HEADER TRANSCRIPTION REGULATOR 27-FEB-08 3CDL

TITLE CRYSTAL STRUCTURE OF A TETR FAMILY TRANSCRIPTIONAL

TITLE 2 REGULATOR FROM PSEUDOMONAS SYRINGAE PV. TOMATO STR. DC3000

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR AEFR;

COMPND 3 CHAIN: A, B;

COMPND 4 ENGINEERED: YES

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. TOMATO STR.

SOURCE 3 DC3000;

SOURCE 4 ORGANISM_COMMON: BACTERIA;

SOURCE 5 STRAIN: DC3000;

SOURCE 6 GENE: AEFR, PSPTO3549;

SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;

SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;

SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;

SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7

KEYWDS APC88582, TETR, PSEUDOMONAS SYRINGAE PV. TOMATO STR. DC3000,

KEYWDS 2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,

KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, DNA-BINDING,

KEYWDS 4 TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSCRIPTION

KEYWDS 5 REGULATOR

EXPDTA X-RAY DIFFRACTION

AUTHOR K.TAN,L.BIGELOW,M.GU,A.JOACHIMIAK,MIDWEST CENTER FOR

AUTHOR 2 STRUCTURAL GENOMICS (MCSG)

REVDAT 1 18-MAR-08 3CDL 0

JRNL AUTH K.TAN,L.BIGELOW,M.GU,A.JOACHIMIAK

JRNL TITL THE CRYSTAL STRUCTURE OF A TETR FAMILY

JRNL TITL 2 TRANSCRIPTIONAL REGULATOR FROM PSEUDOMONAS

JRNL TITL 3 SYRINGAE PV. TOMATO STR. DC3000.

JRNL REF TO BE PUBLISHED

JRNL REFN

REMARK 1

REMARK 2

REMARK 2 RESOLUTION. 2.36 ANGSTROMS.

REMARK 3

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : REFMAC 5.2.0019

REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON

REMARK 3

REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD

REMARK 3

REMARK 3 DATA USED IN REFINEMENT.

REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.26

REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000

REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3

REMARK 3 NUMBER OF REFLECTIONS : 13723

REMARK 3

REMARK 3 FIT TO DATA USED IN REFINEMENT.

REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT

REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM

REMARK 3 R VALUE (WORKING + TEST SET) : 0.210

REMARK 3 R VALUE (WORKING SET) : 0.207

REMARK 3 FREE R VALUE : 0.275

REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000

REMARK 3 FREE R VALUE TEST SET COUNT : 728

REMARK 3

REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.

REMARK 3 TOTAL NUMBER OF BINS USED : 20

REMARK 3 BIN RESOLUTION RANGE HIGH : 2.36

REMARK 3 BIN RESOLUTION RANGE LOW : 2.42

REMARK 3 REFLECTION IN BIN (WORKING SET) : 795

REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.95

REMARK 3 BIN R VALUE (WORKING SET) : 0.2640

REMARK 3 BIN FREE R VALUE SET COUNT : 53

REMARK 3 BIN FREE R VALUE : 0.3200

REMARK 3

REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.

REMARK 3 ALL ATOMS : 3068

REMARK 3

REMARK 3 B VALUES.

REMARK 3 FROM WILSON PLOT (A**2) : NULL

REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.51

REMARK 3 OVERALL ANISOTROPIC B VALUE.

REMARK 3 B11 (A**2) : 0.23000

REMARK 3 B22 (A**2) : 0.17000

REMARK 3 B33 (A**2) : -0.28000

REMARK 3 B12 (A**2) : 0.00000

REMARK 3 B13 (A**2) : 0.16000

REMARK 3 B23 (A**2) : 0.00000

REMARK 3

REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.

REMARK 3 ESU BASED ON R VALUE (A): 0.729

REMARK 3 ESU BASED ON FREE R VALUE (A): 0.316

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.294

REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.490

REMARK 3

REMARK 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT

REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3096 ; 0.015 ; 0.022

REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4194 ; 1.521 ; 1.942

REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 371 ; 6.623 ; 5.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;37.266 ;23.377

