 CB AARG A 80 -43.221 -9.515 -0.254 0.50 35.14 C
ANISOU 621 CB AARG A 80 3788 4330 5232 -205 1678 481 C
ATOM 622 CB BARG A 80 -43.221 -9.514 -0.254 0.50 35.14 C
ANISOU 622 CB BARG A 80 3788 4330 5232 -204 1682 481 C
ATOM 623 CG AARG A 80 -43.411 -10.379 0.987 0.50 46.47 C
ANISOU 623 CG AARG A 80 5579 5949 6127 95 922 293 C
ATOM 624 CG BARG A 80 -43.400 -10.374 0.990 0.50 46.53 C
ANISOU 624 CG BARG A 80 5588 5963 6127 106 921 285 C
ATOM 625 N THR A 81 -40.545 -9.508 -2.352 1.00 24.76 N
ANISOU 625 N THR A 81 2754 3269 3382 -249 229 -224 N
ATOM 626 CA THR A 81 -39.646 -8.510 -2.896 1.00 23.71 C
ANISOU 626 CA THR A 81 2707 3201 3101 -219 115 11 C
ATOM 627 C THR A 81 -39.785 -8.503 -4.417 1.00 23.83 C
ANISOU 627 C THR A 81 2792 2872 3390 -84 -222 33 C
ATOM 628 O THR A 81 -39.762 -9.538 -5.072 1.00 25.56 O
ANISOU 628 O THR A 81 3210 3273 3228 16 -102 -254 O
ATOM 629 CB THR A 81 -38.205 -8.850 -2.482 1.00 24.06 C
ANISOU 629 CB THR A 81 2395 3079 3667 -654 -135 -27 C
ATOM 630 OG1 THR A 81 -38.149 -8.844 -1.044 1.00 26.86 O
ANISOU 630 OG1 THR A 81 2937 3882 3387 -755 -196 152 O
ATOM 631 CG2 THR A 81 -37.249 -7.818 -3.059 1.00 23.68 C
ANISOU 631 CG2 THR A 81 3075 2746 3174 -572 -133 14 C
ATOM 632 N ASN A 82 -39.937 -7.315 -4.998 1.00 22.51 N
ANISOU 632 N ASN A 82 2530 2956 3066 227 25 -249 N
ATOM 633 CA ASN A 82 -39.907 -7.150 -6.443 1.00 23.11 C
ANISOU 633 CA ASN A 82 2537 3127 3116 -271 -197 85 C
ATOM 634 C ASN A 82 -38.458 -7.250 -6.916 1.00 22.47 C
ANISOU 634 C ASN A 82 2782 2883 2871 -65 -162 52 C
ATOM 635 O ASN A 82 -37.563 -6.687 -6.267 1.00 23.98 O
ANISOU 635 O ASN A 82 2562 3515 3033 -156 74 -413 O
ATOM 636 CB ASN A 82 -40.401 -5.784 -6.892 1.00 24.84 C
ANISOU 636 CB ASN A 82 2770 3567 3103 -261 -79 -37 C
ATOM 637 CG ASN A 82 -41.781 -5.472 -6.383 1.00 27.95 C
ANISOU 637 CG ASN A 82 3183 3983 3452 243 -31 258 C
ATOM 638 OD1 ASN A 82 -42.715 -6.209 -6.685 1.00 28.93 O
ANISOU 638 OD1 ASN A 82 2709 4328 3955 1 -229 -392 O
ATOM 639 ND2 ASN A 82 -41.922 -4.430 -5.562 1.00 32.14 N
ANISOU 639 ND2 ASN A 82 3418 4474 4321 533 96 -209 N
ATOM 640 N ILE A 83 -38.220 -7.998 -7.970 1.00 22.01 N
ANISOU 640 N ILE A 83 2421 3032 2908 -191 -159 -117 N
ATOM 641 CA AILE A 83 -36.902 -8.177 -8.546 0.50 21.27 C
ANISOU 641 CA AILE A 83 2443 3123 2513 -236 -391 -147 C
ATOM 642 CA BILE A 83 -36.902 -8.177 -8.546 0.50 21.27 C
ANISOU 642 CA BILE A 83 2443 3123 2513 -236 -391 -147 C
ATOM 643 C ILE A 83 -36.947 -7.684 -9.997 1.00 21.25 C
ANISOU 643 C ILE A 83 2536 2917 2620 298 -37 204 C
ATOM 644 O ILE A 83 -37.642 -8.240 -10.861 1.00 21.86 O
ANISOU 644 O ILE A 83 2493 3168 2647 -200 -232 -104 O
ATOM 645 CB AILE A 83 -36.495 -9.654 -8.509 0.50 23.02 C
ANISOU 645 CB AILE A 83 2714 3332 2701 6 -85 137 C
ATOM 646 CB BILE A 83 -36.495 -9.654 -8.509 0.50 23.02 C
ANISOU 646 CB BILE A 83 2714 3332 2701 6 -84 138 C
ATOM 647 CG1AILE A 83 -36.679 -10.277 -7.151 0.50 28.65 C
ANISOU 647 CG1AILE A 83 3378 4219 3288 13 390 191 C
ATOM 648 CG1BILE A 83 -36.680 -10.277 -7.151 0.50 28.65 C
ANISOU 648 CG1BILE A 83 3380 4218 3288 13 391 192 C
ATOM 649 CG2AILE A 83 -35.068 -9.800 -9.029 0.50 23.57 C
ANISOU 649 CG2AILE A 83 2620 3485 2852 -145 -87 32 C
ATOM 650 CG2BILE A 83 -35.068 -9.800 -9.029 0.50 23.57 C
ANISOU 650 CG2BILE A 83 2620 3485 2852 -145 -87 33 C
ATOM 651 CD1AILE A 83 -35.773 -9.751 -6.103 0.50 29.11 C
ANISOU 651 CD1AILE A 83 3595 4197 3267 -65 233 320 C
ATOM 652 CD1BILE A 83 -35.773 -9.752 -6.102 0.50 29.10 C
ANISOU 652 CD1BILE A 83 3595 4196 3266 -68 235 321 C
ATOM 653 N VAL A 84 -36.221 -6.589 -10.235 1.00 20.88 N
ANISOU 653 N VAL A 84 2245 2918 2772 -74 -207 119 N
ATOM 654 CA VAL A 84 -36.433 -5.814 -11.418 1.00 20.73 C
ANISOU 654 CA VAL A 84 2366 2722 2785 112 -275 101 C
ATOM 655 C VAL A 84 -35.120 -5.668 -12.186 1.00 20.74 C
ANISOU 655 C VAL A 84 2674 2785 2422 107 -247 33 C
ATOM 656 O VAL A 84 -34.085 -5.310 -11.642 1.00 22.23 O
ANISOU 656 O VAL A 84 2617 3177 2651 -21 -387 -95 O
ATOM 657 CB VAL A 84 -36.990 -4.414 -11.069 1.00 24.63 C
ANISOU 657 CB VAL A 84 3224 3004 3130 630 -276 123 C
ATOM 658 CG1 VAL A 84 -37.322 -3.648 -12.321 1.00 25.18 C
ANISOU 658 CG1 VAL A 84 2918 3161 3487 963 -4 105 C
ATOM 659 CG2 VAL A 84 -38.139 -4.474 -10.097 1.00 25.80 C
ANISOU 659 CG2 VAL A 84 2875 3414 3515 459 -72 -162 C
ATOM 660 N GLY A 85 -35.171 -5.893 -13.493 1.00 21.07 N
ANISOU 660 N GLY A 85 2249 2970 2789 -26 -250 -44 N
ATOM 661 CA GLY A 85 -33.990 -5.705 -14.317 1.00 21.73 C
ANISOU 661 CA GLY A 85 2539 2938 2780 313 -293 -77 C
ATOM 662 C GLY A 85 -34.304 -5.856 -15.800 1.00 20.69 C
ANISOU 662 C GLY A 85 2368 2739 2756 401 -280 -108 C
ATOM 663 O GLY A 85 -35.437 -6.099 -16.188 1.00 21.88 O
ANISOU 663 O GLY A 85 2366 3216 2731 -109 -365 -125 O
ATOM 664 N HIS A 86 -33.278 -5.742 -16.627 1.00 20.07 N
ANISOU 664 N HIS A 86 2268 2704 2654 125 -363 -72 N
ATOM 665 CA HIS A 86 -33.390 -6.039 -18.050 1.00 20.03 C
ANISOU 665 CA HIS A 86 2499 2560 2549 -52 -98 61 C
ATOM 666 C HIS A 86 -33.977 -7.447 -18.215 1.00 20.25 C
ANISOU 666 C HIS A 86 2627 2455 2613 -233 -190 -326 C
ATOM 667 O HIS A 86 -33.628 -8.380 -17.489 1.00 21.30 O
ANISOU 667 O HIS A 86 2554 2883 2655 111 -319 -59 O
ATOM 668 CB HIS A 86 -32.009 -5.966 -18.683 1.00 20.59 C
ANISOU 668 CB HIS A 86 2627 2488 2707 178 -97 -139 C
ATOM 669 CG HIS A 86 -31.964 -5.983 -20.151 1.00 22.10 C
ANISOU 669 CG HIS A 86 2823 2889 2687 329 -139 3 C
ATOM 670 ND1 HIS A 86 -32.261 -7.080 -20.923 1.00 23.22 N
ANISOU 670 ND1 HIS A 86 2978 3182 2665 -128 -231 -255 N
ATOM 671 CD2 HIS A 86 -31.622 -4.979 -20.995 1.00 23.58 C
ANISOU 671 CD2 HIS A 86 2798 2964 3198 -27 -617 62 C
ATOM 672 CE1 HIS A 86 -32.087 -6.711 -22.222 1.00 25.71 C
ANISOU 672 CE1 HIS A 86 3787 3449 2531 -208 -118 -213 C
ATOM 673 NE2 HIS A 86 -31.651 -5.456 -22.293 1.00 25.95 N
ANISOU 673 NE2 HIS A 86 3123 3541 3197 -72 -364 37 N
ATOM 674 N PRO A 87 -34.888 -7.650 -19.183 1.00 21.56 N
ANISOU 674 N PRO A 87 2634 2885 2672 22 -502 306 N
ATOM 675 CA PRO A 87 -35.497 -8.956 -19.354 1.00 22.39 C
ANISOU 675 CA PRO A 87 2548 2784 3174 -40 -372 25 C
ATOM 676 C PRO A 87 -34.526 -10.092 -19.598 1.00 21.50 C
ANISOU 676 C PRO A 87 2493 3056 2621 84 -519 -193 C
ATOM 677 O PRO A 87 -34.818 -11.226 -19.239 1.00 22.86 O
ANISOU 677 O PRO A 87 2805 2915 2966 -95 -504 97 O
ATOM 678 CB PRO A 87 -36.431 -8.756 -20.558 1.00 25.34 C
ANISOU 678 CB PRO A 87 2885 3342 3400 -4 -485 33 C
ATOM 679 CG PRO A 87 -35.825 -7.564 -21.306 1.00 24.37 C
ANISOU 679 CG PRO A 87 2972 3363 2924 -12 -432 -41 C
ATOM 680 CD PRO A 87 -35.393 -6.676 -20.166 1.00 23.30 C
ANISOU 680 CD PRO A 87 2613 2996 3242 -217 -582 164 C
ATOM 681 N TRP A 88 -33.389 -9.778 -20.257 1.00 20.63 N
ANISOU 681 N TRP A 88 2602 2522 2712 101 -528 79 N
ATOM 682 CA ATRP A 88 -32.452 -10.847 -20.613 0.50 22.82 C
ANISOU 682 CA ATRP A 88 2832 2822 3016 102 -343 23 C
ATOM 683 CA BTRP A 88 -32.465 -10.861 -20.617 0.50 22.57 C
ANISOU 683 CA BTRP A 88 2784 2836 2958 69 -280 68 C
ATOM 684 C TRP A 88 -31.687 -11.404 -19.413 1.00 22.05 C
ANISOU 684 C TRP A 88 2932 3060 2385 -157 -289 73 C
ATOM 685 O TRP A 88 -30.957 -12.400 -19.504 1.00 23.99 O
ANISOU 685 O TRP A 88 3206 2831 3078 85 -45 -228 O
ATOM 686 CB ATRP A 88 -31.515 -10.415 -21.727 0.50 25.16 C
ANISOU 686 CB ATRP A 88 3222 3443 2896 -140 -439 87 C
ATOM 687 CB BTRP A 88 -31.556 -10.465 -21.771 0.50 24.19 C
ANISOU 687 CB BTRP A 88 3044 3417 2727 -260 -359 130 C
ATOM 688 CG ATRP A 88 -31.802 -11.034 -23.069 0.50 30.15 C
ANISOU 688 CG ATRP A 88 3733 4413 3311 -281 -742 -274 C
ATOM 689 CG BTRP A 88 -32.275 -10.009 -23.021 0.50 25.49 C
ANISOU 689 CG BTRP A 88 2925 3991 2769 -315 -530 69 C
ATOM 690 CD1ATRP A 88 -32.610 -12.092 -23.408 0.50 28.48 C
ANISOU 690 CD1ATRP A 88 3741 4058 3020 306 -746 -125 C
ATOM 691 CD1BTRP A 88 -33.612 -9.860 -23.252 0.50 24.90 C
ANISOU 691 CD1BTRP A 88 3124 3875 2461 -268 -299 -397 C
ATOM 692 CD2ATRP A 88 -31.162 -10.612 -24.291 0.50 30.38 C
ANISOU 692 CD2ATRP A 88 3480 4758 3304 72 -331 52 C
ATOM 693 CD2BTRP A 88 -31.616 -9.608 -24.246 0.50 26.68 C
ANISOU 693 CD2BTRP A 88 2915 4727 2495 -235 -308 -325 C
ATOM 694 NE1ATRP A 88 -32.517 -12.339 -24.758 0.50 30.96 N
ANISOU 694 NE1ATRP A 88 3592 4702 3470 666 -425 134 N
ATOM 695 NE1BTRP A 88 -33.838 -9.396 -24.526 0.50 25.90 N
ANISOU 695 NE1BTRP A 88 2746 4322 2772 -426 -626 -22 N
ATOM 696 CE2ATRP A 88 -31.631 -11.461 -25.316 0.50 29.92 C
ANISOU 696 CE2ATRP A 88 3639 4831 2897 453 -590 86 C
ATOM 697 CE2BTRP A 88 -32.624 -9.225 -25.160 0.50 27.16 C
ANISOU 697 CE2BTRP A 88 3162 4745 2411 -313 -260 -259 C
ATOM 698 CE3ATRP A 88 -30.235 -9.607 -24.615 0.50 29.54 C
ANISOU 698 CE3ATRP A 88 3493 4400 3330 438 -514 489 C
ATOM 699 CE3BTRP A 88 -30.270 -9.515 -24.629 0.50 28.18 C
ANISOU 699 CE3BTRP A 88 3072 4794 2842 -68 -267 107 C
ATOM 700 CZ2ATRP A 88 -31.206 -11.341 -26.637 0.50 34.09 C
ANISOU 700 CZ2ATRP A 88 4175 5409 3368 72 -388 670 C
ATOM 701 CZ2BTRP A 88 -32.330 -8.745 -26.432 0.50 29.37 C
ANISOU 701 CZ2BTRP A 88 2888 5791 2482 -461 -726 586 C
ATOM 702 CZ3ATRP A 88 -29.803 -9.507 -25.918 0.50 31.57 C
ANISOU 702 CZ3ATRP A 88 3926 4673 3396 536 -489 965 C
ATOM 703 CZ3BTRP A 88 -29.980 -9.118 -25.914 0.50 31.23 C
ANISOU 703 CZ3BTRP A 88 3510 5392 2963 -14 -109 199 C
ATOM 704 CH2ATRP A 88 -30.292 -10.353 -26.916 0.50 34.19 C
ANISOU 704 CH2ATRP A 88 3790 5371 3831 282 -414 753 C
ATOM 705 CH2BTRP A 88 -30.996 -8.730 -26.797 0.50 30.54 C
ANISOU 705 CH2BTRP A 88 3294 5581 2727 -629 -282 404 C
ATOM 706 N ASN A 89 -31.858 -10.750 -18.234 1.00 20.65 N
ANISOU 706 N ASN A 89 2544 2892 2408 126 -474 75 N
ATOM 707 CA ASN A 89 -31.308 -11.348 -17.008 1.00 20.07 C
ANISOU 707 CA ASN A 89 2810 2700 2114 -141 -303 -72 C
ATOM 708 C ASN A 89 -31.897 -12.731 -16.764 1.00 21.48 C
ANISOU 708 C ASN A 89 2760 2819 2583 -116 -223 -161 C
ATOM 709 O ASN A 89 -31.230 -13.584 -16.173 1.00 21.49 O
ANISOU 709 O ASN A 89 2659 2822 2685 26 -261 -262 O
ATOM 710 CB ASN A 89 -31.615 -10.509 -15.773 1.00 20.56 C
ANISOU 710 CB ASN A 89 2844 2642 2324 -178 -306 -43 C
ATOM 711 CG ASN A 89 -30.701 -9.298 -15.693 1.00 22.79 C
ANISOU 711 CG ASN A 89 2857 3079 2722 -124 -122 -115 C
ATOM 712 OD1 ASN A 89 -29.483 -9.412 -15.520 1.00 22.27 O
ANISOU 712 OD1 ASN A 89 2511 2868 3083 -4 -251 -218 O
ATOM 713 ND2 ASN A 89 -31.265 -8.111 -15.734 1.00 21.48 N
ANISOU 713 ND2 ASN A 89 2560 2851 2751 29 -368 -254 N
ATOM 714 N GLU A 90 -33.161 -12.945 -17.171 1.00 22.62 N
ANISOU 714 N GLU A 90 2841 3061 2694 21 -547 -99 N
ATOM 715 CA GLU A 90 -33.928 -14.119 -16.710 1.00 21.32 C
ANISOU 715 CA GLU A 90 2541 2777 2782 -73 -213 -398 C
ATOM 716 C GLU A 90 -33.190 -15.453 -16.885 1.00 22.69 C
ANISOU 716 C GLU A 90 2800 2924 2897 -309 -466 -407 C
ATOM 717 O GLU A 90 -33.109 -16.222 -15.902 1.00 23.65 O
ANISOU 717 O GLU A 90 2982 2960 3043 -114 -384 -234 O
ATOM 718 CB GLU A 90 -35.298 -14.137 -17.352 1.00 22.86 C
ANISOU 718 CB GLU A 90 2837 3001 2847 254 -113 -368 C
ATOM 719 CG GLU A 90 -36.209 -15.207 -16.759 1.00 24.12 C
ANISOU 719 CG GLU A 90 2883 3126 3156 -259 -296 -206 C
ATOM 720 CD GLU A 90 -36.786 -14.940 -15.387 1.00 23.88 C
ANISOU 720 CD GLU A 90 2834 3265 2976 -339 -468 -177 C
ATOM 721 OE1 GLU A 90 -37.674 -15.713 -14.979 1.00 25.46 O
ANISOU 721 OE1 GLU A 90 2790 3061 3824 -661 -188 -8 O
ATOM 722 OE2 GLU A 90 -36.325 -13.960 -14.738 1.00 23.96 O
ANISOU 722 OE2 GLU A 90 2694 3357 3054 -215 -148 -292 O
ATOM 723 N PRO A 91 -32.669 -15.824 -18.080 1.00 22.29 N
ANISOU 723 N PRO A 91 2614 3027 2828 -225 -97 -126 N
ATOM 724 CA PRO A 91 -32.006 -17.121 -18.210 1.00 23.69 C
ANISOU 724 CA PRO A 91 2921 2763 3316 -138 102 -213 C
ATOM 725 C PRO A 91 -30.807 -17.262 -17.290 1.00 22.83 C
ANISOU 725 C PRO A 91 2794 2863 3019 -236 59 -249 C
ATOM 726 O PRO A 91 -30.617 -18.320 -16.715 1.00 24.89 O
ANISOU 726 O PRO A 91 2958 2658 3842 -216 -171 -151 O
ATOM 727 CB PRO A 91 -31.611 -17.215 -19.676 1.00 26.73 C
ANISOU 727 CB PRO A 91 3638 3300 3217 -186 -321 -558 C
ATOM 728 CG PRO A 91 -31.670 -15.814 -20.178 1.00 26.91 C
ANISOU 728 CG PRO A 91 4105 3083 3035 -218 110 -817 C
ATOM 729 CD PRO A 91 -32.726 -15.100 -19.363 1.00 24.32 C
ANISOU 729 CD PRO A 91 3172 3035 3035 -29 -204 -368 C
ATOM 730 N TRP A 92 -30.042 -16.157 -17.121 1.00 23.12 N
ANISOU 730 N TRP A 92 2685 3054 3044 -80 -47 -155 N
ATOM 731 CA TRP A 92 -28.845 -16.179 -16.287 1.00 21.06 C
ANISOU 731 CA TRP A 92 2500 2508 2992 -96 -315 -176 C
ATOM 732 C TRP A 92 -29.210 -16.423 -14.835 1.00 21.81 C
ANISOU 732 C TRP A 92 2345 2876 3065 -129 -111 -251 C
ATOM 733 O TRP A 92 -28.679 -17.316 -14.200 1.00 23.95 O
ANISOU 733 O TRP A 92 2769 3008 3323 308 -149 -32 O
ATOM 734 CB TRP A 92 -28.103 -14.848 -16.411 1.00 22.52 C
ANISOU 734 CB TRP A 92 2624 3084 2850 -380 -235 -138 C
ATOM 735 CG TRP A 92 -27.591 -14.501 -17.775 1.00 21.11 C
ANISOU 735 CG TRP A 92 2617 2501 2904 -3 -87 -119 C
ATOM 736 CD1 TRP A 92 -28.231 -13.733 -18.683 1.00 24.38 C
ANISOU 736 CD1 TRP A 92 2776 3396 3090 34 42 208 C
ATOM 737 CD2 TRP A 92 -26.303 -14.798 -18.339 1.00 23.30 C
ANISOU 737 CD2 TRP A 92 2693 2967 3192 -51 282 -322 C
ATOM 738 NE1 TRP A 92 -27.458 -13.549 -19.804 1.00 24.77 N
ANISOU 738 NE1 TRP A 92 3073 3136 3201 60 55 54 N
ATOM 739 CE2 TRP A 92 -26.260 -14.184 -19.602 1.00 24.74 C
ANISOU 739 CE2 TRP A 92 2944 3046 3409 -72 234 -340 C
ATOM 740 CE3 TRP A 92 -25.177 -15.480 -17.880 1.00 25.78 C
ANISOU 740 CE3 TRP A 92 3121 3354 3321 231 41 -222 C
ATOM 741 CZ2 TRP A 92 -25.124 -14.244 -20.408 1.00 27.41 C
ANISOU 741 CZ2 TRP A 92 2892 3664 3860 -224 224 -429 C
ATOM 742 CZ3 TRP A 92 -24.048 -15.563 -18.696 1.00 25.57 C
ANISOU 742 CZ3 TRP A 92 2539 3187 3989 -76 259 -542 C
ATOM 743 CH2 TRP A 92 -24.038 -14.944 -19.937 1.00 27.84 C
ANISOU 743 CH2 TRP A 92 2995 3563 4021 -412 539 -229 C
ATOM 744 N ILE A 93 -30.110 -15.582 -14.307 1.00 20.94 N
ANISOU 744 N ILE A 93 2272 2604 3080 130 -247 35 N
ATOM 745 CA ILE A 93 -30.409 -15.561 -12.877 1.00 20.82 C
ANISOU 745 CA ILE A 93 2419 2611 2883 -8 -189 63 C
ATOM 746 C ILE A 93 -31.247 -16.740 -12.425 1.00 20.95 C
ANISOU 746 C ILE A 93 2376 2592 2991 89 -4 -88 C
ATOM 747 O ILE A 93 -31.203 -17.050 -11.249 1.00 23.94 O
ANISOU 747 O ILE A 93 2829 3432 2836 -317 -440 48 O
ATOM 748 CB ILE A 93 -30.986 -14.221 -12.415 1.00 20.71 C
ANISOU 748 CB ILE A 93 2436 2320 3111 59 -192 69 C
ATOM 749 CG1 ILE A 93 -32.326 -13.911 -12.980 1.00 21.83 C
ANISOU 749 CG1 ILE A 93 2343 2860 3092 352 -175 -105 C
ATOM 750 CG2 ILE A 93 -29.973 -13.083 -12.705 1.00 21.26 C
ANISOU 750 CG2 ILE A 93 2507 2407 3162 266 -314 12 C
ATOM 751 CD1 ILE A 93 -32.946 -12.708 -12.310 1.00 22.85 C
ANISOU 751 CD1 ILE A 93 2564 3147 2971 310 -488 15 C
ATOM 752 N THR A 94 -31.992 -17.382 -13.351 1.00 22.23 N
ANISOU 752 N THR A 94 2557 2724 3165 1 -292 -154 N
ATOM 753 CA THR A 94 -32.745 -18.582 -12.999 1.00 23.70 C
ANISOU 753 CA THR A 94 3012 2507 3487 -141 241 -27 C
ATOM 754 C THR A 94 -31.908 -19.853 -13.200 1.00 25.19 C
ANISOU 754 C THR A 94 2785 2903 3881 -21 -8 40 C
ATOM 755 O THR A 94 -32.344 -20.947 -12.825 1.00 27.69 O
ANISOU 755 O THR A 94 3443 2642 4435 146 219 166 O
ATOM 756 CB THR A 94 -34.029 -18.649 -13.821 1.00 24.97 C
ANISOU 756 CB THR A 94 2899 2703 3888 -196 197 146 C
ATOM 757 OG1 THR A 94 -33.715 -18.773 -15.202 1.00 26.09 O
ANISOU 757 OG1 THR A 94 3106 3262 3543 -215 12 -118 O
ATOM 758 CG2 THR A 94 -34.977 -17.514 -13.485 1.00 26.56 C
ANISOU 758 CG2 THR A 94 3099 3180 3813 -138 50 -103 C
ATOM 759 N GLN A 95 -30.753 -19.712 -13.848 1.00 25.04 N
ANISOU 759 N GLN A 95 2994 2763 3759 -211 -70 -207 N
ATOM 760 CA GLN A 95 -29.918 -20.851 -14.220 1.00 29.19 C
ANISOU 760 CA GLN A 95 3838 3148 4106 -10 54 -143 C
ATOM 761 C GLN A 95 -30.767 -21.865 -14.990 1.00 30.72 C
ANISOU 761 C GLN A 95 3932 3660 4082 -144 404 -319 C
ATOM 762 O GLN A 95 -30.752 -23.038 -14.733 1.00 35.37 O
ANISOU 762 O GLN A 95 4649 3284 5507 -279 658 -534 O
ATOM 763 CB GLN A 95 -29.210 -21.462 -13.019 1.00 32.62 C
ANISOU 763 CB GLN A 95 4209 3344 4840 985 -122 -325 C
ATOM 764 CG GLN A 95 -28.347 -20.475 -12.272 1.00 34.46 C
ANISOU 764 CG GLN A 95 4705 3804 4582 659 -523 -783 C
ATOM 765 CD GLN A 95 -27.309 -21.137 -11.417 1.00 39.55 C
ANISOU 765 CD GLN A 95 5709 3458 5862 1631 -473 -692 C
ATOM 766 OE1 GLN A 95 -26.848 -22.262 -11.697 1.00 41.31 O
ANISOU 766 OE1 GLN A 95 6258 3732 5706 2237 -1368 -1604 O
ATOM 767 NE2 GLN A 95 -26.911 -20.429 -10.376 1.00 42.33 N
ANISOU 767 NE2 GLN A 95 4956 4741 6387 1959 -980 -1428 N
ATOM 768 N ASN A 96 -31.456 -21.350 -16.000 1.00 32.12 N
ANISOU 768 N ASN A 96 3901 4159 4143 -236 206 -1120 N
ATOM 769 CA ASN A 96 -32.338 -22.106 -16.873 1.00 31.53 C
ANISOU 769 CA ASN A 96 4117 3825 4039 -450 217 -839 C
ATOM 770 C ASN A 96 -31.544 -23.282 -17.437 1.00 35.22 C
ANISOU 770 C ASN A 96 4949 4045 4389 -267 701 -1126 C
ATOM 771 O ASN A 96 -30.486 -23.067 -18.007 1.00 33.61 O
ANISOU 771 O ASN A 96 3962 4043 4764 -475 520 -995 O
ATOM 772 CB ASN A 96 -32.860 -21.179 -17.961 1.00 36.99 C
ANISOU 772 CB ASN A 96 3991 4876 5189 305 247 -544 C
ATOM 773 CG ASN A 96 -33.679 -21.911 -18.994 1.00 39.28 C
ANISOU 773 CG ASN A 96 3855 5754 5317 -475 -161 -695 C
ATOM 774 OD1 ASN A 96 -33.148 -22.354 -20.015 1.00 39.63 O
ANISOU 774 OD1 ASN A 96 4642 4671 5744 447 -580 -1497 O
ATOM 775 ND2 ASN A 96 -34.967 -22.068 -18.730 1.00 44.05 N
ANISOU 775 ND2 ASN A 96 4169 7364 5204 -1192 -276 -787 N
ATOM 776 N PRO A 97 -31.987 -24.549 -17.242 1.00 38.69 N
ANISOU 776 N PRO A 97 5388 3612 5701 -1013 1197 -1357 N
ATOM 777 CA PRO A 97 -31.208 -25.725 -17.677 1.00 40.61 C
ANISOU 777 CA PRO A 97 4842 4599 5989 -992 492 -1578 C
ATOM 778 C PRO A 97 -30.739 -25.682 -19.125 1.00 38.27 C
ANISOU 778 C PRO A 97 4710 3972 5859 -782 305 -1420 C
ATOM 779 O PRO A 97 -29.596 -26.036 -19.427 1.00 39.51 O
ANISOU 779 O PRO A 97 4458 4403 6150 -526 642 -1601 O
ATOM 780 CB PRO A 97 -32.200 -26.838 -17.432 1.00 43.01 C
ANISOU 780 CB PRO A 97 6038 4501 5802 -902 881 -1174 C
ATOM 781 CG PRO A 97 -32.854 -26.395 -16.182 1.00 41.08 C
ANISOU 781 CG PRO A 97 4791 4138 6679 -635 1308 -1181 C
ATOM 782 CD PRO A 97 -33.208 -24.936 -16.518 1.00 44.21 C
ANISOU 782 CD PRO A 97 6078 4926 5794 -480 837 -1243 C
ATOM 783 N GLN A 98 -31.646 -25.256 -20.017 1.00 38.18 N
ANISOU 783 N GLN A 98 4727 3709 6072 -1474 514 -1163 N
ATOM 784 CA GLN A 98 -31.319 -25.200 -21.427 1.00 41.73 C
ANISOU 784 CA GLN A 98 4858 4881 6117 -903 790 -1154 C
ATOM 785 C GLN A 98 -30.233 -24.139 -21.629 1.00 37.34 C
ANISOU 785 C GLN A 98 4152 4267 5767 -810 420 -1649 C
ATOM 786 O GLN A 98 -29.301 -24.390 -22.375 1.00 38.16 O
ANISOU 786 O GLN A 98 3882 4632 5984 -1092 828 -1992 O
ATOM 787 CB GLN A 98 -32.538 -24.933 -22.308 1.00 45.06 C
ANISOU 787 CB GLN A 98 4309 5134 7679 -1311 184 -710 C
ATOM 788 CG GLN A 98 -33.452 -26.139 -22.544 1.00 50.64 C
ANISOU 788 CG GLN A 98 4576 6057 8608 -1600 420 -959 C
ATOM 789 N PHE A 99 -30.365 -22.963 -20.978 1.00 35.49 N
ANISOU 789 N PHE A 99 3439 4297 5748 -637 404 -1646 N
ATOM 790 CA PHE A 99 -29.356 -21.895 -21.058 1.00 34.78 C
ANISOU 790 CA PHE A 99 4203 3852 5161 -459 552 -1164 C
ATOM 791 C PHE A 99 -27.988 -22.397 -20.575 1.00 34.98 C
ANISOU 791 C PHE A 99 4074 4115 5103 -504 462 -1176 C
ATOM 792 O PHE A 99 -26.977 -22.149 -21.208 1.00 33.72 O
ANISOU 792 O PHE A 99 3512 3434 5866 -396 695 -1335 O
ATOM 793 CB PHE A 99 -29.788 -20.663 -20.267 1.00 35.97 C
ANISOU 793 CB PHE A 99 4137 3768 5760 99 399 -569 C
ATOM 794 CG PHE A 99 -28.803 -19.514 -20.316 1.00 34.71 C
ANISOU 794 CG PHE A 99 4201 3597 5392 143 430 -62 C
ATOM 795 CD1 PHE A 99 -28.806 -18.620 -21.391 1.00 37.49 C
ANISOU 795 CD1 PHE A 99 5188 3806 5249 -15 476 -444 C
ATOM 796 CD2 PHE A 99 -27.855 -19.355 -19.319 1.00 38.41 C
ANISOU 796 CD2 PHE A 99 5354 3645 5597 175 484 -1046 C
ATOM 797 CE1 PHE A 99 -27.862 -17.610 -21.463 1.00 38.61 C
ANISOU 797 CE1 PHE A 99 5297 3704 5670 -163 190 -382 C
ATOM 798 CE2 PHE A 99 -26.929 -18.334 -19.385 1.00 36.61 C
ANISOU 798 CE2 PHE A 99 5120 2676 6112 -148 199 -936 C
ATOM 799 CZ PHE A 99 -26.921 -17.481 -20.470 1.00 42.64 C
ANISOU 799 CZ PHE A 99 6258 3942 6003 -550 -209 -950 C
ATOM 800 N ILE A 100 -27.961 -23.074 -19.421 1.00 33.34 N
ANISOU 800 N ILE A 100 4278 3834 4556 -613 569 -1288 N
ATOM 801 CA ILE A 100 -26.739 -23.598 -18.832 1.00 38.14 C
ANISOU 801 CA ILE A 100 4526 4148 5816 -442 176 -1286 C
ATOM 802 C ILE A 100 -26.066 -24.594 -19.769 1.00 33.60 C
ANISOU 802 C ILE A 100 4155 3804 4806 -580 535 -1005 C
ATOM 803 O ILE A 100 -24.845 -24.565 -19.910 1.00 35.45 O
ANISOU 803 O ILE A 100 4407 3355 5709 279 520 -416 O
ATOM 804 CB ILE A 100 -27.043 -24.229 -17.459 1.00 39.82 C
ANISOU 804 CB ILE A 100 4616 5012 5504 -702 368 -1215 C
ATOM 805 CG1 ILE A 100 -27.513 -23.164 -16.455 1.00 42.34 C
ANISOU 805 CG1 ILE A 100 5000 5068 6020 -684 60 -1380 C
ATOM 806 CG2 ILE A 100 -25.864 -25.066 -16.944 1.00 42.36 C
ANISOU 806 CG2 ILE A 100 5258 5879 4959 -655 106 -1023 C
ATOM 807 N LYS A 101 -26.864 -25.455 -20.418 1.00 34.04 N
ANISOU 807 N LYS A 101 4227 3681 5027 -278 906 -1071 N
ATOM 808 CA LYS A 101 -26.313 -26.436 -21.337 1.00 37.13 C
ANISOU 808 CA LYS A 101 4520 3864 5723 -504 871 -1658 C
ATOM 809 C LYS A 101 -25.660 -25.676 -22.485 1.00 35.08 C
ANISOU 809 C LYS A 101 4166 3738 5425 -488 387 -1182 C
ATOM 810 O LYS A 101 -24.537 -26.027 -22.869 1.00 36.36 O
ANISOU 810 O LYS A 101 4155 3961 5699 -258 703 -943 O
ATOM 811 CB LYS A 101 -27.368 -27.480 -21.782 1.00 42.17 C
ANISOU 811 CB LYS A 101 4919 4374 6729 -717 812 -1958 C
ATOM 812 CG LYS A 101 -27.045 -28.373 -22.964 1.00 46.91 C
ANISOU 812 CG LYS A 101 5257 5154 7414 -1143 982 -1621 C
ATOM 813 CD LYS A 101 -28.248 -29.076 -23.608 1.00 48.99 C
ANISOU 813 CD LYS A 101 5590 4857 8167 -853 564 -1488 C
ATOM 814 N ARG A 102 -26.349 -24.633 -22.998 1.00 34.06 N
ANISOU 814 N ARG A 102 3687 3835 5419 119 376 -1378 N
ATOM 815 CA ARG A 102 -25.818 -23.805 -24.079 1.00 32.90 C
ANISOU 815 CA ARG A 102 3817 4022 4660 118 -226 -1000 C
ATOM 816 C ARG A 102 -24.540 -23.083 -23.645 1.00 33.29 C
ANISOU 816 C ARG A 102 3688 4143 4818 -131 54 -1164 C
ATOM 817 O ARG A 102 -23.601 -22.971 -24.434 1.00 33.62 O
ANISOU 817 O ARG A 102 3566 4494 4716 2 350 -1038 O
ATOM 818 CB ARG A 102 -26.829 -22.771 -24.596 1.00 40.61 C
ANISOU 818 CB ARG A 102 3704 5756 5968 175 -324 -1101 C
ATOM 819 CG ARG A 102 -27.947 -23.414 -25.406 1.00 46.48 C
ANISOU 819 CG ARG A 102 4919 6119 6622 -176 -448 -840 C
ATOM 820 CD ARG A 102 -29.060 -22.397 -25.699 1.00 52.17 C
ANISOU 820 CD ARG A 102 5934 6625 7264 653 -176 42 C
ATOM 821 NE ARG A 102 -28.557 -21.323 -26.561 1.00 50.48 N
ANISOU 821 NE ARG A 102 6913 5883 6382 797 67 -394 N
ATOM 822 CZ ARG A 102 -28.467 -21.388 -27.887 1.00 54.79 C
ANISOU 822 CZ ARG A 102 8120 6362 6335 -163 -664 229 C
ATOM 823 NH1 ARG A 102 -29.125 -22.311 -28.580 1.00 54.37 N
ANISOU 823 NH1 ARG A 102 9493 5121 6045 437 -462 -769 N
ATOM 824 NH2 ARG A 102 -27.760 -20.485 -28.537 1.00 54.70 N
ANISOU 824 NH2 ARG A 102 7697 7042 6042 -468 115 277 N
ATOM 825 N TYR A 103 -24.567 -22.532 -22.421 1.00 31.98 N
ANISOU 825 N TYR A 103 3580 3880 4690 -330 102 -1102 N
ATOM 826 CA TYR A 103 -23.409 -21.828 -21.862 1.00 31.06 C
ANISOU 826 CA TYR A 103 3445 3813 4545 -53 -301 -1631 C
ATOM 827 C TYR A 103 -22.182 -22.742 -21.824 1.00 31.48 C
ANISOU 827 C TYR A 103 3946 3530 4486 230 -139 -636 C
ATOM 828 O TYR A 103 -21.083 -22.334 -22.217 1.00 32.04 O
ANISOU 828 O TYR A 103 3248 3545 5379 365 -12 -359 O
ATOM 829 CB TYR A 103 -23.793 -21.293 -20.482 1.00 33.72 C
ANISOU 829 CB TYR A 103 4186 3475 5153 -200 -396 -1000 C
ATOM 830 CG TYR A 103 -22.718 -20.540 -19.733 1.00 35.04 C
ANISOU 830 CG TYR A 103 3813 4154 5347 742 -1245 -1236 C
ATOM 831 CD1 TYR A 103 -21.874 -21.248 -18.913 1.00 44.93 C
ANISOU 831 CD1 TYR A 103 5193 4986 6890 1122 -1715 -845 C
ATOM 832 CD2 TYR A 103 -22.577 -19.166 -19.769 1.00 41.50 C
ANISOU 832 CD2 TYR A 103 4840 4689 6240 360 -1364 -1095 C
ATOM 833 CE1 TYR A 103 -20.906 -20.629 -18.149 1.00 51.84 C
ANISOU 833 CE1 TYR A 103 6290 5771 7637 347 -2026 -1058 C
ATOM 834 CE2 TYR A 103 -21.614 -18.514 -18.994 1.00 40.99 C
ANISOU 834 CE2 TYR A 103 5001 3632 6943 -300 -1588 -763 C
ATOM 835 CZ TYR A 103 -20.763 -19.256 -18.189 1.00 50.83 C
ANISOU 835 CZ TYR A 103 5997 5504 7812 -58 -1681 -579 C
ATOM 836 OH TYR A 103 -19.766 -18.783 -17.374 1.00 51.20 O
ANISOU 836 OH TYR A 103 7382 5000 7070 523 -2379 63 O
ATOM 837 N GLN A 104 -22.363 -23.952 -21.290 1.00 32.14 N
ANISOU 837 N GLN A 104 4110 3477 4624 648 123 -350 N
ATOM 838 CA GLN A 104 -21.262 -24.896 -21.157 1.00 34.94 C
ANISOU 838 CA GLN A 104 4456 3706 5112 612 393 126 C
ATOM 839 C GLN A 104 -20.727 -25.270 -22.536 1.00 34.37 C
ANISOU 839 C GLN A 104 4181 4029 4848 845 374 -488 C
ATOM 840 O GLN A 104 -19.515 -25.308 -22.708 1.00 35.97 O
ANISOU 840 O GLN A 104 3976 4064 5625 824 355 135 O
ATOM 841 CB GLN A 104 -21.699 -26.156 -20.415 1.00 40.00 C
ANISOU 841 CB GLN A 104 4989 4869 5340 325 744 602 C
ATOM 842 CG GLN A 104 -21.953 -25.896 -18.934 1.00 44.37 C
ANISOU 842 CG GLN A 104 6101 5766 4990 688 310 1043 C
ATOM 843 CD GLN A 104 -22.783 -26.987 -18.293 1.00 51.47 C
ANISOU 843 CD GLN A 104 7385 6770 5402 -160 1051 220 C
ATOM 844 OE1 GLN A 104 -23.284 -27.881 -18.984 1.00 59.60 O
ANISOU 844 OE1 GLN A 104 8286 5382 8975 368 1791 -798 O
ATOM 845 NE2 GLN A 104 -22.975 -26.908 -16.982 1.00 62.97 N
ANISOU 845 NE2 GLN A 104 8838 9063 6025 83 -61 745 N
ATOM 846 N GLN A 105 -21.627 -25.552 -23.498 1.00 33.79 N
ANISOU 846 N GLN A 105 3862 3851 5128 152 339 -730 N
ATOM 847 CA GLN A 105 -21.215 -25.878 -24.860 1.00 36.27 C
ANISOU 847 CA GLN A 105 4228 4029 5522 370 325 -866 C
ATOM 848 C GLN A 105 -20.460 -24.713 -25.517 1.00 31.68 C
ANISOU 848 C GLN A 105 3839 3455 4741 594 -49 -794 C
ATOM 849 O GLN A 105 -19.423 -24.903 -26.130 1.00 35.90 O
ANISOU 849 O GLN A 105 4098 3788 5752 753 443 -657 O
ATOM 850 CB GLN A 105 -22.410 -26.307 -25.701 1.00 39.10 C
ANISOU 850 CB GLN A 105 4532 4682 5641 143 424 -1600 C
ATOM 851 CG GLN A 105 -22.081 -26.606 -27.152 1.00 42.66 C
ANISOU 851 CG GLN A 105 4726 5861 5621 -567 763 -1117 C
ATOM 852 N PHE A 106 -20.926 -23.478 -25.293 1.00 30.98 N
ANISOU 852 N PHE A 106 3488 3601 4681 630 156 -620 N
ATOM 853 CA PHE A 106 -20.276 -22.318 -25.869 1.00 31.26 C
ANISOU 853 CA PHE A 106 3681 3757 4441 569 282 -279 C
ATOM 854 C PHE A 106 -18.850 -22.201 -25.342 1.00 30.88 C
ANISOU 854 C PHE A 106 3647 3622 4464 591 165 -156 C
ATOM 855 O PHE A 106 -17.912 -21.976 -26.108 1.00 31.48 O
ANISOU 855 O PHE A 106 3283 3952 4725 612 560 -335 O
ATOM 856 CB PHE A 106 -21.089 -21.057 -25.574 1.00 33.62 C
ANISOU 856 CB PHE A 106 4076 3939 4759 657 372 -68 C
ATOM 857 CG PHE A 106 -20.365 -19.799 -26.003 1.00 36.74 C
ANISOU 857 CG PHE A 106 3760 4118 6080 802 754 -440 C
ATOM 858 CD1 PHE A 106 -20.382 -19.376 -27.331 1.00 42.88 C
ANISOU 858 CD1 PHE A 106 4543 5160 6587 478 892 -248 C
ATOM 859 CD2 PHE A 106 -19.679 -19.032 -25.073 1.00 36.10 C
ANISOU 859 CD2 PHE A 106 3171 4010 6535 368 496 -431 C
ATOM 860 CE1 PHE A 106 -19.705 -18.225 -27.716 1.00 42.40 C
ANISOU 860 CE1 PHE A 106 4604 4889 6619 114 993 -129 C
ATOM 861 CE2 PHE A 106 -18.964 -17.912 -25.478 1.00 36.62 C
ANISOU 861 CE2 PHE A 106 3416 4026 6470 127 1202 497 C
ATOM 862 CZ PHE A 106 -19.001 -17.502 -26.786 1.00 39.97 C
ANISOU 862 CZ PHE A 106 4140 4391 6656 347 554 -72 C
ATOM 863 N PHE A 107 -18.686 -22.303 -24.025 1.00 32.09 N
ANISOU 863 N PHE A 107 3058 4222 4911 391 430 -251 N
ATOM 864 CA PHE A 107 -17.362 -22.077 -23.469 1.00 33.45 C
ANISOU 864 CA PHE A 107 2698 4654 5357 327 250 -542 C
ATOM 865 C PHE A 107 -16.407 -23.205 -23.850 1.00 33.99 C
ANISOU 865 C PHE A 107 3578 4157 5180 800 -186 -29 C
ATOM 866 O PHE A 107 -15.236 -22.934 -24.128 1.00 35.79 O
ANISOU 866 O PHE A 107 3208 5390 5000 126 -237 120 O
ATOM 867 CB PHE A 107 -17.458 -21.734 -21.986 1.00 38.89 C
ANISOU 867 CB PHE A 107 3714 5005 6058 266 171 -1114 C
ATOM 868 CG PHE A 107 -17.806 -20.256 -21.862 1.00 44.22 C
ANISOU 868 CG PHE A 107 4232 5359 7211 369 -482 -589 C
ATOM 869 CD1 PHE A 107 -16.821 -19.281 -21.973 1.00 44.91 C
ANISOU 869 CD1 PHE A 107 4887 4911 7266 249 -322 -479 C
ATOM 870 CD2 PHE A 107 -19.117 -19.838 -21.687 1.00 44.09 C
ANISOU 870 CD2 PHE A 107 4427 4878 7447 411 -267 -1416 C
ATOM 871 CE1 PHE A 107 -17.143 -17.936 -21.872 1.00 48.11 C
ANISOU 871 CE1 PHE A 107 4843 5307 8129 87 -96 -930 C
ATOM 872 CE2 PHE A 107 -19.426 -18.495 -21.595 1.00 45.05 C
ANISOU 872 CE2 PHE A 107 3904 5369 7845 255 -767 -923 C
ATOM 873 CZ PHE A 107 -18.446 -17.547 -21.690 1.00 47.47 C
ANISOU 873 CZ PHE A 107 4897 5128 8011 -61 -359 -661 C
ATOM 874 N LEU A 108 -16.902 -24.441 -23.947 1.00 32.99 N
ANISOU 874 N LEU A 108 3662 4213 4658 948 -269 -179 N
ATOM 875 CA LEU A 108 -16.055 -25.531 -24.405 1.00 37.32 C
ANISOU 875 CA LEU A 108 4259 4654 5264 1461 -62 -541 C
ATOM 876 C LEU A 108 -15.598 -25.240 -25.833 1.00 37.01 C
ANISOU 876 C LEU A 108 4087 4085 5892 1399 -114 -446 C
ATOM 877 O LEU A 108 -14.412 -25.278 -26.141 1.00 42.72 O
ANISOU 877 O LEU A 108 4015 5394 6824 1037 61 -588 O
ATOM 878 CB LEU A 108 -16.829 -26.837 -24.269 1.00 39.09 C
ANISOU 878 CB LEU A 108 5165 4293 5396 1242 95 -575 C
ATOM 879 CG LEU A 108 -15.984 -28.096 -24.031 1.00 49.89 C
ANISOU 879 CG LEU A 108 6713 5315 6928 1384 158 -397 C
ATOM 880 CD1 LEU A 108 -16.612 -29.264 -24.748 1.00 52.33 C
ANISOU 880 CD1 LEU A 108 6397 6031 7453 1291 -380 -394 C
ATOM 881 N GLU A 109 -16.531 -24.899 -26.707 1.00 36.23 N
ANISOU 881 N GLU A 109 4390 4034 5343 981 -3 -776 N
ATOM 882 CA GLU A 109 -16.201 -24.597 -28.089 1.00 35.43 C
ANISOU 882 CA GLU A 109 4277 4482 4704 828 192 -476 C
ATOM 883 C GLU A 109 -15.289 -23.389 -28.192 1.00 34.99 C
ANISOU 883 C GLU A 109 4194 4775 4325 900 512 -486 C
ATOM 884 O GLU A 109 -14.375 -23.415 -29.012 1.00 36.47 O
ANISOU 884 O GLU A 109 4119 4838 4899 590 1181 -557 O
ATOM 885 CB GLU A 109 -17.487 -24.368 -28.884 1.00 37.71 C
ANISOU 885 CB GLU A 109 4358 5359 4610 925 213 -381 C
ATOM 886 CG GLU A 109 -18.202 -25.686 -29.121 1.00 47.71 C
ANISOU 886 CG GLU A 109 5831 6171 6126 445 -417 -488 C
ATOM 887 CD GLU A 109 -19.520 -25.572 -29.837 1.00 52.04 C
ANISOU 887 CD GLU A 109 6164 6705 6903 703 -1144 -448 C
ATOM 888 OE1 GLU A 109 -20.239 -26.583 -29.831 1.00 59.82 O
ANISOU 888 OE1 GLU A 109 6805 7821 8102 339 -1613 -1320 O
ATOM 889 OE2 GLU A 109 -19.810 -24.492 -30.375 1.00 62.08 O
ANISOU 889 OE2 GLU A 109 6703 7854 9032 -176 -2177 86 O
ATOM 890 N ALA A 110 -15.595 -22.334 -27.423 1.00 31.35 N
ANISOU 890 N ALA A 110 3187 4286 4438 407 37 -410 N
ATOM 891 CA ALA A 110 -14.762 -21.130 -27.426 1.00 34.01 C
ANISOU 891 CA ALA A 110 3787 4711 4422 298 -91 -353 C
ATOM 892 C ALA A 110 -13.308 -21.443 -27.032 1.00 34.86 C
ANISOU 892 C ALA A 110 3759 4628 4857 455 38 -87 C
ATOM 893 O ALA A 110 -12.389 -20.959 -27.685 1.00 35.52 O
ANISOU 893 O ALA A 110 3865 4897 4735 695 263 257 O
ATOM 894 CB ALA A 110 -15.355 -20.070 -26.548 1.00 35.79 C
ANISOU 894 CB ALA A 110 3622 4710 5267 155 430 -233 C
ATOM 895 N SER A 111 -13.104 -22.277 -25.997 1.00 35.38 N
ANISOU 895 N SER A 111 3503 4964 4975 694 55 -286 N
ATOM 896 CA SER A 111 -11.773 -22.618 -25.534 1.00 35.98 C
ANISOU 896 CA SER A 111 3431 5080 5160 154 6 144 C
ATOM 897 C SER A 111 -10.942 -23.176 -26.674 1.00 36.94 C
ANISOU 897 C SER A 111 3556 5123 5358 702 104 491 C
ATOM 898 O SER A 111 -9.785 -22.796 -26.797 1.00 36.95 O
ANISOU 898 O SER A 111 2886 5745 5407 457 152 394 O
ATOM 899 CB SER A 111 -11.758 -23.565 -24.323 1.00 38.65 C
ANISOU 899 CB SER A 111 3718 5753 5215 -326 -100 355 C
ATOM 900 OG SER A 111 -12.384 -24.826 -24.565 1.00 45.88 O
ANISOU 900 OG SER A 111 5329 5992 6109 -91 -425 397 O
ATOM 901 N VAL A 112 -11.550 -24.054 -27.474 1.00 36.79 N
ANISOU 901 N VAL A 112 3982 4507 5488 1099 517 454 N
ATOM 902 CA VAL A 112 -10.889 -24.686 -28.595 1.00 37.70 C
ANISOU 902 CA VAL A 112 4257 4459 5609 1520 627 643 C
ATOM 903 C VAL A 112 -10.629 -23.650 -29.693 1.00 36.30 C
ANISOU 903 C VAL A 112 4018 4216 5556 981 675 430 C
ATOM 904 O VAL A 112 -9.486 -23.482 -30.104 1.00 41.36 O
ANISOU 904 O VAL A 112 3835 6172 5706 1628 523 154 O
ATOM 905 CB VAL A 112 -11.733 -25.853 -29.128 1.00 44.42 C
ANISOU 905 CB VAL A 112 5389 4847 6640 1323 1535 373 C
ATOM 906 CG1 VAL A 112 -11.050 -26.468 -30.342 1.00 47.85 C
ANISOU 906 CG1 VAL A 112 6321 4753 7106 1264 2126 195 C
ATOM 907 CG2 VAL A 112 -12.000 -26.923 -28.067 1.00 44.61 C
ANISOU 907 CG2 VAL A 112 4514 5242 7195 1733 1744 633 C
ATOM 908 N GLN A 113 -11.677 -22.907 -30.093 1.00 37.57 N
ANISOU 908 N GLN A 113 4305 4789 5180 1458 949 514 N
ATOM 909 CA GLN A 113 -11.600 -21.865 -31.121 1.00 34.17 C
ANISOU 909 CA GLN A 113 4222 3716 5044 1539 691 511 C
ATOM 910 C GLN A 113 -10.463 -20.872 -30.834 1.00 35.85 C
ANISOU 910 C GLN A 113 3624 5289 4708 1162 580 429 C
ATOM 911 O GLN A 113 -9.690 -20.494 -31.735 1.00 38.53 O
ANISOU 911 O GLN A 113 4459 5079 5103 1423 984 200 O
ATOM 912 CB GLN A 113 -12.972 -21.200 -31.312 1.00 40.40 C
ANISOU 912 CB GLN A 113 4433 5503 5413 1335 -64 1401 C
ATOM 913 N PHE A 114 -10.340 -20.465 -29.574 1.00 34.40 N
ANISOU 913 N PHE A 114 3428 4707 4936 871 847 644 N
ATOM 914 CA PHE A 114 -9.369 -19.454 -29.201 1.00 32.08 C
ANISOU 914 CA PHE A 114 3394 4286 4510 651 390 959 C
ATOM 915 C PHE A 114 -7.977 -20.053 -28.994 1.00 33.52 C
ANISOU 915 C PHE A 114 3257 4511 4969 762 738 446 C
ATOM 916 O PHE A 114 -7.035 -19.297 -28.782 1.00 35.33 O
ANISOU 916 O PHE A 114 3697 4427 5298 695 650 482 O
ATOM 917 CB PHE A 114 -9.802 -18.755 -27.923 1.00 35.77 C
ANISOU 917 CB PHE A 114 3561 4439 5589 666 887 920 C
ATOM 918 CG PHE A 114 -11.165 -18.094 -27.967 1.00 36.67 C
ANISOU 918 CG PHE A 114 3387 4286 6260 568 746 847 C
ATOM 919 CD1 PHE A 114 -11.726 -17.644 -29.164 1.00 41.04 C
ANISOU 919 CD1 PHE A 114 4262 4449 6883 1590 -129 279 C
ATOM 920 CD2 PHE A 114 -11.875 -17.925 -26.786 1.00 41.06 C
ANISOU 920 CD2 PHE A 114 4068 4715 6818 1195 992 182 C
ATOM 921 CE1 PHE A 114 -12.962 -17.016 -29.165 1.00 42.80 C
ANISOU 921 CE1 PHE A 114 4485 4422 7356 1328 -64 -262 C
ATOM 922 CE2 PHE A 114 -13.100 -17.272 -26.801 1.00 40.84 C
ANISOU 922 CE2 PHE A 114 3486 4490 7541 613 1171 710 C
ATOM 923 CZ PHE A 114 -13.665 -16.885 -28.000 1.00 42.81 C
ANISOU 923 CZ PHE A 114 4413 4659 7196 1223 250 915 C
ATOM 924 N GLY A 115 -7.867 -21.388 -28.973 1.00 36.31 N
ANISOU 924 N GLY A 115 3768 4642 5386 715 633 1068 N
ATOM 925 CA GLY A 115 -6.613 -22.080 -28.688 1.00 34.21 C
ANISOU 925 CA GLY A 115 3825 4260 4915 466 98 345 C
ATOM 926 C GLY A 115 -6.095 -21.943 -27.253 1.00 35.04 C
ANISOU 926 C GLY A 115 3285 4731 5298 1025 58 946 C
ATOM 927 O GLY A 115 -4.864 -21.891 -27.033 1.00 34.13 O
ANISOU 927 O GLY A 115 2858 4425 5685 472 163 650 O
ATOM 928 N VAL A 116 -7.009 -21.971 -26.279 1.00 31.86 N
ANISOU 928 N VAL A 116 3284 4124 4695 613 6 533 N
ATOM 929 CA VAL A 116 -6.617 -21.938 -24.887 1.00 32.43 C
ANISOU 929 CA VAL A 116 3416 4194 4711 443 515 868 C
ATOM 930 C VAL A 116 -6.100 -23.317 -24.499 1.00 33.85 C
ANISOU 930 C VAL A 116 3599 4115 5145 431 309 899 C
ATOM 931 O VAL A 116 -6.791 -24.336 -24.704 1.00 34.56 O
ANISOU 931 O VAL A 116 3423 4463 5246 440 68 740 O
ATOM 932 CB VAL A 116 -7.716 -21.479 -23.939 1.00 32.62 C
ANISOU 932 CB VAL A 116 3258 4490 4644 760 663 488 C
ATOM 933 CG1 VAL A 116 -7.199 -21.368 -22.512 1.00 38.89 C
ANISOU 933 CG1 VAL A 116 4380 5617 4778 1011 1001 610 C
ATOM 934 CG2 VAL A 116 -8.341 -20.187 -24.402 1.00 35.43 C
ANISOU 934 CG2 VAL A 116 3338 4731 5392 1009 458 578 C
ATOM 935 N PRO A 117 -4.865 -23.394 -23.959 1.00 32.62 N
ANISOU 935 N PRO A 117 3392 4013 4988 333 195 630 N
ATOM 936 CA PRO A 117 -4.318 -24.666 -23.520 1.00 32.07 C
ANISOU 936 CA PRO A 117 3375 4068 4742 833 10 773 C
ATOM 937 C PRO A 117 -5.193 -25.196 -22.405 1.00 34.97 C
ANISOU 937 C PRO A 117 3813 4653 4818 880 228 563 C
ATOM 938 O PRO A 117 -5.564 -24.447 -21.509 1.00 37.63 O
ANISOU 938 O PRO A 117 4030 5096 5174 1357 675 922 O
ATOM 939 CB PRO A 117 -2.942 -24.332 -23.011 1.00 33.91 C
ANISOU 939 CB PRO A 117 3109 4353 5423 848 49 811 C
ATOM 940 CG PRO A 117 -2.581 -23.078 -23.674 1.00 38.27 C
ANISOU 940 CG PRO A 117 3231 4792 6519 390 -263 1077 C
ATOM 941 CD PRO A 117 -3.857 -22.315 -23.833 1.00 34.12 C
ANISOU 941 CD PRO A 117 3272 4077 5614 871 95 537 C
ATOM 942 N GLU A 118 -5.465 -26.483 -22.464 1.00 31.79 N
ANISOU 942 N GLU A 118 3148 3754 5176 1054 839 348 N
ATOM 943 CA GLU A 118 -6.401 -27.104 -21.551 1.00 35.23 C
ANISOU 943 CA GLU A 118 3082 5015 5290 928 586 647 C
ATOM 944 C GLU A 118 -5.959 -26.878 -20.100 1.00 37.65 C
ANISOU 944 C GLU A 118 3676 4958 5671 532 780 825 C
ATOM 945 O GLU A 118 -6.812 -26.773 -19.235 1.00 41.81 O
ANISOU 945 O GLU A 118 4407 5538 5941 1236 1389 763 O
ATOM 946 CB GLU A 118 -6.596 -28.561 -21.967 1.00 36.65 C
ANISOU 946 CB GLU A 118 3306 5189 5431 482 813 864 C
ATOM 947 CG GLU A 118 -7.296 -28.767 -23.304 1.00 44.94 C
ANISOU 947 CG GLU A 118 4456 6076 6543 569 325 437 C
ATOM 948 CD GLU A 118 -6.476 -28.849 -24.588 1.00 49.13 C
ANISOU 948 CD GLU A 118 5312 6913 6441 41 350 -442 C
ATOM 949 OE1 GLU A 118 -6.843 -29.775 -25.368 1.00 55.43 O
ANISOU 949 OE1 GLU A 118 8164 6714 6184 -200 207 -986 O
ATOM 950 OE2 GLU A 118 -5.513 -28.026 -24.823 1.00 45.17 O
ANISOU 950 OE2 GLU A 118 3577 7212 6374 531 -552 403 O
ATOM 951 N VAL A 119 -4.635 -26.802 -19.823 1.00 33.98 N
ANISOU 951 N VAL A 119 3578 5130 4203 1186 161 701 N
ATOM 952 CA VAL A 119 -4.163 -26.670 -18.453 1.00 37.03 C
ANISOU 952 CA VAL A 119 3804 5793 4471 873 497 767 C
ATOM 953 C VAL A 119 -4.623 -25.352 -17.829 1.00 39.05 C
ANISOU 953 C VAL A 119 4502 6194 4143 715 844 898 C
ATOM 954 O VAL A 119 -4.649 -25.261 -16.611 1.00 48.28 O
ANISOU 954 O VAL A 119 5753 8403 4189 1413 1593 207 O
ATOM 955 CB VAL A 119 -2.639 -26.775 -18.307 1.00 37.51 C
ANISOU 955 CB VAL A 119 4346 5726 4178 114 188 834 C
ATOM 956 CG1 VAL A 119 -2.146 -28.154 -18.630 1.00 41.07 C
ANISOU 956 CG1 VAL A 119 4888 6157 4561 307 363 491 C
ATOM 957 CG2 VAL A 119 -1.925 -25.705 -19.101 1.00 40.19 C
ANISOU 957 CG2 VAL A 119 4489 5930 4852 43 722 1077 C
ATOM 958 N LEU A 120 -4.924 -24.330 -18.645 1.00 40.74 N
ANISOU 958 N LEU A 120 3904 6528 5048 1511 810 601 N
ATOM 959 CA LEU A 120 -5.266 -23.027 -18.101 1.00 46.33 C
ANISOU 959 CA LEU A 120 4333 7225 6044 1155 749 -298 C
ATOM 960 C LEU A 120 -6.771 -22.955 -17.852 1.00 49.54 C
ANISOU 960 C LEU A 120 4108 7979 6736 2361 354 -1354 C
ATOM 961 O LEU A 120 -7.215 -22.086 -17.101 1.00 58.93 O
ANISOU 961 O LEU A 120 7902 7310 7179 2483 566 -1542 O
ATOM 962 CB LEU A 120 -4.771 -21.917 -19.035 1.00 48.37 C
ANISOU 962 CB LEU A 120 4742 7387 6248 1348 -139 -161 C
ATOM 963 CG LEU A 120 -3.306 -21.483 -18.871 1.00 55.89 C
ANISOU 963 CG LEU A 120 5450 8190 7597 1289 272 -272 C
ATOM 964 CD1 LEU A 120 -2.527 -22.348 -17.899 1.00 57.54 C
ANISOU 964 CD1 LEU A 120 5573 8296 7993 2273 499 -91 C
ATOM 965 CD2 LEU A 120 -2.556 -21.449 -20.198 1.00 56.46 C
ANISOU 965 CD2 LEU A 120 4788 7993 8670 1395 420 -673 C
ATOM 966 N LEU A 121 -7.539 -23.869 -18.462 1.00 54.24 N
ANISOU 966 N LEU A 121 4279 8791 7540 1749 1292 -2280 N
ATOM 967 CA LEU A 121 -8.999 -23.805 -18.453 1.00 54.59 C
ANISOU 967 CA LEU A 121 3898 9338 7507 2489 781 -1590 C
ATOM 968 C LEU A 121 -9.515 -24.074 -17.049 1.00 61.21 C
ANISOU 968 C LEU A 121 4629 10147 8483 1631 718 -727 C
ATOM 969 O LEU A 121 -8.894 -24.828 -16.295 1.00 51.82 O
ANISOU 969 O LEU A 121 3759 9317 6614 632 135 -215 O
ATOM 970 CB LEU A 121 -9.619 -24.809 -19.420 1.00 56.86 C
ANISOU 970 CB LEU A 121 3819 9730 8056 2225 -152 -567 C
ATOM 971 CG LEU A 121 -9.440 -24.497 -20.908 1.00 59.35 C
ANISOU 971 CG LEU A 121 4288 10338 7924 1454 -244 -507 C
ATOM 972 CD1 LEU A 121 -10.134 -25.539 -21.780 1.00 63.20 C
ANISOU 972 CD1 LEU A 121 4391 10966 8656 837 -131 -363 C
ATOM 973 CD2 LEU A 121 -9.945 -23.085 -21.184 1.00 56.90 C
ANISOU 973 CD2 LEU A 121 3990 10476 7153 1047 -526 18 C
ATOM 974 N PRO A 122 -10.717 -23.533 -16.693 1.00 70.10 N
ANISOU 974 N PRO A 122 5662 11312 9661 1900 947 55 N
ATOM 975 CA PRO A 122 -11.298 -23.756 -15.375 1.00 73.43 C
ANISOU 975 CA PRO A 122 7216 11787 8897 1973 1310 161 C
ATOM 976 C PRO A 122 -11.155 -25.236 -15.040 1.00 76.93 C
ANISOU 976 C PRO A 122 9025 12313 7891 2186 682 856 C
ATOM 977 O PRO A 122 -10.803 -25.589 -13.916 1.00 72.17 O
ANISOU 977 O PRO A 122 8440 12775 6206 1694 257 1558 O
ATOM 978 CB PRO A 122 -12.763 -23.287 -15.497 1.00 77.63 C
ANISOU 978 CB PRO A 122 7321 12003 10173 1492 1046 409 C
ATOM 979 CG PRO A 122 -12.977 -23.099 -16.992 1.00 76.37 C
ANISOU 979 CG PRO A 122 6628 12134 10255 1470 1359 232 C
ATOM 980 CD PRO A 122 -11.605 -22.727 -17.544 1.00 72.01 C
ANISOU 980 CD PRO A 122 5810 11433 10118 2053 1363 97 C
ATOM 981 N GLN A 123 -11.419 -26.078 -16.050 1.00 86.95 N
ANISOU 981 N GLN A 123 10172 13210 9656 1609 1589 -34 N
ATOM 982 CA GLN A 123 -11.159 -27.509 -15.993 1.00102.49 C
ANISOU 982 CA GLN A 123 11703 14684 12556 1827 1077 -768 C
ATOM 983 C GLN A 123 -11.786 -28.073 -14.717 1.00108.04 C
ANISOU 983 C GLN A 123 13351 16034 11665 1368 444 -43 C
ATOM 984 O GLN A 123 -13.013 -28.157 -14.626 1.00116.62 O
ANISOU 984 O GLN A 123 14241 17529 12541 696 1220 503 O
ATOM 985 CB GLN A 123 -9.665 -27.772 -16.215 1.00109.17 C
ANISOU 985 CB GLN A 123 11492 15637 14350 2202 262 -1839 C
ATOM 986 CG GLN A 123 -9.353 -29.222 -16.578 1.00114.23 C
ANISOU 986 CG GLN A 123 11206 16361 15835 2103 -517 -2627 C
ATOM 987 CD GLN A 123 -8.290 -29.360 -17.646 1.00113.11 C
ANISOU 987 CD GLN A 123 10555 15775 16645 2565 -1406 -2985 C
ATOM 988 OE1 GLN A 123 -7.087 -29.423 -17.359 1.00112.67 O
ANISOU 988 OE1 GLN A 123 11454 13894 17459 2696 -3392 -2793 O
ATOM 989 NE2 GLN A 123 -8.737 -29.441 -18.893 1.00106.82 N
ANISOU 989 NE2 GLN A 123 8467 14879 17240 2474 -3001 -3255 N
ATOM 990 N GLY A 124 -10.956 -28.465 -13.742 1.00101.40 N
ANISOU 990 N GLY A 124 12388 15349 10790 1058 -289 -442 N
ATOM 991 CA GLY A 124 -11.449 -28.748 -12.406 1.00 98.93 C
ANISOU 991 CA GLY A 124 12504 14481 10604 500 -612 -1458 C
ATOM 992 C GLY A 124 -11.881 -27.453 -11.727 1.00 89.96 C
ANISOU 992 C GLY A 124 10818 14237 9125 -696 -780 -2115 C
ATOM 993 O GLY A 124 -13.071 -27.146 -11.672 1.00 96.56 O
ANISOU 993 O GLY A 124 11622 16853 8213 -226 -2055 -442 O
ATOM 994 N ALA A 125 -10.888 -26.677 -11.269 1.00 82.82 N
ANISOU 994 N ALA A 125 9970 12339 9160 -454 -412 -2135 N
ATOM 995 CA ALA A 125 -11.153 -25.435 -10.554 1.00 58.30 C
ANISOU 995 CA ALA A 125 6056 9818 6278 -1418 -2045 -1711 C
ATOM 996 C ALA A 125 -9.877 -24.616 -10.342 1.00 63.00 C
ANISOU 996 C ALA A 125 6466 10230 7242 -1034 -1061 -1122 C
ATOM 997 O ALA A 125 -8.804 -25.000 -10.853 1.00 64.70 O
ANISOU 997 O ALA A 125 7139 10756 6686 -1437 -755 -573 O
ATOM 998 CB ALA A 125 -11.851 -25.783 -9.305 1.00 49.04 C
ANISOU 998 CB ALA A 125 1833 10013 6786 -1209 -1559 -2398 C
ATOM 999 N LEU A 126 -10.041 -23.500 -9.589 1.00 38.38 N
ANISOU 999 N LEU A 126 3940 7433 3208 -1078 -446 -439 N
ATOM 1000 CA LEU A 126 -9.323 -22.270 -9.833 1.00 55.94 C
ANISOU 1000 CA LEU A 126 6993 8865 5399 -548 -787 785 C
ATOM 1001 C LEU A 126 -9.243 -21.477 -8.545 1.00 78.19 C
ANISOU 1001 C LEU A 126 10068 11425 8217 -646 -350 -464 C
ATOM 1002 O LEU A 126 -9.216 -20.250 -8.574 1.00 96.03 O
ANISOU 1002 O LEU A 126 12773 11737 11975 -1901 877 504 O
ATOM 1003 CB LEU A 126 -9.993 -21.398 -10.891 1.00 60.69 C
ANISOU 1003 CB LEU A 126 8284 8743 6032 -1036 -940 3331 C
ATOM 1004 CG LEU A 126 -9.226 -21.188 -12.208 1.00 75.96 C
ANISOU 1004 CG LEU A 126 9426 11549 7885 -1296 -313 474 C
ATOM 1005 CD1 LEU A 126 -7.867 -20.917 -11.790 1.00 86.11 C
ANISOU 1005 CD1 LEU A 126 10254 12390 10075 -1102 -367 390 C
ATOM 1006 CD2 LEU A 126 -9.107 -22.281 -13.233 1.00 80.32 C
ANISOU 1006 CD2 LEU A 126 10341 12211 7964 -1467 -735 -521 C
ATOM 1007 N LEU A 127 -9.255 -22.213 -7.434 1.00 97.76 N
ANISOU 1007 N LEU A 127 12567 13857 10720 -718 -295 421 N
ATOM 1008 CA LEU A 127 -9.707 -21.670 -6.141 1.00111.55 C
ANISOU 1008 CA LEU A 127 12654 17795 11935 -288 -1522 -1290 C
ATOM 1009 C LEU A 127 -11.210 -21.311 -6.344 1.00126.65 C
ANISOU 1009 C LEU A 127 12463 20026 15630 341 -2367 -1931 C
ATOM 1010 O LEU A 127 -11.844 -20.905 -5.329 1.00125.92 O
ANISOU 1010 O LEU A 127 11400 21570 14875 -545 -2520 -2291 O
ATOM 1011 CB LEU A 127 -8.864 -20.488 -5.547 1.00120.14 C
ANISOU 1011 CB LEU A 127 14334 19618 11697 -515 -2608 -1607 C
ATOM 1012 CG LEU A 127 -7.438 -20.732 -4.872 1.00130.15 C
ANISOU 1012 CG LEU A 127 15999 21608 11845 -149 -2970 -1523 C
ATOM 1013 CD1 LEU A 127 -6.300 -21.491 -5.725 1.00139.35 C
ANISOU 1013 CD1 LEU A 127 16882 22472 13594 201 -2298 -1478 C
ATOM 1014 CD2 LEU A 127 -6.538 -19.478 -4.307 1.00127.98 C
ANISOU 1014 CD2 LEU A 127 16853 22285 9487 -135 -3689 -1756 C
ATOM 1015 N THR A 128 -11.788 -21.606 -7.609 1.00133.07 N
ANISOU 1015 N THR A 128 11665 20779 18118 832 -4445 -2168 N
ATOM 1016 CA THR A 128 -13.198 -21.300 -8.032 1.00142.18 C
ANISOU 1016 CA THR A 128 13314 20469 20237 1439 -5976 -1645 C
ATOM 1017 C THR A 128 -13.607 -21.778 -9.476 1.00136.58 C
ANISOU 1017 C THR A 128 13680 18187 20029 1374 -4367 -2003 C
ATOM 1018 O THR A 128 -12.920 -21.429 -10.443 1.00144.95 O
ANISOU 1018 O THR A 128 13636 19636 21804 2457 -2574 -981 O
ATOM 1019 CB THR A 128 -13.399 -19.771 -7.748 1.00159.19 C
ANISOU 1019 CB THR A 128 16423 20752 23311 889 -6624 -1053 C
ATOM 1020 OG1 THR A 128 -14.473 -19.074 -8.408 1.00178.83 O
ANISOU 1020 OG1 THR A 128 19838 21388 26721 1711 -6893 302 O
ATOM 1021 CG2 THR A 128 -12.239 -18.929 -8.238 1.00156.41 C
ANISOU 1021 CG2 THR A 128 16427 19783 23219 692 -7375 -479 C
ATOM 1022 N LYS A 129 -14.758 -22.547 -9.624 1.00118.08 N
ANISOU 1022 N LYS A 129 14259 14567 16040 785 -3860 -2686 N
ATOM 1023 CA LYS A 129 -15.113 -23.288 -10.838 1.00 98.01 C
ANISOU 1023 CA LYS A 129 12706 10946 13588 -673 -3038 -1973 C
ATOM 1024 C LYS A 129 -15.809 -22.241 -11.717 1.00105.64 C
ANISOU 1024 C LYS A 129 13934 14496 11707 -884 -2944 -1316 C
ATOM 1025 O LYS A 129 -15.086 -21.474 -12.354 1.00109.13 O
ANISOU 1025 O LYS A 129 13800 17516 10147 -2620 -2271 -1969 O
ATOM 1026 CB LYS A 129 -15.926 -24.608 -10.770 1.00 82.98 C
ANISOU 1026 CB LYS A 129 13289 7205 11034 666 -1625 -2593 C
ATOM 1027 CG LYS A 129 -16.213 -25.369 -9.457 1.00 67.89 C
ANISOU 1027 CG LYS A 129 11648 3010 11138 285 -1090 -2435 C
ATOM 1028 CD LYS A 129 -15.408 -26.618 -9.092 1.00 63.88 C
ANISOU 1028 CD LYS A 129 10175 4450 9646 -827 -943 -942 C
ATOM 1029 CE LYS A 129 -15.349 -26.857 -7.606 1.00 61.01 C
ANISOU 1029 CE LYS A 129 8999 4594 9587 -639 -326 -1371 C
ATOM 1030 NZ LYS A 129 -14.835 -25.710 -6.861 1.00 53.47 N
ANISOU 1030 NZ LYS A 129 7873 4536 7908 740 -219 -1577 N
ATOM 1031 N THR A 130 -17.166 -22.124 -11.665 1.00110.44 N
ANISOU 1031 N THR A 130 13306 15651 13005 -539 -1479 -1023 N
ATOM 1032 CA THR A 130 -17.940 -21.234 -12.544 1.00103.15 C
ANISOU 1032 CA THR A 130 11409 15050 12732 595 -567 -1509 C
ATOM 1033 C THR A 130 -19.453 -21.231 -12.224 1.00 96.70 C
ANISOU 1033 C THR A 130 12211 12357 12174 2170 524 -1556 C
ATOM 1034 O THR A 130 -19.976 -22.298 -11.889 1.00108.41 O
ANISOU 1034 O THR A 130 14836 12692 13663 2522 2452 -1865 O
ATOM 1035 CB THR A 130 -17.700 -21.665 -13.996 1.00110.21 C
ANISOU 1035 CB THR A 130 13031 15672 13170 151 -62 -2275 C
ATOM 1036 OG1 THR A 130 -17.392 -23.059 -13.994 1.00114.66 O
ANISOU 1036 OG1 THR A 130 14351 15326 13889 -430 334 -3795 O
ATOM 1037 CG2 THR A 130 -16.586 -20.878 -14.671 1.00109.05 C
ANISOU 1037 CG2 THR A 130 13174 15698 12561 -66 -30 -1924 C
ATOM 1038 N MET A 131 -20.145 -20.047 -12.366 1.00 73.06 N
ANISOU 1038 N MET A 131 9774 9359 8625 720 -241 -1275 N
ATOM 1039 CA AMET A 131 -21.597 -19.870 -12.194 0.50 53.18 C
ANISOU 1039 CA AMET A 131 8423 6061 5720 1365 -819 -1508 C
ATOM 1040 CA BMET A 131 -21.597 -19.870 -12.194 0.50 53.24 C
ANISOU 1040 CA BMET A 131 8426 6060 5740 1366 -809 -1503 C
ATOM 1041 C MET A 131 -21.998 -20.064 -10.726 1.00 42.27 C
ANISOU 1041 C MET A 131 5536 4364 6161 1699 -410 -1368 C
ATOM 1042 O MET A 131 -23.127 -19.737 -10.240 1.00 33.72 O
ANISOU 1042 O MET A 131 4038 3511 5264 514 -1879 -314 O
ATOM 1043 CB AMET A 131 -22.375 -20.840 -13.086 0.50 62.04 C
ANISOU 1043 CB AMET A 131 8571 8002 6999 112 -1855 -1229 C
ATOM 1044 CB BMET A 131 -22.375 -20.840 -13.086 0.50 62.15 C
ANISOU 1044 CB BMET A 131 8573 7989 7049 109 -1834 -1228 C
ATOM 1045 CG AMET A 131 -22.832 -20.206 -14.396 0.50 66.72 C
ANISOU 1045 CG AMET A 131 10194 8033 7125 -245 -1703 -1100 C
ATOM 1046 CG BMET A 131 -22.835 -20.206 -14.394 0.50 66.90 C
ANISOU 1046 CG BMET A 131 10194 8005 7219 -243 -1676 -1083 C
ATOM 1047 SD AMET A 131 -24.405 -19.336 -14.231 0.50 75.46 S
ANISOU 1047 SD AMET A 131 10485 8920 9266 -1381 -1696 -1760 S
ATOM 1048 SD BMET A 131 -24.405 -19.331 -14.223 0.50 75.73 S
ANISOU 1048 SD BMET A 131 10493 8864 9418 -1383 -1636 -1753 S
ATOM 1049 CE AMET A 131 -24.243 -18.056 -15.478 0.50 68.73 C
ANISOU 1049 CE AMET A 131 9198 9149 7766 -366 -3236 -1218 C
ATOM 1050 CE BMET A 131 -24.249 -18.061 -15.481 0.50 69.36 C
ANISOU 1050 CE BMET A 131 9259 9106 7987 -376 -3100 -1200 C
ATOM 1051 N ILE A 132 -21.045 -20.557 -9.983 1.00 36.84 N
ANISOU 1051 N ILE A 132 5197 3768 5034 1814 -458 -780 N
ATOM 1052 CA ILE A 132 -21.267 -20.893 -8.593 1.00 33.58 C
ANISOU 1052 CA ILE A 132 3502 4121 5138 943 -814 -488 C
ATOM 1053 C ILE A 132 -21.468 -19.644 -7.772 1.00 27.14 C
ANISOU 1053 C ILE A 132 3287 2892 4133 391 -670 -52 C
ATOM 1054 O ILE A 132 -21.958 -19.806 -6.641 1.00 31.51 O
ANISOU 1054 O ILE A 132 3779 3355 4839 -361 -706 295 O
ATOM 1055 CB ILE A 132 -20.086 -21.731 -8.066 1.00 41.51 C
ANISOU 1055 CB ILE A 132 4994 4528 6248 2281 -617 -829 C
ATOM 1056 CG1 ILE A 132 -18.775 -21.038 -8.350 1.00 39.78 C
ANISOU 1056 CG1 ILE A 132 3878 5330 5908 2491 -590 -1146 C
ATOM 1057 CG2 ILE A 132 -20.173 -23.156 -8.589 1.00 51.87 C
ANISOU 1057 CG2 ILE A 132 6442 5526 7740 1945 -550 -440 C
ATOM 1058 CD1 ILE A 132 -17.606 -21.883 -7.869 1.00 48.45 C
ANISOU 1058 CD1 ILE A 132 3870 6334 8206 1627 -1803 -1698 C
ATOM 1059 N TYR A 133 -21.100 -18.430 -8.301 1.00 27.99 N
ANISOU 1059 N TYR A 133 3563 3425 3648 -69 -697 73 N
ATOM 1060 CA TYR A 133 -21.273 -17.232 -7.481 1.00 22.61 C
ANISOU 1060 CA TYR A 133 2747 2754 3088 86 -388 -18 C
ATOM 1061 C TYR A 133 -22.572 -16.498 -7.808 1.00 22.38 C
ANISOU 1061 C TYR A 133 2694 2875 2935 279 -282 46 C
ATOM 1062 O TYR A 133 -22.833 -15.424 -7.256 1.00 22.33 O
ANISOU 1062 O TYR A 133 2687 2793 3005 26 -226 -283 O
ATOM 1063 CB TYR A 133 -20.118 -16.252 -7.735 1.00 23.17 C
ANISOU 1063 CB TYR A 133 2802 2845 3159 21 -137 283 C
ATOM 1064 CG TYR A 133 -18.798 -16.723 -7.175 1.00 21.63 C
ANISOU 1064 CG TYR A 133 2818 2456 2944 -154 -189 73 C
ATOM 1065 CD1 TYR A 133 -18.647 -16.980 -5.816 1.00 21.92 C
ANISOU 1065 CD1 TYR A 133 2426 2830 3073 87 -116 451 C
ATOM 1066 CD2 TYR A 133 -17.694 -16.875 -7.992 1.00 23.79 C
ANISOU 1066 CD2 TYR A 133 3033 3156 2852 333 -19 39 C
ATOM 1067 CE1 TYR A 133 -17.438 -17.408 -5.320 1.00 22.89 C
ANISOU 1067 CE1 TYR A 133 2757 2812 3127 48 -260 250 C
ATOM 1068 CE2 TYR A 133 -16.461 -17.230 -7.482 1.00 24.06 C
ANISOU 1068 CE2 TYR A 133 2590 3449 3104 412 -63 131 C
ATOM 1069 CZ TYR A 133 -16.322 -17.465 -6.126 1.00 23.91 C
ANISOU 1069 CZ TYR A 133 2930 3060 3094 634 -134 442 C
ATOM 1070 OH TYR A 133 -15.109 -17.809 -5.567 1.00 25.72 O
ANISOU 1070 OH TYR A 133 2765 3672 3337 511 -533 433 O
ATOM 1071 N SER A 134 -23.421 -17.142 -8.628 1.00 24.16 N
ANISOU 1071 N SER A 134 2777 2900 3503 466 -328 -92 N
ATOM 1072 CA SER A 134 -24.685 -16.544 -9.027 1.00 23.87 C
ANISOU 1072 CA SER A 134 2803 3071 3195 192 -377 191 C
ATOM 1073 C SER A 134 -25.876 -17.113 -8.227 1.00 22.04 C
ANISOU 1073 C SER A 134 2957 2654 2762 128 -286 -320 C
ATOM 1074 O SER A 134 -25.721 -18.027 -7.412 1.00 24.16 O
ANISOU 1074 O SER A 134 2911 3163 3105 -92 -464 52 O
ATOM 1075 CB SER A 134 -24.886 -16.695 -10.506 1.00 27.37 C
ANISOU 1075 CB SER A 134 3200 3943 3255 658 -360 207 C
ATOM 1076 OG SER A 134 -25.915 -15.804 -10.975 1.00 29.78 O
ANISOU 1076 OG SER A 134 3721 3742 3853 340 -185 -122 O
ATOM 1077 N CYS A 135 -27.041 -16.514 -8.452 1.00 24.14 N
ANISOU 1077 N CYS A 135 2938 2809 3424 128 -276 82 N
ATOM 1078 CA CYS A 135 -28.280 -16.851 -7.765 1.00 23.02 C
ANISOU 1078 CA CYS A 135 2873 2732 3141 218 -258 45 C
ATOM 1079 C CYS A 135 -29.097 -17.859 -8.567 1.00 22.64 C
ANISOU 1079 C CYS A 135 2926 2631 3045 100 -179 -19 C
ATOM 1080 O CYS A 135 -28.666 -18.259 -9.664 1.00 25.37 O
ANISOU 1080 O CYS A 135 3221 3012 3405 10 -93 -335 O
ATOM 1081 CB CYS A 135 -29.073 -15.572 -7.555 1.00 21.27 C
ANISOU 1081 CB CYS A 135 2478 2532 3071 2 -311 -49 C
ATOM 1082 SG CYS A 135 -29.505 -14.752 -9.113 1.00 23.69 S
ANISOU 1082 SG CYS A 135 2936 2863 3202 109 -371 23 S
ATOM 1083 N LYS A 136 -30.267 -18.218 -8.035 1.00 23.70 N
ANISOU 1083 N LYS A 136 3018 2961 3025 -109 102 -91 N
ATOM 1084 CA LYS A 136 -31.233 -19.040 -8.760 1.00 23.88 C
ANISOU 1084 CA LYS A 136 3289 2676 3108 -279 -238 -256 C
ATOM 1085 C LYS A 136 -32.623 -18.506 -8.428 1.00 23.45 C
ANISOU 1085 C LYS A 136 3031 2531 3350 -472 184 308 C
ATOM 1086 O LYS A 136 -33.329 -19.078 -7.582 1.00 29.38 O
ANISOU 1086 O LYS A 136 3367 3223 4574 573 832 1041 O
ATOM 1087 CB LYS A 136 -31.054 -20.531 -8.481 1.00 28.19 C
ANISOU 1087 CB LYS A 136 3923 2939 3847 -398 -580 193 C
ATOM 1088 CG LYS A 136 -31.751 -21.466 -9.410 1.00 34.10 C
ANISOU 1088 CG LYS A 136 3849 3621 5487 -364 -683 -272 C
ATOM 1089 CD LYS A 136 -31.282 -22.921 -9.272 1.00 39.75 C
ANISOU 1089 CD LYS A 136 5307 2734 7061 -746 -266 -107 C
ATOM 1090 CE LYS A 136 -32.019 -23.699 -10.284 1.00 46.25 C
ANISOU 1090 CE LYS A 136 5289 4472 7813 -1088 -395 -985 C
ATOM 1091 NZ LYS A 136 -33.414 -23.928 -9.892 1.00 50.47 N
ANISOU 1091 NZ LYS A 136 5605 5894 7676 -1266 -201 -457 N
ATOM 1092 N ARG A 137 -32.985 -17.400 -9.081 1.00 22.54 N
ANISOU 1092 N ARG A 137 2779 2700 3084 -462 -64 235 N
ATOM 1093 CA ARG A 137 -34.190 -16.673 -8.751 1.00 24.40 C
ANISOU 1093 CA ARG A 137 2763 3030 3478 -372 123 478 C
ATOM 1094 C ARG A 137 -34.674 -15.886 -9.959 1.00 24.33 C
ANISOU 1094 C ARG A 137 2708 2969 3569 -77 -194 448 C
ATOM 1095 O ARG A 137 -33.849 -15.316 -10.673 1.00 25.58 O
ANISOU 1095 O ARG A 137 2803 3318 3596 -259 -118 544 O