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 529 ;22.442 ;15.000

REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;20.993 ;15.000

REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 462 ; 0.117 ; 0.200

REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2349 ; 0.005 ; 0.020

REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL

REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1513 ; 0.236 ; 0.200

REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL

REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2125 ; 0.309 ; 0.200

REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL

REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.153 ; 0.200

REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL

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): 58 ; 0.180 ; 0.200

REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.161 ; 0.200

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): 1916 ; 0.660 ; 1.500

REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL

REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3008 ; 1.062 ; 2.000

REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1360 ; 1.490 ; 3.000

REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1185 ; 2.311 ; 4.500

REMARK 3

REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT

REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL

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 : 0

REMARK 3

REMARK 3 TLS DETAILS

REMARK 3 NUMBER OF TLS GROUPS : 4

REMARK 3

REMARK 3 TLS GROUP : 1

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : A 3 A 65

REMARK 3 ORIGIN FOR THE GROUP (A): 66.7850 -0.1720 -36.4260

REMARK 3 T TENSOR

REMARK 3 T11: 0.2321 T22: -0.1541

REMARK 3 T33: 0.2658 T12: -0.0644

REMARK 3 T13: 0.1682 T23: -0.1041

REMARK 3 L TENSOR

REMARK 3 L11: 6.2147 L22: 5.8872

REMARK 3 L33: 7.5259 L12: -2.7221

REMARK 3 L13: -4.5265 L23: 1.1785

REMARK 3 S TENSOR

REMARK 3 S11: -0.8541 S12: 0.1458 S13: -1.5683

REMARK 3 S21: 0.0584 S22: -0.0543 S23: 0.6831

REMARK 3 S31: 1.5234 S32: -0.1649 S33: 0.9084

REMARK 3

REMARK 3 TLS GROUP : 2

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : A 70 A 199

REMARK 3 ORIGIN FOR THE GROUP (A): 59.5150 14.9000 -13.4030

REMARK 3 T TENSOR

REMARK 3 T11: -0.2058 T22: -0.2100

REMARK 3 T33: -0.1016 T12: 0.0274

REMARK 3 T13: -0.0693 T23: -0.0223

REMARK 3 L TENSOR

REMARK 3 L11: 1.5070 L22: 0.6388

REMARK 3 L33: 4.2513 L12: 0.5151

REMARK 3 L13: -1.3021 L23: -0.8103

REMARK 3 S TENSOR

REMARK 3 S11: -0.0397 S12: 0.0137 S13: -0.2331

REMARK 3 S21: 0.0007 S22: -0.0931 S23: -0.0169

REMARK 3 S31: 0.2871 S32: -0.0260 S33: 0.1328

REMARK 3

REMARK 3 TLS GROUP : 3

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : B 3 B 64

REMARK 3 ORIGIN FOR THE GROUP (A): 58.7650 32.2040 -46.1660

REMARK 3 T TENSOR

REMARK 3 T11: 0.1807 T22: 0.2017

REMARK 3 T33: 0.0706 T12: 0.2129

REMARK 3 T13: 0.0908 T23: 0.1432

REMARK 3 L TENSOR

REMARK 3 L11: 5.5585 L22: 3.9098

REMARK 3 L33: 9.2492 L12: -0.7388

REMARK 3 L13: -0.5339 L23: -1.0694

REMARK 3 S TENSOR

REMARK 3 S11: 0.5587 S12: 0.8202 S13: 0.8080

REMARK 3 S21: -0.1172 S22: -0.1367 S23: -0.1908

REMARK 3 S31: -0.8724 S32: -0.6242 S33: -0.4219

REMARK 3

REMARK 3 TLS GROUP : 4

REMARK 3 NUMBER OF COMPONENTS GROUP : 1

REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI

REMARK 3 RESIDUE RANGE : B 73 B 200

REMARK 3 ORIGIN FOR THE GROUP (A): 55.8450 31.5540 -19.1450

REMARK 3 T TENSOR

REMARK 3 T11: -0.1247 T22: -0.2095

REMARK 3 T33: -0.0233 T12: 0.0501

REMARK 3 T13: -0.0262 T23: 0.0078

REMARK 3 L TENSOR

REMARK 3 L11: 2.1320 L22: 1.2687

REMARK 3 L33: 4.3934 L12: -0.1884

REMARK 3 L13: -0.7252 L23: 0.1857

REMARK 3 S TENSOR

REMARK 3 S11: 0.1947 S12: 0.0945 S13: 0.4467

REMARK 3 S21: 0.0553 S22: 0.0350 S23: -0.0111

REMARK 3 S31: -0.6490 S32: -0.0332 S33: -0.2297

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : MASK

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: HYDROGENS HAVE BEEN ADDED IN THE

REMARK 3 RIDING POSITIONS

REMARK 4

REMARK 4 3CDL COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007

REMARK 100

REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.

REMARK 100 THE RCSB ID CODE IS RCSB046645.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION : 12-FEB-2007

REMARK 200 TEMPERATURE (KELVIN) : 100.0

REMARK 200 PH : 5.50

REMARK 200 NUMBER OF CRYSTALS USED : 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) : Y

REMARK 200 RADIATION SOURCE : APS

REMARK 200 BEAMLINE : 19-ID

REMARK 200 X-RAY GENERATOR MODEL : NULL

REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M

REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915, 0.97937

REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL

REMARK 200 OPTICS : MIRRORS

REMARK 200

REMARK 200 DETECTOR TYPE : CCD

REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315

REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000

REMARK 200 DATA SCALING SOFTWARE : HKL-3000

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14467

REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350

REMARK 200 RESOLUTION RANGE LOW (A) : 33.260

REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000

REMARK 200

REMARK 200 OVERALL.

REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5

REMARK 200 DATA REDUNDANCY : 4.300

REMARK 200 R MERGE (I) : 0.11400

REMARK 200 R SYM (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4700

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42

REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7

REMARK 200 DATA REDUNDANCY IN SHELL : 3.50

REMARK 200 R MERGE FOR SHELL (I) : NULL

REMARK 200 R SYM FOR SHELL (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400

REMARK 200

REMARK 200 DIFFRACTION PROTOCOL: MAD

REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD

REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, RESOLVE, HKL-3000

REMARK 200 STARTING MODEL: NULL

REMARK 200

REMARK 200 REMARK: NULL

REMARK 280

REMARK 280 CRYSTAL

REMARK 280 SOLVENT CONTENT, VS (%): 36.39

REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93

REMARK 280

REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 25% PEG

REMARK 280 3350, 0.1M BIS-TRIS, PH 5.5, VAPOR DIFFUSION, SITTING DROP,

REMARK 280 TEMPERATURE 289K

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1

REMARK 290

REMARK 290 SYMOP SYMMETRY

REMARK 290 NNNMMM OPERATOR

REMARK 290 1555 X,Y,Z

REMARK 290 2555 -X,Y,-Z

REMARK 290 3555 1/2+X,1/2+Y,Z

REMARK 290 4555 1/2-X,1/2+Y,-Z

REMARK 290

REMARK 290 WHERE NNN -> OPERATOR NUMBER

REMARK 290 MMM -> TRANSLATION VECTOR

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

REMARK 290 RELATED MOLECULES.

REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000

REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000

REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 66.15250

REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.70450

REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000

REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.15250

REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.70450

REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000

REMARK 290

REMARK 290 REMARK: NULL

REMARK 300

REMARK 300 BIOMOLECULE: 1

REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM

REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN

REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON

REMARK 300 BURIED SURFACE AREA.

REMARK 350

REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN

REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE

REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS

REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND

REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.

REMARK 350

REMARK 350 BIOMOLECULE: 1

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC

REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC

REMARK 350 SOFTWARE USED: PISA

REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2

REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 18560 ANGSTROM**2

REMARK 350 GAIN IN SOLVENT FREE ENERGY: -34 KCAL/MOL

REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)

REMARK 465

REMARK 465 M RES C SSEQI

REMARK 465 SER A -2

REMARK 465 ASN A -1

REMARK 465 ALA A 0

REMARK 465 MSE A 1

REMARK 465 ARG A 2

REMARK 465 PRO A 66

REMARK 465 PRO A 67

REMARK 465 GLN A 68

REMARK 465 SER A 69

REMARK 465 ALA A 122

REMARK 465 ARG A 123

REMARK 465 ILE A 124

REMARK 465 ASN A 125

REMARK 465 GLU A 126

REMARK 465 ARG A 127

REMARK 465 GLY A 200

REMARK 465 SER B -2

REMARK 465 ASN B -1

REMARK 465 ALA B 0

REMARK 465 MSE B 1

REMARK 465 ARG B 2

REMARK 465 ALA B 65

REMARK 465 PRO B 66

REMARK 465 PRO B 67

REMARK 465 GLN B 68

REMARK 465 SER B 69

REMARK 465 GLU B 70

REMARK 465 VAL B 71

REMARK 465 VAL B 72

REMARK 465 ARG B 127

REMARK 465 GLU B 128

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 NUCELIC ACID: CLOWNEY ET AL 1996

REMARK 500

REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3

REMARK 500 ARG B 41 NE - CZ - NH2 ANGL. DEV. = -4.0 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 THR A 4 -6.96 -142.26