ATOM 1096 CB ARG A 137 -33.930 -15.715 -7.599 1.00 25.95 C
ANISOU 1096 CB ARG A 137 3285 3177 3397 204 -92 536 C
ATOM 1097 CG ARG A 137 -35.145 -14.887 -7.243 1.00 33.92 C
ANISOU 1097 CG ARG A 137 4111 4226 4549 934 -32 455 C
ATOM 1098 CD ARG A 137 -35.467 -14.889 -5.876 1.00 34.81 C
ANISOU 1098 CD ARG A 137 3924 5092 4210 1381 -618 641 C
ATOM 1099 NE ARG A 137 -36.572 -14.063 -5.399 1.00 27.14 N
ANISOU 1099 NE ARG A 137 2795 4262 3253 396 -369 -406 N
ATOM 1100 CZ ARG A 137 -36.714 -13.745 -4.143 1.00 25.95 C
ANISOU 1100 CZ ARG A 137 2852 3991 3017 -315 -186 -152 C
ATOM 1101 NH1 ARG A 137 -35.717 -13.924 -3.306 1.00 29.51 N
ANISOU 1101 NH1 ARG A 137 3134 5231 2847 27 -129 212 N
ATOM 1102 NH2 ARG A 137 -37.780 -13.145 -3.764 1.00 25.28 N
ANISOU 1102 NH2 ARG A 137 2766 3578 3261 -382 -100 -121 N
ATOM 1103 N SER A 138 -36.006 -15.798 -10.137 1.00 23.83 N
ANISOU 1103 N SER A 138 2456 2841 3758 -23 -2 54 N
ATOM 1104 CA SER A 138 -36.573 -15.082 -11.278 1.00 24.52 C
ANISOU 1104 CA SER A 138 2418 3117 3780 136 -211 -215 C
ATOM 1105 C SER A 138 -36.733 -13.583 -11.002 1.00 22.28 C
ANISOU 1105 C SER A 138 2315 3071 3081 27 -286 -73 C
ATOM 1106 O SER A 138 -36.914 -13.156 -9.856 1.00 23.68 O
ANISOU 1106 O SER A 138 2840 3237 2920 -148 -48 88 O
ATOM 1107 CB SER A 138 -37.952 -15.659 -11.585 1.00 24.80 C
ANISOU 1107 CB SER A 138 2957 2756 3710 -166 138 -260 C
ATOM 1108 OG SER A 138 -38.596 -14.991 -12.634 1.00 26.21 O
ANISOU 1108 OG SER A 138 2878 3378 3702 -40 -139 123 O
ATOM 1109 N LEU A 139 -36.742 -12.811 -12.078 1.00 21.67 N
ANISOU 1109 N LEU A 139 2351 3044 2837 232 -16 105 N
ATOM 1110 CA LEU A 139 -37.282 -11.465 -12.048 1.00 21.37 C
ANISOU 1110 CA LEU A 139 2409 2579 3131 202 -20 -17 C
ATOM 1111 C LEU A 139 -38.751 -11.514 -11.704 1.00 22.38 C
ANISOU 1111 C LEU A 139 2578 2992 2932 -238 -411 62 C
ATOM 1112 O LEU A 139 -39.410 -12.542 -12.017 1.00 24.03 O
ANISOU 1112 O LEU A 139 2491 3217 3423 -390 -157 -186 O
ATOM 1113 CB LEU A 139 -37.125 -10.818 -13.420 1.00 23.20 C
ANISOU 1113 CB LEU A 139 2479 3192 3141 -35 -287 14 C
ATOM 1114 CG LEU A 139 -35.707 -10.575 -13.935 1.00 21.62 C
ANISOU 1114 CG LEU A 139 2304 2989 2920 101 -38 128 C
ATOM 1115 CD1 LEU A 139 -35.864 -10.047 -15.347 1.00 24.70 C
ANISOU 1115 CD1 LEU A 139 2597 3237 3550 -141 -164 -187 C
ATOM 1116 CD2 LEU A 139 -34.904 -9.599 -13.112 1.00 21.52 C
ANISOU 1116 CD2 LEU A 139 2306 2848 3024 -211 -196 -111 C
ATOM 1117 N THR A 140 -39.276 -10.434 -11.119 1.00 23.48 N
ANISOU 1117 N THR A 140 2571 3020 3332 -216 -170 -290 N
ATOM 1118 CA THR A 140 -40.733 -10.260 -11.053 1.00 22.81 C
ANISOU 1118 CA THR A 140 2345 2941 3382 -297 -125 29 C
ATOM 1119 C THR A 140 -41.175 -9.279 -12.130 1.00 22.69 C
ANISOU 1119 C THR A 140 2418 3119 3084 -450 -29 -157 C
ATOM 1120 O THR A 140 -42.324 -9.304 -12.530 1.00 25.52 O
ANISOU 1120 O THR A 140 2554 3833 3308 -668 -109 227 O
ATOM 1121 CB THR A 140 -41.149 -9.799 -9.652 1.00 22.73 C
ANISOU 1121 CB THR A 140 2240 3361 3034 -25 3 87 C
ATOM 1122 OG1 THR A 140 -40.513 -8.547 -9.396 1.00 24.37 O
ANISOU 1122 OG1 THR A 140 2595 3252 3414 -281 -289 -110 O
ATOM 1123 CG2 THR A 140 -40.796 -10.886 -8.646 1.00 25.44 C
ANISOU 1123 CG2 THR A 140 2555 3390 3720 -311 76 -241 C
ATOM 1124 N HIS A 141 -40.276 -8.370 -12.532 1.00 23.64 N
ANISOU 1124 N HIS A 141 2739 3252 2992 -189 -131 111 N
ATOM 1125 CA HIS A 141 -40.572 -7.314 -13.479 1.00 23.82 C
ANISOU 1125 CA HIS A 141 2404 3549 3099 129 -372 5 C
ATOM 1126 C HIS A 141 -39.374 -7.037 -14.394 1.00 23.40 C
ANISOU 1126 C HIS A 141 2443 3316 3130 272 -216 152 C
ATOM 1127 O HIS A 141 -38.230 -7.116 -13.935 1.00 24.17 O
ANISOU 1127 O HIS A 141 2749 3362 3072 99 -350 36 O
ATOM 1128 CB HIS A 141 -40.914 -6.020 -12.758 1.00 25.61 C
ANISOU 1128 CB HIS A 141 2961 3597 3173 500 -242 341 C
ATOM 1129 CG HIS A 141 -42.043 -6.123 -11.817 1.00 27.19 C
ANISOU 1129 CG HIS A 141 2731 4028 3570 322 -55 89 C
ATOM 1130 ND1 HIS A 141 -43.354 -5.799 -12.104 1.00 36.01 N
ANISOU 1130 ND1 HIS A 141 3683 5340 4660 844 53 470 N
ATOM 1131 CD2 HIS A 141 -42.010 -6.540 -10.525 1.00 26.66 C
ANISOU 1131 CD2 HIS A 141 2790 3843 3496 270 -889 60 C
ATOM 1132 CE1 HIS A 141 -44.094 -6.035 -11.006 1.00 35.44 C
ANISOU 1132 CE1 HIS A 141 3656 5766 4042 754 165 672 C
ATOM 1133 NE2 HIS A 141 -43.269 -6.485 -10.037 1.00 37.24 N
ANISOU 1133 NE2 HIS A 141 3730 5437 4982 -382 -148 -245 N
ATOM 1134 N THR A 142 -39.663 -6.777 -15.673 1.00 23.88 N
ANISOU 1134 N THR A 142 2506 3444 3124 204 -424 77 N
ATOM 1135 CA THR A 142 -38.663 -6.414 -16.663 1.00 23.28 C
ANISOU 1135 CA THR A 142 2639 3094 3113 320 -701 192 C
ATOM 1136 C THR A 142 -38.738 -4.925 -16.920 1.00 22.74 C
ANISOU 1136 C THR A 142 2514 3199 2926 501 -265 -34 C
ATOM 1137 O THR A 142 -39.818 -4.348 -16.936 1.00 24.40 O
ANISOU 1137 O THR A 142 2324 3068 3878 191 -231 50 O
ATOM 1138 CB THR A 142 -38.780 -7.238 -17.957 1.00 25.56 C
ANISOU 1138 CB THR A 142 3070 3179 3464 449 -152 -169 C
ATOM 1139 OG1 THR A 142 -39.890 -6.805 -18.716 1.00 26.65 O
ANISOU 1139 OG1 THR A 142 3270 3615 3242 132 -698 219 O
ATOM 1140 CG2 THR A 142 -38.820 -8.712 -17.662 1.00 25.04 C
ANISOU 1140 CG2 THR A 142 2922 3118 3472 -40 -201 8 C
ATOM 1141 N VAL A 143 -37.584 -4.335 -17.247 1.00 23.67 N
ANISOU 1141 N VAL A 143 2803 3122 3068 255 -32 152 N
ATOM 1142 CA VAL A 143 -37.484 -2.938 -17.637 1.00 22.16 C
ANISOU 1142 CA VAL A 143 2523 3037 2859 51 -338 8 C
ATOM 1143 C VAL A 143 -36.589 -2.775 -18.860 1.00 22.59 C
ANISOU 1143 C VAL A 143 2636 3013 2934 352 -297 -96 C
ATOM 1144 O VAL A 143 -35.614 -3.509 -19.055 1.00 23.78 O
ANISOU 1144 O VAL A 143 2913 3096 3024 468 19 34 O
ATOM 1145 CB VAL A 143 -36.944 -2.003 -16.534 1.00 23.85 C
ANISOU 1145 CB VAL A 143 3149 3092 2822 78 -437 49 C
ATOM 1146 CG1 VAL A 143 -38.019 -1.742 -15.485 1.00 25.21 C
ANISOU 1146 CG1 VAL A 143 3305 3132 3140 484 -287 223 C
ATOM 1147 CG2 VAL A 143 -35.644 -2.537 -15.961 1.00 23.22 C
ANISOU 1147 CG2 VAL A 143 2701 2808 3315 -110 -807 91 C
ATOM 1148 N ARG A 144 -36.951 -1.793 -19.694 1.00 23.74 N
ANISOU 1148 N ARG A 144 2944 3098 2979 190 -103 249 N
ATOM 1149 CA AARG A 144 -36.180 -1.391 -20.855 0.50 23.66 C
ANISOU 1149 CA AARG A 144 3102 3132 2756 133 -351 173 C
ATOM 1150 CA BARG A 144 -36.191 -1.388 -20.861 0.50 24.55 C
ANISOU 1150 CA BARG A 144 3318 3161 2849 128 -355 230 C
ATOM 1151 C ARG A 144 -36.098 0.142 -20.904 1.00 24.08 C
ANISOU 1151 C ARG A 144 3390 3062 2697 181 -589 252 C
ATOM 1152 O ARG A 144 -36.584 0.853 -20.021 1.00 24.97 O
ANISOU 1152 O ARG A 144 3503 3166 2819 226 -285 106 O
ATOM 1153 CB AARG A 144 -36.822 -2.031 -22.084 0.50 24.21 C
ANISOU 1153 CB AARG A 144 2959 3362 2878 -302 -64 359 C
ATOM 1154 CB BARG A 144 -36.920 -1.911 -22.095 0.50 27.50 C
ANISOU 1154 CB BARG A 144 3668 3618 3163 -352 -164 424 C
ATOM 1155 CG AARG A 144 -36.474 -3.493 -22.297 0.50 23.31 C
ANISOU 1155 CG AARG A 144 2207 3717 2931 -166 318 -64 C
ATOM 1156 CG BARG A 144 -37.032 -3.413 -22.238 0.50 31.82 C
ANISOU 1156 CG BARG A 144 4258 4108 3723 -443 -138 258 C
ATOM 1157 CD AARG A 144 -37.009 -3.941 -23.652 0.50 23.56 C
ANISOU 1157 CD AARG A 144 2268 4025 2658 -761 -45 376 C
ATOM 1158 CD BARG A 144 -35.779 -3.896 -22.805 0.50 35.91 C
ANISOU 1158 CD BARG A 144 4261 5003 4380 -679 -2 341 C
ATOM 1159 NE AARG A 144 -35.984 -4.685 -24.385 0.50 32.71 N
ANISOU 1159 NE AARG A 144 3833 5285 3311 -304 -533 544 N
ATOM 1160 NE BARG A 144 -35.995 -4.911 -23.837 0.50 34.24 N
ANISOU 1160 NE BARG A 144 4412 5558 3039 -419 302 748 N
ATOM 1161 CZ AARG A 144 -34.717 -4.225 -24.378 0.50 30.11 C
ANISOU 1161 CZ AARG A 144 3246 4792 3402 -861 -205 1286 C
ATOM 1162 CZ BARG A 144 -34.965 -5.157 -24.636 0.50 27.59 C
ANISOU 1162 CZ BARG A 144 2629 4781 3072 -358 -291 398 C
ATOM 1163 NH1AARG A 144 -34.211 -3.809 -23.243 0.50 42.06 N
ANISOU 1163 NH1AARG A 144 4671 5613 5696 -1363 9 139 N
ATOM 1164 NH1BARG A 144 -34.830 -6.373 -25.025 0.50 24.01 N
ANISOU 1164 NH1BARG A 144 2554 3629 2939 -331 -458 260 N
ATOM 1165 NH2AARG A 144 -33.935 -4.314 -25.457 0.50 35.32 N
ANISOU 1165 NH2AARG A 144 4840 4822 3757 69 -1231 -481 N
ATOM 1166 NH2BARG A 144 -34.011 -4.248 -24.764 0.50 30.72 N
ANISOU 1166 NH2BARG A 144 3870 3221 4582 -703 -1672 6 N
ATOM 1167 N GLU A 145 -35.445 0.653 -21.955 1.00 24.23 N
ANISOU 1167 N GLU A 145 3445 2934 2829 207 -208 306 N
ATOM 1168 CA GLU A 145 -35.188 2.060 -22.104 1.00 24.85 C
ANISOU 1168 CA GLU A 145 3530 3068 2841 396 -469 2 C
ATOM 1169 C GLU A 145 -36.458 2.879 -21.870 1.00 24.61 C
ANISOU 1169 C GLU A 145 3176 3099 3076 274 -555 340 C
ATOM 1170 O GLU A 145 -37.506 2.620 -22.502 1.00 27.18 O
ANISOU 1170 O GLU A 145 3216 3825 3286 307 -692 153 O
ATOM 1171 CB GLU A 145 -34.701 2.313 -23.530 1.00 28.48 C
ANISOU 1171 CB GLU A 145 3881 3597 3344 402 -330 53 C
ATOM 1172 CG GLU A 145 -34.379 3.767 -23.792 1.00 28.16 C
ANISOU 1172 CG GLU A 145 3779 3629 3293 111 -364 577 C
ATOM 1173 CD GLU A 145 -33.070 4.211 -23.175 1.00 30.56 C
ANISOU 1173 CD GLU A 145 4056 3800 3756 310 -518 686 C
ATOM 1174 OE1 GLU A 145 -33.080 5.289 -22.568 1.00 32.71 O
ANISOU 1174 OE1 GLU A 145 4305 3751 4372 -230 -517 217 O
ATOM 1175 OE2 GLU A 145 -32.052 3.447 -23.272 1.00 30.03 O
ANISOU 1175 OE2 GLU A 145 4088 3919 3402 842 -276 416 O
ATOM 1176 N GLY A 146 -36.302 3.875 -20.994 1.00 26.05 N
ANISOU 1176 N GLY A 146 3522 3280 3095 324 -719 488 N
ATOM 1177 CA GLY A 146 -37.333 4.845 -20.689 1.00 27.88 C
ANISOU 1177 CA GLY A 146 3623 3132 3839 655 -678 304 C
ATOM 1178 C GLY A 146 -38.330 4.443 -19.604 1.00 27.23 C
ANISOU 1178 C GLY A 146 3475 3197 3676 779 -376 164 C
ATOM 1179 O GLY A 146 -39.144 5.269 -19.144 1.00 29.36 O
ANISOU 1179 O GLY A 146 3571 3700 3883 1377 -251 35 O
ATOM 1180 N ASP A 147 -38.206 3.210 -19.123 1.00 25.51 N
ANISOU 1180 N ASP A 147 2898 3447 3348 503 -303 207 N
ATOM 1181 CA ASP A 147 -39.108 2.711 -18.095 1.00 25.68 C
ANISOU 1181 CA ASP A 147 3125 3210 3422 597 -425 46 C
ATOM 1182 C ASP A 147 -38.834 3.333 -16.733 1.00 25.40 C
ANISOU 1182 C ASP A 147 3322 3196 3133 623 -123 29 C
ATOM 1183 O ASP A 147 -37.759 3.866 -16.490 1.00 27.27 O
ANISOU 1183 O ASP A 147 3467 3411 3484 469 -105 121 O
ATOM 1184 CB ASP A 147 -39.081 1.205 -18.010 1.00 26.56 C
ANISOU 1184 CB ASP A 147 3085 3221 3786 760 -191 224 C
ATOM 1185 CG ASP A 147 -39.741 0.482 -19.175 1.00 27.65 C
ANISOU 1185 CG ASP A 147 3313 3731 3461 570 -375 201 C
ATOM 1186 OD1 ASP A 147 -40.455 1.171 -19.994 1.00 30.42 O
ANISOU 1186 OD1 ASP A 147 4119 3956 3484 1089 -680 -246 O
ATOM 1187 OD2 ASP A 147 -39.548 -0.766 -19.231 1.00 27.58 O
ANISOU 1187 OD2 ASP A 147 3233 3422 3824 496 -625 102 O
ATOM 1188 N ARG A 148 -39.871 3.280 -15.877 1.00 28.47 N
ANISOU 1188 N ARG A 148 3489 4042 3286 720 -153 55 N
ATOM 1189 CA ARG A 148 -39.769 3.787 -14.511 1.00 29.72 C
ANISOU 1189 CA ARG A 148 3595 4225 3471 749 235 108 C
ATOM 1190 C ARG A 148 -39.944 2.575 -13.603 1.00 27.86 C
ANISOU 1190 C ARG A 148 3855 3373 3357 61 -341 -49 C
ATOM 1191 O ARG A 148 -40.712 1.691 -13.900 1.00 35.29 O
ANISOU 1191 O ARG A 148 3941 5268 4200 -673 -1031 454 O
ATOM 1192 CB ARG A 148 -40.771 4.911 -14.212 1.00 36.05 C
ANISOU 1192 CB ARG A 148 4151 5468 4076 1371 321 -735 C
ATOM 1193 N ILE A 149 -39.220 2.526 -12.499 1.00 27.73 N
ANISOU 1193 N ILE A 149 3603 3758 3173 -308 -146 -54 N
ATOM 1194 CA ILE A 149 -39.398 1.529 -11.458 1.00 27.43 C
ANISOU 1194 CA ILE A 149 3406 3766 3251 -40 -252 141 C
ATOM 1195 C ILE A 149 -40.198 2.192 -10.347 1.00 26.31 C
ANISOU 1195 C ILE A 149 2676 4073 3246 113 -483 126 C
ATOM 1196 O ILE A 149 -39.852 3.298 -9.895 1.00 27.56 O
ANISOU 1196 O ILE A 149 3408 3818 3245 416 -79 276 O
ATOM 1197 CB ILE A 149 -37.998 1.069 -11.013 1.00 25.75 C
ANISOU 1197 CB ILE A 149 2876 3716 3191 81 -126 -223 C
ATOM 1198 CG1 ILE A 149 -37.285 0.434 -12.193 1.00 28.18 C
ANISOU 1198 CG1 ILE A 149 3705 3941 3062 -228 -50 -30 C
ATOM 1199 CG2 ILE A 149 -38.010 0.133 -9.799 1.00 26.83 C
ANISOU 1199 CG2 ILE A 149 3459 3504 3230 424 -69 -132 C
ATOM 1200 CD1 ILE A 149 -35.803 0.224 -11.966 1.00 28.38 C
ANISOU 1200 CD1 ILE A 149 3212 4135 3434 347 238 246 C
ATOM 1201 N ALA A 150 -41.269 1.508 -9.926 1.00 27.74 N
ANISOU 1201 N ALA A 150 2893 4239 3409 -72 -239 119 N
ATOM 1202 CA ALA A 150 -42.243 2.101 -9.019 1.00 33.36 C
ANISOU 1202 CA ALA A 150 3627 5118 3929 -136 -214 165 C
ATOM 1203 C ALA A 150 -41.607 2.657 -7.751 1.00 29.44 C
ANISOU 1203 C ALA A 150 2921 4656 3609 258 -64 121 C
ATOM 1204 O ALA A 150 -42.016 3.725 -7.289 1.00 32.81 O
ANISOU 1204 O ALA A 150 3670 4399 4398 736 -239 445 O
ATOM 1205 CB ALA A 150 -43.330 1.083 -8.711 1.00 34.19 C
ANISOU 1205 CB ALA A 150 3654 5128 4207 164 -796 610 C
ATOM 1206 N SER A 151 -40.613 1.943 -7.209 1.00 26.59 N
ANISOU 1206 N SER A 151 2919 3901 3284 863 108 75 N
ATOM 1207 CA SER A 151 -39.993 2.325 -5.943 1.00 26.84 C
ANISOU 1207 CA SER A 151 2700 4161 3336 519 134 16 C
ATOM 1208 C SER A 151 -38.968 3.448 -6.109 1.00 25.92 C
ANISOU 1208 C SER A 151 2971 3569 3310 711 58 -120 C
ATOM 1209 O SER A 151 -38.513 3.978 -5.077 1.00 28.58 O
ANISOU 1209 O SER A 151 3760 3639 3458 531 -174 59 O
ATOM 1210 CB SER A 151 -39.348 1.121 -5.268 1.00 27.48 C
ANISOU 1210 CB SER A 151 3204 3625 3612 154 -269 231 C
ATOM 1211 OG SER A 151 -38.296 0.625 -6.055 1.00 26.21 O
ANISOU 1211 OG SER A 151 3527 3334 3096 440 117 86 O
ATOM 1212 N LEU A 152 -38.637 3.810 -7.365 1.00 25.43 N
ANISOU 1212 N LEU A 152 3022 3286 3354 494 -136 -105 N
ATOM 1213 CA LEU A 152 -37.602 4.806 -7.673 1.00 26.92 C
ANISOU 1213 CA LEU A 152 3314 3408 3507 583 -33 8 C
ATOM 1214 C LEU A 152 -38.183 5.852 -8.619 1.00 26.13 C
ANISOU 1214 C LEU A 152 3408 2978 3541 347 -24 141 C
ATOM 1215 O LEU A 152 -37.726 6.007 -9.756 1.00 27.47 O
ANISOU 1215 O LEU A 152 3824 3121 3493 291 -526 299 O
ATOM 1216 CB LEU A 152 -36.378 4.151 -8.310 1.00 25.62 C
ANISOU 1216 CB LEU A 152 3054 3141 3538 389 -141 -32 C
ATOM 1217 CG LEU A 152 -35.641 3.132 -7.453 1.00 26.31 C
ANISOU 1217 CG LEU A 152 3348 2991 3658 297 -258 -124 C
ATOM 1218 CD1 LEU A 152 -34.529 2.555 -8.320 1.00 26.58 C
ANISOU 1218 CD1 LEU A 152 3572 2804 3723 735 -365 10 C
ATOM 1219 CD2 LEU A 152 -35.080 3.830 -6.217 1.00 26.60 C
ANISOU 1219 CD2 LEU A 152 3312 2918 3875 642 -223 -364 C
ATOM 1220 N PRO A 153 -39.219 6.604 -8.205 1.00 28.58 N
ANISOU 1220 N PRO A 153 3656 3494 3708 586 -38 340 N
ATOM 1221 CA PRO A 153 -39.911 7.493 -9.141 1.00 32.07 C
ANISOU 1221 CA PRO A 153 3966 3522 4696 748 -119 642 C
ATOM 1222 C PRO A 153 -39.104 8.581 -9.872 1.00 29.26 C
ANISOU 1222 C PRO A 153 3472 3173 4470 700 -123 143 C
ATOM 1223 O PRO A 153 -39.499 9.032 -10.961 1.00 34.49 O
ANISOU 1223 O PRO A 153 4613 4262 4227 882 -343 409 O
ATOM 1224 CB PRO A 153 -40.966 8.093 -8.234 1.00 33.58 C
ANISOU 1224 CB PRO A 153 3699 3923 5136 846 -3 614 C
ATOM 1225 CG PRO A 153 -40.438 8.007 -6.865 1.00 35.43 C
ANISOU 1225 CG PRO A 153 4307 4330 4826 1078 -157 62 C
ATOM 1226 CD PRO A 153 -39.818 6.622 -6.861 1.00 30.71 C
ANISOU 1226 CD PRO A 153 3568 3748 4353 749 187 150 C
ATOM 1227 N GLU A 154 -37.973 9.002 -9.301 1.00 28.51 N
ANISOU 1227 N GLU A 154 3735 3188 3910 595 33 -170 N
ATOM 1228 CA GLU A 154 -37.231 10.114 -9.892 1.00 29.94 C
ANISOU 1228 CA GLU A 154 3438 3363 4576 766 -148 -251 C
ATOM 1229 C GLU A 154 -36.271 9.625 -10.968 1.00 28.50 C
ANISOU 1229 C GLU A 154 3444 3290 4095 415 91 -107 C
ATOM 1230 O GLU A 154 -35.614 10.427 -11.633 1.00 30.63 O
ANISOU 1230 O GLU A 154 3907 3260 4471 757 144 -292 O
ATOM 1231 CB GLU A 154 -36.425 10.901 -8.860 1.00 32.35 C
ANISOU 1231 CB GLU A 154 4000 3765 4526 520 177 -772 C
ATOM 1232 CG GLU A 154 -37.289 11.549 -7.785 1.00 34.19 C
ANISOU 1232 CG GLU A 154 4018 4588 4384 479 242 -674 C
ATOM 1233 CD GLU A 154 -36.557 12.688 -7.123 1.00 36.04 C
ANISOU 1233 CD GLU A 154 5257 3974 4461 442 430 -254 C
ATOM 1234 OE1 GLU A 154 -36.872 13.831 -7.479 1.00 42.09 O
ANISOU 1234 OE1 GLU A 154 6620 3962 5409 727 -3 -483 O
ATOM 1235 OE2 GLU A 154 -35.635 12.433 -6.319 1.00 38.11 O
ANISOU 1235 OE2 GLU A 154 5705 3844 4930 270 454 -798 O
ATOM 1236 N PHE A 155 -36.173 8.291 -11.112 1.00 26.85 N
ANISOU 1236 N PHE A 155 3496 3054 3652 101 -72 21 N
ATOM 1237 CA PHE A 155 -35.198 7.711 -12.016 1.00 24.89 C
ANISOU 1237 CA PHE A 155 3267 2756 3433 289 -334 -29 C
ATOM 1238 C PHE A 155 -35.837 7.168 -13.292 1.00 25.15 C
ANISOU 1238 C PHE A 155 3297 3031 3228 340 -401 315 C
ATOM 1239 O PHE A 155 -36.997 6.742 -13.298 1.00 29.10 O
ANISOU 1239 O PHE A 155 3907 3709 3440 657 -357 215 O
ATOM 1240 CB PHE A 155 -34.457 6.556 -11.335 1.00 25.72 C
ANISOU 1240 CB PHE A 155 3464 3093 3217 474 -316 -30 C
ATOM 1241 CG PHE A 155 -33.450 7.008 -10.303 1.00 25.62 C
ANISOU 1241 CG PHE A 155 3617 2961 3155 -53 -173 341 C
ATOM 1242 CD1 PHE A 155 -33.826 7.231 -8.987 1.00 26.57 C
ANISOU 1242 CD1 PHE A 155 3414 3367 3313 19 -133 -89 C
ATOM 1243 CD2 PHE A 155 -32.127 7.250 -10.671 1.00 26.40 C
ANISOU 1243 CD2 PHE A 155 3438 3219 3376 53 -46 -180 C
ATOM 1244 CE1 PHE A 155 -32.876 7.644 -8.063 1.00 28.69 C
ANISOU 1244 CE1 PHE A 155 4253 3450 3199 -226 -375 -308 C
ATOM 1245 CE2 PHE A 155 -31.199 7.656 -9.742 1.00 26.58 C
ANISOU 1245 CE2 PHE A 155 3272 3166 3660 65 -25 -227 C
ATOM 1246 CZ PHE A 155 -31.572 7.825 -8.432 1.00 29.60 C
ANISOU 1246 CZ PHE A 155 3685 3567 3995 59 -162 -197 C
ATOM 1247 N THR A 156 -35.055 7.170 -14.360 1.00 25.22 N
ANISOU 1247 N THR A 156 3512 3005 3064 518 -247 -9 N
ATOM 1248 CA ATHR A 156 -35.423 6.548 -15.629 0.50 26.67 C
ANISOU 1248 CA ATHR A 156 3665 3003 3463 705 -444 16 C
ATOM 1249 CA BTHR A 156 -35.447 6.512 -15.602 0.50 27.14 C
ANISOU 1249 CA BTHR A 156 3684 3175 3452 596 -377 32 C
ATOM 1250 C THR A 156 -34.413 5.450 -15.954 1.00 25.03 C
ANISOU 1250 C THR A 156 3546 2650 3314 489 -182 100 C
ATOM 1251 O THR A 156 -33.218 5.629 -15.794 1.00 26.54 O
ANISOU 1251 O THR A 156 3416 3328 3338 617 -412 144 O
ATOM 1252 CB ATHR A 156 -35.416 7.635 -16.709 0.50 28.66 C
ANISOU 1252 CB ATHR A 156 4307 2945 3638 1351 -824 236 C
ATOM 1253 CB BTHR A 156 -35.560 7.530 -16.733 0.50 31.66 C
ANISOU 1253 CB BTHR A 156 4665 3692 3672 961 -656 423 C
ATOM 1254 OG1ATHR A 156 -36.486 8.519 -16.372 0.50 30.67 O
ANISOU 1254 OG1ATHR A 156 4921 2979 3754 2080 -526 15 O
ATOM 1255 OG1BTHR A 156 -35.963 6.791 -17.875 0.50 41.03 O
ANISOU 1255 OG1BTHR A 156 6103 5047 4442 814 -49 557 O
ATOM 1256 CG2ATHR A 156 -35.611 7.089 -18.107 0.50 33.46 C
ANISOU 1256 CG2ATHR A 156 5388 3326 4001 1173 -329 627 C
ATOM 1257 CG2BTHR A 156 -34.237 8.157 -17.097 0.50 32.08 C
ANISOU 1257 CG2BTHR A 156 4904 3471 3814 1151 -94 706 C
ATOM 1258 N VAL A 157 -34.920 4.318 -16.450 1.00 23.27 N
ANISOU 1258 N VAL A 157 2777 2759 3304 246 -189 104 N
ATOM 1259 CA VAL A 157 -34.066 3.242 -16.902 1.00 22.40 C
ANISOU 1259 CA VAL A 157 2655 2817 3040 159 -391 204 C
ATOM 1260 C VAL A 157 -33.458 3.612 -18.262 1.00 22.97 C
ANISOU 1260 C VAL A 157 3133 2536 3058 204 -559 -45 C
ATOM 1261 O VAL A 157 -34.184 3.957 -19.186 1.00 24.96 O
ANISOU 1261 O VAL A 157 3138 3397 2949 480 -439 71 O
ATOM 1262 CB VAL A 157 -34.843 1.922 -17.006 1.00 24.35 C
ANISOU 1262 CB VAL A 157 2705 3061 3484 253 -420 19 C
ATOM 1263 CG1 VAL A 157 -34.004 0.820 -17.659 1.00 24.96 C
ANISOU 1263 CG1 VAL A 157 3002 3376 3108 65 -260 135 C
ATOM 1264 CG2 VAL A 157 -35.360 1.464 -15.649 1.00 25.41 C
ANISOU 1264 CG2 VAL A 157 3016 3459 3178 46 -68 -85 C
ATOM 1265 N ILE A 158 -32.121 3.480 -18.353 1.00 23.93 N
ANISOU 1265 N ILE A 158 3358 2813 2923 331 -140 165 N
ATOM 1266 CA AILE A 158 -31.314 3.667 -19.552 0.25 23.34 C
ANISOU 1266 CA AILE A 158 3405 2468 2997 472 -13 45 C
ATOM 1267 CA BILE A 158 -31.314 3.667 -19.552 0.25 23.35 C
ANISOU 1267 CA BILE A 158 3401 2470 3001 472 -12 42 C
ATOM 1268 CA CILE A 158 -31.408 3.633 -19.605 0.50 23.78 C
ANISOU 1268 CA CILE A 158 3213 2680 3143 508 -349 101 C
ATOM 1269 C ILE A 158 -30.689 2.319 -19.924 1.00 23.40 C
ANISOU 1269 C ILE A 158 3027 2703 3160 394 -77 -76 C
ATOM 1270 O ILE A 158 -29.991 1.702 -19.107 1.00 25.55 O
ANISOU 1270 O ILE A 158 3837 3026 2844 243 -569 123 O
ATOM 1271 CB AILE A 158 -30.197 4.721 -19.335 0.25 23.08 C
ANISOU 1271 CB AILE A 158 3705 2020 3045 569 640 64 C
ATOM 1272 CB BILE A 158 -30.198 4.722 -19.334 0.25 23.10 C
ANISOU 1272 CB BILE A 158 3698 2023 3055 571 641 56 C
ATOM 1273 CB CILE A 158 -30.466 4.859 -19.585 0.50 32.11 C
ANISOU 1273 CB CILE A 158 4510 3353 4336 -52 198 244 C
ATOM 1274 CG1AILE A 158 -30.750 6.018 -18.749 0.25 23.76 C
ANISOU 1274 CG1AILE A 158 3916 1806 3306 448 752 169 C
ATOM 1275 CG1BILE A 158 -30.752 6.019 -18.750 0.25 23.79 C
ANISOU 1275 CG1BILE A 158 3903 1812 3323 450 756 155 C
ATOM 1276 CG1CILE A 158 -29.278 4.747 -20.465 0.50 38.40 C
ANISOU 1276 CG1CILE A 158 4456 4135 6001 230 -274 262 C
ATOM 1277 CG2AILE A 158 -29.484 5.035 -20.649 0.25 24.84 C
ANISOU 1277 CG2AILE A 158 3847 2486 3104 597 411 12 C
ATOM 1278 CG2BILE A 158 -29.483 5.034 -20.648 0.25 24.86 C
ANISOU 1278 CG2BILE A 158 3840 2488 3118 598 413 5 C
ATOM 1279 CG2CILE A 158 -29.960 5.215 -18.197 0.50 34.37 C
ANISOU 1279 CG2CILE A 158 4109 3964 4988 -23 -980 520 C
ATOM 1280 CD1AILE A 158 -31.824 6.577 -19.620 0.25 23.59 C
ANISOU 1280 CD1AILE A 158 3806 1890 3265 611 643 342 C
ATOM 1281 CD1BILE A 158 -31.820 6.581 -19.626 0.25 23.64 C
ANISOU 1281 CD1BILE A 158 3784 1906 3294 612 648 319 C
ATOM 1282 CD1CILE A 158 -28.223 5.765 -20.074 0.50 40.35 C
ANISOU 1282 CD1CILE A 158 4629 3945 6757 126 -377 534 C
ATOM 1283 N GLU A 159 -30.923 1.855 -21.158 1.00 22.82 N
ANISOU 1283 N GLU A 159 3188 2603 2879 464 -139 16 N
ATOM 1284 CA GLU A 159 -30.186 0.694 -21.593 1.00 22.36 C
ANISOU 1284 CA GLU A 159 2877 2821 2798 184 -179 221 C
ATOM 1285 C GLU A 159 -28.744 1.109 -21.901 1.00 23.10 C
ANISOU 1285 C GLU A 159 3210 2747 2818 86 -182 111 C
ATOM 1286 O GLU A 159 -28.505 2.016 -22.697 1.00 24.81 O
ANISOU 1286 O GLU A 159 3226 3012 3188 245 -204 683 O
ATOM 1287 CB GLU A 159 -30.823 0.011 -22.798 1.00 24.47 C
ANISOU 1287 CB GLU A 159 3356 3188 2753 242 -169 -77 C
ATOM 1288 CG GLU A 159 -32.137 -0.650 -22.471 1.00 25.12 C
ANISOU 1288 CG GLU A 159 3134 3419 2989 35 -162 -124 C
ATOM 1289 CD GLU A 159 -32.852 -1.235 -23.672 1.00 26.01 C
ANISOU 1289 CD GLU A 159 3293 3777 2812 -104 -227 -340 C
ATOM 1290 OE1 GLU A 159 -34.101 -1.169 -23.699 1.00 26.96 O
ANISOU 1290 OE1 GLU A 159 3177 3762 3306 216 -275 -250 O
ATOM 1291 OE2 GLU A 159 -32.169 -1.738 -24.617 1.00 29.16 O
ANISOU 1291 OE2 GLU A 159 3845 3855 3380 94 -239 -361 O
ATOM 1292 N THR A 160 -27.783 0.386 -21.283 1.00 23.90 N
ANISOU 1292 N THR A 160 3348 2938 2794 -11 -95 267 N
ATOM 1293 CA THR A 160 -26.373 0.704 -21.392 1.00 22.39 C
ANISOU 1293 CA THR A 160 3246 2556 2705 -147 -51 428 C
ATOM 1294 C THR A 160 -25.580 -0.534 -21.758 1.00 22.45 C
ANISOU 1294 C THR A 160 3040 3049 2439 -40 -75 155 C
ATOM 1295 O THR A 160 -24.708 -0.975 -20.986 1.00 22.73 O
ANISOU 1295 O THR A 160 3068 2760 2807 -44 -140 77 O
ATOM 1296 CB THR A 160 -25.847 1.379 -20.109 1.00 22.51 C
ANISOU 1296 CB THR A 160 2989 2528 3034 322 -127 31 C
ATOM 1297 OG1 THR A 160 -26.267 0.671 -18.937 1.00 22.11 O
ANISOU 1297 OG1 THR A 160 3186 2706 2511 28 -120 256 O
ATOM 1298 CG2 THR A 160 -26.353 2.809 -20.046 1.00 24.88 C
ANISOU 1298 CG2 THR A 160 3509 2842 3104 -42 -19 508 C
ATOM 1299 N PRO A 161 -25.929 -1.211 -22.876 1.00 22.79 N
ANISOU 1299 N PRO A 161 2925 2987 2748 30 127 139 N
ATOM 1300 CA PRO A 161 -25.250 -2.434 -23.283 1.00 23.96 C
ANISOU 1300 CA PRO A 161 3330 2947 2829 217 50 -71 C
ATOM 1301 C PRO A 161 -23.792 -2.229 -23.637 1.00 23.98 C
ANISOU 1301 C PRO A 161 3530 2928 2654 -130 221 -180 C
ATOM 1302 O PRO A 161 -23.340 -1.129 -23.902 1.00 24.92 O
ANISOU 1302 O PRO A 161 3379 2861 3228 -102 110 264 O
ATOM 1303 CB PRO A 161 -26.045 -2.880 -24.485 1.00 25.70 C
ANISOU 1303 CB PRO A 161 3352 3467 2945 -85 34 -87 C
ATOM 1304 CG PRO A 161 -26.484 -1.575 -25.064 1.00 26.62 C
ANISOU 1304 CG PRO A 161 3742 3208 3164 -125 -324 -226 C
ATOM 1305 CD PRO A 161 -26.882 -0.773 -23.894 1.00 24.64 C
ANISOU 1305 CD PRO A 161 3381 3163 2817 44 -192 401 C
ATOM 1306 N GLY A 162 -23.051 -3.332 -23.624 1.00 24.85 N
ANISOU 1306 N GLY A 162 3571 2786 3085 -99 110 288 N
ATOM 1307 CA GLY A 162 -21.652 -3.321 -23.953 1.00 27.32 C
ANISOU 1307 CA GLY A 162 3502 3485 3392 -169 229 167 C
ATOM 1308 C GLY A 162 -20.869 -4.149 -22.931 1.00 24.93 C
ANISOU 1308 C GLY A 162 3417 3297 2758 -93 193 216 C
ATOM 1309 O GLY A 162 -20.328 -5.221 -23.254 1.00 29.26 O
ANISOU 1309 O GLY A 162 4039 3519 3559 138 133 28 O
ATOM 1310 N HIS A 163 -20.833 -3.655 -21.698 1.00 24.21 N
ANISOU 1310 N HIS A 163 2864 3400 2937 -53 228 82 N
ATOM 1311 CA HIS A 163 -20.225 -4.402 -20.624 1.00 24.09 C
ANISOU 1311 CA HIS A 163 3132 3098 2924 -99 90 600 C
ATOM 1312 C HIS A 163 -20.906 -5.764 -20.486 1.00 23.40 C
ANISOU 1312 C HIS A 163 2988 2943 2958 58 163 56 C
ATOM 1313 O HIS A 163 -20.256 -6.773 -20.240 1.00 25.28 O
ANISOU 1313 O HIS A 163 2988 2705 3911 96 -37 250 O
ATOM 1314 CB HIS A 163 -20.340 -3.613 -19.316 1.00 25.89 C
ANISOU 1314 CB HIS A 163 3154 3391 3293 -510 275 281 C
ATOM 1315 CG HIS A 163 -19.821 -4.366 -18.142 1.00 25.00 C
ANISOU 1315 CG HIS A 163 3353 3205 2942 -17 -60 301 C
ATOM 1316 ND1 HIS A 163 -18.475 -4.538 -17.893 1.00 26.37 N
ANISOU 1316 ND1 HIS A 163 2978 3530 3513 -343 -110 234 N
ATOM 1317 CD2 HIS A 163 -20.461 -4.996 -17.135 1.00 24.13 C
ANISOU 1317 CD2 HIS A 163 2927 3046 3197 -481 56 147 C
ATOM 1318 CE1 HIS A 163 -18.313 -5.241 -16.765 1.00 26.39 C
ANISOU 1318 CE1 HIS A 163 2971 3522 3534 -205 79 356 C
ATOM 1319 NE2 HIS A 163 -19.491 -5.506 -16.283 1.00 22.36 N
ANISOU 1319 NE2 HIS A 163 2993 2616 2887 76 -71 458 N
ATOM 1320 N ALA A 164 -22.217 -5.770 -20.605 1.00 22.97 N
ANISOU 1320 N ALA A 164 2733 2648 3348 73 223 34 N
ATOM 1321 CA ALA A 164 -23.035 -6.985 -20.623 1.00 21.45 C
ANISOU 1321 CA ALA A 164 2837 2401 2911 156 80 247 C
ATOM 1322 C ALA A 164 -24.283 -6.685 -21.450 1.00 22.03 C
ANISOU 1322 C ALA A 164 2755 2680 2933 13 -132 133 C
ATOM 1323 O ALA A 164 -24.713 -5.542 -21.504 1.00 22.48 O
ANISOU 1323 O ALA A 164 2795 2602 3145 241 -6 114 O
ATOM 1324 CB ALA A 164 -23.452 -7.379 -19.216 1.00 23.42 C
ANISOU 1324 CB ALA A 164 3122 2765 3011 71 -234 199 C
ATOM 1325 N SER A 165 -24.912 -7.728 -21.979 1.00 22.49 N
ANISOU 1325 N SER A 165 2836 2829 2880 225 -191 -45 N
ATOM 1326 CA SER A 165 -26.118 -7.599 -22.769 1.00 22.22 C
ANISOU 1326 CA SER A 165 2864 2829 2750 264 -190 -81 C
ATOM 1327 C SER A 165 -27.290 -7.121 -21.923 1.00 21.49 C
ANISOU 1327 C SER A 165 2967 2528 2670 193 -52 -289 C
ATOM 1328 O SER A 165 -28.254 -6.536 -22.469 1.00 25.43 O
ANISOU 1328 O SER A 165 3237 3371 3053 686 -248 -44 O
ATOM 1329 CB SER A 165 -26.465 -8.896 -23.482 1.00 24.23 C
ANISOU 1329 CB SER A 165 2559 3424 3222 35 -11 -612 C
ATOM 1330 OG SER A 165 -26.559 -9.997 -22.624 1.00 24.36 O
ANISOU 1330 OG SER A 165 3225 2963 3067 76 232 -325 O
ATOM 1331 N THR A 166 -27.226 -7.434 -20.641 1.00 20.74 N
ANISOU 1331 N THR A 166 2715 2644 2521 107 -348 -24 N
ATOM 1332 CA THR A 166 -28.308 -7.148 -19.699 1.00 20.74 C
ANISOU 1332 CA THR A 166 2680 2674 2526 351 -159 -33 C
ATOM 1333 C THR A 166 -28.118 -5.812 -19.016 1.00 21.01 C
ANISOU 1333 C THR A 166 2641 2513 2829 132 -436 33 C