REMARK 500 PRO A 48 -18.10 -47.08

REMARK 500 VAL A 71 -15.24 56.17

REMARK 500 PHE A 165 -68.23 -125.81

REMARK 500 PHE A 171 35.90 -144.23

REMARK 500 LYS B 40 -39.13 -37.10

REMARK 500 LEU B 61 -84.94 -76.27

REMARK 500 TRP B 62 3.46 -69.24

REMARK 500 PRO B 75 -86.69 -24.32

REMARK 500 PHE B 165 -74.24 -130.53

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 LEU B 76 VAL B 77 144.27

REMARK 500

REMARK 500 REMARK: NULL

REMARK 900

REMARK 900 RELATED ENTRIES

REMARK 900 RELATED ID: APC88582 RELATED DB: TARGETDB

DBREF 3CDL A 1 200 UNP Q87Z81 Q87Z81_PSESM 1 200

DBREF 3CDL B 1 200 UNP Q87Z81 Q87Z81_PSESM 1 200

SEQADV 3CDL SER A -2 UNP Q87Z81 EXPRESSION TAG

SEQADV 3CDL ASN A -1 UNP Q87Z81 EXPRESSION TAG

SEQADV 3CDL ALA A 0 UNP Q87Z81 EXPRESSION TAG

SEQADV 3CDL SER B -2 UNP Q87Z81 EXPRESSION TAG

SEQADV 3CDL ASN B -1 UNP Q87Z81 EXPRESSION TAG

SEQADV 3CDL ALA B 0 UNP Q87Z81 EXPRESSION TAG

SEQRES 1 A 203 SER ASN ALA MSE ARG LEU THR ASP GLN LYS ARG GLU SER

SEQRES 2 A 203 ILE VAL GLN ALA ALA ILE ALA GLU PHE GLY ASP ARG GLY

SEQRES 3 A 203 PHE GLU ILE THR SER MSE ASP ARG ILE ALA ALA ARG ALA

SEQRES 4 A 203 GLU VAL SER LYS ARG THR VAL TYR ASN HIS PHE PRO SER

SEQRES 5 A 203 LYS GLU GLU LEU PHE ALA GLU MSE LEU GLN ARG LEU TRP

SEQRES 6 A 203 ASN CYS ALA PRO PRO GLN SER GLU VAL VAL TYR ARG PRO

SEQRES 7 A 203 LEU VAL SER LEU ARG GLU GLN LEU LEU GLU LEU LEU TRP

SEQRES 8 A 203 GLY LYS MSE ARG ASN LEU THR ASP SER SER PHE LEU ASP

SEQRES 9 A 203 LEU ALA ARG VAL VAL VAL GLY ALA THR ILE HIS SER PRO

SEQRES 10 A 203 GLU ARG ALA GLN VAL TRP LEU ALA ARG ILE ASN GLU ARG

SEQRES 11 A 203 GLU GLU THR PHE SER ALA TRP ILE ARG ALA ALA GLN LYS

SEQRES 12 A 203 ASP GLY ARG LEU LYS PRO VAL ASP PRO GLY PHE ALA ALA

SEQRES 13 A 203 THR GLN MSE HIS ALA LEU LEU LYS SER PHE ALA PHE TRP

SEQRES 14 A 203 PRO GLN VAL THR PHE ASN ALA ALA LEU LEU THR PRO GLN

SEQRES 15 A 203 GLU GLN SER ASN VAL VAL GLU SER ALA LEU ASN MSE PHE

SEQRES 16 A 203 LEU GLY TRP TYR GLU ILE PRO GLY

SEQRES 1 B 203 SER ASN ALA MSE ARG LEU THR ASP GLN LYS ARG GLU SER

SEQRES 2 B 203 ILE VAL GLN ALA ALA ILE ALA GLU PHE GLY ASP ARG GLY

SEQRES 3 B 203 PHE GLU ILE THR SER MSE ASP ARG ILE ALA ALA ARG ALA

SEQRES 4 B 203 GLU VAL SER LYS ARG THR VAL TYR ASN HIS PHE PRO SER

SEQRES 5 B 203 LYS GLU GLU LEU PHE ALA GLU MSE LEU GLN ARG LEU TRP

SEQRES 6 B 203 ASN CYS ALA PRO PRO GLN SER GLU VAL VAL TYR ARG PRO

SEQRES 7 B 203 LEU VAL SER LEU ARG GLU GLN LEU LEU GLU LEU LEU TRP

SEQRES 8 B 203 GLY LYS MSE ARG ASN LEU THR ASP SER SER PHE LEU ASP

SEQRES 9 B 203 LEU ALA ARG VAL VAL VAL GLY ALA THR ILE HIS SER PRO

SEQRES 10 B 203 GLU ARG ALA GLN VAL TRP LEU ALA ARG ILE ASN GLU ARG

SEQRES 11 B 203 GLU GLU THR PHE SER ALA TRP ILE ARG ALA ALA GLN LYS

SEQRES 12 B 203 ASP GLY ARG LEU LYS PRO VAL ASP PRO GLY PHE ALA ALA

SEQRES 13 B 203 THR GLN MSE HIS ALA LEU LEU LYS SER PHE ALA PHE TRP

SEQRES 14 B 203 PRO GLN VAL THR PHE ASN ALA ALA LEU LEU THR PRO GLN

SEQRES 15 B 203 GLU GLN SER ASN VAL VAL GLU SER ALA LEU ASN MSE PHE

SEQRES 16 B 203 LEU GLY TRP TYR GLU ILE PRO GLY

MODRES 3CDL MSE A 29 MET SELENOMETHIONINE

MODRES 3CDL MSE A 57 MET SELENOMETHIONINE

MODRES 3CDL MSE A 91 MET SELENOMETHIONINE

MODRES 3CDL MSE A 156 MET SELENOMETHIONINE

MODRES 3CDL MSE A 191 MET SELENOMETHIONINE

MODRES 3CDL MSE B 29 MET SELENOMETHIONINE

MODRES 3CDL MSE B 57 MET SELENOMETHIONINE

MODRES 3CDL MSE B 91 MET SELENOMETHIONINE

MODRES 3CDL MSE B 156 MET SELENOMETHIONINE

MODRES 3CDL MSE B 191 MET SELENOMETHIONINE

HET MSE A 29 8

HET MSE A 57 8

HET MSE A 91 8

HET MSE A 156 8

HET MSE A 191 8

HET MSE B 29 8

HET MSE B 57 8

HET MSE B 91 8

HET MSE B 156 13

HET MSE B 191 8

HETNAM MSE SELENOMETHIONINE

FORMUL 1 MSE 10(C5 H11 N O2 SE)

FORMUL 3 HOH *41(H2 O)

HELIX 1 1 THR A 4 GLY A 23 1 20

HELIX 2 2 SER A 28 ALA A 36 1 9

HELIX 3 3 SER A 39 ASN A 45 1 7

HELIX 4 4 SER A 49 CYS A 64 1 16

HELIX 5 5 SER A 78 THR A 95 1 18

HELIX 6 6 ASP A 96 HIS A 112 1 17

HELIX 7 7 SER A 113 GLN A 118 1 6

HELIX 8 8 GLU A 128 ASP A 141 1 14

HELIX 9 9 ASP A 148 PHE A 165 1 18

HELIX 10 10 PHE A 165 ASN A 172 1 8

HELIX 11 11 THR A 177 GLU A 197 1 21

HELIX 12 12 ASP B 5 ARG B 22 1 18

HELIX 13 13 SER B 28 GLU B 37 1 10

HELIX 14 14 SER B 39 PHE B 47 1 9

HELIX 15 15 SER B 49 TRP B 62 1 14

HELIX 16 16 SER B 78 THR B 95 1 18

HELIX 17 17 ASP B 96 HIS B 112 1 17

HELIX 18 18 SER B 113 ARG B 123 1 11

HELIX 19 19 GLU B 129 ASP B 141 1 13

HELIX 20 20 ASP B 148 PHE B 165 1 18

HELIX 21 21 PHE B 165 ASN B 172 1 8

HELIX 22 22 THR B 177 GLU B 197 1 21

CRYST1 132.305 53.409 55.829 90.00 113.25 90.00 C 1 2 1 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 0.007558 0.000000 0.003247 0.00000

SCALE2 0.000000 0.018723 0.000000 0.00000

SCALE3 0.000000 0.000000 0.019495 0.00000

ATOM 1 N LEU A 3 71.340 -17.709 -36.590 1.00 64.35 N

ATOM 2 CA LEU A 3 72.259 -16.690 -37.290 1.00 64.13 C

ATOM 3 C LEU A 3 71.646 -15.282 -37.211 1.00 63.98 C

ATOM 4 O LEU A 3 71.801 -14.468 -38.132 1.00 63.87 O

ATOM 5 CB LEU A 3 72.516 -17.070 -38.798 1.00 64.16 C

ATOM 6 CG LEU A 3 72.694 -18.613 -39.117 1.00 64.22 C

ATOM 7 CD1 LEU A 3 71.225 -19.316 -39.450 1.00 64.38 C

ATOM 8 CD2 LEU A 3 73.713 -18.710 -40.318 1.00 64.17 C

ATOM 9 N THR A 4 70.972 -14.999 -36.092 1.00 63.83 N

ATOM 10 CA THR A 4 70.125 -13.801 -35.956 1.00 63.57 C

ATOM 11 C THR A 4 70.166 -13.125 -34.568 1.00 63.35 C

ATOM 12 O THR A 4 69.593 -12.031 -34.380 1.00 63.48 O

ATOM 13 CB THR A 4 68.649 -14.110 -36.380 1.00 63.71 C

ATOM 14 OG1 THR A 4 67.745 -13.165 -35.786 1.00 63.63 O

ATOM 15 CG2 THR A 4 68.248 -15.536 -35.980 1.00 63.51 C

ATOM 16 N ASP A 5 70.841 -13.773 -33.612 1.00 62.81 N

ATOM 17 CA ASP A 5 71.023 -13.243 -32.251 1.00 62.27 C

ATOM 18 C ASP A 5 71.690 -11.872 -32.314 1.00 61.83 C

ATOM 19 O ASP A 5 71.119 -10.850 -31.906 1.00 61.51 O

ATOM 20 CB ASP A 5 71.898 -14.187 -31.416 1.00 62.29 C

ATOM 21 CG ASP A 5 71.265 -15.550 -31.209 1.00 62.41 C

ATOM 22 OD1 ASP A 5 71.707 -16.512 -31.878 1.00 62.33 O

ATOM 23 OD2 ASP A 5 70.333 -15.658 -30.378 1.00 61.99 O

ATOM 24 N GLN A 6 72.911 -11.887 -32.849 1.00 61.18 N

ATOM 25 CA GLN A 6 73.689 -10.687 -33.107 1.00 60.32 C

ATOM 26 C GLN A 6 72.854 -9.711 -33.906 1.00 59.55 C

ATOM 27 O GLN A 6 72.678 -8.568 -33.496 1.00 59.68 O

ATOM 28 CB GLN A 6 74.943 -11.034 -33.916 1.00 60.36 C

ATOM 29 CG GLN A 6 75.704 -12.258 -33.419 1.00 60.38 C

ATOM 30 CD GLN A 6 76.395 -13.019 -34.540 1.00 60.35 C

ATOM 31 OE1 GLN A 6 76.377 -14.249 -34.562 1.00 60.43 O

ATOM 32 NE2 GLN A 6 77.000 -12.294 -35.476 1.00 60.24 N

ATOM 33 N LYS A 7 72.319 -10.189 -35.030 1.00 58.50 N

ATOM 34 CA LYS A 7 71.749 -9.325 -36.060 1.00 57.43 C

ATOM 35 C LYS A 7 70.659 -8.360 -35.584 1.00 56.62 C

ATOM 36 O LYS A 7 70.759 -7.161 -35.851 1.00 56.73 O

ATOM 37 CB LYS A 7 71.307 -10.136 -37.281 1.00 57.39 C

ATOM 38 CG LYS A 7 72.469 -10.458 -38.205 1.00 57.60 C

ATOM 39 CD LYS A 7 72.107 -11.495 -39.280 1.00 57.59 C

ATOM 40 CE LYS A 7 73.467 -12.019 -39.947 1.00 57.98 C

ATOM 41 NZ LYS A 7 74.321 -10.891 -40.538 1.00 57.25 N

ATOM 42 N ARG A 8 69.672 -8.842 -34.841 1.00 55.45 N

ATOM 43 CA ARG A 8 68.627 -7.943 -34.401 1.00 54.14 C

ATOM 44 C ARG A 8 69.207 -6.784 -33.636 1.00 53.24 C

ATOM 45 O ARG A 8 69.036 -5.648 -33.990 1.00 52.70 O

ATOM 46 CB ARG A 8 67.601 -8.621 -33.521 1.00 54.14 C

ATOM 47 CG ARG A 8 66.680 -7.589 -32.886 1.00 54.55 C

ATOM 48 CD ARG A 8 65.526 -8.152 -32.108 1.00 55.96 C

ATOM 49 NE ARG A 8 64.233 -7.761 -32.659 1.00 55.41 N

ATOM 50 CZ ARG A 8 63.424 -6.871 -32.111 1.00 54.64 C

ATOM 51 NH1 ARG A 8 62.266 -6.609 -32.671 1.00 54.38 N

ATOM 52 NH2 ARG A 8 63.759 -6.268 -31.000 1.00 53.90 N

ATOM 53 N GLU A 9 69.887 -7.098 -32.564 1.00 52.05 N

ATOM 54 CA GLU A 9 70.469 -6.071 -31.704 1.00 51.08 C

ATOM 55 C GLU A 9 71.359 -5.111 -32.490 1.00 50.33 C

ATOM 56 O GLU A 9 71.293 -3.892 -32.303 1.00 50.13 O

ATOM 57 CB GLU A 9 71.267 -6.706 -30.563 1.00 51.00 C

ATOM 58 CG GLU A 9 71.782 -5.698 -29.530 1.00 51.38 C

ATOM 59 CD GLU A 9 70.664 -4.955 -28.774 1.00 51.60 C

ATOM 60 OE1 GLU A 9 69.469 -5.259 -28.991 1.00 52.13 O

ATOM 61 OE2 GLU A 9 70.987 -4.067 -27.949 1.00 50.24 O

ATOM 62 N SER A 10 72.180 -5.687 -33.364 1.00 49.14 N

ATOM 63 CA SER A 10 73.112 -4.956 -34.202 1.00 48.39 C

ATOM 64 C SER A 10 72.398 -3.929 -35.078 1.00 47.95 C

ATOM 65 O SER A 10 72.907 -2.826 -35.324 1.00 47.28 O

ATOM 66 CB SER A 10 73.865 -5.941 -35.084 1.00 48.30 C

ATOM 67 OG SER A 10 75.005 -5.338 -35.647 1.00 49.35 O

ATOM 68 N ILE A 11 71.210 -4.294 -35.547 1.00 47.34 N

ATOM 69 CA ILE A 11 70.447 -3.379 -36.377 1.00 46.65 C

ATOM 70 C ILE A 11 69.652 -2.365 -35.531 1.00 46.36 C