ATOM 1334 O THR A 166 -28.891 -5.513 -18.100 1.00 22.35 O
ANISOU 1334 O THR A 166 2636 2890 2966 30 -409 -84 O
ATOM 1335 CB THR A 166 -28.314 -8.261 -18.658 1.00 19.76 C
ANISOU 1335 CB THR A 166 2281 2641 2588 146 -403 -15 C
ATOM 1336 OG1 THR A 166 -26.998 -8.306 -18.101 1.00 20.04 O
ANISOU 1336 OG1 THR A 166 2495 2483 2637 62 -155 -1 O
ATOM 1337 CG2 THR A 166 -28.686 -9.613 -19.207 1.00 21.97 C
ANISOU 1337 CG2 THR A 166 2428 3198 2722 113 -150 -25 C
ATOM 1338 N HIS A 167 -27.169 -4.999 -19.486 1.00 20.90 N
ANISOU 1338 N HIS A 167 2857 2490 2595 -119 55 184 N
ATOM 1339 CA HIS A 167 -26.765 -3.836 -18.680 1.00 20.32 C
ANISOU 1339 CA HIS A 167 2756 2429 2534 265 -122 151 C
ATOM 1340 C HIS A 167 -27.723 -2.664 -18.817 1.00 21.25 C
ANISOU 1340 C HIS A 167 2596 2675 2805 104 28 68 C
ATOM 1341 O HIS A 167 -27.980 -2.192 -19.917 1.00 21.81 O
ANISOU 1341 O HIS A 167 2956 2670 2660 114 -180 16 O
ATOM 1342 CB HIS A 167 -25.318 -3.451 -19.015 1.00 21.81 C
ANISOU 1342 CB HIS A 167 2697 2803 2785 -72 -174 219 C
ATOM 1343 CG HIS A 167 -24.686 -2.698 -17.920 1.00 22.07 C
ANISOU 1343 CG HIS A 167 2788 2844 2754 51 -76 -54 C
ATOM 1344 ND1 HIS A 167 -24.930 -1.364 -17.688 1.00 21.55 N
ANISOU 1344 ND1 HIS A 167 2840 2488 2859 -205 183 -41 N
ATOM 1345 CD2 HIS A 167 -23.938 -3.152 -16.865 1.00 21.98 C
ANISOU 1345 CD2 HIS A 167 2860 2608 2884 68 -270 188 C
ATOM 1346 CE1 HIS A 167 -24.302 -1.016 -16.565 1.00 23.62 C
ANISOU 1346 CE1 HIS A 167 2805 3091 3078 -225 -280 -103 C
ATOM 1347 NE2 HIS A 167 -23.690 -2.078 -16.053 1.00 22.03 N
ANISOU 1347 NE2 HIS A 167 2572 2770 3027 140 -272 145 N
ATOM 1348 N ILE A 168 -28.095 -2.112 -17.668 1.00 20.99 N
ANISOU 1348 N ILE A 168 2629 2753 2592 56 -73 146 N
ATOM 1349 CA ILE A 168 -28.926 -0.911 -17.580 1.00 21.68 C
ANISOU 1349 CA ILE A 168 2944 2512 2781 80 -229 199 C
ATOM 1350 C ILE A 168 -28.280 0.024 -16.549 1.00 21.32 C
ANISOU 1350 C ILE A 168 2765 2780 2555 138 -282 241 C
ATOM 1351 O ILE A 168 -27.516 -0.432 -15.676 1.00 21.37 O
ANISOU 1351 O ILE A 168 2719 2613 2787 192 -290 -77 O
ATOM 1352 CB ILE A 168 -30.379 -1.187 -17.212 1.00 21.12 C
ANISOU 1352 CB ILE A 168 2739 2495 2790 142 -90 171 C
ATOM 1353 CG1 ILE A 168 -30.515 -1.721 -15.794 1.00 21.65 C
ANISOU 1353 CG1 ILE A 168 2808 2793 2624 482 -18 102 C
ATOM 1354 CG2 ILE A 168 -30.990 -2.116 -18.258 1.00 22.40 C
ANISOU 1354 CG2 ILE A 168 2802 2996 2712 -178 -197 131 C
ATOM 1355 CD1 ILE A 168 -31.934 -1.992 -15.311 1.00 24.53 C
ANISOU 1355 CD1 ILE A 168 3233 3355 2732 527 17 379 C
ATOM 1356 N SER A 169 -28.603 1.298 -16.645 1.00 22.09 N
ANISOU 1356 N SER A 169 2949 2720 2725 303 -136 199 N
ATOM 1357 CA SER A 169 -28.197 2.319 -15.687 1.00 21.64 C
ANISOU 1357 CA SER A 169 2536 2545 3140 257 -26 235 C
ATOM 1358 C SER A 169 -29.469 3.100 -15.320 1.00 21.98 C
ANISOU 1358 C SER A 169 2832 2584 2935 326 -215 154 C
ATOM 1359 O SER A 169 -30.443 3.039 -16.064 1.00 24.16 O
ANISOU 1359 O SER A 169 3195 2856 3128 387 -392 -185 O
ATOM 1360 CB SER A 169 -27.091 3.204 -16.260 1.00 22.34 C
ANISOU 1360 CB SER A 169 2877 2676 2933 162 -328 178 C
ATOM 1361 OG SER A 169 -25.973 2.463 -16.735 1.00 22.60 O
ANISOU 1361 OG SER A 169 2767 2449 3369 73 -70 36 O
ATOM 1362 N LEU A 170 -29.445 3.829 -14.200 1.00 22.27 N
ANISOU 1362 N LEU A 170 2900 2738 2825 308 -119 -201 N
ATOM 1363 CA LEU A 170 -30.604 4.558 -13.731 1.00 22.97 C
ANISOU 1363 CA LEU A 170 3202 2322 3202 235 -95 -131 C
ATOM 1364 C LEU A 170 -30.244 6.037 -13.683 1.00 24.41 C
ANISOU 1364 C LEU A 170 3275 2685 3313 -24 40 -1 C
ATOM 1365 O LEU A 170 -29.316 6.405 -12.964 1.00 26.19 O
ANISOU 1365 O LEU A 170 3357 2985 3610 222 -352 306 O
ATOM 1366 CB LEU A 170 -31.020 4.041 -12.353 1.00 24.32 C
ANISOU 1366 CB LEU A 170 3373 2767 3100 111 146 -238 C
ATOM 1367 CG LEU A 170 -31.313 2.549 -12.243 1.00 24.54 C
ANISOU 1367 CG LEU A 170 3332 2857 3134 36 -82 105 C
ATOM 1368 CD1 LEU A 170 -31.658 2.137 -10.841 1.00 27.55 C
ANISOU 1368 CD1 LEU A 170 3801 3466 3200 -309 -283 -194 C
ATOM 1369 CD2 LEU A 170 -32.332 2.031 -13.223 1.00 25.63 C
ANISOU 1369 CD2 LEU A 170 3329 3148 3263 -168 78 -31 C
ATOM 1370 N TYR A 171 -31.000 6.861 -14.442 1.00 26.10 N
ANISOU 1370 N TYR A 171 3657 2992 3268 178 -345 126 N
ATOM 1371 CA TYR A 171 -30.700 8.285 -14.550 1.00 25.78 C
ANISOU 1371 CA TYR A 171 3531 2882 3384 294 -200 205 C
ATOM 1372 C TYR A 171 -31.739 9.118 -13.818 1.00 24.79 C
ANISOU 1372 C TYR A 171 2847 3094 3480 71 -111 130 C
ATOM 1373 O TYR A 171 -32.926 8.925 -14.040 1.00 26.49 O
ANISOU 1373 O TYR A 171 3194 2956 3916 320 76 -160 O
ATOM 1374 CB TYR A 171 -30.677 8.715 -16.025 1.00 25.53 C
ANISOU 1374 CB TYR A 171 3391 3127 3183 600 -456 60 C
ATOM 1375 CG TYR A 171 -30.359 10.178 -16.269 1.00 26.90 C
ANISOU 1375 CG TYR A 171 4052 2996 3173 624 -35 82 C
ATOM 1376 CD1 TYR A 171 -29.116 10.693 -15.933 1.00 31.64 C
ANISOU 1376 CD1 TYR A 171 4549 3332 4140 215 -134 179 C
ATOM 1377 CD2 TYR A 171 -31.273 11.047 -16.832 1.00 32.37 C
ANISOU 1377 CD2 TYR A 171 4692 3608 4000 452 -595 -207 C
ATOM 1378 CE1 TYR A 171 -28.779 12.024 -16.133 1.00 32.28 C
ANISOU 1378 CE1 TYR A 171 5275 3212 3777 637 178 214 C
ATOM 1379 CE2 TYR A 171 -30.940 12.385 -17.067 1.00 35.21 C
ANISOU 1379 CE2 TYR A 171 5256 3771 4349 607 41 239 C
ATOM 1380 CZ TYR A 171 -29.685 12.871 -16.747 1.00 33.41 C
ANISOU 1380 CZ TYR A 171 5538 3072 4086 495 16 759 C
ATOM 1381 OH TYR A 171 -29.356 14.210 -16.921 1.00 36.19 O
ANISOU 1381 OH TYR A 171 6111 3056 4582 752 -70 864 O
ATOM 1382 N ARG A 172 -31.299 10.085 -13.025 1.00 26.23 N
ANISOU 1382 N ARG A 172 3222 3110 3635 149 12 -2 N
ATOM 1383 CA ARG A 172 -32.176 11.000 -12.318 1.00 28.06 C
ANISOU 1383 CA ARG A 172 4191 2871 3601 486 -352 -131 C
ATOM 1384 C ARG A 172 -32.029 12.383 -12.956 1.00 30.34 C
ANISOU 1384 C ARG A 172 4325 3187 4015 430 96 95 C
ATOM 1385 O ARG A 172 -31.031 13.085 -12.736 1.00 30.85 O
ANISOU 1385 O ARG A 172 4513 3155 4051 684 1 94 O
ATOM 1386 CB ARG A 172 -31.779 11.056 -10.834 1.00 28.06 C
ANISOU 1386 CB ARG A 172 4423 2664 3576 39 -144 -134 C
ATOM 1387 CG ARG A 172 -32.791 11.892 -10.067 1.00 29.41 C
ANISOU 1387 CG ARG A 172 4531 2629 4014 556 -184 -604 C
ATOM 1388 CD ARG A 172 -32.762 11.628 -8.608 1.00 31.70 C
ANISOU 1388 CD ARG A 172 4280 3746 4017 533 515 -525 C
ATOM 1389 NE ARG A 172 -31.470 11.973 -8.018 1.00 30.38 N
ANISOU 1389 NE ARG A 172 4259 3162 4122 202 -286 -489 N
ATOM 1390 CZ ARG A 172 -31.067 11.693 -6.785 1.00 30.63 C
ANISOU 1390 CZ ARG A 172 4487 3164 3988 387 118 -326 C
ATOM 1391 NH1 ARG A 172 -31.799 10.930 -6.020 1.00 30.38 N
ANISOU 1391 NH1 ARG A 172 4299 3422 3821 399 -237 233 N
ATOM 1392 NH2 ARG A 172 -29.891 12.155 -6.346 1.00 33.77 N
ANISOU 1392 NH2 ARG A 172 4955 3725 4152 70 -315 104 N
ATOM 1393 N GLU A 173 -33.024 12.756 -13.770 1.00 30.81 N
ANISOU 1393 N GLU A 173 4651 3282 3775 149 -33 76 N
ATOM 1394 CA GLU A 173 -32.982 13.999 -14.532 1.00 33.39 C
ANISOU 1394 CA GLU A 173 5064 3084 4539 583 -72 173 C
ATOM 1395 C GLU A 173 -32.882 15.222 -13.625 1.00 32.78 C
ANISOU 1395 C GLU A 173 5234 3214 4005 595 -169 340 C
ATOM 1396 O GLU A 173 -32.257 16.186 -14.007 1.00 36.77 O
ANISOU 1396 O GLU A 173 5695 2963 5311 385 377 576 O
ATOM 1397 CB GLU A 173 -34.180 14.070 -15.475 1.00 38.42 C
ANISOU 1397 CB GLU A 173 5704 4251 4642 -94 -622 949 C
ATOM 1398 N ARG A 174 -33.464 15.161 -12.419 1.00 35.39 N
ANISOU 1398 N ARG A 174 5956 2946 4546 715 -379 7 N
ATOM 1399 CA ARG A 174 -33.502 16.321 -11.541 1.00 33.29 C
ANISOU 1399 CA ARG A 174 5298 2949 4400 785 79 -163 C
ATOM 1400 C ARG A 174 -32.105 16.909 -11.324 1.00 32.69 C
ANISOU 1400 C ARG A 174 4802 2833 4786 464 -341 51 C
ATOM 1401 O ARG A 174 -31.937 18.128 -11.430 1.00 36.20 O
ANISOU 1401 O ARG A 174 6085 2420 5250 530 413 371 O
ATOM 1402 CB ARG A 174 -34.173 16.027 -10.200 1.00 35.62 C
ANISOU 1402 CB ARG A 174 5677 3139 4717 451 10 -560 C
ATOM 1403 CG ARG A 174 -34.125 17.209 -9.241 1.00 37.12 C
ANISOU 1403 CG ARG A 174 5685 3308 5112 130 290 -897 C
ATOM 1404 CD ARG A 174 -34.934 16.929 -7.998 1.00 36.91 C
ANISOU 1404 CD ARG A 174 6095 3223 4705 -178 285 -841 C
ATOM 1405 NE ARG A 174 -34.623 15.671 -7.308 1.00 38.32 N
ANISOU 1405 NE ARG A 174 6186 3403 4969 -180 445 -230 N
ATOM 1406 CZ ARG A 174 -33.540 15.434 -6.587 1.00 37.23 C
ANISOU 1406 CZ ARG A 174 5638 3952 4555 -173 772 -37 C
ATOM 1407 NH1 ARG A 174 -33.410 14.291 -5.958 1.00 37.83 N
ANISOU 1407 NH1 ARG A 174 6162 3429 4781 -3 752 -520 N
ATOM 1408 NH2 ARG A 174 -32.610 16.353 -6.448 1.00 37.37 N
ANISOU 1408 NH2 ARG A 174 5770 3745 4682 169 638 -412 N
ATOM 1409 N ASP A 175 -31.136 16.058 -10.948 1.00 31.95 N
ANISOU 1409 N ASP A 175 5442 2156 4540 853 15 -54 N
ATOM 1410 CA ASP A 175 -29.791 16.495 -10.613 1.00 31.26 C
ANISOU 1410 CA ASP A 175 4710 2416 4751 350 -58 -72 C
ATOM 1411 C ASP A 175 -28.677 15.814 -11.423 1.00 31.44 C
ANISOU 1411 C ASP A 175 4803 2360 4782 415 -25 -91 C
ATOM 1412 O ASP A 175 -27.485 16.074 -11.172 1.00 33.07 O
ANISOU 1412 O ASP A 175 4665 3161 4738 106 -96 -164 O
ATOM 1413 CB ASP A 175 -29.537 16.276 -9.134 1.00 35.80 C
ANISOU 1413 CB ASP A 175 5688 3042 4871 258 240 -79 C
ATOM 1414 CG ASP A 175 -29.619 14.836 -8.642 1.00 33.16 C
ANISOU 1414 CG ASP A 175 4873 3156 4571 -238 276 -1 C
ATOM 1415 OD1 ASP A 175 -30.020 13.963 -9.459 1.00 31.33 O
ANISOU 1415 OD1 ASP A 175 4506 2960 4437 -79 -65 -173 O
ATOM 1416 OD2 ASP A 175 -29.287 14.611 -7.448 1.00 33.54 O
ANISOU 1416 OD2 ASP A 175 5056 3398 4289 23 20 -284 O
ATOM 1417 N GLY A 176 -29.040 14.975 -12.397 1.00 32.45 N
ANISOU 1417 N GLY A 176 5372 2965 3993 160 185 325 N
ATOM 1418 CA GLY A 176 -28.073 14.393 -13.337 1.00 29.40 C
ANISOU 1418 CA GLY A 176 4198 2834 4139 237 -166 367 C
ATOM 1419 C GLY A 176 -27.295 13.222 -12.760 1.00 27.03 C
ANISOU 1419 C GLY A 176 3799 2832 3639 37 -175 334 C
ATOM 1420 O GLY A 176 -26.299 12.820 -13.349 1.00 29.76 O
ANISOU 1420 O GLY A 176 4110 3165 4034 -15 -174 43 O
ATOM 1421 N VAL A 177 -27.787 12.646 -11.652 1.00 26.95 N
ANISOU 1421 N VAL A 177 3708 2854 3680 342 10 237 N
ATOM 1422 CA VAL A 177 -27.102 11.507 -11.032 1.00 26.64 C
ANISOU 1422 CA VAL A 177 4128 2332 3663 -3 -530 -12 C
ATOM 1423 C VAL A 177 -27.427 10.245 -11.831 1.00 25.58 C
ANISOU 1423 C VAL A 177 3580 2343 3795 17 -262 85 C
ATOM 1424 O VAL A 177 -28.572 10.018 -12.198 1.00 27.26 O
ANISOU 1424 O VAL A 177 4027 2379 3950 138 -332 82 O
ATOM 1425 CB VAL A 177 -27.469 11.356 -9.546 1.00 30.80 C
ANISOU 1425 CB VAL A 177 4601 2986 4114 -116 -579 -55 C
ATOM 1426 CG1 VAL A 177 -27.078 9.989 -8.988 1.00 31.73 C
ANISOU 1426 CG1 VAL A 177 4679 3300 4074 365 -352 -76 C
ATOM 1427 CG2 VAL A 177 -26.838 12.475 -8.715 1.00 32.01 C
ANISOU 1427 CG2 VAL A 177 5007 3326 3830 98 -703 -406 C
ATOM 1428 N LEU A 178 -26.414 9.443 -12.110 1.00 25.56 N
ANISOU 1428 N LEU A 178 3915 2438 3359 213 -406 -77 N
ATOM 1429 CA LEU A 178 -26.576 8.150 -12.764 1.00 24.85 C
ANISOU 1429 CA LEU A 178 3483 2550 3407 -262 -232 34 C
ATOM 1430 C LEU A 178 -26.121 7.055 -11.812 1.00 24.60 C
ANISOU 1430 C LEU A 178 3375 2743 3227 66 -103 54 C
ATOM 1431 O LEU A 178 -25.006 7.134 -11.310 1.00 25.41 O
ANISOU 1431 O LEU A 178 3445 2682 3527 -285 -150 169 O
ATOM 1432 CB LEU A 178 -25.720 8.082 -14.030 1.00 25.94 C
ANISOU 1432 CB LEU A 178 3757 2518 3579 -204 -53 270 C
ATOM 1433 CG LEU A 178 -25.945 6.837 -14.889 1.00 25.46 C
ANISOU 1433 CG LEU A 178 3727 2700 3245 -60 -12 239 C
ATOM 1434 CD1 LEU A 178 -27.231 6.974 -15.692 1.00 24.70 C
ANISOU 1434 CD1 LEU A 178 3496 2479 3411 160 48 332 C
ATOM 1435 CD2 LEU A 178 -24.815 6.569 -15.792 1.00 26.36 C
ANISOU 1435 CD2 LEU A 178 3645 3111 3259 -117 -241 151 C
ATOM 1436 N ILE A 179 -26.987 6.074 -11.548 1.00 22.98 N
ANISOU 1436 N ILE A 179 3176 2560 2996 280 -123 -29 N
ATOM 1437 CA ILE A 179 -26.548 4.851 -10.908 1.00 22.67 C
ANISOU 1437 CA ILE A 179 3253 2213 3147 224 -172 157 C
ATOM 1438 C ILE A 179 -26.096 3.993 -12.076 1.00 22.31 C
ANISOU 1438 C ILE A 179 2987 2354 3134 -27 -61 121 C
ATOM 1439 O ILE A 179 -26.928 3.488 -12.838 1.00 23.47 O
ANISOU 1439 O ILE A 179 3061 2597 3259 49 -173 143 O
ATOM 1440 CB ILE A 179 -27.660 4.218 -10.056 1.00 24.70 C
ANISOU 1440 CB ILE A 179 3213 3004 3169 137 -158 15 C
ATOM 1441 CG1 ILE A 179 -28.172 5.219 -9.011 1.00 28.99 C
ANISOU 1441 CG1 ILE A 179 4039 3519 3458 614 297 53 C
ATOM 1442 CG2 ILE A 179 -27.132 2.925 -9.429 1.00 26.15 C
ANISOU 1442 CG2 ILE A 179 3328 3115 3492 -9 154 353 C
ATOM 1443 CD1 ILE A 179 -29.369 4.780 -8.167 1.00 33.00 C
ANISOU 1443 CD1 ILE A 179 4783 3784 3969 837 471 53 C
ATOM 1444 N GLY A 180 -24.765 3.914 -12.290 1.00 22.94 N
ANISOU 1444 N GLY A 180 2765 2710 3242 -96 -175 214 N
ATOM 1445 CA GLY A 180 -24.241 3.497 -13.587 1.00 23.79 C
ANISOU 1445 CA GLY A 180 3310 2624 3104 144 158 -55 C
ATOM 1446 C GLY A 180 -24.078 2.001 -13.791 1.00 22.85 C
ANISOU 1446 C GLY A 180 2979 2679 3024 324 -66 217 C
ATOM 1447 O GLY A 180 -23.973 1.570 -14.949 1.00 23.64 O
ANISOU 1447 O GLY A 180 3346 2796 2840 -39 -3 127 O
ATOM 1448 N GLY A 181 -24.030 1.218 -12.695 1.00 21.07 N
ANISOU 1448 N GLY A 181 2650 2413 2943 -68 -75 -189 N
ATOM 1449 CA GLY A 181 -23.548 -0.137 -12.866 1.00 21.81 C
ANISOU 1449 CA GLY A 181 2741 2720 2824 -39 -66 -38 C
ATOM 1450 C GLY A 181 -22.080 -0.144 -13.280 1.00 21.87 C
ANISOU 1450 C GLY A 181 2629 2655 3026 18 -141 178 C
ATOM 1451 O GLY A 181 -21.301 0.709 -12.831 1.00 23.49 O
ANISOU 1451 O GLY A 181 2980 2770 3177 -548 -321 280 O
ATOM 1452 N ASP A 182 -21.743 -1.082 -14.179 1.00 21.81 N
ANISOU 1452 N ASP A 182 2926 2580 2779 -290 -319 17 N
ATOM 1453 CA ASP A 182 -20.393 -1.250 -14.652 1.00 21.87 C
ANISOU 1453 CA ASP A 182 2615 2936 2757 -261 -142 153 C
ATOM 1454 C ASP A 182 -20.148 -0.618 -16.027 1.00 23.00 C
ANISOU 1454 C ASP A 182 2846 2663 3230 -216 -71 222 C
ATOM 1455 O ASP A 182 -19.139 -0.895 -16.662 1.00 24.78 O
ANISOU 1455 O ASP A 182 2780 3043 3594 207 386 329 O
ATOM 1456 CB ASP A 182 -20.008 -2.718 -14.637 1.00 22.63 C
ANISOU 1456 CB ASP A 182 2994 2694 2910 -251 -212 455 C
ATOM 1457 CG ASP A 182 -19.844 -3.361 -13.257 1.00 21.06 C
ANISOU 1457 CG ASP A 182 2616 2651 2735 -359 51 207 C
ATOM 1458 OD1 ASP A 182 -20.053 -2.597 -12.238 1.00 22.94 O
ANISOU 1458 OD1 ASP A 182 3002 2741 2974 -55 -63 205 O
ATOM 1459 OD2 ASP A 182 -19.566 -4.618 -13.209 1.00 21.64 O
ANISOU 1459 OD2 ASP A 182 3137 1976 3108 -30 -4 389 O
ATOM 1460 N ALA A 183 -21.045 0.249 -16.484 1.00 23.46 N
ANISOU 1460 N ALA A 183 3035 2672 3206 -14 202 440 N
ATOM 1461 CA ALA A 183 -20.883 0.851 -17.792 1.00 24.27 C
ANISOU 1461 CA ALA A 183 3146 2831 3247 -130 -17 521 C
ATOM 1462 C ALA A 183 -19.659 1.748 -17.867 1.00 25.75 C
ANISOU 1462 C ALA A 183 3278 3069 3435 -139 231 333 C
ATOM 1463 O ALA A 183 -18.986 1.738 -18.894 1.00 30.71 O
ANISOU 1463 O ALA A 183 4268 3880 3521 -796 565 460 O
ATOM 1464 CB ALA A 183 -22.103 1.618 -18.214 1.00 25.87 C
ANISOU 1464 CB ALA A 183 3359 2970 3498 -87 -356 586 C
ATOM 1465 N LEU A 184 -19.370 2.442 -16.761 1.00 25.74 N
ANISOU 1465 N LEU A 184 3265 3012 3502 -329 239 471 N
ATOM 1466 CA LEU A 184 -18.258 3.373 -16.695 1.00 27.91 C
ANISOU 1466 CA LEU A 184 3731 3039 3834 -376 341 158 C
ATOM 1467 C LEU A 184 -17.682 3.308 -15.286 1.00 30.72 C
ANISOU 1467 C LEU A 184 3601 3807 4265 -316 -20 -39 C
ATOM 1468 O LEU A 184 -18.361 3.674 -14.306 1.00 36.78 O
ANISOU 1468 O LEU A 184 4915 4213 4846 600 -764 89 O
ATOM 1469 CB LEU A 184 -18.730 4.776 -17.021 1.00 31.82 C
ANISOU 1469 CB LEU A 184 4082 3169 4837 -677 370 567 C
ATOM 1470 CG LEU A 184 -17.598 5.788 -17.204 1.00 35.29 C
ANISOU 1470 CG LEU A 184 4466 3687 5255 -655 703 792 C
ATOM 1471 CD1 LEU A 184 -16.558 5.374 -18.253 1.00 39.46 C
ANISOU 1471 CD1 LEU A 184 5455 4149 5390 -994 909 247 C
ATOM 1472 CD2 LEU A 184 -18.187 7.144 -17.587 1.00 41.77 C
ANISOU 1472 CD2 LEU A 184 6423 3789 5658 -11 91 962 C
ATOM 1473 N ILE A 185 -16.496 2.736 -15.185 1.00 31.68 N
ANISOU 1473 N ILE A 185 3566 4104 4368 202 -54 229 N
ATOM 1474 CA ILE A 185 -15.791 2.596 -13.916 1.00 31.69 C
ANISOU 1474 CA ILE A 185 3650 3756 4634 -461 -101 55 C
ATOM 1475 C ILE A 185 -14.550 3.485 -13.979 1.00 33.51 C
ANISOU 1475 C ILE A 185 3765 3631 5338 -424 55 360 C
ATOM 1476 O ILE A 185 -13.824 3.478 -14.975 1.00 36.77 O
ANISOU 1476 O ILE A 185 4628 4027 5314 -321 546 854 O
ATOM 1477 CB ILE A 185 -15.443 1.116 -13.693 1.00 33.31 C
ANISOU 1477 CB ILE A 185 3574 4230 4852 -246 -375 486 C
ATOM 1478 CG1 ILE A 185 -16.703 0.286 -13.658 1.00 33.77 C
ANISOU 1478 CG1 ILE A 185 4064 4676 4092 -869 -598 266 C
ATOM 1479 CG2 ILE A 185 -14.605 0.911 -12.427 1.00 34.54 C
ANISOU 1479 CG2 ILE A 185 4053 4095 4976 -579 -571 285 C
ATOM 1480 CD1 ILE A 185 -16.439 -1.184 -13.685 1.00 35.91 C
ANISOU 1480 CD1 ILE A 185 4499 4818 4326 -491 -323 605 C
ATOM 1481 N GLY A 186 -14.334 4.246 -12.911 1.00 34.58 N
ANISOU 1481 N GLY A 186 4283 4329 4525 -275 115 1012 N
ATOM 1482 CA GLY A 186 -13.309 5.270 -12.869 1.00 34.60 C
ANISOU 1482 CA GLY A 186 3683 3878 5585 -446 -370 828 C
ATOM 1483 C GLY A 186 -11.864 4.787 -13.014 1.00 41.26 C
ANISOU 1483 C GLY A 186 4423 5155 6097 -337 242 930 C
ATOM 1484 O GLY A 186 -11.038 5.490 -13.616 1.00 46.50 O
ANISOU 1484 O GLY A 186 5333 5423 6910 -915 687 1008 O
ATOM 1485 N HIS A 187 -11.561 3.620 -12.438 1.00 39.44 N
ANISOU 1485 N HIS A 187 3884 4760 6339 -412 -484 368 N
ATOM 1486 CA HIS A 187 -10.178 3.202 -12.249 1.00 44.01 C
ANISOU 1486 CA HIS A 187 4516 5751 6455 -308 -375 586 C
ATOM 1487 C HIS A 187 -9.767 2.151 -13.272 1.00 43.46 C
ANISOU 1487 C HIS A 187 3847 5467 7198 -766 -445 -454 C
ATOM 1488 O HIS A 187 -8.555 1.947 -13.482 1.00 51.61 O
ANISOU 1488 O HIS A 187 4179 7166 8266 -381 -41 151 O
ATOM 1489 CB HIS A 187 -9.916 2.762 -10.797 1.00 44.52 C
ANISOU 1489 CB HIS A 187 4773 6274 5867 -962 -1384 759 C
ATOM 1490 CG HIS A 187 -10.725 1.601 -10.302 1.00 47.44 C
ANISOU 1490 CG HIS A 187 5466 5910 6650 -775 -437 1559 C
ATOM 1491 ND1 HIS A 187 -12.067 1.727 -10.019 1.00 46.69 N
ANISOU 1491 ND1 HIS A 187 5623 5860 6257 -1057 -787 855 N
ATOM 1492 CD2 HIS A 187 -10.415 0.309 -10.057 1.00 53.68 C
ANISOU 1492 CD2 HIS A 187 5948 6862 7588 203 -148 1588 C
ATOM 1493 CE1 HIS A 187 -12.543 0.549 -9.611 1.00 47.74 C
ANISOU 1493 CE1 HIS A 187 5580 6481 6077 -223 -470 2001 C
ATOM 1494 NE2 HIS A 187 -11.553 -0.328 -9.616 1.00 54.56 N
ANISOU 1494 NE2 HIS A 187 6954 5532 8244 -180 -334 1284 N
ATOM 1495 N ILE A 188 -10.751 1.473 -13.875 1.00 42.22 N
ANISOU 1495 N ILE A 188 4023 4920 7099 -706 -41 -78 N
ATOM 1496 CA ILE A 188 -10.456 0.378 -14.791 1.00 40.93 C
ANISOU 1496 CA ILE A 188 4589 4917 6046 -130 -523 -508 C
ATOM 1497 C ILE A 188 -11.491 0.336 -15.918 1.00 42.82 C
ANISOU 1497 C ILE A 188 4423 5836 6012 -49 -247 -338 C
ATOM 1498 O ILE A 188 -12.650 0.722 -15.767 1.00 41.98 O
ANISOU 1498 O ILE A 188 4477 4703 6771 -154 112 281 O
ATOM 1499 CB ILE A 188 -10.372 -0.959 -14.031 1.00 47.26 C
ANISOU 1499 CB ILE A 188 6516 4921 6521 -1097 -378 68 C
ATOM 1500 N SER A 189 -11.054 -0.113 -17.093 1.00 42.52 N
ANISOU 1500 N SER A 189 4231 5442 6482 -399 -217 -521 N
ATOM 1501 CA SER A 189 -11.974 -0.249 -18.208 1.00 39.95 C
ANISOU 1501 CA SER A 189 5218 3912 6048 -206 -201 -316 C
ATOM 1502 C SER A 189 -12.948 -1.381 -17.870 1.00 41.27 C
ANISOU 1502 C SER A 189 4643 4409 6631 -576 -254 183 C
ATOM 1503 O SER A 189 -12.609 -2.270 -17.071 1.00 43.44 O
ANISOU 1503 O SER A 189 5321 5158 6025 -647 -1558 467 O
ATOM 1504 CB SER A 189 -11.219 -0.496 -19.489 1.00 48.31 C
ANISOU 1504 CB SER A 189 6115 5896 6343 588 387 19 C
ATOM 1505 OG SER A 189 -10.296 -1.547 -19.268 1.00 53.09 O
ANISOU 1505 OG SER A 189 5988 7187 6997 975 -37 -686 O
ATOM 1506 N SER A 190 -14.151 -1.297 -18.438 1.00 39.14 N
ANISOU 1506 N SER A 190 4670 4727 5475 -435 -212 118 N
ATOM 1507 CA SER A 190 -15.249 -2.214 -18.163 1.00 39.85 C
ANISOU 1507 CA SER A 190 4456 5073 5613 -301 427 -191 C
ATOM 1508 C SER A 190 -15.683 -2.854 -19.479 1.00 40.76 C
ANISOU 1508 C SER A 190 4352 5526 5609 167 233 -433 C
ATOM 1509 O SER A 190 -16.874 -3.021 -19.719 1.00 37.18 O
ANISOU 1509 O SER A 190 4094 4610 5422 -409 685 -143 O
ATOM 1510 CB SER A 190 -16.436 -1.510 -17.490 1.00 36.54 C
ANISOU 1510 CB SER A 190 3573 5862 4449 -774 928 -277 C
ATOM 1511 OG SER A 190 -16.579 -0.174 -17.903 1.00 42.49 O
ANISOU 1511 OG SER A 190 4854 5831 5460 123 -113 -561 O
ATOM 1512 N ASN A 191 -14.684 -3.246 -20.297 1.00 39.00 N
ANISOU 1512 N ASN A 191 4718 5018 5081 -439 58 -895 N
ATOM 1513 CA ASN A 191 -14.913 -3.616 -21.680 1.00 37.91 C
ANISOU 1513 CA ASN A 191 4713 4172 5519 -315 764 -538 C
ATOM 1514 C ASN A 191 -15.816 -4.846 -21.744 1.00 34.11 C
ANISOU 1514 C ASN A 191 3289 4944 4726 -754 131 -418 C
ATOM 1515 O ASN A 191 -15.916 -5.555 -20.781 1.00 37.31 O
ANISOU 1515 O ASN A 191 4442 4550 5185 -368 -22 491 O
ATOM 1516 CB ASN A 191 -13.598 -3.921 -22.362 1.00 38.84 C
ANISOU 1516 CB ASN A 191 4179 4784 5794 -422 812 -500 C
ATOM 1517 CG ASN A 191 -12.930 -2.645 -22.822 1.00 43.13 C
ANISOU 1517 CG ASN A 191 5425 4783 6180 -971 1400 67 C
ATOM 1518 OD1 ASN A 191 -13.505 -1.545 -22.672 1.00 50.78 O
ANISOU 1518 OD1 ASN A 191 5902 5881 7509 -388 513 -305 O
ATOM 1519 ND2 ASN A 191 -11.740 -2.763 -23.381 1.00 46.72 N
ANISOU 1519 ND2 ASN A 191 5776 5507 6469 273 1277 551 N
ATOM 1520 N PRO A 192 -16.450 -5.153 -22.900 1.00 40.30 N
ANISOU 1520 N PRO A 192 4812 5344 5158 -654 181 44 N
ATOM 1521 CA PRO A 192 -17.354 -6.285 -23.003 1.00 31.20 C
ANISOU 1521 CA PRO A 192 3144 4742 3969 64 92 119 C
ATOM 1522 C PRO A 192 -16.788 -7.579 -22.459 1.00 32.29 C
ANISOU 1522 C PRO A 192 2471 4836 4961 231 540 505 C
ATOM 1523 O PRO A 192 -15.704 -7.945 -22.840 1.00 35.69 O
ANISOU 1523 O PRO A 192 3652 4863 5044 618 974 774 O
ATOM 1524 CB PRO A 192 -17.588 -6.391 -24.536 1.00 33.25 C
ANISOU 1524 CB PRO A 192 3092 4844 4696 807 -70 302 C
ATOM 1525 CG PRO A 192 -17.462 -4.979 -25.017 1.00 39.63 C
ANISOU 1525 CG PRO A 192 4861 5090 5107 423 -236 663 C
ATOM 1526 CD PRO A 192 -16.354 -4.407 -24.164 1.00 44.44 C
ANISOU 1526 CD PRO A 192 5786 5739 5361 -143 -395 85 C
ATOM 1527 N ILE A 193 -17.587 -8.221 -21.583 1.00 34.68 N
ANISOU 1527 N ILE A 193 3095 5493 4589 -309 610 -147 N
ATOM 1528 CA ILE A 193 -17.374 -9.557 -21.077 1.00 32.66 C
ANISOU 1528 CA ILE A 193 3617 4342 4449 -1072 -38 -273 C
ATOM 1529 C ILE A 193 -18.087 -10.546 -21.996 1.00 33.50 C
ANISOU 1529 C ILE A 193 3711 4487 4531 -694 -325 -149 C
ATOM 1530 O ILE A 193 -19.293 -10.417 -22.175 1.00 33.30 O
ANISOU 1530 O ILE A 193 3858 4080 4712 -116 81 -237 O
ATOM 1531 CB ILE A 193 -17.902 -9.653 -19.629 1.00 35.87 C
ANISOU 1531 CB ILE A 193 3737 5496 4396 -767 250 -754 C
ATOM 1532 CG1 ILE A 193 -17.272 -8.557 -18.701 1.00 40.68 C
ANISOU 1532 CG1 ILE A 193 3985 6971 4500 -1358 1000 -821 C
ATOM 1533 CG2 ILE A 193 -17.738 -11.069 -19.069 1.00 35.34 C
ANISOU 1533 CG2 ILE A 193 3300 4944 5185 -608 716 -400 C
ATOM 1534 CD1 ILE A 193 -15.772 -8.520 -18.749 1.00 46.57 C
ANISOU 1534 CD1 ILE A 193 4142 7940 5611 -887 934 -893 C
ATOM 1535 N LEU A 194 -17.310 -11.454 -22.617 1.00 30.44 N
ANISOU 1535 N LEU A 194 3093 4545 3930 -77 219 101 N
ATOM 1536 CA LEU A 194 -17.851 -12.433 -23.567 1.00 32.61 C
ANISOU 1536 CA LEU A 194 3462 4961 3968 -455 212 97 C
ATOM 1537 C LEU A 194 -19.053 -13.212 -23.047 1.00 29.47 C
ANISOU 1537 C LEU A 194 3117 4578 3502 -204 -74 188 C
ATOM 1538 O LEU A 194 -19.016 -13.742 -21.952 1.00 32.01 O
ANISOU 1538 O LEU A 194 3403 4859 3900 81 -146 63 O
ATOM 1539 CB LEU A 194 -16.801 -13.446 -24.004 1.00 39.05 C
ANISOU 1539 CB LEU A 194 2654 6637 5546 344 540 134 C
ATOM 1540 CG LEU A 194 -16.156 -13.236 -25.369 1.00 50.68 C
ANISOU 1540 CG LEU A 194 5126 8083 6047 843 265 -635 C
ATOM 1541 CD1 LEU A 194 -15.143 -14.333 -25.524 1.00 52.57 C
ANISOU 1541 CD1 LEU A 194 4790 8573 6611 939 927 -366 C
ATOM 1542 CD2 LEU A 194 -17.185 -13.306 -26.475 1.00 50.21 C
ANISOU 1542 CD2 LEU A 194 5831 7431 5813 1078 177 -2687 C
ATOM 1543 N GLU A 195 -20.063 -13.386 -23.909 1.00 27.43 N
ANISOU 1543 N GLU A 195 2723 4051 3648 287 -117 -404 N
ATOM 1544 CA GLU A 195 -21.260 -14.145 -23.571 1.00 24.54 C
ANISOU 1544 CA GLU A 195 2665 3339 3318 340 -55 -385 C
ATOM 1545 C GLU A 195 -21.602 -15.120 -24.676 1.00 26.29 C
ANISOU 1545 C GLU A 195 2762 3601 3625 602 2 -216 C
ATOM 1546 O GLU A 195 -21.337 -14.841 -25.854 1.00 28.35 O
ANISOU 1546 O GLU A 195 3151 3727 3894 181 297 -556 O
ATOM 1547 CB GLU A 195 -22.450 -13.176 -23.486 1.00 25.16 C
ANISOU 1547 CB GLU A 195 2624 3519 3418 423 -17 11 C
ATOM 1548 CG GLU A 195 -22.317 -12.169 -22.364 1.00 24.66 C
ANISOU 1548 CG GLU A 195 2876 3320 3172 -179 19 -317 C
ATOM 1549 CD GLU A 195 -23.466 -11.171 -22.281 1.00 24.72 C
ANISOU 1549 CD GLU A 195 2732 3617 3043 72 -74 -124 C
ATOM 1550 OE1 GLU A 195 -24.452 -11.354 -23.064 1.00 25.30 O
ANISOU 1550 OE1 GLU A 195 3159 3293 3162 272 -239 -323 O
ATOM 1551 OE2 GLU A 195 -23.381 -10.200 -21.502 1.00 23.55 O
ANISOU 1551 OE2 GLU A 195 2926 2916 3104 -21 34 -104 O
ATOM 1552 N PRO A 196 -22.329 -16.209 -24.341 1.00 27.78 N
ANISOU 1552 N PRO A 196 2941 3379 4233 405 -474 -519 N
ATOM 1553 CA PRO A 196 -22.898 -17.072 -25.371 1.00 29.26 C
ANISOU 1553 CA PRO A 196 2952 3722 4443 801 -199 -954 C
ATOM 1554 C PRO A 196 -23.995 -16.327 -26.122 1.00 29.61 C
ANISOU 1554 C PRO A 196 2993 4017 4240 234 -378 -601 C
ATOM 1555 O PRO A 196 -24.663 -15.472 -25.546 1.00 29.91 O
ANISOU 1555 O PRO A 196 3338 4111 3915 763 -402 -287 O
ATOM 1556 CB PRO A 196 -23.403 -18.281 -24.608 1.00 31.10 C
ANISOU 1556 CB PRO A 196 3323 3466 5028 105 234 -991 C
ATOM 1557 CG PRO A 196 -23.513 -17.868 -23.176 1.00 38.97 C
ANISOU 1557 CG PRO A 196 4684 4698 5424 -6 62 -603 C
ATOM 1558 CD PRO A 196 -22.666 -16.629 -22.979 1.00 32.63 C
ANISOU 1558 CD PRO A 196 3661 4170 4567 549 -321 -452 C
ATOM 1559 N PRO A 197 -24.265 -16.712 -27.384 1.00 33.96 N
ANISOU 1559 N PRO A 197 3299 5224 4382 547 -381 -713 N
ATOM 1560 CA PRO A 197 -25.450 -16.248 -28.089 1.00 37.75 C
ANISOU 1560 CA PRO A 197 4166 5301 4875 688 -646 -664 C
ATOM 1561 C PRO A 197 -26.659 -16.770 -27.325 1.00 30.94 C
ANISOU 1561 C PRO A 197 3759 3607 4388 421 -1344 -266 C
ATOM 1562 O PRO A 197 -26.663 -17.920 -26.865 1.00 32.79 O
ANISOU 1562 O PRO A 197 3773 3557 5130 859 -569 193 O
ATOM 1563 CB PRO A 197 -25.367 -16.858 -29.487 1.00 40.96 C
ANISOU 1563 CB PRO A 197 4832 6287 4444 458 -819 -884 C
ATOM 1564 CG PRO A 197 -23.944 -17.331 -29.611 1.00 45.12 C
ANISOU 1564 CG PRO A 197 5201 6766 5175 890 -553 -920 C
ATOM 1565 CD PRO A 197 -23.441 -17.628 -28.198 1.00 41.24 C
ANISOU 1565 CD PRO A 197 4601 6157 4910 736 -541 -1187 C
ATOM 1566 N TYR A 198 -27.704 -15.943 -27.248 1.00 29.45 N
ANISOU 1566 N TYR A 198 3544 3570 4077 574 -773 101 N
ATOM 1567 CA TYR A 198 -28.948 -16.393 -26.678 1.00 29.51 C
ANISOU 1567 CA TYR A 198 3846 3549 3816 446 -677 -123 C
ATOM 1568 C TYR A 198 -29.629 -17.312 -27.687 1.00 28.83 C
ANISOU 1568 C TYR A 198 3331 3512 4112 492 -476 -501 C
ATOM 1569 O TYR A 198 -29.414 -17.204 -28.895 1.00 29.48 O
ANISOU 1569 O TYR A 198 3490 3562 4149 788 -916 -521 O
ATOM 1570 CB TYR A 198 -29.839 -15.198 -26.366 1.00 27.44 C
ANISOU 1570 CB TYR A 198 3821 3177 3428 348 -436 -60 C
ATOM 1571 CG TYR A 198 -29.386 -14.317 -25.211 1.00 25.08 C