ATOM 71 O ILE A 11 69.336 -1.279 -36.007 1.00 46.10 O

ATOM 72 CB ILE A 11 69.610 -4.127 -37.502 1.00 46.84 C

ATOM 73 CG1 ILE A 11 68.101 -4.139 -37.228 1.00 47.24 C

ATOM 74 CG2 ILE A 11 70.186 -5.517 -37.827 1.00 45.63 C

ATOM 75 CD1 ILE A 11 67.357 -3.015 -37.968 1.00 46.14 C

ATOM 76 N VAL A 12 69.347 -2.713 -34.281 1.00 45.93 N

ATOM 77 CA VAL A 12 68.706 -1.752 -33.386 1.00 45.73 C

ATOM 78 C VAL A 12 69.749 -0.736 -32.939 1.00 45.60 C

ATOM 79 O VAL A 12 69.439 0.451 -32.805 1.00 45.21 O

ATOM 80 CB VAL A 12 68.014 -2.400 -32.134 1.00 45.94 C

ATOM 81 CG1 VAL A 12 67.218 -1.355 -31.360 1.00 44.82 C

ATOM 82 CG2 VAL A 12 67.105 -3.557 -32.522 1.00 44.89 C

ATOM 83 N GLN A 13 70.977 -1.204 -32.709 1.00 45.51 N

ATOM 84 CA GLN A 13 72.074 -0.306 -32.355 1.00 45.70 C

ATOM 85 C GLN A 13 72.398 0.646 -33.502 1.00 45.37 C

ATOM 86 O GLN A 13 72.561 1.866 -33.305 1.00 45.71 O

ATOM 87 CB GLN A 13 73.317 -1.084 -31.918 1.00 45.90 C

ATOM 88 CG GLN A 13 73.204 -1.716 -30.549 1.00 47.49 C

ATOM 89 CD GLN A 13 72.305 -0.910 -29.619 1.00 50.36 C

ATOM 90 OE1 GLN A 13 72.653 0.199 -29.184 1.00 51.47 O

ATOM 91 NE2 GLN A 13 71.131 -1.463 -29.317 1.00 50.93 N

ATOM 92 N ALA A 14 72.477 0.083 -34.700 1.00 45.16 N

ATOM 93 CA ALA A 14 72.631 0.869 -35.912 1.00 45.06 C

ATOM 94 C ALA A 14 71.597 1.996 -35.937 1.00 45.05 C

ATOM 95 O ALA A 14 71.957 3.174 -35.993 1.00 45.84 O

ATOM 96 CB ALA A 14 72.487 -0.010 -37.118 1.00 44.64 C

ATOM 97 N ALA A 15 70.320 1.629 -35.859 1.00 44.19 N

ATOM 98 CA ALA A 15 69.238 2.592 -35.956 1.00 43.72 C

ATOM 99 C ALA A 15 69.305 3.644 -34.864 1.00 43.75 C

ATOM 100 O ALA A 15 69.025 4.803 -35.132 1.00 43.93 O

ATOM 101 CB ALA A 15 67.882 1.885 -35.955 1.00 43.39 C

ATOM 102 N ILE A 16 69.681 3.241 -33.644 1.00 43.63 N

ATOM 103 CA ILE A 16 69.855 4.168 -32.518 1.00 43.24 C

ATOM 104 C ILE A 16 70.952 5.197 -32.812 1.00 44.01 C

ATOM 105 O ILE A 16 70.759 6.407 -32.595 1.00 43.54 O

ATOM 106 CB ILE A 16 70.163 3.444 -31.186 1.00 43.37 C

ATOM 107 CG1 ILE A 16 68.966 2.623 -30.686 1.00 42.08 C

ATOM 108 CG2 ILE A 16 70.540 4.452 -30.113 1.00 42.79 C

ATOM 109 CD1 ILE A 16 69.297 1.756 -29.505 1.00 38.44 C

ATOM 110 N ALA A 17 72.096 4.713 -33.312 1.00 44.49 N

ATOM 111 CA ALA A 17 73.187 5.599 -33.721 1.00 44.88 C

ATOM 112 C ALA A 17 72.759 6.527 -34.874 1.00 45.41 C

ATOM 113 O ALA A 17 72.979 7.727 -34.810 1.00 45.93 O

ATOM 114 CB ALA A 17 74.455 4.791 -34.086 1.00 44.58 C

ATOM 115 N GLU A 18 72.110 5.984 -35.909 1.00 45.88 N

ATOM 116 CA GLU A 18 71.778 6.785 -37.095 1.00 45.85 C

ATOM 117 C GLU A 18 70.656 7.787 -36.857 1.00 46.58 C

ATOM 118 O GLU A 18 70.796 8.989 -37.180 1.00 46.75 O

ATOM 119 CB GLU A 18 71.481 5.901 -38.300 1.00 46.09 C

ATOM 120 CG GLU A 18 72.676 5.113 -38.807 1.00 44.78 C

ATOM 121 CD GLU A 18 73.713 5.983 -39.469 1.00 46.72 C

ATOM 122 OE1 GLU A 18 73.404 7.145 -39.833 1.00 47.02 O

ATOM 123 OE2 GLU A 18 74.853 5.505 -39.641 1.00 48.03 O

ATOM 124 N PHE A 19 69.551 7.291 -36.299 1.00 46.55 N

ATOM 125 CA PHE A 19 68.475 8.138 -35.796 1.00 46.56 C

ATOM 126 C PHE A 19 69.005 9.265 -34.845 1.00 47.30 C

ATOM 127 O PHE A 19 68.732 10.458 -35.044 1.00 46.01 O

ATOM 128 CB PHE A 19 67.418 7.277 -35.076 1.00 46.72 C

ATOM 129 CG PHE A 19 66.582 6.367 -35.991 1.00 45.91 C

ATOM 130 CD1 PHE A 19 65.925 5.257 -35.453 1.00 47.20 C

ATOM 131 CD2 PHE A 19 66.412 6.634 -37.340 1.00 45.29 C

ATOM 132 CE1 PHE A 19 65.123 4.417 -36.246 1.00 46.56 C

ATOM 133 CE2 PHE A 19 65.622 5.802 -38.147 1.00 45.71 C

ATOM 134 CZ PHE A 19 64.977 4.694 -37.599 1.00 46.82 C

ATOM 135 N GLY A 20 69.770 8.881 -33.815 1.00 47.88 N

ATOM 136 CA GLY A 20 70.337 9.849 -32.865 1.00 48.30 C

ATOM 137 C GLY A 20 71.086 10.997 -33.539 1.00 49.62 C

ATOM 138 O GLY A 20 70.994 12.156 -33.083 1.00 49.55 O

ATOM 139 N ASP A 21 71.817 10.668 -34.616 1.00 49.78 N

ATOM 140 CA ASP A 21 72.583 11.628 -35.409 1.00 50.87 C

ATOM 141 C ASP A 21 71.769 12.546 -36.324 1.00 50.23 C

ATOM 142 O ASP A 21 71.842 13.767 -36.180 1.00 50.90 O

ATOM 143 CB ASP A 21 73.617 10.890 -36.254 1.00 52.24 C

ATOM 144 CG ASP A 21 74.753 10.323 -35.414 1.00 56.52 C

ATOM 145 OD1 ASP A 21 75.059 10.930 -34.349 1.00 59.78 O

ATOM 146 OD2 ASP A 21 75.340 9.278 -35.825 1.00 61.87 O

ATOM 147 N ARG A 22 71.015 11.977 -37.264 1.00 49.05 N

ATOM 148 CA ARG A 22 70.294 12.782 -38.255 1.00 48.35 C

ATOM 149 C ARG A 22 68.757 12.844 -38.102 1.00 47.62 C

ATOM 150 O ARG A 22 68.071 13.469 -38.908 1.00 48.02 O

ATOM 151 CB ARG A 22 70.664 12.328 -39.676 1.00 48.50 C

ATOM 152 CG ARG A 22 72.173 12.258 -39.983 1.00 48.89 C

ATOM 153 CD ARG A 22 72.498 12.090 -41.490 1.00 49.02 C

ATOM 154 NE ARG A 22 71.725 10.998 -42.068 1.00 52.06 N

ATOM 155 CZ ARG A 22 71.048 11.069 -43.209 1.00 54.82 C

ATOM 156 NH1 ARG A 22 71.094 12.171 -43.957 1.00 54.07 N

ATOM 157 NH2 ARG A 22 70.357 10.005 -43.629 1.00 56.78 N

ATOM 158 N GLY A 23 68.209 12.198 -37.085 1.00 47.04 N

ATOM 159 CA GLY A 23 66.768 12.133 -36.906 1.00 46.05 C

ATOM 160 C GLY A 23 66.130 10.888 -37.501 1.00 46.03 C

ATOM 161 O GLY A 23 66.701 10.208 -38.348 1.00 46.33 O

ATOM 162 N PHE A 24 64.911 10.621 -37.064 1.00 45.93 N

ATOM 163 CA PHE A 24 64.171 9.453 -37.449 1.00 45.78 C

ATOM 164 C PHE A 24 63.787 9.465 -38.925 1.00 45.91 C

ATOM 165 O PHE A 24 63.984 8.465 -39.596 1.00 45.98 O

ATOM 166 CB PHE A 24 62.910 9.345 -36.580 1.00 46.07 C

ATOM 167 CG PHE A 24 62.036 8.173 -36.913 1.00 45.62 C

ATOM 168 CD1 PHE A 24 62.305 6.919 -36.382 1.00 45.22 C

ATOM 169 CD2 PHE A 24 60.948 8.325 -37.761 1.00 46.29 C

ATOM 170 CE1 PHE A 24 61.498 5.816 -36.695 1.00 46.31 C

ATOM 171 CE2 PHE A 24 60.130 7.242 -38.072 1.00 47.46 C

ATOM 172 CZ PHE A 24 60.411 5.975 -37.535 1.00 46.25 C

ATOM 173 N GLU A 25 63.255 10.591 -39.413 1.00 45.67 N

ATOM 174 CA GLU A 25 62.602 10.676 -40.727 1.00 45.86 C

ATOM 175 C GLU A 25 63.549 10.561 -41.925 1.00 45.51 C

ATOM 176 O GLU A 25 63.290 9.841 -42.883 1.00 45.10 O

ATOM 177 CB GLU A 25 61.804 11.979 -40.810 1.00 46.59 C

ATOM 178 CG GLU A 25 60.529 12.010 -39.946 1.00 47.80 C

ATOM 179 CD GLU A 25 59.316 11.398 -40.654 1.00 51.42 C

ATOM 180 OE1 GLU A 25 58.339 11.074 -39.950 1.00 53.98 O

ATOM 181 OE2 GLU A 25 59.324 11.228 -41.902 1.00 50.73 O

ATOM 182 N ILE A 26 64.654 11.288 -41.834 1.00 45.98 N

ATOM 183 CA ILE A 26 65.689 11.379 -42.858 1.00 45.26 C

ATOM 184 C ILE A 26 66.519 10.112 -42.885 1.00 45.38 C

ATOM 185 O ILE A 26 67.114 9.802 -43.914 1.00 46.35 O

ATOM 186 CB ILE A 26 66.600 12.617 -42.576 1.00 45.46 C

ATOM 187 CG1 ILE A 26 67.409 13.047 -43.807 1.00 45.23 C

ATOM 188 CG2 ILE A 26 67.490 12.378 -41.377 1.00 44.78 C

ATOM 189 CD1 ILE A 26 68.027 14.468 -43.668 1.00 44.63 C

ATOM 190 N THR A 27 66.584 9.389 -41.766 1.00 45.26 N

ATOM 191 CA THR A 27 67.242 8.078 -41.760 1.00 45.14 C

ATOM 192 C THR A 27 66.340 7.071 -42.484 1.00 45.70 C

ATOM 193 O THR A 27 65.152 6.924 -42.148 1.00 45.92 O

ATOM 194 CB THR A 27 67.613 7.573 -40.339 1.00 44.72 C

ATOM 195 OG1 THR A 27 68.326 8.581 -39.628 1.00 43.89 O

ATOM 196 CG2 THR A 27 68.514 6.356 -40.412 1.00 45.38 C

ATOM 197 N SER A 28 66.912 6.416 -43.495 1.00 45.81 N

ATOM 198 CA SER A 28 66.237 5.413 -44.291 1.00 46.29 C

ATOM 199 C SER A 28 66.803 4.051 -43.971 1.00 46.89 C

ATOM 200 O SER A 28 67.909 3.934 -43.451 1.00 46.96 O

ATOM 201 CB SER A 28 66.483 5.676 -45.772 1.00 46.37 C

ATOM 202 OG SER A 28 67.841 5.386 -46.094 1.00 46.21 O

HETATM 203 N MSE A 29 66.061 3.024 -44.363 1.00 47.42 N

HETATM 204 CA MSE A 29 66.368 1.648 -44.031 1.00 48.21 C

HETATM 205 C MSE A 29 67.722 1.137 -44.492 1.00 48.06 C

HETATM 206 O MSE A 29 68.445 0.498 -43.708 1.00 48.09 O

HETATM 207 CB MSE A 29 65.315 0.734 -44.630 1.00 49.32 C

HETATM 208 CG MSE A 29 64.873 -0.301 -43.676 1.00 51.54 C

HETATM 209 SE MSE A 29 63.989 0.624 -42.213 0.85 59.45 SE

HETATM 210 CE MSE A 29 62.458 -0.603 -42.109 1.00 53.55 C

ATOM 211 N ASP A 30 68.063 1.350 -45.760 1.00 47.24 N