ANISOU 1571 CG TYR A 198 3129 2911 3489 431 -417 -88 C
ATOM 1572 CD1 TYR A 198 -29.751 -14.612 -23.898 1.00 28.70 C
ANISOU 1572 CD1 TYR A 198 3389 3886 3631 -8 -218 19 C
ATOM 1573 CD2 TYR A 198 -28.600 -13.192 -25.420 1.00 28.27 C
ANISOU 1573 CD2 TYR A 198 3917 3303 3522 246 -643 368 C
ATOM 1574 CE1 TYR A 198 -29.384 -13.795 -22.837 1.00 26.80 C
ANISOU 1574 CE1 TYR A 198 3023 3542 3618 156 -42 -80 C
ATOM 1575 CE2 TYR A 198 -28.189 -12.399 -24.364 1.00 27.24 C
ANISOU 1575 CE2 TYR A 198 3670 3412 3266 -73 -368 -42 C
ATOM 1576 CZ TYR A 198 -28.563 -12.707 -23.072 1.00 25.96 C
ANISOU 1576 CZ TYR A 198 2770 3586 3508 -16 -309 -37 C
ATOM 1577 OH TYR A 198 -28.219 -11.889 -22.064 1.00 26.07 O
ANISOU 1577 OH TYR A 198 2964 3483 3459 60 -107 -258 O
ATOM 1578 N GLU A 199 -30.528 -18.161 -27.190 1.00 34.25 N
ANISOU 1578 N GLU A 199 3694 4002 5318 -42 -1795 282 N
ATOM 1579 CA GLU A 199 -31.354 -18.953 -28.094 1.00 34.89 C
ANISOU 1579 CA GLU A 199 4367 3479 5412 -45 -1880 40 C
ATOM 1580 C GLU A 199 -32.163 -17.996 -28.947 1.00 33.23 C
ANISOU 1580 C GLU A 199 3843 3315 5466 -164 -1399 10 C
ATOM 1581 O GLU A 199 -32.726 -17.044 -28.432 1.00 35.15 O
ANISOU 1581 O GLU A 199 3813 3948 5593 -224 -1125 241 O
ATOM 1582 CB GLU A 199 -32.258 -19.890 -27.291 1.00 42.05 C
ANISOU 1582 CB GLU A 199 4549 4234 7193 -143 -1927 482 C
ATOM 1583 CG GLU A 199 -33.449 -20.459 -28.051 1.00 51.91 C
ANISOU 1583 CG GLU A 199 5598 5344 8782 -786 -2455 -92 C
ATOM 1584 CD GLU A 199 -33.357 -21.838 -28.666 1.00 62.40 C
ANISOU 1584 CD GLU A 199 6665 6338 10705 938 -2445 -227 C
ATOM 1585 OE1 GLU A 199 -32.239 -22.406 -28.814 1.00 77.10 O
ANISOU 1585 OE1 GLU A 199 8422 8669 12203 869 -1654 -1153 O
ATOM 1586 OE2 GLU A 199 -34.463 -22.359 -28.959 1.00 68.35 O
ANISOU 1586 OE2 GLU A 199 6718 6913 12339 904 -2198 150 O
ATOM 1587 N GLY A 200 -32.159 -18.218 -30.259 1.00 37.33 N
ANISOU 1587 N GLY A 200 4005 4218 5959 202 -1783 263 N
ATOM 1588 CA GLY A 200 -32.924 -17.356 -31.119 1.00 33.40 C
ANISOU 1588 CA GLY A 200 3374 4160 5154 -512 -1453 254 C
ATOM 1589 C GLY A 200 -32.167 -16.158 -31.636 1.00 33.38 C
ANISOU 1589 C GLY A 200 3673 3925 5086 -64 -1265 -221 C
ATOM 1590 O GLY A 200 -32.632 -15.514 -32.580 1.00 32.81 O
ANISOU 1590 O GLY A 200 3632 3995 4838 525 -1055 -469 O
ATOM 1591 N GLU A 201 -31.030 -15.858 -31.006 1.00 28.63 N
ANISOU 1591 N GLU A 201 2916 3449 4513 325 -1007 -151 N
ATOM 1592 CA GLU A 201 -30.256 -14.708 -31.421 1.00 30.73 C
ANISOU 1592 CA GLU A 201 2983 3685 5008 569 -868 73 C
ATOM 1593 C GLU A 201 -29.540 -15.049 -32.724 1.00 32.61 C
ANISOU 1593 C GLU A 201 3244 4383 4762 469 -1106 -446 C
ATOM 1594 O GLU A 201 -28.715 -15.970 -32.822 1.00 37.31 O
ANISOU 1594 O GLU A 201 3947 4977 5250 1871 -909 -346 O
ATOM 1595 CB GLU A 201 -29.350 -14.242 -30.293 1.00 33.42 C
ANISOU 1595 CB GLU A 201 3544 4139 5013 -29 -681 -201 C
ATOM 1596 CG GLU A 201 -28.492 -13.045 -30.659 1.00 34.44 C
ANISOU 1596 CG GLU A 201 3657 4888 4543 -283 -708 350 C
ATOM 1597 CD GLU A 201 -27.702 -12.546 -29.463 1.00 41.21 C
ANISOU 1597 CD GLU A 201 5968 4890 4800 -207 -1986 120 C
ATOM 1598 OE1 GLU A 201 -27.259 -13.418 -28.671 1.00 36.39 O
ANISOU 1598 OE1 GLU A 201 4073 3932 5821 719 -1459 -366 O
ATOM 1599 OE2 GLU A 201 -27.568 -11.307 -29.265 1.00 50.62 O
ANISOU 1599 OE2 GLU A 201 7566 5427 6239 18 -1930 -538 O
ATOM 1600 N ILE A 202 -29.844 -14.275 -33.740 1.00 30.32 N
ANISOU 1600 N ILE A 202 3342 3490 4686 345 -977 -163 N
ATOM 1601 CA ILE A 202 -29.256 -14.465 -35.040 1.00 37.14 C
ANISOU 1601 CA ILE A 202 4123 4796 5191 466 -842 -181 C
ATOM 1602 C ILE A 202 -27.985 -13.662 -34.970 1.00 41.94 C
ANISOU 1602 C ILE A 202 4979 5606 5350 84 -206 285 C
ATOM 1603 O ILE A 202 -26.917 -14.137 -35.372 1.00 41.09 O
ANISOU 1603 O ILE A 202 3295 6505 5813 -42 258 662 O
ATOM 1604 CB ILE A 202 -30.203 -13.943 -36.137 1.00 39.17 C
ANISOU 1604 CB ILE A 202 6102 4368 4413 655 -1205 -769 C
ATOM 1605 CG1 ILE A 202 -31.402 -14.878 -36.324 1.00 41.33 C
ANISOU 1605 CG1 ILE A 202 4712 6715 4277 -178 -895 -360 C
ATOM 1606 CG2 ILE A 202 -29.413 -13.676 -37.408 1.00 49.49 C
ANISOU 1606 CG2 ILE A 202 6994 6357 5452 260 -974 -192 C
ATOM 1607 N GLU A 203 -28.155 -12.484 -34.323 1.00 43.90 N
ANISOU 1607 N GLU A 203 5353 5719 5607 -640 -355 483 N
ATOM 1608 CA GLU A 203 -27.044 -11.584 -34.127 1.00 48.69 C
ANISOU 1608 CA GLU A 203 6785 6488 5228 -911 -257 -142 C
ATOM 1609 C GLU A 203 -27.313 -10.605 -32.994 1.00 47.77 C
ANISOU 1609 C GLU A 203 5797 6235 6119 -971 -352 -101 C
ATOM 1610 O GLU A 203 -28.451 -10.298 -32.620 1.00 47.57 O
ANISOU 1610 O GLU A 203 5712 6077 6285 -1078 -765 864 O
ATOM 1611 CB GLU A 203 -26.779 -10.764 -35.384 1.00 47.54 C
ANISOU 1611 CB GLU A 203 6253 6867 4942 -330 -858 474 C
ATOM 1612 CG GLU A 203 -27.791 -9.643 -35.620 1.00 41.31 C
ANISOU 1612 CG GLU A 203 4597 5920 5179 -506 -995 225 C
ATOM 1613 CD GLU A 203 -27.351 -8.829 -36.827 1.00 45.08 C
ANISOU 1613 CD GLU A 203 5220 6478 5432 -160 548 706 C
ATOM 1614 OE1 GLU A 203 -26.419 -9.352 -37.545 1.00 51.96 O
ANISOU 1614 OE1 GLU A 203 6392 8177 5175 937 85 551 O
ATOM 1615 OE2 GLU A 203 -27.942 -7.730 -37.062 1.00 36.01 O
ANISOU 1615 OE2 GLU A 203 4069 5328 4287 -196 323 572 O
ATOM 1616 N ARG A 204 -26.206 -10.047 -32.559 1.00 40.39 N
ANISOU 1616 N ARG A 204 2689 6440 6219 156 -651 -100 N
ATOM 1617 CA ARG A 204 -26.154 -9.006 -31.548 1.00 50.19 C
ANISOU 1617 CA ARG A 204 5305 7299 6465 -262 -151 23 C
ATOM 1618 C ARG A 204 -25.350 -7.855 -32.134 1.00 45.13 C
ANISOU 1618 C ARG A 204 5191 6499 5456 -84 -68 -276 C
ATOM 1619 O ARG A 204 -24.731 -8.007 -33.169 1.00 43.65 O
ANISOU 1619 O ARG A 204 5217 6118 5248 -753 -893 520 O
ATOM 1620 CB ARG A 204 -25.444 -9.448 -30.258 1.00 54.81 C
ANISOU 1620 CB ARG A 204 6945 8508 5371 -850 -947 440 C
ATOM 1621 CG ARG A 204 -24.061 -10.075 -30.426 1.00 59.84 C
ANISOU 1621 CG ARG A 204 7285 8922 6531 -1292 -503 924 C
ATOM 1622 CD ARG A 204 -23.372 -10.206 -29.084 1.00 62.30 C
ANISOU 1622 CD ARG A 204 7152 8622 7897 -1702 -834 1981 C
ATOM 1623 NE ARG A 204 -22.318 -11.222 -28.939 1.00 70.02 N
ANISOU 1623 NE ARG A 204 8151 8838 9615 -1363 274 1590 N
ATOM 1624 CZ ARG A 204 -21.129 -11.252 -29.539 1.00 67.03 C
ANISOU 1624 CZ ARG A 204 9457 8687 7323 -711 495 1809 C
ATOM 1625 NH1 ARG A 204 -20.099 -11.839 -28.923 1.00 66.44 N
ANISOU 1625 NH1 ARG A 204 9278 8101 7867 -473 296 1504 N
ATOM 1626 NH2 ARG A 204 -20.940 -10.589 -30.671 1.00 55.37 N
ANISOU 1626 NH2 ARG A 204 9101 8221 3716 -1178 -525 519 N
ATOM 1627 N ALA A 205 -25.322 -6.720 -31.444 1.00 45.55 N
ANISOU 1627 N ALA A 205 4945 6672 5690 -703 17 -399 N
ATOM 1628 CA ALA A 205 -24.465 -5.654 -31.880 1.00 39.92 C
ANISOU 1628 CA ALA A 205 4798 6110 4258 -160 -1001 -967 C
ATOM 1629 C ALA A 205 -23.033 -6.120 -31.660 1.00 41.55 C
ANISOU 1629 C ALA A 205 4379 5907 5501 330 -248 -446 C
ATOM 1630 O ALA A 205 -22.753 -6.857 -30.712 1.00 43.53 O
ANISOU 1630 O ALA A 205 4769 6043 5728 -659 307 -130 O
ATOM 1631 CB ALA A 205 -24.776 -4.383 -31.121 1.00 44.03 C
ANISOU 1631 CB ALA A 205 4858 6734 5137 414 -1453 -1050 C
ATOM 1632 N GLN A 206 -22.148 -5.682 -32.544 1.00 40.82 N
ANISOU 1632 N GLN A 206 4724 6291 4495 -152 -515 -150 N
ATOM 1633 CA GLN A 206 -20.720 -5.801 -32.309 1.00 34.82 C
ANISOU 1633 CA GLN A 206 3915 4927 4389 470 -488 -271 C
ATOM 1634 C GLN A 206 -20.462 -5.281 -30.894 1.00 35.64 C
ANISOU 1634 C GLN A 206 4264 4328 4949 -119 -582 229 C
ATOM 1635 O GLN A 206 -20.709 -4.116 -30.600 1.00 33.45 O
ANISOU 1635 O GLN A 206 3620 4057 5034 225 -328 -5 O
ATOM 1636 CB GLN A 206 -20.088 -4.932 -33.399 1.00 35.60 C
ANISOU 1636 CB GLN A 206 4352 4847 4327 571 -898 -185 C
ATOM 1637 CG GLN A 206 -18.659 -5.300 -33.773 1.00 37.36 C
ANISOU 1637 CG GLN A 206 4454 4760 4979 408 -782 370 C
ATOM 1638 CD GLN A 206 -17.754 -5.366 -32.568 1.00 38.62 C
ANISOU 1638 CD GLN A 206 3653 5249 5774 397 -1007 149 C
ATOM 1639 OE1 GLN A 206 -17.520 -4.350 -31.918 1.00 39.67 O
ANISOU 1639 OE1 GLN A 206 4421 4580 6071 804 -145 -433 O
ATOM 1640 NE2 GLN A 206 -17.239 -6.561 -32.286 1.00 39.16 N
ANISOU 1640 NE2 GLN A 206 3347 4443 7088 649 -303 232 N
ATOM 1641 N PRO A 207 -20.050 -6.112 -29.931 1.00 34.56 N
ANISOU 1641 N PRO A 207 4323 4593 4216 -280 -373 623 N
ATOM 1642 CA PRO A 207 -19.991 -5.672 -28.541 1.00 36.17 C
ANISOU 1642 CA PRO A 207 3656 5080 5008 -486 -679 -224 C
ATOM 1643 C PRO A 207 -19.139 -4.471 -28.186 1.00 32.19 C
ANISOU 1643 C PRO A 207 3542 4186 4501 117 -82 -47 C
ATOM 1644 O PRO A 207 -19.569 -3.676 -27.364 1.00 32.22 O
ANISOU 1644 O PRO A 207 3281 3626 5335 -157 122 -550 O
ATOM 1645 CB PRO A 207 -19.472 -6.891 -27.862 1.00 36.42 C
ANISOU 1645 CB PRO A 207 3661 5273 4903 -544 -521 481 C
ATOM 1646 CG PRO A 207 -19.977 -8.037 -28.680 1.00 33.78 C
ANISOU 1646 CG PRO A 207 3070 5253 4511 -618 17 35 C
ATOM 1647 CD PRO A 207 -19.753 -7.542 -30.102 1.00 36.52 C
ANISOU 1647 CD PRO A 207 3757 4896 5222 -602 -564 -29 C
ATOM 1648 N MET A 208 -17.902 -4.416 -28.699 1.00 36.07 N
ANISOU 1648 N MET A 208 3461 4756 5487 248 392 -1060 N
ATOM 1649 CA MET A 208 -17.058 -3.258 -28.456 1.00 33.04 C
ANISOU 1649 CA MET A 208 3289 4690 4574 -49 379 -400 C
ATOM 1650 C MET A 208 -17.701 -2.002 -29.055 1.00 32.89 C
ANISOU 1650 C MET A 208 3185 4703 4610 133 364 -482 C
ATOM 1651 O MET A 208 -17.664 -0.966 -28.424 1.00 34.95 O
ANISOU 1651 O MET A 208 3848 4763 4667 -140 523 -364 O
ATOM 1652 CB MET A 208 -15.653 -3.456 -29.017 1.00 34.36 C
ANISOU 1652 CB MET A 208 3720 4449 4888 63 341 -873 C
ATOM 1653 CG MET A 208 -14.604 -2.458 -28.617 1.00 37.52 C
ANISOU 1653 CG MET A 208 4997 4799 4461 -301 244 -620 C
ATOM 1654 SD MET A 208 -14.143 -2.649 -26.899 1.00 43.46 S
ANISOU 1654 SD MET A 208 4859 6255 5397 -281 44 45 S
ATOM 1655 CE MET A 208 -13.674 -4.365 -26.735 1.00 43.62 C
ANISOU 1655 CE MET A 208 6521 5810 4242 -716 -801 1050 C
ATOM 1656 N LEU A 209 -18.263 -2.076 -30.281 1.00 34.97 N
ANISOU 1656 N LEU A 209 4263 4304 4720 848 229 -758 N
ATOM 1657 CA LEU A 209 -18.867 -0.885 -30.878 1.00 36.16 C
ANISOU 1657 CA LEU A 209 4191 4895 4654 483 -285 -655 C
ATOM 1658 C LEU A 209 -20.060 -0.465 -30.013 1.00 34.99 C
ANISOU 1658 C LEU A 209 4154 5212 3928 501 154 -427 C
ATOM 1659 O LEU A 209 -20.268 0.716 -29.789 1.00 38.08 O
ANISOU 1659 O LEU A 209 5202 5061 4204 514 176 205 O
ATOM 1660 CB LEU A 209 -19.263 -0.943 -32.354 1.00 37.90 C
ANISOU 1660 CB LEU A 209 5089 4640 4672 -99 74 -24 C
ATOM 1661 N GLN A 210 -20.828 -1.428 -29.506 1.00 36.15 N
ANISOU 1661 N GLN A 210 4370 4958 4408 514 -279 -560 N
ATOM 1662 CA GLN A 210 -21.952 -1.148 -28.614 1.00 33.72 C
ANISOU 1662 CA GLN A 210 3976 4900 3936 675 -251 366 C
ATOM 1663 C GLN A 210 -21.480 -0.468 -27.329 1.00 30.00 C
ANISOU 1663 C GLN A 210 3697 3785 3917 133 304 286 C
ATOM 1664 O GLN A 210 -22.100 0.497 -26.877 1.00 30.25 O
ANISOU 1664 O GLN A 210 3815 3737 3940 569 492 231 O
ATOM 1665 CB GLN A 210 -22.658 -2.477 -28.363 1.00 39.56 C
ANISOU 1665 CB GLN A 210 4082 5815 5132 601 145 345 C
ATOM 1666 CG GLN A 210 -23.986 -2.361 -27.641 1.00 44.01 C
ANISOU 1666 CG GLN A 210 5054 6354 5315 450 374 450 C
ATOM 1667 CD GLN A 210 -24.748 -3.672 -27.732 1.00 51.78 C
ANISOU 1667 CD GLN A 210 5151 7538 6986 -677 -529 -368 C
ATOM 1668 OE1 GLN A 210 -24.207 -4.763 -27.467 1.00 54.15 O
ANISOU 1668 OE1 GLN A 210 5331 7505 7736 -891 -1333 759 O
ATOM 1669 NE2 GLN A 210 -26.006 -3.570 -28.128 1.00 57.19 N
ANISOU 1669 NE2 GLN A 210 5079 9786 6866 543 -601 -606 N
ATOM 1670 N TYR A 211 -20.419 -1.014 -26.722 1.00 28.77 N
ANISOU 1670 N TYR A 211 3644 3335 3951 21 61 193 N
ATOM 1671 CA TYR A 211 -19.849 -0.421 -25.516 1.00 26.40 C
ANISOU 1671 CA TYR A 211 3158 3277 3595 -59 -29 240 C
ATOM 1672 C TYR A 211 -19.461 1.030 -25.823 1.00 27.63 C
ANISOU 1672 C TYR A 211 4085 3110 3303 -100 450 601 C
ATOM 1673 O TYR A 211 -19.773 1.910 -25.071 1.00 27.30 O
ANISOU 1673 O TYR A 211 3596 3380 3396 -75 339 257 O
ATOM 1674 CB TYR A 211 -18.662 -1.247 -25.032 1.00 27.27 C
ANISOU 1674 CB TYR A 211 3338 3251 3773 66 -6 589 C
ATOM 1675 CG TYR A 211 -17.968 -0.737 -23.775 1.00 28.95 C
ANISOU 1675 CG TYR A 211 3530 3677 3795 128 -175 130 C
ATOM 1676 CD1 TYR A 211 -18.473 -0.999 -22.509 1.00 33.69 C
ANISOU 1676 CD1 TYR A 211 3773 4602 4427 -834 275 4 C
ATOM 1677 CD2 TYR A 211 -16.788 -0.004 -23.845 1.00 34.90 C
ANISOU 1677 CD2 TYR A 211 4265 4399 4597 -198 -315 132 C
ATOM 1678 CE1 TYR A 211 -17.854 -0.544 -21.361 1.00 32.70 C
ANISOU 1678 CE1 TYR A 211 3671 4611 4143 -477 -273 -39 C
ATOM 1679 CE2 TYR A 211 -16.165 0.467 -22.691 1.00 36.15 C
ANISOU 1679 CE2 TYR A 211 4801 4572 4362 -33 -250 156 C
ATOM 1680 CZ TYR A 211 -16.698 0.193 -21.450 1.00 33.19 C
ANISOU 1680 CZ TYR A 211 3920 3976 4713 0 -82 -157 C
ATOM 1681 OH TYR A 211 -16.103 0.667 -20.299 1.00 40.43 O
ANISOU 1681 OH TYR A 211 4573 5771 5016 -219 -416 106 O
ATOM 1682 N ASN A 212 -18.763 1.258 -26.943 1.00 31.30 N
ANISOU 1682 N ASN A 212 4260 3602 4029 127 794 818 N
ATOM 1683 CA ASN A 212 -18.343 2.601 -27.332 1.00 31.69 C
ANISOU 1683 CA ASN A 212 4205 3754 4082 176 706 1252 C
ATOM 1684 C ASN A 212 -19.555 3.525 -27.548 1.00 32.68 C
ANISOU 1684 C ASN A 212 4532 3771 4113 17 1069 841 C
ATOM 1685 O ASN A 212 -19.540 4.707 -27.165 1.00 34.81 O
ANISOU 1685 O ASN A 212 4988 3862 4375 -129 593 645 O
ATOM 1686 CB ASN A 212 -17.416 2.518 -28.539 1.00 35.83 C
ANISOU 1686 CB ASN A 212 3910 4468 5235 316 922 955 C
ATOM 1687 CG ASN A 212 -16.087 1.840 -28.245 1.00 33.76 C
ANISOU 1687 CG ASN A 212 4734 4286 3807 764 494 1167 C
ATOM 1688 OD1 ASN A 212 -15.687 1.638 -27.085 1.00 35.91 O
ANISOU 1688 OD1 ASN A 212 4081 4965 4599 -351 373 1044 O
ATOM 1689 ND2 ASN A 212 -15.324 1.617 -29.302 1.00 41.14 N
ANISOU 1689 ND2 ASN A 212 5171 5341 5119 432 1022 878 N
ATOM 1690 N GLU A 213 -20.623 2.999 -28.159 1.00 32.41 N
ANISOU 1690 N GLU A 213 4939 4117 3257 820 680 723 N
ATOM 1691 CA GLU A 213 -21.815 3.791 -28.378 1.00 34.50 C
ANISOU 1691 CA GLU A 213 5042 4245 3822 1005 862 653 C
ATOM 1692 C GLU A 213 -22.483 4.139 -27.054 1.00 29.04 C
ANISOU 1692 C GLU A 213 4527 3110 3396 304 116 370 C
ATOM 1693 O GLU A 213 -22.943 5.263 -26.877 1.00 30.47 O
ANISOU 1693 O GLU A 213 4861 2972 3743 727 301 678 O
ATOM 1694 CB GLU A 213 -22.749 3.095 -29.358 1.00 37.78 C
ANISOU 1694 CB GLU A 213 5445 4875 4034 1108 537 -156 C
ATOM 1695 CG GLU A 213 -22.265 3.229 -30.801 1.00 47.71 C
ANISOU 1695 CG GLU A 213 7134 6349 4643 1465 -54 333 C
ATOM 1696 CD GLU A 213 -21.924 4.616 -31.388 1.00 54.10 C
ANISOU 1696 CD GLU A 213 7429 7007 6118 738 424 463 C
ATOM 1697 OE1 GLU A 213 -22.710 5.602 -31.216 1.00 52.58 O
ANISOU 1697 OE1 GLU A 213 8615 6343 5021 1268 170 61 O
ATOM 1698 OE2 GLU A 213 -20.864 4.698 -32.091 1.00 56.58 O
ANISOU 1698 OE2 GLU A 213 8338 6864 6298 715 1600 995 O
ATOM 1699 N THR A 214 -22.489 3.195 -26.121 1.00 28.68 N
ANISOU 1699 N THR A 214 4502 3103 3292 90 298 256 N
ATOM 1700 CA THR A 214 -23.023 3.469 -24.807 1.00 27.64 C
ANISOU 1700 CA THR A 214 4270 3107 3123 -201 159 706 C
ATOM 1701 C THR A 214 -22.204 4.571 -24.132 1.00 27.67 C
ANISOU 1701 C THR A 214 3560 3439 3514 -34 147 685 C
ATOM 1702 O THR A 214 -22.795 5.516 -23.580 1.00 27.77 O
ANISOU 1702 O THR A 214 3919 2943 3688 211 395 587 O
ATOM 1703 CB THR A 214 -23.055 2.178 -24.009 1.00 24.59 C
ANISOU 1703 CB THR A 214 3463 2741 3138 258 -65 487 C
ATOM 1704 OG1 THR A 214 -24.115 1.350 -24.503 1.00 26.16 O
ANISOU 1704 OG1 THR A 214 3045 3229 3668 -13 153 201 O
ATOM 1705 CG2 THR A 214 -23.259 2.437 -22.527 1.00 26.77 C
ANISOU 1705 CG2 THR A 214 3713 3104 3353 117 9 520 C
ATOM 1706 N LEU A 215 -20.859 4.487 -24.244 1.00 27.60 N
ANISOU 1706 N LEU A 215 3806 2920 3761 -373 96 555 N
ATOM 1707 CA LEU A 215 -20.002 5.534 -23.679 1.00 29.15 C
ANISOU 1707 CA LEU A 215 3763 3307 4005 208 11 590 C
ATOM 1708 C LEU A 215 -20.323 6.911 -24.276 1.00 27.44 C
ANISOU 1708 C LEU A 215 3390 3156 3877 -183 206 562 C
ATOM 1709 O LEU A 215 -20.469 7.906 -23.559 1.00 30.03 O
ANISOU 1709 O LEU A 215 4294 3029 4088 -117 368 625 O
ATOM 1710 CB LEU A 215 -18.532 5.187 -23.838 1.00 31.25 C
ANISOU 1710 CB LEU A 215 3901 3290 4683 -360 198 774 C
ATOM 1711 CG LEU A 215 -18.022 4.038 -22.958 1.00 31.72 C
ANISOU 1711 CG LEU A 215 3684 3237 5132 -48 180 714 C
ATOM 1712 CD1 LEU A 215 -16.530 4.069 -23.089 1.00 36.14 C
ANISOU 1712 CD1 LEU A 215 4266 3857 5610 183 -355 343 C
ATOM 1713 CD2 LEU A 215 -18.392 4.143 -21.525 1.00 34.74 C
ANISOU 1713 CD2 LEU A 215 3987 3768 5446 -203 -545 683 C
ATOM 1714 N LYS A 216 -20.437 6.984 -25.584 1.00 30.50 N
ANISOU 1714 N LYS A 216 4480 3164 3943 349 454 867 N
ATOM 1715 CA LYS A 216 -20.732 8.244 -26.250 1.00 31.31 C
ANISOU 1715 CA LYS A 216 4410 3046 4439 -96 315 1012 C
ATOM 1716 C LYS A 216 -22.095 8.806 -25.833 1.00 32.44 C
ANISOU 1716 C LYS A 216 4640 3418 4267 -259 400 530 C
ATOM 1717 O LYS A 216 -22.251 10.020 -25.624 1.00 31.66 O
ANISOU 1717 O LYS A 216 4519 3536 3976 -44 121 599 O
ATOM 1718 CB LYS A 216 -20.638 8.028 -27.771 1.00 33.39 C
ANISOU 1718 CB LYS A 216 4600 3732 4354 281 655 1376 C
ATOM 1719 CG LYS A 216 -19.228 7.777 -28.291 1.00 37.18 C
ANISOU 1719 CG LYS A 216 5224 4368 4535 177 499 1400 C
ATOM 1720 CD LYS A 216 -19.174 7.363 -29.760 1.00 43.03 C
ANISOU 1720 CD LYS A 216 5894 5570 4885 478 866 1499 C
ATOM 1721 CE LYS A 216 -17.790 7.030 -30.214 1.00 51.63 C
ANISOU 1721 CE LYS A 216 6968 7271 5379 676 612 925 C
ATOM 1722 NZ LYS A 216 -17.738 6.698 -31.639 1.00 59.82 N
ANISOU 1722 NZ LYS A 216 8633 8573 5523 97 958 914 N
ATOM 1723 N ARG A 217 -23.074 7.909 -25.656 1.00 29.99 N
ANISOU 1723 N ARG A 217 4846 2987 3562 213 258 708 N
ATOM 1724 CA ARG A 217 -24.378 8.331 -25.210 1.00 30.43 C
ANISOU 1724 CA ARG A 217 4603 3341 3616 288 112 939 C
ATOM 1725 C ARG A 217 -24.281 8.962 -23.816 1.00 30.05 C
ANISOU 1725 C ARG A 217 4110 3328 3979 141 -98 877 C
ATOM 1726 O ARG A 217 -24.887 10.022 -23.592 1.00 31.65 O
ANISOU 1726 O ARG A 217 4801 3109 4116 632 63 527 O
ATOM 1727 CB ARG A 217 -25.369 7.170 -25.296 1.00 32.84 C
ANISOU 1727 CB ARG A 217 5163 3239 4076 327 -213 748 C
ATOM 1728 CG ARG A 217 -26.705 7.681 -24.815 1.00 35.83 C
ANISOU 1728 CG ARG A 217 4633 4313 4667 -118 -59 625 C
ATOM 1729 CD ARG A 217 -27.722 6.611 -24.824 1.00 41.05 C
ANISOU 1729 CD ARG A 217 4761 4555 6281 -205 797 1101 C
ATOM 1730 NE ARG A 217 -28.867 7.116 -24.066 1.00 39.16 N
ANISOU 1730 NE ARG A 217 4366 4210 6303 322 754 1003 N
ATOM 1731 CZ ARG A 217 -29.845 6.330 -23.699 1.00 34.65 C
ANISOU 1731 CZ ARG A 217 4098 3880 5189 -14 904 1085 C
ATOM 1732 NH1 ARG A 217 -29.654 5.021 -23.773 1.00 34.03 N
ANISOU 1732 NH1 ARG A 217 5187 3587 4156 -96 124 943 N
ATOM 1733 NH2 ARG A 217 -30.958 6.893 -23.235 1.00 36.56 N
ANISOU 1733 NH2 ARG A 217 4957 3841 5093 714 742 988 N
ATOM 1734 N LEU A 218 -23.541 8.299 -22.910 1.00 30.58 N
ANISOU 1734 N LEU A 218 4200 3424 3993 508 294 826 N
ATOM 1735 CA LEU A 218 -23.389 8.788 -21.547 1.00 28.41 C
ANISOU 1735 CA LEU A 218 4097 3046 3652 145 -223 924 C
ATOM 1736 C LEU A 218 -22.703 10.144 -21.555 1.00 28.57 C
ANISOU 1736 C LEU A 218 4068 3183 3605 -42 41 775 C
ATOM 1737 O LEU A 218 -23.080 11.019 -20.784 1.00 30.65 O
ANISOU 1737 O LEU A 218 4152 3055 4437 282 446 553 O
ATOM 1738 CB LEU A 218 -22.624 7.792 -20.686 1.00 30.35 C
ANISOU 1738 CB LEU A 218 4730 3037 3764 298 122 787 C
ATOM 1739 CG LEU A 218 -23.362 6.474 -20.430 1.00 30.64 C
ANISOU 1739 CG LEU A 218 4842 2827 3973 261 772 648 C
ATOM 1740 CD1 LEU A 218 -22.461 5.537 -19.664 1.00 36.32 C
ANISOU 1740 CD1 LEU A 218 5870 3343 4587 566 801 1076 C
ATOM 1741 CD2 LEU A 218 -24.678 6.665 -19.733 1.00 33.00 C
ANISOU 1741 CD2 LEU A 218 5357 3311 3869 160 911 333 C
ATOM 1742 N ALA A 219 -21.736 10.306 -22.456 1.00 30.18 N
ANISOU 1742 N ALA A 219 4362 2825 4280 -260 353 900 N
ATOM 1743 CA ALA A 219 -20.979 11.562 -22.549 1.00 34.34 C
ANISOU 1743 CA ALA A 219 4869 2980 5199 -352 147 904 C
ATOM 1744 C ALA A 219 -21.838 12.736 -22.991 1.00 34.80 C
ANISOU 1744 C ALA A 219 5404 3241 4577 74 411 948 C
ATOM 1745 O ALA A 219 -21.518 13.904 -22.700 1.00 37.21 O
ANISOU 1745 O ALA A 219 5102 2948 6088 193 -11 1158 O
ATOM 1746 CB ALA A 219 -19.775 11.418 -23.456 1.00 34.40 C
ANISOU 1746 CB ALA A 219 5002 2954 5112 -283 296 846 C
ATOM 1747 N ARG A 220 -22.877 12.418 -23.752 1.00 33.85 N
ANISOU 1747 N ARG A 220 5276 3321 4264 86 178 391 N
ATOM 1748 CA ARG A 220 -23.820 13.403 -24.280 1.00 36.60 C
ANISOU 1748 CA ARG A 220 5863 3486 4557 591 127 1094 C
ATOM 1749 C ARG A 220 -24.948 13.745 -23.296 1.00 36.44 C
ANISOU 1749 C ARG A 220 5670 3556 4618 656 -284 850 C
ATOM 1750 O ARG A 220 -25.700 14.731 -23.492 1.00 43.04 O
ANISOU 1750 O ARG A 220 6082 4891 5381 1246 773 550 O
ATOM 1751 CB ARG A 220 -24.398 12.903 -25.617 1.00 37.77 C
ANISOU 1751 CB ARG A 220 6650 3279 4423 1335 12 1095 C
ATOM 1752 CG ARG A 220 -23.409 12.875 -26.772 1.00 45.49 C
ANISOU 1752 CG ARG A 220 7201 5180 4901 1539 -95 952 C
ATOM 1753 CD ARG A 220 -24.087 12.491 -28.107 1.00 48.47 C
ANISOU 1753 CD ARG A 220 7979 5264 5172 1344 -410 558 C
ATOM 1754 NE ARG A 220 -24.924 11.280 -28.022 1.00 58.04 N
ANISOU 1754 NE ARG A 220 9647 6092 6312 1187 -154 527 N
ATOM 1755 CZ ARG A 220 -24.659 10.082 -28.551 1.00 52.77 C
ANISOU 1755 CZ ARG A 220 9175 6254 4622 911 -885 829 C
ATOM 1756 NH1 ARG A 220 -23.484 9.850 -29.090 1.00 57.43 N
ANISOU 1756 NH1 ARG A 220 8065 7250 6506 1953 -1856 709 N
ATOM 1757 NH2 ARG A 220 -25.569 9.122 -28.544 1.00 55.12 N
ANISOU 1757 NH2 ARG A 220 10585 5722 4635 -97 -626 1647 N
ATOM 1758 N MET A 221 -25.117 12.886 -22.278 1.00 34.76 N
ANISOU 1758 N MET A 221 4892 3706 4608 342 140 457 N
ATOM 1759 CA AMET A 221 -26.140 13.089 -21.282 0.50 35.65 C
ANISOU 1759 CA AMET A 221 5402 3827 4316 587 -89 635 C
ATOM 1760 CA BMET A 221 -26.129 13.060 -21.260 0.50 36.76 C
ANISOU 1760 CA BMET A 221 5651 3878 4438 425 -338 569 C
ATOM 1761 C MET A 221 -25.653 14.164 -20.310 1.00 38.13 C
ANISOU 1761 C MET A 221 6154 3876 4456 894 -110 668 C
ATOM 1762 O MET A 221 -24.468 14.470 -20.178 1.00 42.01 O
ANISOU 1762 O MET A 221 7092 4154 4715 -773 -321 630 O
ATOM 1763 CB AMET A 221 -26.443 11.767 -20.573 0.50 34.99 C
ANISOU 1763 CB AMET A 221 4744 3968 4584 640 700 346 C
ATOM 1764 CB BMET A 221 -26.359 11.731 -20.519 0.50 38.31 C
ANISOU 1764 CB BMET A 221 5614 3960 4984 142 -148 226 C
ATOM 1765 CG AMET A 221 -27.094 10.761 -21.475 0.50 34.08 C
ANISOU 1765 CG AMET A 221 4444 3817 4688 1115 916 297 C
ATOM 1766 CG BMET A 221 -27.791 11.225 -20.547 0.50 41.55 C
ANISOU 1766 CG BMET A 221 5920 4269 5600 61 -820 206 C
ATOM 1767 SD AMET A 221 -27.568 9.230 -20.658 0.50 38.08 S
ANISOU 1767 SD AMET A 221 5344 3754 5373 1040 967 579 S
ATOM 1768 SD BMET A 221 -28.024 9.528 -19.985 0.50 41.26 S
ANISOU 1768 SD BMET A 221 5397 3930 6348 186 -704 206 S
ATOM 1769 CE AMET A 221 -28.589 9.778 -19.293 0.50 34.56 C
ANISOU 1769 CE AMET A 221 4383 4502 4246 698 1252 1423 C
ATOM 1770 CE BMET A 221 -27.395 8.647 -21.417 0.50 46.16 C
ANISOU 1770 CE BMET A 221 6877 4175 6487 -108 -47 214 C
ATOM 1771 N ASN A 222 -26.565 14.733 -19.593 1.00 42.03 N
ANISOU 1771 N ASN A 222 6766 4918 4284 1494 -466 238 N
ATOM 1772 CA ASN A 222 -26.137 15.736 -18.642 1.00 43.29 C
ANISOU 1772 CA ASN A 222 7435 4237 4775 462 -22 391 C
ATOM 1773 C ASN A 222 -25.906 15.029 -17.314 1.00 39.27 C
ANISOU 1773 C ASN A 222 5875 4595 4451 688 -267 654 C
ATOM 1774 O ASN A 222 -26.830 14.950 -16.526 1.00 43.43 O
ANISOU 1774 O ASN A 222 6891 4490 5120 2066 -75 -557 O
ATOM 1775 CB ASN A 222 -27.186 16.829 -18.577 1.00 49.45 C
ANISOU 1775 CB ASN A 222 8256 4560 5972 1225 120 512 C
ATOM 1776 CG ASN A 222 -26.700 17.946 -17.695 1.00 64.37 C
ANISOU 1776 CG ASN A 222 9871 5851 8733 241 937 -901 C
ATOM 1777 OD1 ASN A 222 -27.494 18.594 -16.996 1.00 76.45 O
ANISOU 1777 OD1 ASN A 222 11535 8617 8896 385 2451 -751 O
ATOM 1778 ND2 ASN A 222 -25.394 18.187 -17.736 1.00 73.12 N
ANISOU 1778 ND2 ASN A 222 9948 7199 10634 238 943 -923 N
ATOM 1779 N ILE A 223 -24.757 14.359 -17.143 1.00 35.06 N
ANISOU 1779 N ILE A 223 5098 3560 4663 -128 -352 784 N
ATOM 1780 CA ILE A 223 -24.548 13.595 -15.915 1.00 29.51 C
ANISOU 1780 CA ILE A 223 4084 3144 3983 34 402 631 C
ATOM 1781 C ILE A 223 -23.611 14.352 -14.976 1.00 31.01 C
ANISOU 1781 C ILE A 223 4073 2943 4767 124 408 446 C
ATOM 1782 O ILE A 223 -22.493 14.727 -15.357 1.00 35.93 O
ANISOU 1782 O ILE A 223 4331 3815 5507 -567 566 450 O
ATOM 1783 CB ILE A 223 -24.023 12.176 -16.235 1.00 30.77 C
ANISOU 1783 CB ILE A 223 4175 3248 4267 -14 387 415 C
ATOM 1784 CG1 ILE A 223 -25.061 11.328 -16.997 1.00 28.95 C
ANISOU 1784 CG1 ILE A 223 4118 3051 3832 416 -54 454 C
ATOM 1785 CG2 ILE A 223 -23.562 11.458 -14.974 1.00 30.09 C
ANISOU 1785 CG2 ILE A 223 4469 2694 4269 -26 230 498 C
ATOM 1786 CD1 ILE A 223 -24.460 10.104 -17.654 1.00 31.67 C
ANISOU 1786 CD1 ILE A 223 4230 3265 4540 -59 124 368 C
ATOM 1787 N SER A 224 -24.096 14.598 -13.768 1.00 30.47 N
ANISOU 1787 N SER A 224 4450 2570 4558 201 -381 235 N
ATOM 1788 CA SER A 224 -23.335 15.238 -12.709 1.00 33.96 C
ANISOU 1788 CA SER A 224 4544 3013 5347 -263 -408 -60 C
ATOM 1789 C SER A 224 -22.367 14.292 -12.012 1.00 32.53 C
ANISOU 1789 C SER A 224 4172 2912 5275 -524 -355 215 C
ATOM 1790 O SER A 224 -21.309 14.738 -11.616 1.00 40.37 O
ANISOU 1790 O SER A 224 4498 3127 7713 -508 -1206 449 O
ATOM 1791 CB SER A 224 -24.236 15.867 -11.695 1.00 33.95 C
ANISOU 1791 CB SER A 224 4667 3328 4904 98 -453 -100 C
ATOM 1792 OG SER A 224 -25.176 14.968 -11.130 1.00 33.77 O
ANISOU 1792 OG SER A 224 5032 3197 4601 16 -299 30 O
ATOM 1793 N ARG A 225 -22.795 13.053 -11.778 1.00 31.56 N
ANISOU 1793 N ARG A 225 4165 2456 5370 -445 -555 237 N
ATOM 1794 CA ARG A 225 -22.059 12.117 -10.954 1.00 30.46 C
ANISOU 1794 CA ARG A 225 4540 2288 4746 -102 -211 -51 C
ATOM 1795 C ARG A 225 -22.537 10.726 -11.328 1.00 30.51 C
ANISOU 1795 C ARG A 225 4105 2672 4815 -530 -474 213 C
ATOM 1796 O ARG A 225 -23.768 10.519 -11.392 1.00 29.47 O
ANISOU 1796 O ARG A 225 3972 2657 4568 37 -362 -45 O
ATOM 1797 CB ARG A 225 -22.322 12.428 -9.486 1.00 34.82 C
ANISOU 1797 CB ARG A 225 5089 2687 5453 -930 -476 -494 C
ATOM 1798 CG ARG A 225 -21.820 11.509 -8.406 1.00 38.14 C
ANISOU 1798 CG ARG A 225 5325 3414 5750 -200 -4 -127 C
ATOM 1799 CD ARG A 225 -22.362 12.048 -7.076 1.00 40.82 C
ANISOU 1799 CD ARG A 225 6185 4173 5153 -591 -426 -204 C
ATOM 1800 NE ARG A 225 -21.769 11.331 -5.961 1.00 45.18 N
ANISOU 1800 NE ARG A 225 6535 4089 6541 -326 -481 2 N
ATOM 1801 CZ ARG A 225 -22.206 11.368 -4.716 1.00 48.46 C
ANISOU 1801 CZ ARG A 225 7179 4478 6757 192 706 -484 C
ATOM 1802 NH1 ARG A 225 -21.601 10.586 -3.806 1.00 47.99 N
ANISOU 1802 NH1 ARG A 225 6883 5078 6271 -334 425 -1198 N
ATOM 1803 NH2 ARG A 225 -23.237 12.165 -4.397 1.00 53.07 N
ANISOU 1803 NH2 ARG A 225 6939 4791 8433 -35 -331 148 N
ATOM 1804 N VAL A 226 -21.588 9.819 -11.602 1.00 28.09 N
ANISOU 1804 N VAL A 226 3740 2715 4220 -616 -440 -14 N
ATOM 1805 CA VAL A 226 -21.934 8.412 -11.764 1.00 25.94 C
ANISOU 1805 CA VAL A 226 3865 2682 3308 -536 -336 113 C
ATOM 1806 C VAL A 226 -21.617 7.688 -10.464 1.00 25.44 C
ANISOU 1806 C VAL A 226 3274 2656 3737 34 -362 179 C
ATOM 1807 O VAL A 226 -20.477 7.743 -10.015 1.00 28.03 O
ANISOU 1807 O VAL A 226 3731 2992 3926 -242 -214 72 O
ATOM 1808 CB VAL A 226 -21.159 7.753 -12.920 1.00 27.83 C
ANISOU 1808 CB VAL A 226 3926 3035 3614 -288 35 14 C
ATOM 1809 CG1 VAL A 226 -21.499 6.268 -13.036 1.00 29.57 C
ANISOU 1809 CG1 VAL A 226 4600 3165 3472 -633 -22 45 C
ATOM 1810 CG2 VAL A 226 -21.320 8.491 -14.260 1.00 27.76 C
ANISOU 1810 CG2 VAL A 226 4338 2995 3216 -19 -31 16 C
ATOM 1811 N LEU A 227 -22.610 7.029 -9.883 1.00 24.51 N
ANISOU 1811 N LEU A 227 3343 2667 3302 -122 -377 122 N
ATOM 1812 CA LEU A 227 -22.422 6.098 -8.784 1.00 24.65 C
ANISOU 1812 CA LEU A 227 3378 2661 3328 -21 -557 129 C
ATOM 1813 C LEU A 227 -22.133 4.732 -9.397 1.00 24.83 C
ANISOU 1813 C LEU A 227 3520 2795 3119 -269 -282 152 C
ATOM 1814 O LEU A 227 -23.041 4.132 -9.967 1.00 24.80 O
ANISOU 1814 O LEU A 227 3231 2815 3378 75 -237 237 O
ATOM 1815 CB LEU A 227 -23.669 6.047 -7.902 1.00 26.12 C
ANISOU 1815 CB LEU A 227 3860 2777 3289 -256 -319 -95 C
ATOM 1816 CG LEU A 227 -24.209 7.395 -7.412 1.00 29.41 C
ANISOU 1816 CG LEU A 227 4011 3548 3616 -156 41 -208 C
ATOM 1817 CD1 LEU A 227 -25.449 7.178 -6.600 1.00 28.93 C
ANISOU 1817 CD1 LEU A 227 3890 3181 3922 445 327 -682 C
ATOM 1818 CD2 LEU A 227 -23.177 8.093 -6.658 1.00 32.22 C
ANISOU 1818 CD2 LEU A 227 4135 3648 4458 -257 143 -724 C
ATOM 1819 N SER A 228 -20.875 4.308 -9.368 1.00 24.70 N
ANISOU 1819 N SER A 228 3313 2623 3448 -13 -127 169 N
ATOM 1820 CA SER A 228 -20.432 3.179 -10.162 1.00 24.98 C
ANISOU 1820 CA SER A 228 3034 2699 3760 -93 232 258 C
ATOM 1821 C SER A 228 -20.561 1.871 -9.392 1.00 23.30 C
ANISOU 1821 C SER A 228 2859 2508 3485 -225 -15 159 C
ATOM 1822 O SER A 228 -20.629 1.844 -8.152 1.00 24.57 O
ANISOU 1822 O SER A 228 3387 2718 3231 -201 31 25 O
ATOM 1823 CB SER A 228 -19.005 3.348 -10.558 1.00 30.51 C
ANISOU 1823 CB SER A 228 3796 2658 5138 -273 964 480 C
ATOM 1824 OG SER A 228 -18.612 2.381 -11.509 1.00 37.26 O
ANISOU 1824 OG SER A 228 4844 3670 5643 78 934 182 O
ATOM 1825 N GLY A 229 -20.615 0.775 -10.152 1.00 23.35 N
ANISOU 1825 N GLY A 229 3159 2684 3030 55 -65 -125 N
ATOM 1826 CA GLY A 229 -20.664 -0.547 -9.554 1.00 22.77 C
ANISOU 1826 CA GLY A 229 2984 2159 3506 -272 -21 134 C
ATOM 1827 C GLY A 229 -19.394 -0.910 -8.799 1.00 22.78 C
ANISOU 1827 C GLY A 229 3053 2536 3067 -543 8 13 C
ATOM 1828 O GLY A 229 -19.431 -1.765 -7.938 1.00 23.67 O
ANISOU 1828 O GLY A 229 3188 2864 2942 -436 -115 216 O
ATOM 1829 N HIS A 230 -18.268 -0.262 -9.168 1.00 23.08 N
ANISOU 1829 N HIS A 230 2888 2810 3073 22 -386 336 N
ATOM 1830 CA HIS A 230 -17.008 -0.510 -8.512 1.00 22.53 C
ANISOU 1830 CA HIS A 230 2668 2494 3400 -653 -313 271 C
ATOM 1831 C HIS A 230 -16.221 0.784 -8.399 1.00 25.80 C
ANISOU 1831 C HIS A 230 3127 2927 3749 -550 -437 -6 C
ATOM 1832 O HIS A 230 -16.204 1.577 -9.311 1.00 27.68 O
ANISOU 1832 O HIS A 230 3622 2997 3900 -479 -555 20 O
ATOM 1833 CB HIS A 230 -16.187 -1.546 -9.266 1.00 22.77 C
ANISOU 1833 CB HIS A 230 2584 2889 3179 -103 -277 502 C
ATOM 1834 CG HIS A 230 -16.883 -2.836 -9.482 1.00 22.73 C
ANISOU 1834 CG HIS A 230 2531 2658 3448 -315 -187 386 C
ATOM 1835 ND1 HIS A 230 -16.974 -3.809 -8.506 1.00 22.27 N
ANISOU 1835 ND1 HIS A 230 2782 2585 3095 -467 -436 273 N
ATOM 1836 CD2 HIS A 230 -17.578 -3.282 -10.535 1.00 23.21 C
ANISOU 1836 CD2 HIS A 230 2741 2860 3216 -112 -203 536 C
ATOM 1837 CE1 HIS A 230 -17.727 -4.819 -8.995 1.00 20.48 C
ANISOU 1837 CE1 HIS A 230 2823 2454 2502 -591 -434 52 C
ATOM 1838 NE2 HIS A 230 -18.123 -4.481 -10.209 1.00 21.78 N
ANISOU 1838 NE2 HIS A 230 2690 2425 3159 -688 -178 37 N
ATOM 1839 N GLY A 231 -15.577 0.967 -7.252 1.00 29.68 N
ANISOU 1839 N GLY A 231 4153 2718 4405 -751 -1239 108 N
ATOM 1840 CA GLY A 231 -14.693 2.109 -7.112 1.00 29.68 C
ANISOU 1840 CA GLY A 231 4018 3148 4112 -713 -1377 277 C
ATOM 1841 C GLY A 231 -15.399 3.438 -6.843 1.00 29.50 C
ANISOU 1841 C GLY A 231 3825 3191 4192 -702 -787 -228 C
ATOM 1842 O GLY A 231 -16.562 3.482 -6.455 1.00 29.00 O
ANISOU 1842 O GLY A 231 3577 3331 4111 -773 -607 -19 O
ATOM 1843 N GLU A 232 -14.658 4.534 -7.083 1.00 29.65 N
ANISOU 1843 N GLU A 232 3834 3273 4158 -752 -928 314 N
ATOM 1844 CA GLU A 232 -15.161 5.836 -6.678 1.00 29.19 C
ANISOU 1844 CA GLU A 232 3691 3135 4264 -665 -736 253 C
ATOM 1845 C GLU A 232 -16.100 6.406 -7.736 1.00 27.23 C
ANISOU 1845 C GLU A 232 3415 2987 3943 -777 -186 311 C
ATOM 1846 O GLU A 232 -16.129 5.963 -8.887 1.00 30.17 O
ANISOU 1846 O GLU A 232 4264 3426 3774 -176 -340 140 O
ATOM 1847 CB GLU A 232 -13.994 6.782 -6.416 1.00 34.61 C
ANISOU 1847 CB GLU A 232 4791 3068 5290 -1091 -910 16 C
ATOM 1848 CG GLU A 232 -13.120 6.356 -5.231 1.00 40.81 C
ANISOU 1848 CG GLU A 232 5110 3975 6421 -981 -1781 183 C
ATOM 1849 CD GLU A 232 -13.921 6.048 -3.964 1.00 49.83 C
ANISOU 1849 CD GLU A 232 7431 4892 6612 61 -1351 -51 C
ATOM 1850 OE1 GLU A 232 -14.563 6.977 -3.439 1.00 54.89 O
ANISOU 1850 OE1 GLU A 232 7445 6994 6418 642 -2021 -1075 O
ATOM 1851 OE2 GLU A 232 -13.990 4.878 -3.534 1.00 61.54 O
ANISOU 1851 OE2 GLU A 232 8424 6447 8513 328 -2250 1338 O
ATOM 1852 N ASP A 233 -16.873 7.411 -7.319 1.00 30.02 N
ANISOU 1852 N ASP A 233 4053 3245 4107 -275 -300 -37 N
ATOM 1853 CA ASP A 233 -17.792 8.047 -8.249 1.00 28.11 C
ANISOU 1853 CA ASP A 233 3844 2739 4098 -626 -492 33 C
ATOM 1854 C ASP A 233 -16.996 8.624 -9.423 1.00 29.50 C
ANISOU 1854 C ASP A 233 3786 3262 4161 -842 -476 124 C
ATOM 1855 O ASP A 233 -15.869 9.089 -9.205 1.00 31.63 O
ANISOU 1855 O ASP A 233 3919 3656 4442 -961 -497 461 O
ATOM 1856 CB ASP A 233 -18.572 9.146 -7.544 1.00 30.61 C
ANISOU 1856 CB ASP A 233 4183 3245 4201 -188 -281 -369 C
ATOM 1857 CG ASP A 233 -19.467 8.727 -6.399 1.00 32.26 C
ANISOU 1857 CG ASP A 233 3990 4236 4032 -25 -628 -466 C
ATOM 1858 OD1 ASP A 233 -19.665 7.509 -6.223 1.00 34.11 O
ANISOU 1858 OD1 ASP A 233 4474 3973 4511 -436 -283 11 O
ATOM 1859 OD2 ASP A 233 -19.904 9.658 -5.663 1.00 35.39 O
ANISOU 1859 OD2 ASP A 233 4544 4110 4792 -322 18 -868 O
ATOM 1860 N VAL A 234 -17.667 8.746 -10.588 1.00 29.56 N
ANISOU 1860 N VAL A 234 3988 2960 4284 -815 -631 414 N
ATOM 1861 CA VAL A 234 -17.150 9.425 -11.761 1.00 30.09 C
ANISOU 1861 CA VAL A 234 3981 3002 4451 -381 -240 344 C
ATOM 1862 C VAL A 234 -17.818 10.806 -11.876 1.00 30.44 C
ANISOU 1862 C VAL A 234 4085 3068 4412 -185 -900 -231 C
ATOM 1863 O VAL A 234 -19.020 10.901 -11.981 1.00 30.72 O
ANISOU 1863 O VAL A 234 4066 3047 4558 -621 -303 105 O
ATOM 1864 CB VAL A 234 -17.342 8.588 -13.034 1.00 31.87 C
ANISOU 1864 CB VAL A 234 4424 3340 4345 -191 -459 451 C
ATOM 1865 CG1 VAL A 234 -16.825 9.311 -14.256 1.00 34.65 C
ANISOU 1865 CG1 VAL A 234 4939 3534 4693 -389 -13 833 C
ATOM 1866 CG2 VAL A 234 -16.640 7.255 -12.964 1.00 31.83 C
ANISOU 1866 CG2 VAL A 234 4149 3433 4511 -413 -59 519 C
ATOM 1867 N LEU A 235 -17.016 11.874 -11.742 1.00 32.96 N
ANISOU 1867 N LEU A 235 4644 3372 4507 -831 -265 -235 N
ATOM 1868 CA LEU A 235 -17.539 13.239 -11.839 1.00 34.97 C
ANISOU 1868 CA LEU A 235 5165 3515 4607 -488 -38 24 C
ATOM 1869 C LEU A 235 -17.328 13.819 -13.240 1.00 33.65 C
ANISOU 1869 C LEU A 235 4470 3760 4554 -338 52 341 C
ATOM 1870 O LEU A 235 -18.064 14.707 -13.647 1.00 41.53 O
ANISOU 1870 O LEU A 235 5848 3862 6071 28 690 680 O
ATOM 1871 CB LEU A 235 -16.970 14.179 -10.770 1.00 39.10 C
ANISOU 1871 CB LEU A 235 5720 4153 4983 -531 241 -426 C
ATOM 1872 CG LEU A 235 -17.162 13.745 -9.313 1.00 43.29 C
ANISOU 1872 CG LEU A 235 6389 4959 5100 -1123 290 -900 C
ATOM 1873 CD1 LEU A 235 -16.756 14.800 -8.310 1.00 50.65 C
ANISOU 1873 CD1 LEU A 235 7669 5490 6087 -1373 -161 -815 C
ATOM 1874 CD2 LEU A 235 -18.586 13.362 -9.101 1.00 47.59 C
ANISOU 1874 CD2 LEU A 235 7091 5207 5783 -1040 647 -403 C
ATOM 1875 N ASP A 236 -16.345 13.327 -13.994 1.00 33.33 N
ANISOU 1875 N ASP A 236 4908 3371 4385 -689 429 239 N
ATOM 1876 CA ASP A 236 -16.087 13.860 -15.326 1.00 35.12 C
ANISOU 1876 CA ASP A 236 5193 3692 4460 -624 481 154 C
ATOM 1877 C ASP A 236 -16.269 12.767 -16.369 1.00 31.21 C
ANISOU 1877 C ASP A 236 4418 3191 4248 -849 366 263 C
ATOM 1878 O ASP A 236 -15.304 12.164 -16.816 1.00 33.75 O
ANISOU 1878 O ASP A 236 4344 3328 5152 -433 501 35 O
ATOM 1879 CB ASP A 236 -14.712 14.506 -15.409 1.00 39.22 C
ANISOU 1879 CB ASP A 236 5558 4075 5269 -1132 638 -101 C
ATOM 1880 CG ASP A 236 -14.279 15.012 -16.774 1.00 40.30 C
ANISOU 1880 CG ASP A 236 4923 4858 5531 -1279 384 267 C
ATOM 1881 OD1 ASP A 236 -15.165 15.251 -17.644 1.00 40.83 O
ANISOU 1881 OD1 ASP A 236 6129 3651 5733 -890 99 104 O
ATOM 1882 OD2 ASP A 236 -13.051 15.220 -16.946 1.00 47.49 O
ANISOU 1882 OD2 ASP A 236 5175 6038 6829 -2333 1131 833 O
ATOM 1883 N VAL A 237 -17.529 12.562 -16.776 1.00 33.26 N
ANISOU 1883 N VAL A 237 4619 3729 4289 -265 399 511 N
ATOM 1884 CA VAL A 237 -17.878 11.486 -17.688 1.00 31.14 C
ANISOU 1884 CA VAL A 237 4593 3012 4228 -329 318 413 C
ATOM 1885 C VAL A 237 -17.275 11.748 -19.062 1.00 31.84 C
ANISOU 1885 C VAL A 237 4507 3236 4356 -184 564 849 C
ATOM 1886 O VAL A 237 -16.752 10.838 -19.693 1.00 34.46 O
ANISOU 1886 O VAL A 237 4209 3888 4998 -121 690 498 O
ATOM 1887 CB VAL A 237 -19.403 11.365 -17.789 1.00 30.98 C
ANISOU 1887 CB VAL A 237 4059 3512 4200 363 663 916 C
ATOM 1888 CG1 VAL A 237 -19.850 10.454 -18.938 1.00 34.58 C
ANISOU 1888 CG1 VAL A 237 5054 3648 4438 -19 353 937 C
ATOM 1889 CG2 VAL A 237 -19.997 10.947 -16.446 1.00 33.22 C
ANISOU 1889 CG2 VAL A 237 4167 3875 4580 354 490 1048 C
ATOM 1890 N VAL A 238 -17.390 12.988 -19.557 1.00 33.41 N
ANISOU 1890 N VAL A 238 4493 3688 4513 -324 254 990 N
ATOM 1891 CA VAL A 238 -16.849 13.296 -20.874 1.00 35.15 C
ANISOU 1891 CA VAL A 238 4818 3853 4682 -529 344 1019 C
ATOM 1892 C VAL A 238 -15.354 12.979 -20.935 1.00 34.53 C
ANISOU 1892 C VAL A 238 4769 3630 4719 -992 77 668 C
ATOM 1893 O VAL A 238 -14.876 12.328 -21.877 1.00 36.79 O
ANISOU 1893 O VAL A 238 5046 3713 5219 -462 1056 570 O
ATOM 1894 CB VAL A 238 -17.135 14.754 -21.252 1.00 38.19 C
ANISOU 1894 CB VAL A 238 4982 3809 5718 -786 305 1070 C
ATOM 1895 CG1 VAL A 238 -16.303 15.156 -22.449 1.00 41.74 C
ANISOU 1895 CG1 VAL A 238 6051 4526 5283 -426 168 1579 C
ATOM 1896 CG2 VAL A 238 -18.598 15.051 -21.461 1.00 39.10 C
ANISOU 1896 CG2 VAL A 238 5863 3332 5660 -790 134 663 C
ATOM 1897 N GLY A 239 -14.617 13.431 -19.909 1.00 35.20 N
ANISOU 1897 N GLY A 239 4665 3844 4867 -902 265 327 N
ATOM 1898 CA GLY A 239 -13.179 13.198 -19.834 1.00 39.03 C
ANISOU 1898 CA GLY A 239 5034 4707 5089 -988 395 33 C
ATOM 1899 C GLY A 239 -12.823 11.713 -19.812 1.00 35.87 C
ANISOU 1899 C GLY A 239 4703 4521 4403 -1089 298 388 C
ATOM 1900 O GLY A 239 -11.902 11.276 -20.509 1.00 39.34 O
ANISOU 1900 O GLY A 239 4332 5577 5038 -1015 642 -77 O
ATOM 1901 N LEU A 240 -13.582 10.953 -19.001 1.00 37.83 N
ANISOU 1901 N LEU A 240 5615 4061 4697 -1254 481 905 N
ATOM 1902 CA LEU A 240 -13.305 9.541 -18.818 1.00 38.18 C
ANISOU 1902 CA LEU A 240 5324 4349 4834 -30 603 572 C
ATOM 1903 C LEU A 240 -13.601 8.801 -20.117 1.00 32.35 C
ANISOU 1903 C LEU A 240 3953 3714 4623 -70 44 394 C
ATOM 1904 O LEU A 240 -12.807 7.980 -20.576 1.00 35.77 O
ANISOU 1904 O LEU A 240 4508 4254 4828 522 588 179 O
ATOM 1905 CB LEU A 240 -14.096 8.971 -17.646 1.00 37.69 C
ANISOU 1905 CB LEU A 240 5237 3609 5474 -30 802 875 C
ATOM 1906 CG LEU A 240 -13.716 7.530 -17.329 1.00 40.24 C
ANISOU 1906 CG LEU A 240 5771 4281 5237 720 841 774 C
ATOM 1907 CD1 LEU A 240 -12.193 7.409 -17.188 1.00 47.42 C
ANISOU 1907 CD1 LEU A 240 6384 5805 5827 689 398 165 C
ATOM 1908 CD2 LEU A 240 -14.430 7.045 -16.103 1.00 40.26 C
ANISOU 1908 CD2 LEU A 240 6571 4009 4717 813 1244 422 C
ATOM 1909 N VAL A 241 -14.728 9.144 -20.743 1.00 32.85 N
ANISOU 1909 N VAL A 241 3914 3777 4790 -101 371 539 N
ATOM 1910 CA VAL A 241 -15.090 8.504 -21.991 1.00 31.81 C
ANISOU 1910 CA VAL A 241 4112 3496 4476 -636 330 695 C
ATOM 1911 C VAL A 241 -14.015 8.761 -23.048 1.00 33.04 C
ANISOU 1911 C VAL A 241 3739 4058 4755 -405 427 676 C
ATOM 1912 O VAL A 241 -13.632 7.861 -23.777 1.00 36.22 O
ANISOU 1912 O VAL A 241 4131 4185 5447 273 936 531 O
ATOM 1913 CB VAL A 241 -16.477 8.975 -22.449 1.00 30.72 C
ANISOU 1913 CB VAL A 241 3717 3308 4649 -620 337 490 C
ATOM 1914 CG1 VAL A 241 -16.720 8.645 -23.907 1.00 30.68 C
ANISOU 1914 CG1 VAL A 241 3751 3348 4559 -468 468 326 C
ATOM 1915 CG2 VAL A 241 -17.556 8.372 -21.573 1.00 30.35 C
ANISOU 1915 CG2 VAL A 241 3674 3497 4362 -410 287 478 C
ATOM 1916 N ASN A 242 -13.598 10.011 -23.198 1.00 35.34 N
ANISOU 1916 N ASN A 242 4229 3831 5369 -587 1077 775 N
ATOM 1917 CA ASN A 242 -12.592 10.341 -24.203 1.00 35.75 C
ANISOU 1917 CA ASN A 242 4378 4011 5196 -706 1238 416 C
ATOM 1918 C ASN A 242 -11.327 9.509 -24.009 1.00 36.67 C
ANISOU 1918 C ASN A 242 4186 4732 5015 -1124 604 453 C
ATOM 1919 O ASN A 242 -10.770 8.976 -24.984 1.00 40.80 O
ANISOU 1919 O ASN A 242 4999 5315 5189 -681 1121 482 O
ATOM 1920 CB ASN A 242 -12.310 11.838 -24.216 1.00 37.18 C
ANISOU 1920 CB ASN A 242 4877 4284 4968 -578 1503 497 C
ATOM 1921 CG ASN A 242 -13.424 12.609 -24.873 1.00 42.96 C
ANISOU 1921 CG ASN A 242 6197 4672 5454 -282 1323 712 C
ATOM 1922 OD1 ASN A 242 -14.175 12.059 -25.687 1.00 52.73 O
ANISOU 1922 OD1 ASN A 242 7212 5509 7315 48 125 1127 O
ATOM 1923 ND2 ASN A 242 -13.511 13.895 -24.579 1.00 51.39 N
ANISOU 1923 ND2 ASN A 242 7181 4796 7550 -512 1129 867 N
ATOM 1924 N GLU A 243 -10.890 9.415 -22.743 1.00 37.15 N
ANISOU 1924 N GLU A 243 4380 5041 4694 -494 328 -162 N
ATOM 1925 CA GLU A 243 -9.704 8.650 -22.382 1.00 40.53 C
ANISOU 1925 CA GLU A 243 4463 5611 5327 4 386 260 C
ATOM 1926 C GLU A 243 -9.870 7.170 -22.752 1.00 39.21 C
ANISOU 1926 C GLU A 243 4585 5757 4555 -163 599 -94 C
ATOM 1927 O GLU A 243 -8.954 6.538 -23.276 1.00 41.51 O
ANISOU 1927 O GLU A 243 4762 6385 4625 -1 642 -90 O
ATOM 1928 CB GLU A 243 -9.435 8.820 -20.887 1.00 43.80 C
ANISOU 1928 CB GLU A 243 4641 6147 5856 867 395 513 C
ATOM 1929 CG GLU A 243 -8.243 8.011 -20.369 1.00 50.80 C
ANISOU 1929 CG GLU A 243 5448 7458 6396 1348 -471 471 C
ATOM 1930 CD GLU A 243 -8.350 7.591 -18.904 1.00 64.26 C
ANISOU 1930 CD GLU A 243 8379 8701 7336 1303 -759 398 C
ATOM 1931 OE1 GLU A 243 -8.154 6.386 -18.595 1.00 76.08 O
ANISOU 1931 OE1 GLU A 243 9481 9566 9860 3052 -589 187 O
ATOM 1932 OE2 GLU A 243 -8.653 8.466 -18.062 1.00 68.89 O
ANISOU 1932 OE2 GLU A 243 9678 9369 7129 -199 -2311 -699 O
ATOM 1933 N ARG A 244 -11.041 6.612 -22.432 1.00 36.14 N
ANISOU 1933 N ARG A 244 3933 5460 4340 293 474 -248 N
ATOM 1934 CA ARG A 244 -11.297 5.204 -22.657 1.00 38.91 C
ANISOU 1934 CA ARG A 244 4584 5487 4713 887 77 291 C
ATOM 1935 C ARG A 244 -11.355 4.889 -24.155 1.00 34.06 C
ANISOU 1935 C ARG A 244 4339 4894 3710 113 792 468 C
ATOM 1936 O ARG A 244 -10.823 3.855 -24.582 1.00 35.95 O
ANISOU 1936 O ARG A 244 4359 4516 4784 160 706 44 O
ATOM 1937 CB ARG A 244 -12.559 4.752 -21.926 1.00 38.72 C
ANISOU 1937 CB ARG A 244 4771 5697 4244 878 212 1077 C
ATOM 1938 CG ARG A 244 -12.454 4.770 -20.403 1.00 43.11 C
ANISOU 1938 CG ARG A 244 5803 5770 4806 997 414 1204 C
ATOM 1939 CD ARG A 244 -11.390 3.772 -19.895 1.00 42.57 C
ANISOU 1939 CD ARG A 244 5707 6202 4265 613 -80 1194 C
ATOM 1940 NE ARG A 244 -10.987 3.963 -18.499 1.00 42.62 N
ANISOU 1940 NE ARG A 244 5694 5610 4889 -220 329 1403 N
ATOM 1941 CZ ARG A 244 -11.864 3.790 -17.510 1.00 39.83 C
ANISOU 1941 CZ ARG A 244 5072 5077 4984 -380 618 1233 C
ATOM 1942 NH1 ARG A 244 -11.548 4.026 -16.253 1.00 43.08 N
ANISOU 1942 NH1 ARG A 244 4631 5736 6003 -669 -129 1027 N
ATOM 1943 NH2 ARG A 244 -13.068 3.365 -17.822 1.00 41.43 N
ANISOU 1943 NH2 ARG A 244 4782 4864 6097 -197 513 768 N
ATOM 1944 N LEU A 245 -12.027 5.761 -24.925 1.00 33.96 N
ANISOU 1944 N LEU A 245 3618 4756 4529 -220 791 652 N
ATOM 1945 CA LEU A 245 -12.105 5.604 -26.374 1.00 33.80 C
ANISOU 1945 CA LEU A 245 4268 3920 4654 -51 689 352 C
ATOM 1946 C LEU A 245 -10.700 5.678 -26.979 1.00 34.76 C
ANISOU 1946 C LEU A 245 3823 4418 4966 -256 543 348 C
ATOM 1947 O LEU A 245 -10.371 4.910 -27.886 1.00 38.88 O
ANISOU 1947 O LEU A 245 4861 4895 5016 -912 926 367 O
ATOM 1948 CB LEU A 245 -13.020 6.671 -26.976 1.00 35.32 C
ANISOU 1948 CB LEU A 245 3959 4891 4571 234 352 81 C
ATOM 1949 CG LEU A 245 -14.511 6.544 -26.642 1.00 36.59 C
ANISOU 1949 CG LEU A 245 4069 4737 5095 432 630 156 C
ATOM 1950 CD1 LEU A 245 -15.263 7.729 -27.178 1.00 40.96 C
ANISOU 1950 CD1 LEU A 245 4944 5840 4779 -251 654 718 C
ATOM 1951 CD2 LEU A 245 -15.086 5.247 -27.164 1.00 40.42 C
ANISOU 1951 CD2 LEU A 245 4638 5101 5620 661 561 -32 C
ATOM 1952 N GLN A 246 -9.863 6.601 -26.476 1.00 35.70 N
ANISOU 1952 N GLN A 246 4131 4307 5125 -673 937 352 N
ATOM 1953 CA GLN A 246 -8.492 6.742 -26.974 1.00 38.77 C
ANISOU 1953 CA GLN A 246 4367 5197 5168 -571 1286 -440 C
ATOM 1954 C GLN A 246 -7.704 5.453 -26.709 1.00 40.47 C
ANISOU 1954 C GLN A 246 4332 5601 5443 -357 931 148 C
ATOM 1955 O GLN A 246 -6.987 4.942 -27.596 1.00 41.97 O
ANISOU 1955 O GLN A 246 5109 4858 5978 -588 1414 303 O
ATOM 1956 CB GLN A 246 -7.836 7.992 -26.372 1.00 43.58 C
ANISOU 1956 CB GLN A 246 5017 6169 5374 -1143 1156 -1060 C
ATOM 1957 N LYS A 247 -7.861 4.920 -25.488 1.00 37.21 N
ANISOU 1957 N LYS A 247 3960 4912 5267 -335 1127 -126 N
ATOM 1958 CA LYS A 247 -7.127 3.732 -25.071 1.00 37.70 C
ANISOU 1958 CA LYS A 247 3666 5003 5656 -138 938 429 C
ATOM 1959 C LYS A 247 -7.557 2.532 -25.910 1.00 37.90 C
ANISOU 1959 C LYS A 247 3958 5030 5412 -199 880 325 C
ATOM 1960 O LYS A 247 -6.736 1.698 -26.282 1.00 39.86 O
ANISOU 1960 O LYS A 247 4468 4630 6046 -70 1048 583 O
ATOM 1961 CB LYS A 247 -7.216 3.467 -23.564 1.00 41.21 C
ANISOU 1961 CB LYS A 247 4138 5266 6255 499 1488 441 C
ATOM 1962 N GLN A 248 -8.858 2.442 -26.192 1.00 36.57 N
ANISOU 1962 N GLN A 248 3900 4800 5195 170 1049 406 N
ATOM 1963 CA GLN A 248 -9.399 1.336 -26.964 1.00 36.91 C
ANISOU 1963 CA GLN A 248 4530 3841 5654 540 1138 101 C
ATOM 1964 C GLN A 248 -8.819 1.359 -28.376 1.00 36.14 C
ANISOU 1964 C GLN A 248 4577 3921 5234 180 1107 701 C
ATOM 1965 O GLN A 248 -8.433 0.330 -28.917 1.00 39.59 O
ANISOU 1965 O GLN A 248 5790 3847 5404 138 1182 272 O
ATOM 1966 CB GLN A 248 -10.925 1.373 -26.977 1.00 39.08 C
ANISOU 1966 CB GLN A 248 4659 4495 5693 318 228 230 C
ATOM 1967 CG GLN A 248 -11.531 0.077 -27.503 1.00 44.78 C
ANISOU 1967 CG GLN A 248 6108 4705 6202 -383 1045 406 C
ATOM 1968 CD GLN A 248 -11.804 0.083 -28.988 1.00 51.15 C
ANISOU 1968 CD GLN A 248 6496 5772 7164 177 785 293 C
ATOM 1969 OE1 GLN A 248 -12.393 1.040 -29.518 1.00 50.36 O
ANISOU 1969 OE1 GLN A 248 6744 5751 6638 1044 1601 554 O
ATOM 1970 NE2 GLN A 248 -11.357 -0.983 -29.662 1.00 51.44 N
ANISOU 1970 NE2 GLN A 248 6239 5184 8123 -92 788 -147 N
ATOM 1971 N GLU A 249 -8.747 2.547 -28.958 1.00 38.17 N
ANISOU 1971 N GLU A 249 4997 4208 5296 -202 860 853 N
ATOM 1972 CA GLU A 249 -8.200 2.692 -30.294 1.00 38.40 C
ANISOU 1972 CA GLU A 249 5315 4066 5208 -18 1049 658 C
ATOM 1973 C GLU A 249 -6.734 2.259 -30.326 1.00 35.98 C
ANISOU 1973 C GLU A 249 4628 4134 4909 -169 500 669 C
ATOM 1974 O GLU A 249 -6.308 1.520 -31.222 1.00 39.11 O
ANISOU 1974 O GLU A 249 5118 4575 5166 447 704 394 O
ATOM 1975 CB GLU A 249 -8.384 4.133 -30.756 1.00 43.36 C
ANISOU 1975 CB GLU A 249 6075 4428 5971 674 1165 1422 C
ATOM 1976 CG GLU A 249 -7.845 4.324 -32.171 1.00 51.26 C
ANISOU 1976 CG GLU A 249 7437 5543 6497 78 1561 1262 C
ATOM 1977 CD GLU A 249 -8.429 5.486 -32.940 1.00 59.69 C
ANISOU 1977 CD GLU A 249 9560 5716 7402 455 1370 1360 C
ATOM 1978 OE1 GLU A 249 -8.886 5.269 -34.091 1.00 70.83 O
ANISOU 1978 OE1 GLU A 249 10624 7936 8352 355 901 1228 O
ATOM 1979 OE2 GLU A 249 -8.397 6.602 -32.382 1.00 70.31 O
ANISOU 1979 OE2 GLU A 249 12543 6332 7841 -123 1682 871 O
ATOM 1980 N ALA A 250 -5.951 2.719 -29.341 1.00 36.95 N
ANISOU 1980 N ALA A 250 4102 4912 5023 82 733 352 N
ATOM 1981 CA ALA A 250 -4.547 2.326 -29.261 1.00 37.90 C
ANISOU 1981 CA ALA A 250 4166 4802 5432 97 831 797 C
ATOM 1982 C ALA A 250 -4.407 0.815 -29.170 1.00 38.60 C
ANISOU 1982 C ALA A 250 4740 4659 5266 -169 1230 546 C
ATOM 1983 O ALA A 250 -3.579 0.242 -29.861 1.00 38.52 O
ANISOU 1983 O ALA A 250 4432 4374 5830 209 1825 827 O
ATOM 1984 CB ALA A 250 -3.870 2.974 -28.087 1.00 38.51 C
ANISOU 1984 CB ALA A 250 4028 5173 5432 86 561 1438 C
ATOM 1985 N ARG A 251 -5.229 0.168 -28.333 1.00 37.98 N
ANISOU 1985 N ARG A 251 4372 4648 5413 -252 1605 902 N
ATOM 1986 CA ARG A 251 -5.113 -1.266 -28.163 1.00 41.56 C
ANISOU 1986 CA ARG A 251 5200 4853 5735 1 1165 1009 C
ATOM 1987 C ARG A 251 -5.455 -1.992 -29.457 1.00 37.56 C
ANISOU 1987 C ARG A 251 4121 4493 5656 609 1024 1056 C
ATOM 1988 O ARG A 251 -4.842 -3.005 -29.805 1.00 41.92 O
ANISOU 1988 O ARG A 251 5507 4303 6117 607 1274 1062 O
ATOM 1989 CB ARG A 251 -5.990 -1.723 -26.994 1.00 43.11 C
ANISOU 1989 CB ARG A 251 5298 4923 6158 -453 1722 1007 C
ATOM 1990 CG ARG A 251 -5.829 -3.222 -26.797 1.00 48.23 C
ANISOU 1990 CG ARG A 251 7140 4444 6741 218 1634 1051 C
ATOM 1991 CD ARG A 251 -6.522 -3.790 -25.555 1.00 51.98 C
ANISOU 1991 CD ARG A 251 7384 5828 6539 -260 1328 1264 C
ATOM 1992 NE ARG A 251 -5.805 -3.356 -24.353 1.00 54.69 N
ANISOU 1992 NE ARG A 251 6300 7491 6988 -374 748 1223 N
ATOM 1993 CZ ARG A 251 -6.271 -3.405 -23.114 1.00 58.97 C
ANISOU 1993 CZ ARG A 251 7113 7725 7567 155 855 1382 C
ATOM 1994 NH1 ARG A 251 -7.509 -3.836 -22.866 1.00 57.87 N
ANISOU 1994 NH1 ARG A 251 6454 7742 7790 928 420 1753 N
ATOM 1995 NH2 ARG A 251 -5.488 -3.008 -22.120 1.00 61.20 N
ANISOU 1995 NH2 ARG A 251 7326 7989 7937 450 724 1386 N
ATOM 1996 N ALA A 252 -6.455 -1.484 -30.164 1.00 40.01 N
ANISOU 1996 N ALA A 252 5010 4634 5557 769 1319 927 N
ATOM 1997 CA ALA A 252 -6.872 -2.112 -31.393 1.00 43.23 C
ANISOU 1997 CA ALA A 252 5324 5080 6022 1093 1206 947 C
ATOM 1998 C ALA A 252 -5.699 -2.063 -32.353 1.00 39.72 C
ANISOU 1998 C ALA A 252 5294 4477 5320 434 1177 983 C
ATOM 1999 O ALA A 252 -5.396 -3.066 -32.986 1.00 44.58 O
ANISOU 1999 O ALA A 252 6097 5359 5483 933 1474 650 O
ATOM 2000 CB ALA A 252 -8.093 -1.429 -31.961 1.00 44.97 C
ANISOU 2000 CB ALA A 252 5221 5609 6258 1317 1328 1603 C
ATOM 2001 N PHE A 253 -5.037 -0.896 -32.435 1.00 40.37 N
ANISOU 2001 N PHE A 253 5466 4361 5512 360 1025 415 N
ATOM 2002 CA PHE A 253 -3.878 -0.764 -33.302 1.00 41.81 C
ANISOU 2002 CA PHE A 253 5397 4626 5862 754 1399 942 C
ATOM 2003 C PHE A 253 -2.767 -1.712 -32.854 1.00 44.22 C
ANISOU 2003 C PHE A 253 6106 4666 6029 840 1176 746 C
ATOM 2004 O PHE A 253 -2.090 -2.288 -33.698 1.00 44.71 O
ANISOU 2004 O PHE A 253 6229 5187 5570 785 2565 876 O
ATOM 2005 CB PHE A 253 -3.367 0.673 -33.370 1.00 42.01 C
ANISOU 2005 CB PHE A 253 6055 4632 5276 768 1507 683 C
ATOM 2006 CG PHE A 253 -4.115 1.544 -34.372 1.00 42.87 C
ANISOU 2006 CG PHE A 253 6078 4845 5366 1374 1605 1366 C
ATOM 2007 CD1 PHE A 253 -4.018 1.294 -35.743 1.00 46.59 C
ANISOU 2007 CD1 PHE A 253 5765 5770 6168 1391 1755 1629 C
ATOM 2008 CD2 PHE A 253 -4.905 2.607 -33.947 1.00 49.48 C
ANISOU 2008 CD2 PHE A 253 7361 6397 5043 1616 2078 1758 C
ATOM 2009 CE1 PHE A 253 -4.700 2.078 -36.661 1.00 50.08 C
ANISOU 2009 CE1 PHE A 253 7182 5684 6162 1277 2123 2075 C
ATOM 2010 CE2 PHE A 253 -5.567 3.402 -34.870 1.00 50.73 C
ANISOU 2010 CE2 PHE A 253 6593 5861 6820 2550 1837 1173 C
ATOM 2011 CZ PHE A 253 -5.466 3.133 -36.227 1.00 49.87 C
ANISOU 2011 CZ PHE A 253 6605 6650 5694 1993 2305 2161 C
ATOM 2012 N LYS A 254 -2.561 -1.844 -31.538 1.00 44.02 N
ANISOU 2012 N LYS A 254 5139 5216 6370 1173 1620 1457 N
ATOM 2013 CA LYS A 254 -1.509 -2.714 -31.033 1.00 41.78 C
ANISOU 2013 CA LYS A 254 5406 4664 5804 812 1372 1838 C
ATOM 2014 C LYS A 254 -1.772 -4.142 -31.499 1.00 43.40 C
ANISOU 2014 C LYS A 254 5428 4902 6159 808 1769 1073 C
ATOM 2015 O LYS A 254 -0.851 -4.786 -31.970 1.00 45.00 O
ANISOU 2015 O LYS A 254 4686 4846 7567 707 1920 896 O
ATOM 2016 CB LYS A 254 -1.387 -2.633 -29.505 1.00 40.71 C
ANISOU 2016 CB LYS A 254 4312 5025 6129 635 1383 1848 C
ATOM 2017 CG LYS A 254 -0.353 -3.543 -28.900 1.00 42.18 C
ANISOU 2017 CG LYS A 254 4886 4587 6554 1575 1517 1255 C
ATOM 2018 CD LYS A 254 -0.224 -3.404 -27.391 1.00 45.20 C
ANISOU 2018 CD LYS A 254 5165 5044 6964 1025 1039 814 C
ATOM 2019 CE LYS A 254 0.845 -4.316 -26.856 1.00 49.58 C
ANISOU 2019 CE LYS A 254 6813 4766 7258 902 846 718 C
ATOM 2020 NZ LYS A 254 0.898 -4.169 -25.400 1.00 58.68 N
ANISOU 2020 NZ LYS A 254 7237 6726 8333 -231 934 894 N
ATOM 2021 N VAL A 255 -3.020 -4.617 -31.354 1.00 41.24 N
ANISOU 2021 N VAL A 255 5205 4547 5917 1118 1838 1458 N
ATOM 2022 CA VAL A 255 -3.400 -5.939 -31.824 1.00 40.61 C
ANISOU 2022 CA VAL A 255 5643 3697 6089 1437 1672 1492 C
ATOM 2023 C VAL A 255 -3.156 -6.061 -33.326 1.00 45.04 C
ANISOU 2023 C VAL A 255 7242 4235 5636 1800 1708 1102 C
ATOM 2024 O VAL A 255 -2.599 -7.061 -33.795 1.00 43.56 O
ANISOU 2024 O VAL A 255 6897 4410 5245 1114 1499 708 O
ATOM 2025 CB VAL A 255 -4.859 -6.296 -31.481 1.00 42.46 C
ANISOU 2025 CB VAL A 255 5596 4307 6229 864 1371 1153 C
ATOM 2026 CG1 VAL A 255 -5.288 -7.594 -32.148 1.00 44.56 C
ANISOU 2026 CG1 VAL A 255 5876 4399 6656 401 1783 781 C
ATOM 2027 CG2 VAL A 255 -5.084 -6.325 -29.970 1.00 39.34 C
ANISOU 2027 CG2 VAL A 255 4880 4160 5906 534 799 1255 C
ATOM 2028 N LEU A 256 -3.585 -5.043 -34.092 1.00 46.09 N
ANISOU 2028 N LEU A 256 7851 4408 5254 1763 2352 1239 N
ATOM 2029 CA LEU A 256 -3.406 -5.111 -35.537 1.00 47.91 C
ANISOU 2029 CA LEU A 256 8331 4562 5310 1628 1873 921 C
ATOM 2030 C LEU A 256 -1.918 -5.259 -35.887 1.00 50.98 C
ANISOU 2030 C LEU A 256 8087 5157 6126 750 2378 870 C
ATOM 2031 O LEU A 256 -1.557 -6.131 -36.697 1.00 51.71 O
ANISOU 2031 O LEU A 256 8532 4512 6604 664 2283 499 O
ATOM 2032 CB LEU A 256 -4.074 -3.921 -36.205 1.00 49.83 C
ANISOU 2032 CB LEU A 256 9040 4826 5065 1665 2863 1350 C
ATOM 2033 CG LEU A 256 -4.134 -3.963 -37.733 1.00 55.27 C
ANISOU 2033 CG LEU A 256 9669 5367 5963 1718 1851 868 C
ATOM 2034 CD1 LEU A 256 -5.074 -5.062 -38.237 1.00 59.29 C
ANISOU 2034 CD1 LEU A 256 9676 5642 7209 1912 1693 735 C
ATOM 2035 CD2 LEU A 256 -4.585 -2.600 -38.156 1.00 57.86 C
ANISOU 2035 CD2 LEU A 256 10253 6128 5604 1440 1897 2410 C
ATOM 2036 N ASN A 257 -1.051 -4.485 -35.207 1.00 48.59 N
ANISOU 2036 N ASN A 257 6774 4986 6701 1337 2112 1303 N
ATOM 2037 CA ASN A 257 0.386 -4.514 -35.469 1.00 48.07 C
ANISOU 2037 CA ASN A 257 7006 4735 6523 986 2217 1212 C
ATOM 2038 C ASN A 257 1.012 -5.832 -35.001 1.00 51.38 C
ANISOU 2038 C ASN A 257 7285 5218 7019 1219 2498 1822 C
ATOM 2039 O ASN A 257 1.970 -6.307 -35.616 1.00 52.41 O
ANISOU 2039 O ASN A 257 7113 5279 7521 269 2684 1127 O
ATOM 2040 CB ASN A 257 1.063 -3.270 -34.911 1.00 47.11 C
ANISOU 2040 CB ASN A 257 6805 5022 6072 1099 1869 1621 C
ATOM 2041 CG ASN A 257 0.811 -2.102 -35.835 1.00 46.57 C
ANISOU 2041 CG ASN A 257 7077 4425 6190 1312 1971 1170 C
ATOM 2042 OD1 ASN A 257 0.029 -1.193 -35.535 1.00 52.63 O
ANISOU 2042 OD1 ASN A 257 7737 4839 7419 1007 2251 628 O
ATOM 2043 ND2 ASN A 257 1.361 -2.167 -37.023 1.00 47.21 N
ANISOU 2043 ND2 ASN A 257 7096 4648 6193 1270 2730 1938 N
ATOM 2044 N LEU A 258 0.470 -6.438 -33.933 1.00 50.41 N
ANISOU 2044 N LEU A 258 6707 5714 6732 728 2700 1866 N
ATOM 2045 CA LEU A 258 0.988 -7.715 -33.459 1.00 52.85 C
ANISOU 2045 CA LEU A 258 6912 5664 7504 1449 2975 1119 C
ATOM 2046 C LEU A 258 0.795 -8.783 -34.528 1.00 56.05 C
ANISOU 2046 C LEU A 258 7020 5927 8351 1221 2383 437 C
ATOM 2047 O LEU A 258 1.683 -9.608 -34.752 1.00 55.76 O
ANISOU 2047 O LEU A 258 7114 5568 8506 978 2923 436 O
ATOM 2048 CB LEU A 258 0.313 -8.158 -32.161 1.00 48.30 C
ANISOU 2048 CB LEU A 258 5884 4602 7867 1439 3186 1762 C
ATOM 2049 CG LEU A 258 0.827 -7.470 -30.892 1.00 55.26 C
ANISOU 2049 CG LEU A 258 6727 6460 7809 1431 3063 1796 C
ATOM 2050 CD1 LEU A 258 -0.111 -7.734 -29.718 1.00 58.28 C
ANISOU 2050 CD1 LEU A 258 7201 6774 8168 1466 3241 2120 C
ATOM 2051 CD2 LEU A 258 2.243 -7.931 -30.579 1.00 56.61 C
ANISOU 2051 CD2 LEU A 258 7293 6054 8162 1140 2118 2199 C
ATOM 2052 N LEU A 259 -0.393 -8.763 -35.138 1.00 46.41 N
ANISOU 2052 N LEU A 259 5721 4334 7578 1411 2044 406 N
ATOM 2053 CA LEU A 259 -0.815 -9.740 -36.129 1.00 51.00 C
ANISOU 2053 CA LEU A 259 6619 5706 7053 677 2157 599 C
ATOM 2054 C LEU A 259 -0.040 -9.605 -37.432 1.00 52.11 C
ANISOU 2054 C LEU A 259 7238 5365 7197 642 1954 740 C
ATOM 2055 O LEU A 259 0.298 -10.606 -38.049 1.00 49.46 O
ANISOU 2055 O LEU A 259 6178 6111 6502 1616 2224 951 O
ATOM 2056 CB LEU A 259 -2.321 -9.562 -36.353 1.00 48.06 C
ANISOU 2056 CB LEU A 259 6079 5411 6769 1242 1472 1461 C
ATOM 2057 CG LEU A 259 -3.260 -10.062 -35.242 1.00 49.25 C
ANISOU 2057 CG LEU A 259 6209 5874 6628 1588 1745 1092 C
ATOM 2058 CD1 LEU A 259 -4.704 -9.779 -35.627 1.00 51.88 C
ANISOU 2058 CD1 LEU A 259 6222 6485 7003 782 2083 815 C
ATOM 2059 CD2 LEU A 259 -3.114 -11.547 -34.940 1.00 47.27 C
ANISOU 2059 CD2 LEU A 259 6097 5764 6099 882 1686 1059 C
ATOM 2060 N LYS A 260 0.176 -8.370 -37.868 1.00 55.58 N
ANISOU 2060 N LYS A 260 7677 6132 7307 4 3030 776 N
ATOM 2061 CA LYS A 260 1.043 -8.115 -39.011 1.00 62.44 C
ANISOU 2061 CA LYS A 260 8986 7097 7640 310 2887 1691 C
ATOM 2062 C LYS A 260 2.375 -8.848 -38.836 1.00 69.09 C
ANISOU 2062 C LYS A 260 8267 7743 10242 -79 3183 1443 C
ATOM 2063 O LYS A 260 2.825 -9.502 -39.771 1.00 76.19 O
ANISOU 2063 O LYS A 260 11773 7001 10176 1828 662 -2081 O
ATOM 2064 CB LYS A 260 1.118 -6.598 -39.208 1.00 72.18 C
ANISOU 2064 CB LYS A 260 10675 7657 9092 931 1672 824 C
ATOM 2065 CG LYS A 260 -0.049 -6.103 -40.046 1.00 71.19 C
ANISOU 2065 CG LYS A 260 11075 5847 10128 419 1868 1770 C
ATOM 2066 CD LYS A 260 -0.327 -4.611 -39.961 1.00 73.58 C
ANISOU 2066 CD LYS A 260 11199 6398 10358 130 2285 1444 C
ATOM 2067 CE LYS A 260 -1.227 -4.149 -41.057 1.00 71.16 C
ANISOU 2067 CE LYS A 260 10844 5683 10512 -123 2590 2624 C
ATOM 2068 NZ LYS A 260 -1.411 -2.701 -40.997 1.00 74.13 N
ANISOU 2068 NZ LYS A 260 11653 6251 10261 659 2916 2899 N
ATOM 2069 N ALA A 261 2.979 -8.770 -37.639 1.00 61.69 N
ANISOU 2069 N ALA A 261 6441 7524 9476 -308 5149 3025 N
ATOM 2070 CA ALA A 261 4.246 -9.439 -37.363 1.00 61.26 C
ANISOU 2070 CA ALA A 261 6451 6797 10027 -293 5201 1613 C
ATOM 2071 C ALA A 261 4.089 -10.963 -37.360 1.00 67.09 C
ANISOU 2071 C ALA A 261 7893 6382 11215 295 4506 1356 C
ATOM 2072 O ALA A 261 4.827 -11.673 -38.043 1.00 62.24 O
ANISOU 2072 O ALA A 261 7747 6044 9858 -1590 5544 1250 O
ATOM 2073 CB ALA A 261 4.811 -8.951 -36.049 1.00 66.56 C
ANISOU 2073 CB ALA A 261 7544 7670 10076 -752 4874 1936 C
ATOM 2074 N GLN A 262 3.148 -11.497 -36.577 1.00 67.20 N
ANISOU 2074 N GLN A 262 8207 6240 11087 222 4623 954 N
ATOM 2075 CA GLN A 262 2.972 -12.944 -36.525 1.00 63.61 C
ANISOU 2075 CA GLN A 262 8126 6100 9941 185 3425 565 C
ATOM 2076 C GLN A 262 1.482 -13.269 -36.497 1.00 60.09 C
ANISOU 2076 C GLN A 262 7545 5942 9343 430 3001 -157 C
ATOM 2077 O GLN A 262 0.813 -12.826 -35.572 1.00 53.28 O
ANISOU 2077 O GLN A 262 6971 3977 9296 350 2851 -157 O
ATOM 2078 CB GLN A 262 3.650 -13.533 -35.283 1.00 68.94 C
ANISOU 2078 CB GLN A 262 6756 8521 10918 1143 2875 351 C
ATOM 2079 N PRO A 263 0.894 -14.023 -37.465 1.00 60.34 N
ANISOU 2079 N PRO A 263 7847 7086 7994 578 3413 -324 N
ATOM 2080 CA PRO A 263 -0.509 -14.441 -37.336 1.00 60.28 C
ANISOU 2080 CA PRO A 263 7591 6381 8934 1005 2066 216 C
ATOM 2081 C PRO A 263 -0.689 -15.341 -36.104 1.00 58.90 C
ANISOU 2081 C PRO A 263 7072 6489 8816 343 2886 344 C
ATOM 2082 O PRO A 263 0.186 -16.148 -35.779 1.00 70.21 O
ANISOU 2082 O PRO A 263 10518 5254 10904 -953 1066 2029 O
ATOM 2083 CB PRO A 263 -0.820 -15.135 -38.677 1.00 62.63 C
ANISOU 2083 CB PRO A 263 8045 7404 8349 1071 2751 -276 C
ATOM 2084 CG PRO A 263 0.256 -14.621 -39.622 1.00 62.64 C
ANISOU 2084 CG PRO A 263 7912 7617 8270 959 2890 -396 C
ATOM 2085 CD PRO A 263 1.502 -14.479 -38.732 1.00 65.69 C
ANISOU 2085 CD PRO A 263 8720 7895 8344 233 3082 -548 C
ATOM 2086 N MET A 264 -1.794 -15.168 -35.360 1.00 53.84 N
ANISOU 2086 N MET A 264 6981 5631 7845 679 2170 1125 N
ATOM 2087 CA MET A 264 -1.852 -15.804 -34.059 1.00 50.64 C
ANISOU 2087 CA MET A 264 5358 6031 7854 515 2241 342 C
ATOM 2088 C MET A 264 -3.264 -16.265 -33.742 1.00 46.91 C
ANISOU 2088 C MET A 264 5198 6253 6374 328 2369 588 C
ATOM 2089 O MET A 264 -4.230 -15.732 -34.290 1.00 45.29 O
ANISOU 2089 O MET A 264 5381 6575 5253 641 2539 1038 O
ATOM 2090 CB MET A 264 -1.433 -14.829 -32.959 1.00 49.34 C
ANISOU 2090 CB MET A 264 5429 5773 7545 975 1562 541 C
ATOM 2091 CG MET A 264 0.049 -14.589 -32.894 1.00 51.83 C
ANISOU 2091 CG MET A 264 5765 6216 7712 390 2068 87 C
ATOM 2092 SD MET A 264 0.417 -13.442 -31.557 1.00 51.71 S
ANISOU 2092 SD MET A 264 5535 5717 8393 586 2302 873 S
ATOM 2093 CE MET A 264 0.076 -11.966 -32.526 1.00 55.61 C
ANISOU 2093 CE MET A 264 7086 5022 9020 45 1925 509 C
ATOM 2094 N THR A 265 -3.350 -17.220 -32.814 1.00 40.34 N
ANISOU 2094 N THR A 265 4514 4519 6296 788 2104 1 N
ATOM 2095 CA THR A 265 -4.653 -17.504 -32.196 1.00 39.89 C
ANISOU 2095 CA THR A 265 4713 4495 5950 601 1825 887 C
ATOM 2096 C THR A 265 -5.027 -16.362 -31.246 1.00 41.78 C
ANISOU 2096 C THR A 265 4319 5002 6553 796 1101 580 C
ATOM 2097 O THR A 265 -4.177 -15.540 -30.868 1.00 38.21 O
ANISOU 2097 O THR A 265 4177 5093 5247 1100 761 998 O
ATOM 2098 CB THR A 265 -4.611 -18.823 -31.405 1.00 35.61 C
ANISOU 2098 CB THR A 265 3504 4793 5232 1448 690 1425 C
ATOM 2099 OG1 THR A 265 -3.742 -18.609 -30.293 1.00 40.49 O
ANISOU 2099 OG1 THR A 265 4281 5314 5790 1265 1232 1306 O
ATOM 2100 CG2 THR A 265 -4.267 -20.019 -32.265 1.00 39.68 C
ANISOU 2100 CG2 THR A 265 4174 5629 5273 897 1071 1034 C
ATOM 2101 N ALA A 266 -6.288 -16.373 -30.772 1.00 34.93 N
ANISOU 2101 N ALA A 266 3272 4451 5547 534 965 828 N
ATOM 2102 CA ALA A 266 -6.734 -15.405 -29.782 1.00 33.55 C
ANISOU 2102 CA ALA A 266 3298 4196 5255 757 700 883 C
ATOM 2103 C ALA A 266 -5.900 -15.531 -28.513 1.00 33.57 C
ANISOU 2103 C ALA A 266 3290 3814 5651 704 578 591 C
ATOM 2104 O ALA A 266 -5.529 -14.514 -27.923 1.00 35.46 O
ANISOU 2104 O ALA A 266 3489 4227 5756 498 361 668 O
ATOM 2105 CB ALA A 266 -8.220 -15.577 -29.500 1.00 31.45 C
ANISOU 2105 CB ALA A 266 3440 3707 4801 574 569 846 C
ATOM 2106 N PHE A 267 -5.614 -16.790 -28.114 1.00 33.43 N
ANISOU 2106 N PHE A 267 3317 4119 5265 731 807 1046 N
ATOM 2107 CA PHE A 267 -4.875 -17.025 -26.889 1.00 32.89 C
ANISOU 2107 CA PHE A 267 2920 4350 5228 605 588 531 C
ATOM 2108 C PHE A 267 -3.482 -16.426 -27.033 1.00 33.16 C
ANISOU 2108 C PHE A 267 2659 4149 5792 410 382 566 C
ATOM 2109 O PHE A 267 -2.983 -15.818 -26.100 1.00 38.68 O
ANISOU 2109 O PHE A 267 3411 5470 5814 210 418 -61 O
ATOM 2110 CB PHE A 267 -4.785 -18.501 -26.496 1.00 36.72 C
ANISOU 2110 CB PHE A 267 3990 4441 5523 756 652 676 C
ATOM 2111 CG PHE A 267 -3.895 -18.736 -25.290 1.00 35.89 C
ANISOU 2111 CG PHE A 267 3542 4775 5318 920 634 101 C
ATOM 2112 CD1 PHE A 267 -4.305 -18.369 -24.014 1.00 35.05 C
ANISOU 2112 CD1 PHE A 267 4390 4067 4861 153 267 428 C
ATOM 2113 CD2 PHE A 267 -2.634 -19.321 -25.446 1.00 38.89 C
ANISOU 2113 CD2 PHE A 267 3569 4657 6551 470 618 485 C
ATOM 2114 CE1 PHE A 267 -3.481 -18.589 -22.922 1.00 38.07 C
ANISOU 2114 CE1 PHE A 267 4100 4591 5774 -14 -214 75 C
ATOM 2115 CE2 PHE A 267 -1.823 -19.505 -24.354 1.00 38.24 C
ANISOU 2115 CE2 PHE A 267 4160 4347 6023 171 672 512 C
ATOM 2116 CZ PHE A 267 -2.262 -19.172 -23.094 1.00 38.38 C
ANISOU 2116 CZ PHE A 267 3787 4877 5918 -229 603 -84 C
ATOM 2117 N GLU A 268 -2.884 -16.633 -28.199 1.00 34.13 N
ANISOU 2117 N GLU A 268 2986 4120 5861 513 755 627 N
ATOM 2118 CA GLU A 268 -1.541 -16.119 -28.440 1.00 37.36 C
ANISOU 2118 CA GLU A 268 2982 4547 6663 802 727 918 C
ATOM 2119 C GLU A 268 -1.481 -14.598 -28.365 1.00 38.92 C
ANISOU 2119 C GLU A 268 3350 5021 6418 733 487 501 C
ATOM 2120 O GLU A 268 -0.550 -14.033 -27.811 1.00 43.56 O
ANISOU 2120 O GLU A 268 3664 6095 6793 29 795 682 O
ATOM 2121 CB GLU A 268 -1.074 -16.630 -29.792 1.00 36.91 C
ANISOU 2121 CB GLU A 268 3583 3817 6625 661 1119 777 C
ATOM 2122 CG GLU A 268 -0.648 -18.091 -29.739 1.00 42.32 C
ANISOU 2122 CG GLU A 268 3845 4386 7847 1294 778 731 C
ATOM 2123 CD GLU A 268 -0.178 -18.584 -31.095 1.00 51.09 C
ANISOU 2123 CD GLU A 268 4918 6330 8163 1492 1713 139 C
ATOM 2124 OE1 GLU A 268 -0.856 -18.406 -32.136 1.00 48.24 O
ANISOU 2124 OE1 GLU A 268 4092 5547 8689 596 1752 527 O
ATOM 2125 OE2 GLU A 268 0.899 -19.206 -31.069 1.00 63.02 O
ANISOU 2125 OE2 GLU A 268 5934 7959 10052 2395 -197 121 O
ATOM 2126 N VAL A 269 -2.506 -13.930 -28.900 1.00 40.43 N
ANISOU 2126 N VAL A 269 3538 5623 6200 844 1447 944 N
ATOM 2127 CA VAL A 269 -2.578 -12.477 -28.835 1.00 36.65 C
ANISOU 2127 CA VAL A 269 3585 4818 5523 799 1163 871 C
ATOM 2128 C VAL A 269 -2.714 -12.090 -27.372 1.00 37.00 C
ANISOU 2128 C VAL A 269 3352 4435 6269 545 716 778 C
ATOM 2129 O VAL A 269 -2.090 -11.137 -26.930 1.00 36.87 O
ANISOU 2129 O VAL A 269 3747 4366 5896 1 784 732 O
ATOM 2130 CB VAL A 269 -3.746 -11.933 -29.675 1.00 38.30 C
ANISOU 2130 CB VAL A 269 4177 4754 5620 771 1439 342 C
ATOM 2131 CG1 VAL A 269 -3.861 -10.411 -29.575 1.00 38.30 C
ANISOU 2131 CG1 VAL A 269 4235 4727 5589 553 1196 445 C
ATOM 2132 CG2 VAL A 269 -3.678 -12.361 -31.133 1.00 36.91 C
ANISOU 2132 CG2 VAL A 269 4407 4457 5161 512 1230 691 C
ATOM 2133 N CYS A 270 -3.580 -12.821 -26.651 1.00 34.80 N
ANISOU 2133 N CYS A 270 3141 4769 5310 43 673 996 N
ATOM 2134 CA CYS A 270 -3.859 -12.570 -25.241 1.00 36.97 C
ANISOU 2134 CA CYS A 270 3758 4647 5641 -38 346 707 C
ATOM 2135 C CYS A 270 -2.551 -12.571 -24.438 1.00 33.79 C
ANISOU 2135 C CYS A 270 3564 3511 5765 92 147 328 C
ATOM 2136 O CYS A 270 -2.295 -11.681 -23.630 1.00 39.73 O
ANISOU 2136 O CYS A 270 4224 4920 5950 -598 444 740 O
ATOM 2137 CB CYS A 270 -4.905 -13.567 -24.734 1.00 31.85 C
ANISOU 2137 CB CYS A 270 2937 4224 4939 163 -417 182 C
ATOM 2138 SG CYS A 270 -5.340 -13.264 -23.010 1.00 39.84 S
ANISOU 2138 SG CYS A 270 3915 5488 5733 -11 24 710 S
ATOM 2139 N VAL A 271 -1.688 -13.566 -24.687 1.00 37.94 N
ANISOU 2139 N VAL A 271 3105 4657 6653 -162 531 17 N
ATOM 2140 CA VAL A 271 -0.419 -13.677 -23.977 1.00 39.18 C
ANISOU 2140 CA VAL A 271 3163 4958 6765 537 219 442 C
ATOM 2141 C VAL A 271 0.500 -12.502 -24.308 1.00 39.69 C
ANISOU 2141 C VAL A 271 4034 4319 6727 -190 -386 234 C
ATOM 2142 O VAL A 271 1.272 -12.045 -23.451 1.00 42.83 O
ANISOU 2142 O VAL A 271 4272 5302 6700 561 -965 722 O
ATOM 2143 CB VAL A 271 0.305 -15.005 -24.285 1.00 41.83 C
ANISOU 2143 CB VAL A 271 3508 5421 6963 91 90 265 C
ATOM 2144 CG1 VAL A 271 1.669 -15.016 -23.625 1.00 47.08 C
ANISOU 2144 CG1 VAL A 271 3756 6554 7577 16 99 434 C
ATOM 2145 CG2 VAL A 271 -0.509 -16.207 -23.834 1.00 44.56 C
ANISOU 2145 CG2 VAL A 271 3726 6167 7039 -95 -474 588 C
ATOM 2146 N LYS A 272 0.454 -12.030 -25.566 1.00 39.55 N
ANISOU 2146 N LYS A 272 3757 4404 6867 -308 247 600 N
ATOM 2147 CA LYS A 272 1.232 -10.852 -25.946 1.00 42.59 C
ANISOU 2147 CA LYS A 272 4245 4642 7294 -797 718 531 C
ATOM 2148 C LYS A 272 0.686 -9.590 -25.286 1.00 40.93 C
ANISOU 2148 C LYS A 272 3386 4751 7415 -684 -23 529 C
ATOM 2149 O LYS A 272 1.507 -8.770 -24.835 1.00 42.41 O
ANISOU 2149 O LYS A 272 3791 4319 8003 -759 178 -143 O
ATOM 2150 CB LYS A 272 1.239 -10.550 -27.446 1.00 47.83 C
ANISOU 2150 CB LYS A 272 5564 5025 7584 -349 760 1296 C
ATOM 2151 CG LYS A 272 1.741 -11.687 -28.314 1.00 55.49 C
ANISOU 2151 CG LYS A 272 6610 5619 8853 -176 910 874 C
ATOM 2152 CD LYS A 272 3.256 -11.830 -28.374 1.00 59.11 C
ANISOU 2152 CD LYS A 272 6989 5556 9914 157 782 1060 C
ATOM 2153 CE LYS A 272 3.730 -12.367 -29.701 1.00 64.80 C
ANISOU 2153 CE LYS A 272 8698 6735 9188 -391 778 1271 C
ATOM 2154 N LEU A 273 -0.662 -9.437 -25.262 1.00 44.35 N
ANISOU 2154 N LEU A 273 3774 5532 7545 -433 -230 1040 N
ATOM 2155 CA LEU A 273 -1.279 -8.227 -24.728 1.00 43.35 C
ANISOU 2155 CA LEU A 273 3439 5889 7142 -451 -170 939 C
ATOM 2156 C LEU A 273 -1.162 -8.187 -23.210 1.00 47.36 C
ANISOU 2156 C LEU A 273 4293 5449 8253 -518 -451 979 C
ATOM 2157 O LEU A 273 -0.981 -7.108 -22.637 1.00 52.38 O
ANISOU 2157 O LEU A 273 5344 4909 9647 -593 -163 500 O
ATOM 2158 CB LEU A 273 -2.757 -8.114 -25.078 1.00 41.83 C
ANISOU 2158 CB LEU A 273 3489 5185 7221 -1089 -163 1181 C
ATOM 2159 CG LEU A 273 -3.107 -7.684 -26.488 1.00 44.65 C
ANISOU 2159 CG LEU A 273 4627 5842 6495 -839 94 1282 C
ATOM 2160 CD1 LEU A 273 -4.607 -7.788 -26.589 1.00 39.80 C
ANISOU 2160 CD1 LEU A 273 4289 4768 6066 -202 79 1406 C
ATOM 2161 CD2 LEU A 273 -2.641 -6.270 -26.757 1.00 45.10 C
ANISOU 2161 CD2 LEU A 273 4899 5448 6790 -478 183 1558 C
ATOM 2162 N PHE A 274 -1.339 -9.361 -22.578 1.00 39.31 N
ANISOU 2162 N PHE A 274 2929 4863 7143 -480 -271 1189 N
ATOM 2163 CA PHE A 274 -1.383 -9.445 -21.129 1.00 44.46 C
ANISOU 2163 CA PHE A 274 4174 5209 7509 -174 -194 1115 C
ATOM 2164 C PHE A 274 -0.332 -10.439 -20.639 1.00 48.81 C
ANISOU 2164 C PHE A 274 4206 6149 8192 494 -61 629 C
ATOM 2165 O PHE A 274 -0.662 -11.535 -20.169 1.00 47.47 O
ANISOU 2165 O PHE A 274 3829 6022 8186 49 45 194 O
ATOM 2166 CB PHE A 274 -2.822 -9.823 -20.762 1.00 44.08 C
ANISOU 2166 CB PHE A 274 4078 6121 6549 -68 26 1185 C
ATOM 2167 CG PHE A 274 -3.867 -8.876 -21.335 1.00 43.83 C
ANISOU 2167 CG PHE A 274 3730 5652 7271 163 -730 248 C
ATOM 2168 CD1 PHE A 274 -3.973 -7.571 -20.877 1.00 44.96 C
ANISOU 2168 CD1 PHE A 274 4009 6296 6775 138 -1341 42 C
ATOM 2169 CD2 PHE A 274 -4.723 -9.274 -22.355 1.00 39.69 C
ANISOU 2169 CD2 PHE A 274 3366 5183 6530 -181 316 1105 C
ATOM 2170 CE1 PHE A 274 -4.892 -6.704 -21.425 1.00 47.03 C
ANISOU 2170 CE1 PHE A 274 3230 6566 8074 1330 -546 -174 C
ATOM 2171 CE2 PHE A 274 -5.677 -8.421 -22.859 1.00 42.20 C
ANISOU 2171 CE2 PHE A 274 3343 5463 7229 48 348 557 C
ATOM 2172 CZ PHE A 274 -5.750 -7.138 -22.414 1.00 44.31 C
ANISOU 2172 CZ PHE A 274 3220 5902 7714 -150 -188 -156 C
ATOM 2173 N PRO A 275 0.971 -10.093 -20.701 1.00 45.85 N
ANISOU 2173 N PRO A 275 4340 4779 8300 561 -646 0 N
ATOM 2174 CA PRO A 275 2.017 -11.078 -20.404 1.00 49.44 C
ANISOU 2174 CA PRO A 275 4295 6021 8468 1299 -451 719 C
ATOM 2175 C PRO A 275 2.046 -11.552 -18.953 1.00 50.82 C
ANISOU 2175 C PRO A 275 4375 7427 7507 1058 -825 330 C
ATOM 2176 O PRO A 275 2.621 -12.607 -18.662 1.00 48.92 O
ANISOU 2176 O PRO A 275 4380 7492 6716 -8 -498 -530 O
ATOM 2177 CB PRO A 275 3.297 -10.344 -20.811 1.00 52.37 C
ANISOU 2177 CB PRO A 275 5575 5467 8855 705 -756 810 C
ATOM 2178 CG PRO A 275 2.954 -8.885 -20.623 1.00 51.99 C
ANISOU 2178 CG PRO A 275 5622 5363 8769 553 -558 720 C
ATOM 2179 CD PRO A 275 1.509 -8.776 -21.046 1.00 46.46 C
ANISOU 2179 CD PRO A 275 4627 5322 7704 603 423 1119 C
ATOM 2180 N THR A 276 1.423 -10.772 -18.059 1.00 52.02 N
ANISOU 2180 N THR A 276 4479 7601 7684 1371 296 1070 N
ATOM 2181 CA THR A 276 1.422 -11.039 -16.630 1.00 60.84 C
ANISOU 2181 CA THR A 276 5802 9072 8241 1137 -78 775 C
ATOM 2182 C THR A 276 0.050 -11.552 -16.185 1.00 65.60 C
ANISOU 2182 C THR A 276 7433 9106 8385 227 -304 1956 C
ATOM 2183 O THR A 276 -0.033 -12.479 -15.394 1.00 72.87 O
ANISOU 2183 O THR A 276 8921 9868 8896 1840 -324 2997 O
ATOM 2184 CB THR A 276 1.830 -9.752 -15.908 1.00 68.55 C
ANISOU 2184 CB THR A 276 6582 9963 9501 740 185 606 C
ATOM 2185 OG1 THR A 276 0.939 -8.720 -16.320 1.00 72.36 O
ANISOU 2185 OG1 THR A 276 7494 9824 10176 1173 1022 1682 O
ATOM 2186 CG2 THR A 276 3.246 -9.320 -16.252 1.00 71.37 C
ANISOU 2186 CG2 THR A 276 7672 9867 9580 217 485 -229 C
ATOM 2187 N LEU A 277 -1.030 -10.967 -16.711 1.00 63.96 N
ANISOU 2187 N LEU A 277 6217 9884 8202 -719 -879 1617 N
ATOM 2188 CA LEU A 277 -2.367 -11.212 -16.193 1.00 67.11 C
ANISOU 2188 CA LEU A 277 7239 9983 8277 -1133 -892 834 C
ATOM 2189 C LEU A 277 -3.004 -12.479 -16.770 1.00 62.13 C
ANISOU 2189 C LEU A 277 5691 9978 7938 -396 -2240 836 C
ATOM 2190 O LEU A 277 -3.966 -12.972 -16.193 1.00 71.96 O
ANISOU 2190 O LEU A 277 6679 12214 8446 -1488 -1925 1194 O
ATOM 2191 CB LEU A 277 -3.212 -9.979 -16.493 1.00 67.58 C
ANISOU 2191 CB LEU A 277 8251 9245 8182 -1345 -811 937 C
ATOM 2192 CG LEU A 277 -2.737 -8.666 -15.861 1.00 72.51 C
ANISOU 2192 CG LEU A 277 9769 9529 8252 -1364 -791 1051 C
ATOM 2193 CD1 LEU A 277 -3.473 -7.504 -16.501 1.00 70.87 C
ANISOU 2193 CD1 LEU A 277 9198 8808 8922 -1470 -776 1010 C
ATOM 2194 CD2 LEU A 277 -2.937 -8.672 -14.348 1.00 71.92 C
ANISOU 2194 CD2 LEU A 277 10259 8998 8067 -976 -239 1310 C
ATOM 2195 N TYR A 278 -2.477 -13.025 -17.877 1.00 57.13 N
ANISOU 2195 N TYR A 278 5939 7794 7974 488 -2527 1059 N
ATOM 2196 CA TYR A 278 -3.170 -14.103 -18.578 1.00 55.05 C
ANISOU 2196 CA TYR A 278 6014 6785 8118 293 -1675 1376 C
ATOM 2197 C TYR A 278 -3.307 -15.364 -17.718 1.00 56.38 C
ANISOU 2197 C TYR A 278 5870 6524 9030 -736 -1411 1675 C
ATOM 2198 O TYR A 278 -4.244 -16.127 -17.923 1.00 57.11 O
ANISOU 2198 O TYR A 278 5531 6356 9814 -1545 -633 2262 O
ATOM 2199 CB TYR A 278 -2.514 -14.498 -19.906 1.00 52.94 C
ANISOU 2199 CB TYR A 278 5096 7260 7758 864 -1180 803 C
ATOM 2200 CG TYR A 278 -1.258 -15.352 -19.847 1.00 54.97 C
ANISOU 2200 CG TYR A 278 5753 6457 8674 1708 -595 -584 C
ATOM 2201 CD1 TYR A 278 -1.326 -16.744 -19.818 1.00 58.33 C
ANISOU 2201 CD1 TYR A 278 5026 6967 10169 1410 95 -42 C
ATOM 2202 CD2 TYR A 278 -0.004 -14.761 -19.880 1.00 62.75 C
ANISOU 2202 CD2 TYR A 278 5936 8065 9840 1383 -326 -79 C
ATOM 2203 CE1 TYR A 278 -0.177 -17.519 -19.801 1.00 59.71 C
ANISOU 2203 CE1 TYR A 278 6415 5490 10782 2348 238 -1152 C
ATOM 2204 CE2 TYR A 278 1.154 -15.526 -19.860 1.00 63.32 C
ANISOU 2204 CE2 TYR A 278 6275 7212 10572 2244 -250 239 C
ATOM 2205 CZ TYR A 278 1.065 -16.905 -19.820 1.00 64.73 C
ANISOU 2205 CZ TYR A 278 6622 7033 10939 1503 -236 -975 C
ATOM 2206 OH TYR A 278 2.215 -17.628 -19.805 1.00 66.73 O
ANISOU 2206 OH TYR A 278 7433 6780 11141 2617 45 -10 O
ATOM 2207 N GLU A 279 -2.373 -15.616 -16.796 1.00 57.59 N
ANISOU 2207 N GLU A 279 7209 5966 8707 -921 -1278 2010 N
ATOM 2208 CA GLU A 279 -2.461 -16.785 -15.931 1.00 59.35 C
ANISOU 2208 CA GLU A 279 6951 6647 8950 236 -2518 3086 C
ATOM 2209 C GLU A 279 -3.450 -16.554 -14.785 1.00 64.51 C
ANISOU 2209 C GLU A 279 9200 7371 7939 -818 -1729 3165 C
ATOM 2210 O GLU A 279 -4.236 -17.447 -14.463 1.00 69.03 O
ANISOU 2210 O GLU A 279 10456 8346 7427 -1683 -1953 2373 O
ATOM 2211 N LYS A 280 -3.417 -15.348 -14.191 1.00 72.47 N
ANISOU 2211 N LYS A 280 10929 9609 6996 -1272 -1464 2285 N
ATOM 2212 CA LYS A 280 -4.233 -14.993 -13.034 1.00 73.48 C
ANISOU 2212 CA LYS A 280 10885 10162 6871 -1824 -1290 1664 C
ATOM 2213 C LYS A 280 -5.692 -14.701 -13.410 1.00 71.64 C
ANISOU 2213 C LYS A 280 9784 10594 6840 -2724 182 901 C
ATOM 2214 O LYS A 280 -6.598 -15.102 -12.667 1.00 65.07 O
ANISOU 2214 O LYS A 280 9292 9832 5600 -2935 632 -381 O
ATOM 2215 CB LYS A 280 -3.610 -13.794 -12.304 1.00 74.51 C
ANISOU 2215 CB LYS A 280 11221 10230 6858 -1906 -2139 1985 C
ATOM 2216 N GLN A 281 -5.904 -13.980 -14.531 1.00 73.44 N
ANISOU 2216 N GLN A 281 10011 10844 7048 -2483 462 946 N
ATOM 2217 CA GLN A 281 -7.224 -13.584 -15.022 1.00 68.37 C
ANISOU 2217 CA GLN A 281 9518 10580 5878 -2727 570 416 C
ATOM 2218 C GLN A 281 -7.357 -13.923 -16.516 1.00 69.84 C
ANISOU 2218 C GLN A 281 8737 11725 6076 -2383 1134 -766 C
ATOM 2219 O GLN A 281 -6.418 -14.400 -17.143 1.00 81.92 O
ANISOU 2219 O GLN A 281 10831 13484 6809 -1226 2104 241 O
ATOM 2220 CB GLN A 281 -7.470 -12.093 -14.758 1.00 66.65 C
ANISOU 2220 CB GLN A 281 9615 10433 5274 -2650 322 -148 C
ATOM 2221 CG GLN A 281 -7.646 -11.726 -13.286 1.00 70.10 C
ANISOU 2221 CG GLN A 281 11139 9314 6183 -1999 -206 -161 C
ATOM 2222 CD GLN A 281 -7.284 -10.290 -12.974 1.00 66.17 C
ANISOU 2222 CD GLN A 281 10567 8837 5736 -1416 -1033 -297 C
ATOM 2223 OE1 GLN A 281 -6.215 -10.015 -12.421 1.00 65.77 O
ANISOU 2223 OE1 GLN A 281 9647 6088 9253 28 -1445 -476 O
ATOM 2224 NE2 GLN A 281 -8.157 -9.355 -13.324 1.00 65.75 N
ANISOU 2224 NE2 GLN A 281 11022 9010 4950 -1014 -499 1160 N
ATOM 2225 N LEU A 282 -8.542 -13.686 -17.086 1.00 73.29 N
ANISOU 2225 N LEU A 282 10422 11794 5629 -1809 420 -466 N
ATOM 2226 CA LEU A 282 -8.837 -14.084 -18.459 1.00 69.93 C
ANISOU 2226 CA LEU A 282 10291 9819 6461 -1326 -115 1115 C
ATOM 2227 C LEU A 282 -9.907 -13.153 -19.021 1.00 64.97 C
ANISOU 2227 C LEU A 282 8129 9787 6768 -716 -168 1825 C
ATOM 2228 O LEU A 282 -11.110 -13.391 -18.861 1.00 68.25 O
ANISOU 2228 O LEU A 282 6135 11591 8207 430 4244 1866 O
ATOM 2229 CB LEU A 282 -9.229 -15.552 -18.600 1.00 68.47 C
ANISOU 2229 CB LEU A 282 10806 8656 6552 -1186 -1752 -1095 C
ATOM 2230 CG LEU A 282 -10.075 -16.145 -17.466 1.00 71.33 C
ANISOU 2230 CG LEU A 282 10018 9225 7859 -1291 -1629 -1926 C
ATOM 2231 CD1 LEU A 282 -11.575 -15.985 -17.687 1.00 69.36 C
ANISOU 2231 CD1 LEU A 282 9635 9115 7603 -561 -2309 -2971 C
ATOM 2232 CD2 LEU A 282 -9.708 -17.613 -17.255 1.00 68.97 C
ANISOU 2232 CD2 LEU A 282 10226 8820 7158 -1530 -1736 -933 C
ATOM 2233 N PRO A 283 -9.457 -12.051 -19.677 1.00 47.53 N
ANISOU 2233 N PRO A 283 6841 7211 4007 965 1287 1459 N
ATOM 2234 CA PRO A 283 -10.282 -11.223 -20.572 1.00 47.00 C
ANISOU 2234 CA PRO A 283 4549 7444 5865 868 1312 1346 C
ATOM 2235 C PRO A 283 -9.818 -10.878 -22.012 1.00 54.27 C
ANISOU 2235 C PRO A 283 5297 8964 6358 2825 2701 -511 C
ATOM 2236 O PRO A 283 -8.597 -11.171 -22.507 1.00 51.38 O
ANISOU 2236 O PRO A 283 4116 8679 6726 264 -40 -2714 O
ATOM 2237 CB PRO A 283 -10.051 -10.036 -19.690 1.00 47.95 C
ANISOU 2237 CB PRO A 283 4464 7635 6119 2234 3491 553 C
ATOM 2238 CG PRO A 283 -8.514 -10.056 -19.489 1.00 57.86 C
ANISOU 2238 CG PRO A 283 5889 8169 7926 1827 748 491 C
ATOM 2239 CD PRO A 283 -8.100 -11.509 -19.640 1.00 55.70 C
ANISOU 2239 CD PRO A 283 7493 6833 6836 1105 -374 -256 C
ATOM 2240 N LEU A 284 -10.875 -10.185 -22.570 1.00 54.67 N
ANISOU 2240 N LEU A 284 5819 7871 7084 755 1816 -60 N
ATOM 2241 CA LEU A 284 -10.836 -9.219 -23.629 1.00 47.62 C
ANISOU 2241 CA LEU A 284 4777 8114 5202 2701 23 -968 C
ATOM 2242 C LEU A 284 -10.106 -10.016 -24.710 1.00 57.08 C
ANISOU 2242 C LEU A 284 5591 10176 5920 588 1015 -1028 C
ATOM 2243 O LEU A 284 -10.265 -11.259 -24.828 1.00 71.45 O
ANISOU 2243 O LEU A 284 4620 14328 8198 3043 1849 -1698 O
ATOM 2244 CB LEU A 284 -10.114 -7.934 -23.144 1.00 47.46 C
ANISOU 2244 CB LEU A 284 5083 7694 5255 3796 1159 -238 C
ATOM 2245 CG LEU A 284 -10.772 -6.558 -23.402 1.00 60.71 C
ANISOU 2245 CG LEU A 284 7549 9044 6475 2138 625 630 C
ATOM 2246 CD1 LEU A 284 -9.861 -5.556 -24.137 1.00 60.72 C
ANISOU 2246 CD1 LEU A 284 7398 9011 6660 1163 618 -52 C
ATOM 2247 CD2 LEU A 284 -12.093 -6.639 -24.138 1.00 70.22 C
ANISOU 2247 CD2 LEU A 284 7449 10559 8673 2550 515 1009 C
ATOM 2248 N THR A 285 -9.265 -9.311 -25.425 1.00 43.67 N
ANISOU 2248 N THR A 285 4802 5982 5808 -1787 -169 -346 N
ATOM 2249 CA THR A 285 -8.545 -9.829 -26.575 1.00 34.60 C
ANISOU 2249 CA THR A 285 3351 4269 5524 537 327 723 C
ATOM 2250 C THR A 285 -9.516 -10.184 -27.707 1.00 33.09 C
ANISOU 2250 C THR A 285 3237 4013 5321 331 795 431 C
ATOM 2251 O THR A 285 -9.433 -9.616 -28.783 1.00 34.94 O
ANISOU 2251 O THR A 285 3695 4082 5500 701 963 568 O
ATOM 2252 CB THR A 285 -7.622 -11.004 -26.261 1.00 34.36 C
ANISOU 2252 CB THR A 285 3228 4411 5417 468 650 401 C
ATOM 2253 OG1 THR A 285 -6.709 -10.649 -25.212 1.00 33.92 O
ANISOU 2253 OG1 THR A 285 2821 4229 5836 96 548 936 O
ATOM 2254 CG2 THR A 285 -6.892 -11.438 -27.517 1.00 37.60 C
ANISOU 2254 CG2 THR A 285 3539 5172 5574 311 761 501 C
ATOM 2255 N ILE A 286 -10.454 -11.110 -27.446 1.00 34.42 N
ANISOU 2255 N ILE A 286 3421 4230 5428 414 798 440 N
ATOM 2256 CA ILE A 286 -11.445 -11.515 -28.421 1.00 33.74 C
ANISOU 2256 CA ILE A 286 3953 4050 4816 734 878 304 C
ATOM 2257 C ILE A 286 -12.320 -10.314 -28.768 1.00 34.51 C
ANISOU 2257 C ILE A 286 3608 4573 4932 747 630 -211 C
ATOM 2258 O ILE A 286 -12.632 -10.116 -29.945 1.00 36.94 O
ANISOU 2258 O ILE A 286 3789 5091 5154 924 403 745 O
ATOM 2259 CB ILE A 286 -12.248 -12.719 -27.909 1.00 38.20 C
ANISOU 2259 CB ILE A 286 4285 4478 5753 552 725 -31 C
ATOM 2260 CG1 ILE A 286 -11.351 -13.931 -27.794 1.00 39.63 C
ANISOU 2260 CG1 ILE A 286 4549 4785 5725 603 1540 -270 C
ATOM 2261 CG2 ILE A 286 -13.449 -12.984 -28.812 1.00 38.01 C
ANISOU 2261 CG2 ILE A 286 4147 4892 5402 1098 650 374 C
ATOM 2262 N SER A 287 -12.682 -9.488 -27.761 1.00 32.19 N
ANISOU 2262 N SER A 287 3545 4118 4568 915 632 592 N
ATOM 2263 CA SER A 287 -13.437 -8.284 -28.070 1.00 34.49 C
ANISOU 2263 CA SER A 287 4218 4300 4584 1186 802 655 C
ATOM 2264 C SER A 287 -12.727 -7.414 -29.104 1.00 34.75 C
ANISOU 2264 C SER A 287 3580 5080 4542 435 633 331 C
ATOM 2265 O SER A 287 -13.391 -6.868 -29.988 1.00 35.52 O
ANISOU 2265 O SER A 287 4278 4944 4274 1078 74 223 O
ATOM 2266 N GLU A 288 -11.397 -7.240 -28.936 1.00 35.49 N
ANISOU 2266 N GLU A 288 3637 4943 4903 448 354 311 N
ATOM 2267 CA GLU A 288 -10.618 -6.410 -29.851 1.00 34.27 C
ANISOU 2267 CA GLU A 288 3707 4393 4922 725 330 641 C
ATOM 2268 C GLU A 288 -10.523 -7.065 -31.231 1.00 36.20 C
ANISOU 2268 C GLU A 288 4058 4853 4843 859 550 477 C
ATOM 2269 O GLU A 288 -10.790 -6.416 -32.238 1.00 37.41 O
ANISOU 2269 O GLU A 288 4669 5414 4131 796 488 704 O
ATOM 2270 CB GLU A 288 -9.195 -6.172 -29.356 1.00 35.47 C
ANISOU 2270 CB GLU A 288 3921 4632 4924 273 188 337 C
ATOM 2271 CG GLU A 288 -9.169 -5.347 -28.078 1.00 39.99 C
ANISOU 2271 CG GLU A 288 4529 5240 5426 456 830 400 C
ATOM 2272 CD GLU A 288 -9.595 -3.913 -28.207 1.00 46.09 C
ANISOU 2272 CD GLU A 288 6003 5487 6021 983 816 195 C
ATOM 2273 OE1 GLU A 288 -9.470 -3.298 -29.279 1.00 49.92 O
ANISOU 2273 OE1 GLU A 288 6587 4873 7509 703 1185 1484 O
ATOM 2274 OE2 GLU A 288 -10.101 -3.442 -27.170 1.00 55.83 O
ANISOU 2274 OE2 GLU A 288 7190 7334 6688 1615 110 -67 O
ATOM 2275 N ASN A 289 -10.255 -8.381 -31.248 1.00 33.41 N
ANISOU 2275 N ASN A 289 3486 4398 4811 722 585 489 N
ATOM 2276 CA ASN A 289 -10.164 -9.104 -32.503 1.00 32.68 C
ANISOU 2276 CA ASN A 289 4238 3739 4440 635 623 717 C
ATOM 2277 C ASN A 289 -11.487 -9.051 -33.259 1.00 34.53 C
ANISOU 2277 C ASN A 289 4160 4622 4339 611 948 207 C
ATOM 2278 O ASN A 289 -11.485 -8.802 -34.456 1.00 38.99 O
ANISOU 2278 O ASN A 289 5693 4788 4332 364 500 104 O
ATOM 2279 CB ASN A 289 -9.739 -10.554 -32.332 1.00 34.83 C
ANISOU 2279 CB ASN A 289 4335 3824 5076 394 826 347 C
ATOM 2280 CG ASN A 289 -8.286 -10.713 -31.993 1.00 36.11 C
ANISOU 2280 CG ASN A 289 4041 4940 4737 7 821 1250 C
ATOM 2281 OD1 ASN A 289 -7.396 -10.246 -32.758 1.00 43.89 O
ANISOU 2281 OD1 ASN A 289 4998 5745 5932 -557 1032 919 O
ATOM 2282 ND2 ASN A 289 -8.048 -11.662 -31.098 1.00 42.93 N
ANISOU 2282 ND2 ASN A 289 4553 6739 5019 -89 1126 1006 N
ATOM 2283 N VAL A 290 -12.604 -9.223 -32.533 1.00 39.73 N
ANISOU 2283 N VAL A 290 4765 5904 4425 551 928 157 N
ATOM 2284 CA VAL A 290 -13.923 -9.243 -33.137 1.00 37.02 C
ANISOU 2284 CA VAL A 290 5007 4936 4124 367 744 -612 C
ATOM 2285 C VAL A 290 -14.296 -7.863 -33.699 1.00 41.69 C
ANISOU 2285 C VAL A 290 5964 5470 4405 599 393 -641 C
ATOM 2286 O VAL A 290 -14.952 -7.755 -34.745 1.00 42.55 O
ANISOU 2286 O VAL A 290 6294 5756 4117 439 510 -423 O
ATOM 2287 CB VAL A 290 -14.968 -9.837 -32.175 1.00 35.24 C
ANISOU 2287 CB VAL A 290 4393 4233 4761 460 223 -323 C
ATOM 2288 CG1 VAL A 290 -16.360 -9.572 -32.693 1.00 47.63 C
ANISOU 2288 CG1 VAL A 290 5761 5909 6427 -410 -216 498 C
ATOM 2289 CG2 VAL A 290 -14.834 -11.365 -31.982 1.00 45.19 C
ANISOU 2289 CG2 VAL A 290 5694 4545 6931 -763 -1904 101 C
ATOM 2290 N GLY A 291 -13.882 -6.810 -32.990 1.00 35.18 N
ANISOU 2290 N GLY A 291 4894 4259 4212 468 -209 295 N
ATOM 2291 CA GLY A 291 -14.034 -5.415 -33.382 1.00 38.58 C
ANISOU 2291 CA GLY A 291 4650 4932 5077 943 -132 1103 C
ATOM 2292 C GLY A 291 -13.307 -5.141 -34.700 1.00 41.77 C
ANISOU 2292 C GLY A 291 6086 5124 4660 1075 278 569 C
ATOM 2293 O GLY A 291 -13.870 -4.546 -35.618 1.00 47.08 O
ANISOU 2293 O GLY A 291 7758 5395 4734 1719 376 311 O
ATOM 2294 N GLN A 292 -12.074 -5.652 -34.810 1.00 44.96 N
ANISOU 2294 N GLN A 292 6371 5183 5530 1307 796 216 N
ATOM 2295 CA GLN A 292 -11.239 -5.507 -35.996 1.00 48.72 C
ANISOU 2295 CA GLN A 292 7250 4705 6559 506 1044 -241 C
ATOM 2296 C GLN A 292 -11.751 -6.365 -37.160 1.00 54.31 C
ANISOU 2296 C GLN A 292 6975 5593 8068 764 1215 -2355 C
ATOM 2297 O GLN A 292 -11.719 -5.905 -38.289 1.00 53.94 O
ANISOU 2297 O GLN A 292 8941 5238 6317 731 -1932 1249 O
ATOM 2298 CB GLN A 292 -9.788 -5.777 -35.591 1.00 46.62 C
ANISOU 2298 CB GLN A 292 7157 4260 6298 870 2908 241 C
ATOM 2299 CG GLN A 292 -9.340 -4.728 -34.587 1.00 53.47 C
ANISOU 2299 CG GLN A 292 7898 5874 6546 1110 2421 698 C
ATOM 2300 CD GLN A 292 -7.862 -4.665 -34.373 1.00 57.00 C
ANISOU 2300 CD GLN A 292 7856 6792 7008 964 4041 1361 C
ATOM 2301 OE1 GLN A 292 -7.207 -5.678 -34.110 1.00 65.73 O
ANISOU 2301 OE1 GLN A 292 9416 6364 9194 1865 3006 1150 O
ATOM 2302 NE2 GLN A 292 -7.332 -3.468 -34.575 1.00 69.43 N
ANISOU 2302 NE2 GLN A 292 10299 6778 9304 935 3431 1318 N
ATOM 2303 N LEU A 293 -12.269 -7.573 -36.880 1.00 56.00 N
ANISOU 2303 N LEU A 293 8315 5702 7261 944 -39 -1594 N
ATOM 2304 CA LEU A 293 -12.847 -8.438 -37.900 1.00 54.18 C
ANISOU 2304 CA LEU A 293 9782 5958 4846 799 896 -461 C
ATOM 2305 C LEU A 293 -14.112 -7.800 -38.483 1.00 61.63 C
ANISOU 2305 C LEU A 293 10420 7181 5815 461 836 -267 C
ATOM 2306 O LEU A 293 -14.248 -7.786 -39.700 1.00 67.74 O
ANISOU 2306 O LEU A 293 12664 8210 4865 299 669 31 O
ATOM 2307 CB LEU A 293 -13.128 -9.845 -37.386 1.00 56.40 C
ANISOU 2307 CB LEU A 293 10280 6451 4697 94 1405 -305 C
ATOM 2308 N ASP A 294 -15.038 -7.300 -37.642 1.00 54.56 N
ANISOU 2308 N ASP A 294 11067 5601 4063 931 998 -55 N
ATOM 2309 CA ASP A 294 -16.014 -6.300 -38.061 1.00 59.81 C
ANISOU 2309 CA ASP A 294 10433 7153 5139 864 826 0 C
ATOM 2310 C ASP A 294 -15.121 -5.202 -38.639 1.00 64.30 C
ANISOU 2310 C ASP A 294 9930 7802 6698 1225 913 771 C
ATOM 2311 O ASP A 294 -13.907 -5.353 -38.603 1.00 88.30 O
ANISOU 2311 O ASP A 294 11364 10775 11412 233 123 548 O
ATOM 2312 CB ASP A 294 -16.932 -5.923 -36.892 1.00 57.98 C
ANISOU 2312 CB ASP A 294 9256 5707 7065 -517 1367 684 C
ATOM 2313 CG ASP A 294 -18.249 -5.163 -37.125 1.00 64.41 C
ANISOU 2313 CG ASP A 294 10161 5811 8501 -1234 43 678 C
ATOM 2314 OD1 ASP A 294 -18.187 -3.930 -37.386 1.00 68.32 O
ANISOU 2314 OD1 ASP A 294 12181 5796 7980 -1216 -562 -51 O
ATOM 2315 OD2 ASP A 294 -19.373 -5.765 -36.881 1.00 65.31 O
ANISOU 2315 OD2 ASP A 294 10778 6904 7132 -919 -514 1224 O
ATOM 2316 N PHE A 295 -15.637 -4.134 -39.231 1.00 69.59 N
ANISOU 2316 N PHE A 295 11294 8657 6492 2083 1542 1004 N
ATOM 2317 CA PHE A 295 -14.730 -3.058 -39.614 1.00 75.72 C
ANISOU 2317 CA PHE A 295 11709 8688 8372 1459 377 1047 C
ATOM 2318 C PHE A 295 -13.658 -3.526 -40.616 1.00 79.84 C
ANISOU 2318 C PHE A 295 11611 9347 9377 1245 -531 207 C
ATOM 2319 O PHE A 295 -12.806 -2.729 -41.001 1.00 76.92 O
ANISOU 2319 O PHE A 295 12778 10150 6297 1349 843 239 O
ATOM 2320 CB PHE A 295 -14.123 -2.459 -38.333 1.00 69.76 C
ANISOU 2320 CB PHE A 295 11724 7764 7020 1984 158 1585 C
ATOM 2321 CG PHE A 295 -14.774 -1.183 -37.803 1.00 79.71 C
ANISOU 2321 CG PHE A 295 12362 9111 8815 2002 1525 -717 C
ATOM 2322 CD1 PHE A 295 -16.021 -0.749 -38.259 1.00 82.66 C
ANISOU 2322 CD1 PHE A 295 12213 9998 9197 1781 1659 -1099 C
ATOM 2323 CD2 PHE A 295 -14.115 -0.396 -36.858 1.00 86.54 C
ANISOU 2323 CD2 PHE A 295 12243 11644 8993 2358 1999 -1212 C
ATOM 2324 CE1 PHE A 295 -16.585 0.435 -37.789 1.00 90.62 C
ANISOU 2324 CE1 PHE A 295 13206 10660 10567 2342 1500 -841 C
ATOM 2325 CE2 PHE A 295 -14.682 0.789 -36.390 1.00 90.17 C
ANISOU 2325 CE2 PHE A 295 12983 11792 9486 1929 1956 -1170 C
ATOM 2326 CZ PHE A 295 -15.920 1.197 -36.846 1.00 91.61 C
ANISOU 2326 CZ PHE A 295 13672 10227 10910 3042 1542 -1097 C
ATOM 2327 N LEU A 296 -13.663 -4.811 -41.005 1.00 78.06 N
ANISOU 2327 N LEU A 296 11125 8206 10327 1085 -3616 -261 N
ATOM 2328 CA LEU A 296 -12.907 -5.346 -42.139 1.00 74.94 C
ANISOU 2328 CA LEU A 296 10694 8498 9283 -801 -4808 1244 C
ATOM 2329 C LEU A 296 -11.402 -4.983 -42.092 1.00 93.33 C
ANISOU 2329 C LEU A 296 14305 9557 11598 1489 -5971 2269 C
ATOM 2330 O LEU A 296 -10.837 -4.528 -43.147 1.00 96.00 O
ANISOU 2330 O LEU A 296 16081 10140 10254 -6141 2574 2699 O
ATOM 2331 CB LEU A 296 -13.617 -4.882 -43.419 1.00 78.89 C
ANISOU 2331 CB LEU A 296 10348 10426 9203 -511 -4580 244 C
ATOM 2332 CG LEU A 296 -14.809 -5.725 -43.901 1.00 82.91 C
ANISOU 2332 CG LEU A 296 10055 11775 9674 892 -4084 55 C
ATOM 2333 CD1 LEU A 296 -14.524 -7.228 -43.896 1.00 87.37 C
ANISOU 2333 CD1 LEU A 296 10582 12211 10402 951 -3971 660 C
ATOM 2334 CD2 LEU A 296 -16.080 -5.423 -43.121 1.00 83.23 C
ANISOU 2334 CD2 LEU A 296 10683 11780 9160 2011 -3734 -273 C
ATOM 2335 N ALA A 297 -10.810 -5.242 -40.882 1.00 87.34 N
ANISOU 2335 N ALA A 297 12996 13682 6507 1462 -2888 3063 N
ATOM 2336 CA ALA A 297 -9.455 -4.860 -40.429 1.00 81.51 C
ANISOU 2336 CA ALA A 297 13591 12008 5371 553 -2521 2511 C
ATOM 2337 C ALA A 297 -8.526 -6.096 -40.424 1.00 69.59 C
ANISOU 2337 C ALA A 297 11678 9554 5210 -384 -1731 1335 C
ATOM 2338 O ALA A 297 -7.290 -6.168 -40.726 1.00 85.48 O
ANISOU 2338 O ALA A 297 11821 11538 9120 1802 -3687 593 O
ATOM 2339 CB ALA A 297 -9.634 -4.293 -39.012 1.00 83.80 C
ANISOU 2339 CB ALA A 297 14105 10449 7287 851 -2375 1109 C
ATOM 2340 N TYR A 298 -9.133 -7.218 -40.067 1.00 85.80 N
ANISOU 2340 N TYR A 298 13285 11704 7613 123 -1795 -297 N
ATOM 2341 CA TYR A 298 -8.361 -8.426 -39.894 1.00 75.08 C
ANISOU 2341 CA TYR A 298 12620 11037 4871 -1926 -872 -1327 C
ATOM 2342 C TYR A 298 -9.232 -9.555 -40.420 1.00 65.41 C
ANISOU 2342 C TYR A 298 12519 8450 3884 -384 -180 423 C
ATOM 2343 O TYR A 298 -10.456 -9.434 -40.435 1.00 61.43 O
ANISOU 2343 O TYR A 298 11899 8691 2750 23 593 1098 O
ATOM 2344 N ASN A 299 -8.569 -10.620 -40.869 1.00 67.45 N
ANISOU 2344 N ASN A 299 14617 7310 3701 -148 867 -78 N
ATOM 2345 CA ASN A 299 -9.235 -11.789 -41.402 1.00 75.48 C
ANISOU 2345 CA ASN A 299 14986 7535 6159 181 589 975 C
ATOM 2346 C ASN A 299 -8.969 -12.940 -40.438 1.00 76.44 C
ANISOU 2346 C ASN A 299 15115 6692 7237 -480 580 1586 C
ATOM 2347 O ASN A 299 -7.944 -12.954 -39.755 1.00 86.68 O
ANISOU 2347 O ASN A 299 15995 8170 8768 -1109 786 1732 O
ATOM 2348 CB ASN A 299 -8.754 -12.159 -42.806 1.00 74.65 C
ANISOU 2348 CB ASN A 299 14825 7199 6338 1118 880 33 C
ATOM 2349 CG ASN A 299 -8.032 -11.061 -43.565 1.00 77.86 C
ANISOU 2349 CG ASN A 299 14250 8925 6409 772 1489 -965 C
ATOM 2350 OD1 ASN A 299 -7.973 -9.905 -43.134 1.00 84.16 O
ANISOU 2350 OD1 ASN A 299 13428 10638 7910 1099 1775 -2197 O
ATOM 2351 ND2 ASN A 299 -7.457 -11.409 -44.709 1.00 81.62 N
ANISOU 2351 ND2 ASN A 299 13583 10606 6824 309 2290 33 N
ATOM 2352 N GLN A 300 -9.897 -13.897 -40.391 1.00 78.17 N
ANISOU 2352 N GLN A 300 14334 7602 7766 -486 -220 1873 N
ATOM 2353 CA GLN A 300 -9.689 -15.114 -39.618 1.00 75.50 C
ANISOU 2353 CA GLN A 300 13677 6355 8655 774 -530 844 C
ATOM 2354 C GLN A 300 -9.423 -16.278 -40.569 1.00 77.91 C
ANISOU 2354 C GLN A 300 12613 8830 8158 595 -55 253 C
ATOM 2355 O GLN A 300 -10.234 -16.588 -41.439 1.00 79.66 O
ANISOU 2355 O GLN A 300 12010 10166 8092 -1213 466 -386 O
ATOM 2356 CB GLN A 300 -10.787 -15.553 -38.642 1.00 81.13 C
ANISOU 2356 CB GLN A 300 13096 8230 9499 382 -770 -182 C
ATOM 2357 CG GLN A 300 -12.122 -14.821 -38.745 1.00 82.10 C
ANISOU 2357 CG GLN A 300 13523 7383 10289 491 -1073 602 C
ATOM 2358 CD GLN A 300 -12.343 -13.872 -37.594 1.00 79.68 C
ANISOU 2358 CD GLN A 300 12941 8083 9252 274 -1476 194 C
ATOM 2359 OE1 GLN A 300 -13.283 -14.022 -36.804 1.00 84.65 O
ANISOU 2359 OE1 GLN A 300 12020 9775 10369 -354 -1622 1543 O
ATOM 2360 NE2 GLN A 300 -11.456 -12.899 -37.478 1.00 88.18 N
ANISOU 2360 NE2 GLN A 300 13009 9507 10987 -217 -1344 863 N
ATOM 2361 N GLN A 301 -8.271 -16.924 -40.371 1.00 73.22 N
ANISOU 2361 N GLN A 301 13018 5980 8822 1426 684 -60 N
ATOM 2362 CA GLN A 301 -7.955 -18.189 -41.010 1.00 74.60 C
ANISOU 2362 CA GLN A 301 13483 6796 8063 765 598 -162 C
ATOM 2363 C GLN A 301 -8.674 -19.279 -40.226 1.00 76.74 C
ANISOU 2363 C GLN A 301 13857 6363 8937 1058 92 634 C
ATOM 2364 O GLN A 301 -8.091 -19.947 -39.363 1.00 79.38 O
ANISOU 2364 O GLN A 301 13474 7292 9396 968 1550 2433 O
ATOM 2365 CB GLN A 301 -6.447 -18.432 -41.076 1.00 73.29 C
ANISOU 2365 CB GLN A 301 13431 7617 6800 1164 313 80 C
ATOM 2366 N VAL A 302 -9.979 -19.391 -40.496 1.00 80.82 N
ANISOU 2366 N VAL A 302 14958 7183 8567 276 -222 186 N
ATOM 2367 CA VAL A 302 -10.781 -20.474 -39.957 1.00 70.48 C
ANISOU 2367 CA VAL A 302 14671 5843 6265 -20 -684 -182 C
ATOM 2368 C VAL A 302 -10.443 -21.711 -40.790 1.00 75.37 C
ANISOU 2368 C VAL A 302 15346 6712 6577 889 -477 -193 C
ATOM 2369 O VAL A 302 -10.089 -21.586 -41.965 1.00 83.06 O
ANISOU 2369 O VAL A 302 15687 7746 8126 506 1968 -985 O
ATOM 2370 CB VAL A 302 -12.285 -20.129 -39.986 1.00 66.12 C
ANISOU 2370 CB VAL A 302 14327 5043 5753 428 -462 -697 C
ATOM 2371 CG1 VAL A 302 -13.111 -21.122 -39.185 1.00 69.88 C
ANISOU 2371 CG1 VAL A 302 14264 6937 5351 629 -576 -158 C
ATOM 2372 CG2 VAL A 302 -12.576 -18.715 -39.491 1.00 64.66 C
ANISOU 2372 CG2 VAL A 302 14246 4215 6108 -411 -857 -109 C
ATOM 2373 N MET A 303 -10.520 -22.900 -40.183 1.00 73.44 N
ANISOU 2373 N MET A 303 15031 5400 7472 957 -519 -660 N
ATOM 2374 CA MET A 303 -10.116 -24.119 -40.870 1.00 79.45 C
ANISOU 2374 CA MET A 303 14447 6157 9583 157 -32 -1179 C
ATOM 2375 C MET A 303 -9.724 -25.203 -39.870 1.00 81.69 C
ANISOU 2375 C MET A 303 13247 6778 11016 -946 -34 -1158 C
ATOM 2376 O MET A 303 -10.281 -26.299 -39.918 1.00 88.64 O
ANISOU 2376 O MET A 303 14388 7124 12169 -1920 -347 -2292 O
ATOM 2377 CB MET A 303 -8.911 -23.889 -41.793 1.00 78.75 C
ANISOU 2377 CB MET A 303 14417 5592 9910 436 -157 -1091 C
ATOM 2378 N ILE A 304 -8.734 -24.903 -39.013 1.00 71.97 N
ANISOU 2378 N ILE A 304 11275 6204 9867 -968 1112 -2994 N
ATOM 2379 CA ILE A 304 -8.138 -25.903 -38.141 1.00 71.80 C
ANISOU 2379 CA ILE A 304 9192 7687 10400 -1399 440 -2069 C
ATOM 2380 C ILE A 304 -9.165 -26.316 -37.092 1.00 74.93 C
ANISOU 2380 C ILE A 304 9369 8844 10256 -690 398 -2658 C
ATOM 2381 O ILE A 304 -9.527 -27.488 -36.990 1.00 91.62 O
ANISOU 2381 O ILE A 304 12079 10626 12105 -1894 86 -913 O
ATOM 2382 CB ILE A 304 -6.848 -25.382 -37.480 1.00 71.80 C
ANISOU 2382 CB ILE A 304 8765 6908 11606 -2217 779 -2124 C
ATOM 2383 N ASP A 305 -9.640 -25.305 -36.365 1.00 56.10 N
ANISOU 2383 N ASP A 305 4737 8747 7832 -687 -76 -3079 N
ATOM 2384 CA ASP A 305 -10.479 -25.412 -35.171 1.00 57.80 C
ANISOU 2384 CA ASP A 305 6171 7914 7875 126 -711 -1735 C
ATOM 2385 C ASP A 305 -10.014 -24.305 -34.246 1.00 43.01 C
ANISOU 2385 C ASP A 305 4179 5982 6179 1926 -923 -1040 C
ATOM 2386 O ASP A 305 -10.830 -23.534 -33.714 1.00 48.22 O
ANISOU 2386 O ASP A 305 4519 7189 6615 1187 408 -1130 O
ATOM 2387 CB ASP A 305 -10.397 -26.725 -34.401 1.00 60.12 C
ANISOU 2387 CB ASP A 305 5666 8491 8687 -45 -1094 -1975 C
ATOM 2388 CG ASP A 305 -11.546 -27.700 -34.615 1.00 64.31 C
ANISOU 2388 CG ASP A 305 6277 8186 9971 -131 -1364 -2665 C
ATOM 2389 OD1 ASP A 305 -12.701 -27.237 -34.680 1.00 72.36 O
ANISOU 2389 OD1 ASP A 305 6486 9490 11517 1197 -731 -2767 O
ATOM 2390 OD2 ASP A 305 -11.280 -28.920 -34.645 1.00 75.24 O
ANISOU 2390 OD2 ASP A 305 8577 8550 11460 226 -1103 -3429 O
ATOM 2391 N LYS A 306 -8.688 -24.247 -34.092 1.00 46.89 N
ANISOU 2391 N LYS A 306 5343 5684 6790 1300 435 -718 N
ATOM 2392 CA LYS A 306 -8.041 -23.069 -33.550 1.00 42.76 C
ANISOU 2392 CA LYS A 306 4986 6162 5099 1325 670 -176 C
ATOM 2393 C LYS A 306 -7.973 -22.028 -34.662 1.00 46.20 C
ANISOU 2393 C LYS A 306 5389 6327 5837 1517 1142 106 C
ATOM 2394 O LYS A 306 -7.175 -22.170 -35.587 1.00 44.23 O
ANISOU 2394 O LYS A 306 5428 6051 5325 2374 1617 -704 O
ATOM 2395 CB LYS A 306 -6.676 -23.376 -32.946 1.00 42.16 C
ANISOU 2395 CB LYS A 306 4502 6239 5276 1285 970 -193 C
ATOM 2396 CG LYS A 306 -6.757 -24.391 -31.818 1.00 45.60 C
ANISOU 2396 CG LYS A 306 4917 6573 5837 810 1299 -600 C
ATOM 2397 CD LYS A 306 -6.600 -25.871 -32.157 1.00 47.91 C
ANISOU 2397 CD LYS A 306 4055 6328 7821 879 426 -257 C
ATOM 2398 CE LYS A 306 -7.315 -26.701 -31.136 1.00 51.99 C
ANISOU 2398 CE LYS A 306 5219 7362 7171 1257 1948 -983 C
ATOM 2399 NZ LYS A 306 -7.843 -25.993 -29.950 1.00 61.61 N
ANISOU 2399 NZ LYS A 306 6074 8403 8932 426 1284 -1018 N
ATOM 2400 N SER A 307 -8.835 -21.002 -34.557 1.00 42.90 N
ANISOU 2400 N SER A 307 5185 5713 5402 2034 1182 -44 N
ATOM 2401 CA SER A 307 -8.880 -19.929 -35.535 1.00 42.15 C
ANISOU 2401 CA SER A 307 5549 4923 5544 1567 1319 -37 C
ATOM 2402 C SER A 307 -7.541 -19.192 -35.531 1.00 46.85 C
ANISOU 2402 C SER A 307 6553 5615 5633 1772 1118 548 C
ATOM 2403 O SER A 307 -6.907 -19.002 -34.483 1.00 45.19 O
ANISOU 2403 O SER A 307 5663 5910 5596 1616 1934 942 O
ATOM 2404 CB SER A 307 -10.080 -18.987 -35.295 1.00 44.05 C
ANISOU 2404 CB SER A 307 6038 5454 5246 2206 1043 1024 C
ATOM 2405 OG SER A 307 -11.326 -19.680 -35.391 1.00 57.30 O
ANISOU 2405 OG SER A 307 7772 8936 5065 1021 2171 524 O
ATOM 2406 N SER A 308 -7.096 -18.781 -36.723 1.00 48.72 N
ANISOU 2406 N SER A 308 7155 5949 5407 1514 2082 -529 N
ATOM 2407 CA ASER A 308 -5.883 -17.992 -36.848 0.50 47.71 C
ANISOU 2407 CA ASER A 308 7023 5460 5647 1271 2316 -781 C
ATOM 2408 CA BSER A 308 -5.886 -17.989 -36.841 0.50 50.31 C
ANISOU 2408 CA BSER A 308 7657 5436 6022 1202 2007 -530 C
ATOM 2409 C SER A 308 -6.237 -16.607 -37.384 1.00 52.04 C
ANISOU 2409 C SER A 308 8433 5521 5821 334 1716 -464 C
ATOM 2410 O SER A 308 -6.929 -16.479 -38.394 1.00 53.99 O
ANISOU 2410 O SER A 308 9833 5688 4991 755 1344 -1260 O
ATOM 2411 CB ASER A 308 -4.853 -18.689 -37.722 0.50 50.91 C
ANISOU 2411 CB ASER A 308 6699 5907 6737 1114 2743 -983 C
ATOM 2412 CB BSER A 308 -4.851 -18.705 -37.684 0.50 54.08 C
ANISOU 2412 CB BSER A 308 7826 5633 7089 1504 2306 -721 C
ATOM 2413 OG ASER A 308 -3.681 -17.894 -37.844 0.50 49.32 O
ANISOU 2413 OG ASER A 308 5975 5674 7091 1091 2886 -520 O
ATOM 2414 OG BSER A 308 -4.241 -19.738 -36.915 0.50 50.40 O
ANISOU 2414 OG BSER A 308 7199 4753 7199 2011 2959 -714 O
ATOM 2415 N LYS A 309 -5.783 -15.564 -36.684 1.00 50.80 N
ANISOU 2415 N LYS A 309 8932 4991 5377 270 1403 -481 N
ATOM 2416 CA ALYS A 309 -6.091 -14.208 -37.106 0.50 52.52 C
ANISOU 2416 CA ALYS A 309 8511 5050 6395 962 1332 -726 C
ATOM 2417 CA BLYS A 309 -6.083 -14.201 -37.093 0.50 52.25 C
ANISOU 2417 CA BLYS A 309 8728 5099 6026 848 1070 -840 C
ATOM 2418 C LYS A 309 -4.941 -13.662 -37.976 1.00 51.09 C
ANISOU 2418 C LYS A 309 8069 5120 6224 1141 1990 -1962 C
ATOM 2419 O LYS A 309 -3.759 -13.777 -37.537 1.00 54.69 O
ANISOU 2419 O LYS A 309 8359 6603 5818 479 2350 -747 O
ATOM 2420 CB ALYS A 309 -6.461 -13.356 -35.884 0.50 49.41 C
ANISOU 2420 CB ALYS A 309 8010 4835 5930 1103 1138 -370 C
ATOM 2421 CB BLYS A 309 -6.325 -13.312 -35.865 0.50 50.02 C
ANISOU 2421 CB BLYS A 309 8681 5132 5193 890 324 -661 C
ATOM 2422 CG ALYS A 309 -7.834 -13.661 -35.274 0.50 48.07 C
ANISOU 2422 CG ALYS A 309 7378 5032 5855 1479 1049 -212 C
ATOM 2423 CG BLYS A 309 -7.496 -13.681 -34.949 0.50 47.88 C
ANISOU 2423 CG BLYS A 309 8063 5392 4735 1193 -13 -653 C
ATOM 2424 CD ALYS A 309 -7.852 -14.679 -34.130 0.50 44.97 C
ANISOU 2424 CD ALYS A 309 6606 4882 5600 1678 786 -252 C
ATOM 2425 CD BLYS A 309 -8.869 -13.103 -35.298 0.50 43.71 C
ANISOU 2425 CD BLYS A 309 8177 5078 3351 1148 -837 -602 C
ATOM 2426 CE ALYS A 309 -9.204 -15.277 -33.795 0.50 48.14 C
ANISOU 2426 CE ALYS A 309 6921 5189 6182 1920 626 156 C
ATOM 2427 CE BLYS A 309 -9.923 -13.572 -34.324 0.50 45.67 C
ANISOU 2427 CE BLYS A 309 8473 5094 3786 1556 -456 -768 C
ATOM 2428 NZ ALYS A 309 -10.371 -14.393 -33.607 0.50 45.72 N
ANISOU 2428 NZ ALYS A 309 6527 4594 6251 2789 358 5 N
ATOM 2429 NZ BLYS A 309 -9.539 -14.767 -33.557 0.50 51.70 N
ANISOU 2429 NZ BLYS A 309 10317 5396 3930 458 -500 -110 N
TER 2430 LYS A 309
HETATM 2431 ZN ZN A 466 -20.015 -6.504 -14.504 1.00 24.60 Zn
ANISOU 2431 ZN ZN A 466 3016 3133 3197 133 -121 171 Zn
HETATM 2432 ZN ZN A 467 -19.253 -5.732 -11.469 1.00 23.80 Zn
ANISOU 2432 ZN ZN A 467 2798 3009 3235 -142 -217 152 Zn
HETATM 2433 O HOH A 501 -19.800 -7.403 -12.519 1.00 26.60 O
ANISOU 2433 O HOH A 501 3363 3525 3219 238 -848 -284 O
HETATM 2434 O HOH A 502 -36.477 -1.793 13.149 1.00 40.83 O
ANISOU 2434 O HOH A 502 4858 4149 6508 -1495 98 -3064 O
HETATM 2435 O HOH A 503 -17.655 -16.545 1.650 1.00 23.57 O
ANISOU 2435 O HOH A 503 3100 2616 3240 449 -401 280 O
HETATM 2436 O HOH A 504 -33.524 -14.416 -25.862 1.00 49.42 O
ANISOU 2436 O HOH A 504 4554 7273 6951 783 -443 984 O
HETATM 2437 O HOH A 505 -39.475 -7.685 1.700 1.00 38.51 O
ANISOU 2437 O HOH A 505 5272 4136 5223 -167 -288 -520 O
HETATM 2438 O HOH A 506 -29.871 -25.292 -13.876 1.00 43.37 O
ANISOU 2438 O HOH A 506 5599 3896 6985 -58 315 651 O
HETATM 2439 O HOH A 507 -20.858 3.005 -14.266 1.00 27.96 O
ANISOU 2439 O HOH A 507 3907 2980 3736 -538 -203 195 O
HETATM 2440 O HOH A 508 -34.959 7.005 -22.102 1.00 39.61 O
ANISOU 2440 O HOH A 508 4461 3304 7285 863 266 81 O
HETATM 2441 O HOH A 509 -30.292 -3.473 -24.209 1.00 33.92 O
ANISOU 2441 O HOH A 509 4542 4322 4022 1094 -1017 -804 O
HETATM 2442 O HOH A 510 -36.765 4.089 5.487 1.00 40.80 O
ANISOU 2442 O HOH A 510 5489 5837 4175 1657 -461 -997 O
HETATM 2443 O HOH A 511 -28.270 -27.780 -17.976 1.00 49.99 O
ANISOU 2443 O HOH A 511 5737 5481 7774 518 717 -803 O
HETATM 2444 O HOH A 512 -23.486 -18.596 -0.034 1.00 46.49 O
ANISOU 2444 O HOH A 512 4140 7836 5688 -308 98 -1848 O
HETATM 2445 O HOH A 513 -30.666 -21.953 -30.876 1.00 82.17 O
ANISOU 2445 O HOH A 513 10986 8105 12129 -2923 -3546 516 O
HETATM 2446 O HOH A 514 -19.728 14.367 -15.660 1.00 42.75 O
ANISOU 2446 O HOH A 514 5333 5000 5911 -567 180 -577 O
HETATM 2447 O HOH A 515 -28.640 -15.948 -3.827 1.00 25.45 O
ANISOU 2447 O HOH A 515 3081 2751 3839 -240 -101 300 O
HETATM 2448 O HOH A 516 -36.809 3.086 -2.861 1.00 26.78 O
ANISOU 2448 O HOH A 516 3599 3301 3276 582 244 -104 O
HETATM 2449 O HOH A 517 -40.322 2.900 -22.020 1.00 46.03 O
ANISOU 2449 O HOH A 517 4917 6257 6315 530 -1156 787 O
HETATM 2450 O HOH A 518 -27.674 10.312 -27.418 1.00 62.50 O
ANISOU 2450 O HOH A 518 12106 5375 6265 598 -1142 595 O
HETATM 2451 O HOH A 519 -12.893 1.066 -22.596 1.00 47.87 O
ANISOU 2451 O HOH A 519 5965 6161 6064 -1724 341 685 O
HETATM 2452 O HOH A 520 -43.856 5.446 -8.259 1.00 51.14 O
ANISOU 2452 O HOH A 520 5186 5632 8612 959 149 418 O
HETATM 2453 O HOH A 521 -28.681 -6.358 -25.145 1.00 47.57 O
ANISOU 2453 O HOH A 521 8909 5425 3739 88 -1134 700 O
HETATM 2454 O HOH A 522 -19.064 5.064 -7.268 1.00 32.68 O
ANISOU 2454 O HOH A 522 3894 4160 4361 -1025 -857 286 O
HETATM 2455 O HOH A 523 -40.396 -14.919 2.116 1.00 46.62 O
ANISOU 2455 O HOH A 523 5885 6058 5770 -1488 950 3009 O
HETATM 2456 O HOH A 524 -24.000 0.569 7.324 1.00 38.35 O
ANISOU 2456 O HOH A 524 4878 3076 6619 -709 415 59 O
HETATM 2457 O HOH A 525 -39.778 -12.215 -5.665 1.00 28.36 O
ANISOU 2457 O HOH A 525 3604 3625 3547 -171 180 167 O
HETATM 2458 O HOH A 526 -36.215 -8.792 1.163 1.00 24.54 O
ANISOU 2458 O HOH A 526 3067 2897 3361 -256 -45 -182 O
HETATM 2459 O HOH A 527 -37.466 6.299 -4.037 1.00 39.31 O
ANISOU 2459 O HOH A 527 4573 5034 5327 -286 -172 -1004 O
HETATM 2460 O HOH A 528 -17.378 -12.576 -1.158 1.00 26.50 O
ANISOU 2460 O HOH A 528 3689 2948 3432 -435 -141 426 O
HETATM 2461 O HOH A 529 -30.347 -18.809 -24.518 1.00 43.89 O
ANISOU 2461 O HOH A 529 5744 5059 5873 -784 -1263 821 O
HETATM 2462 O HOH A 530 -16.615 -3.924 2.608 1.00 44.27 O
ANISOU 2462 O HOH A 530 4901 6036 5882 -656 -1636 195 O
HETATM 2463 O HOH A 531 -38.391 -13.684 -7.586 1.00 26.20 O
ANISOU 2463 O HOH A 531 3265 3566 3125 -329 116 66 O
HETATM 2464 O HOH A 532 -28.474 -3.637 -22.216 1.00 24.44 O
ANISOU 2464 O HOH A 532 3450 2831 3005 -2 -536 132 O
HETATM 2465 O HOH A 533 -30.473 -2.428 13.513 1.00 40.96 O
ANISOU 2465 O HOH A 533 4748 5016 5799 -990 1236 -1322 O
HETATM 2466 O HOH A 534 -24.072 -0.964 -8.527 1.00 24.15 O
ANISOU 2466 O HOH A 534 3383 2667 3124 -331 -477 317 O
HETATM 2467 O HOH A 535 -24.105 1.408 -9.937 1.00 24.69 O
ANISOU 2467 O HOH A 535 3492 2694 3197 96 -331 88 O
HETATM 2468 O HOH A 536 -4.374 1.256 -24.904 1.00 49.63 O
ANISOU 2468 O HOH A 536 5314 6930 6614 1086 359 216 O
HETATM 2469 O HOH A 537 -39.361 -4.776 -20.534 1.00 28.21 O
ANISOU 2469 O HOH A 537 3784 3685 3248 411 -743 379 O
HETATM 2470 O HOH A 538 -16.151 -6.862 -29.665 1.00 37.12 O
ANISOU 2470 O HOH A 538 3889 4740 5474 1027 -554 -515 O
HETATM 2471 O HOH A 539 -24.093 -3.856 12.172 1.00 36.97 O
ANISOU 2471 O HOH A 539 5205 4980 3862 1065 -1072 -651 O
HETATM 2472 O HOH A 540 -18.281 -10.596 5.587 1.00 27.42 O
ANISOU 2472 O HOH A 540 3144 3581 3693 -102 -797 -121 O
HETATM 2473 O HOH A 541 -44.030 -8.106 -14.413 1.00 38.48 O
ANISOU 2473 O HOH A 541 3016 6084 5521 -13 -815 1740 O
HETATM 2474 O HOH A 542 -34.456 9.934 -5.773 1.00 32.71 O
ANISOU 2474 O HOH A 542 4857 3595 3975 690 454 -180 O
HETATM 2475 O HOH A 543 -35.381 -12.061 3.512 1.00 39.05 O
ANISOU 2475 O HOH A 543 5619 5002 4217 840 477 24 O
HETATM 2476 O HOH A 544 -35.734 13.255 -11.835 1.00 34.77 O
ANISOU 2476 O HOH A 544 5248 3193 4768 882 -1 -399 O
HETATM 2477 O HOH A 545 -24.497 -11.047 -25.890 1.00 38.07 O
ANISOU 2477 O HOH A 545 4775 5414 4275 1119 438 -444 O
HETATM 2478 O HOH A 546 -21.843 -1.101 -20.958 1.00 24.40 O
ANISOU 2478 O HOH A 546 2961 3082 3227 -69 11 198 O
HETATM 2479 O HOH A 547 -37.740 3.287 3.123 1.00 33.23 O
ANISOU 2479 O HOH A 547 4361 3879 4387 -66 246 -359 O
HETATM 2480 O HOH A 548 -39.689 -1.075 2.193 1.00 37.59 O
ANISOU 2480 O HOH A 548 5591 4272 4419 -932 1369 -282 O
HETATM 2481 O HOH A 549 -20.396 11.658 -27.067 1.00 50.73 O
ANISOU 2481 O HOH A 549 9525 4477 5272 44 166 2107 O
HETATM 2482 O HOH A 550 -20.211 -11.358 -26.094 1.00 42.18 O
ANISOU 2482 O HOH A 550 5002 5994 5029 1113 177 768 O
HETATM 2483 O HOH A 551 -14.589 -1.603 -6.126 1.00 41.79 O
ANISOU 2483 O HOH A 551 4850 4910 6119 -643 -1304 773 O
HETATM 2484 O HOH A 552 -4.543 -29.983 -27.082 1.00 46.07 O
ANISOU 2484 O HOH A 552 4718 5361 7427 108 -425 500 O
HETATM 2485 O HOH A 553 -40.685 -1.179 -7.274 1.00 30.35 O
ANISOU 2485 O HOH A 553 3218 4045 4269 65 -255 90 O
HETATM 2486 O HOH A 554 -24.491 15.353 -8.337 1.00 42.64 O
ANISOU 2486 O HOH A 554 6642 4693 4864 -658 -609 -254 O
HETATM 2487 O HOH A 555 -13.543 7.963 -10.544 1.00 50.97 O
ANISOU 2487 O HOH A 555 4255 8149 6961 -450 192 920 O
HETATM 2488 O HOH A 556 -20.865 -13.380 -13.597 1.00 39.88 O
ANISOU 2488 O HOH A 556 6043 5338 3770 2297 368 81 O
HETATM 2489 O HOH A 557 -23.338 -28.685 -22.556 1.00 57.68 O
ANISOU 2489 O HOH A 557 6671 6130 9114 -728 2049 -714 O
HETATM 2490 O HOH A 558 -6.497 -20.874 -41.645 1.00 64.13 O
ANISOU 2490 O HOH A 558 10451 6583 7331 2798 504 -1170 O
HETATM 2491 O HOH A 559 -15.476 -15.476 -0.000 0.50 27.98 O
ANISOU 2491 O HOH A 559 2896 2896 4840 -370 327 -327 O
HETATM 2492 O HOH A 560 -31.567 14.191 -3.599 1.00 51.59 O
ANISOU 2492 O HOH A 560 6453 7824 5324 1447 165 -115 O
HETATM 2493 O HOH A 561 -24.969 -20.876 -7.977 1.00 45.70 O
ANISOU 2493 O HOH A 561 4813 4578 7971 273 -1231 1036 O
HETATM 2494 O HOH A 562 -27.108 -17.079 1.062 1.00 37.24 O
ANISOU 2494 O HOH A 562 5144 4154 4852 -68 -112 -484 O
HETATM 2495 O HOH A 563 -19.137 -5.341 6.043 1.00 38.98 O
ANISOU 2495 O HOH A 563 5461 5109 4239 -225 -703 -555 O
HETATM 2496 O HOH A 564 -26.150 17.405 -14.453 1.00 51.14 O
ANISOU 2496 O HOH A 564 9093 4605 5734 1323 670 511 O
HETATM 2497 O HOH A 565 -36.553 7.938 -6.480 1.00 27.65 O
ANISOU 2497 O HOH A 565 3873 3065 3566 253 23 -35 O
HETATM 2498 O HOH A 566 -37.466 -13.348 4.328 1.00 51.05 O
ANISOU 2498 O HOH A 566 6140 7773 5482 -774 1009 507 O
HETATM 2499 O HOH A 567 -19.020 -8.907 7.571 1.00 37.55 O
ANISOU 2499 O HOH A 567 4659 4988 4621 451 -1040 -968 O
HETATM 2500 O HOH A 568 -39.334 1.140 4.027 1.00 41.87 O
ANISOU 2500 O HOH A 568 5276 5683 4951 1289 395 21 O
HETATM 2501 O HOH A 569 -17.852 -1.745 6.171 1.00 61.33 O
ANISOU 2501 O HOH A 569 8145 5791 9366 -31 -1073 1191 O
HETATM 2502 O HOH A 570 -17.744 10.789 -26.759 1.00 46.70 O
ANISOU 2502 O HOH A 570 5948 5313 6483 640 315 1605 O
HETATM 2503 O HOH A 571 -39.468 -16.086 -7.364 1.00 39.39 O
ANISOU 2503 O HOH A 571 4638 4286 6041 -298 0 -1061 O
HETATM 2504 O HOH A 572 -16.679 -9.583 -29.028 1.00 43.06 O
ANISOU 2504 O HOH A 572 5078 5628 5655 1085 489 682 O
HETATM 2505 O HOH A 573 -38.381 -0.572 6.086 1.00 48.75 O
ANISOU 2505 O HOH A 573 7484 5684 5354 5 -273 -1548 O
HETATM 2506 O HOH A 574 -41.944 -6.541 1.768 1.00 65.35 O
ANISOU 2506 O HOH A 574 7297 10113 7420 2558 -1112 -2352 O
HETATM 2507 O HOH A 575 -42.012 -2.247 1.983 1.00 43.08 O
ANISOU 2507 O HOH A 575 4229 5196 6941 -150 103 -161 O
HETATM 2508 O HOH A 576 -16.698 -6.169 4.700 1.00 44.60 O
ANISOU 2508 O HOH A 576 5955 4865 6125 111 -1115 -404 O
HETATM 2509 O HOH A 577 -2.745 -0.414 -44.815 1.00102.99 O
ANISOU 2509 O HOH A 577 10971 11525 16635 -2703 1151 -4430 O
HETATM 2510 O HOH A 578 -17.071 -12.917 6.847 1.00 35.78 O
ANISOU 2510 O HOH A 578 6134 2891 4572 -186 -1821 524 O
HETATM 2511 O HOH A 579 -18.501 8.193 2.214 1.00 51.76 O
ANISOU 2511 O HOH A 579 5337 7667 6661 -218 323 -1671 O
CONECT 504 2431
CONECT 521 2431
CONECT 537 2432
CONECT 547 2432
CONECT 1319 2431
CONECT 1459 2431 2432
CONECT 1838 2432
CONECT 2431 1459 504 521 1319
CONECT 2432 1838 1459 537 547
END
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elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.
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