ATOM 212 CA ASP A 30 69.334 0.800 -46.190 1.00 46.93 C

ATOM 213 C ASP A 30 70.506 1.661 -45.761 1.00 45.73 C

ATOM 214 O ASP A 30 71.642 1.282 -45.935 1.00 45.55 O

ATOM 215 CB ASP A 30 69.372 0.274 -47.655 1.00 47.85 C

ATOM 216 CG ASP A 30 69.049 1.330 -48.698 1.00 48.88 C

ATOM 217 OD1 ASP A 30 68.858 2.508 -48.335 1.00 51.48 O

ATOM 218 OD2 ASP A 30 69.005 0.960 -49.893 1.00 48.46 O

ATOM 219 N ARG A 31 70.206 2.788 -45.127 1.00 45.21 N

ATOM 220 CA ARG A 31 71.212 3.550 -44.393 1.00 44.71 C

ATOM 221 C ARG A 31 71.500 2.869 -43.061 1.00 44.03 C

ATOM 222 O ARG A 31 72.651 2.733 -42.650 1.00 44.58 O

ATOM 223 CB ARG A 31 70.758 4.988 -44.163 1.00 44.51 C

ATOM 224 CG ARG A 31 71.542 5.714 -43.104 1.00 44.71 C

ATOM 225 CD ARG A 31 72.859 6.176 -43.662 1.00 49.05 C

ATOM 226 NE ARG A 31 73.481 7.234 -42.864 1.00 52.05 N

ATOM 227 CZ ARG A 31 73.784 8.453 -43.300 1.00 53.26 C

ATOM 228 NH1 ARG A 31 74.363 9.312 -42.476 1.00 54.39 N

ATOM 229 NH2 ARG A 31 73.536 8.817 -44.552 1.00 53.58 N

ATOM 230 N ILE A 32 70.444 2.452 -42.387 1.00 43.17 N

ATOM 231 CA ILE A 32 70.577 1.606 -41.206 1.00 43.06 C

ATOM 232 C ILE A 32 71.214 0.245 -41.544 1.00 42.75 C

ATOM 233 O ILE A 32 72.106 -0.203 -40.825 1.00 42.53 O

ATOM 234 CB ILE A 32 69.223 1.413 -40.525 1.00 43.00 C

ATOM 235 CG1 ILE A 32 68.803 2.724 -39.882 1.00 41.33 C

ATOM 236 CG2 ILE A 32 69.283 0.248 -39.524 1.00 43.18 C

ATOM 237 CD1 ILE A 32 67.344 2.879 -39.690 1.00 43.13 C

ATOM 238 N ALA A 33 70.761 -0.379 -42.637 1.00 42.66 N

ATOM 239 CA ALA A 33 71.348 -1.628 -43.167 1.00 42.87 C

ATOM 240 C ALA A 33 72.845 -1.524 -43.404 1.00 43.09 C

ATOM 241 O ALA A 33 73.585 -2.491 -43.173 1.00 42.98 O

ATOM 242 CB ALA A 33 70.655 -2.047 -44.462 1.00 42.97 C

ATOM 243 N ALA A 34 73.281 -0.351 -43.866 1.00 43.13 N

ATOM 244 CA ALA A 34 74.697 -0.091 -44.086 1.00 43.94 C

ATOM 245 C ALA A 34 75.500 0.008 -42.786 1.00 44.26 C

ATOM 246 O ALA A 34 76.531 -0.628 -42.653 1.00 44.32 O

ATOM 247 CB ALA A 34 74.894 1.151 -44.936 1.00 43.63 C

ATOM 248 N ARG A 35 75.025 0.801 -41.838 1.00 45.24 N

ATOM 249 CA ARG A 35 75.699 0.954 -40.556 1.00 46.30 C

ATOM 250 C ARG A 35 75.734 -0.348 -39.757 1.00 47.00 C

ATOM 251 O ARG A 35 76.667 -0.585 -38.981 1.00 47.11 O

ATOM 252 CB ARG A 35 75.032 2.050 -39.737 1.00 46.34 C

ATOM 253 CG ARG A 35 75.718 2.292 -38.402 1.00 47.44 C

ATOM 254 CD ARG A 35 76.907 3.215 -38.551 1.00 49.82 C

ATOM 255 NE ARG A 35 76.525 4.569 -38.168 1.00 50.70 N

ATOM 256 CZ ARG A 35 76.867 5.134 -37.015 1.00 51.85 C

ATOM 257 NH1 ARG A 35 76.452 6.376 -36.734 1.00 52.34 N

ATOM 258 NH2 ARG A 35 77.626 4.453 -36.146 1.00 49.79 N

ATOM 259 N ALA A 36 74.713 -1.183 -39.948 1.00 47.83 N

ATOM 260 CA ALA A 36 74.625 -2.489 -39.301 1.00 48.20 C

ATOM 261 C ALA A 36 75.326 -3.578 -40.104 1.00 48.82 C

ATOM 262 O ALA A 36 75.473 -4.716 -39.630 1.00 49.03 O

ATOM 263 CB ALA A 36 73.175 -2.859 -39.073 1.00 48.32 C

ATOM 264 N GLU A 37 75.741 -3.237 -41.320 1.00 49.24 N

ATOM 265 CA GLU A 37 76.505 -4.140 -42.171 1.00 50.04 C

ATOM 266 C GLU A 37 75.731 -5.406 -42.542 1.00 50.37 C

ATOM 267 O GLU A 37 76.290 -6.498 -42.590 1.00 50.42 O

ATOM 268 CB GLU A 37 77.828 -4.509 -41.506 1.00 50.09 C

ATOM 269 CG GLU A 37 78.747 -3.339 -41.243 1.00 51.25 C

ATOM 270 CD GLU A 37 80.134 -3.790 -40.834 1.00 52.40 C

ATOM 271 OE1 GLU A 37 80.730 -3.154 -39.943 1.00 53.02 O

ATOM 272 OE2 GLU A 37 80.631 -4.787 -41.402 1.00 53.80 O

ATOM 273 N VAL A 38 74.440 -5.238 -42.802 1.00 51.05 N

ATOM 274 CA VAL A 38 73.557 -6.320 -43.225 1.00 51.84 C

ATOM 275 C VAL A 38 72.789 -5.843 -44.448 1.00 52.75 C

ATOM 276 O VAL A 38 72.656 -4.646 -44.671 1.00 52.67 O

ATOM 277 CB VAL A 38 72.543 -6.732 -42.113 1.00 51.58 C

ATOM 278 CG1 VAL A 38 73.218 -7.540 -41.026 1.00 51.47 C

ATOM 279 CG2 VAL A 38 71.855 -5.500 -41.500 1.00 51.81 C

ATOM 280 N SER A 39 72.285 -6.787 -45.234 1.00 54.35 N

ATOM 281 CA SER A 39 71.443 -6.495 -46.398 1.00 55.67 C

ATOM 282 C SER A 39 70.195 -5.722 -45.955 1.00 56.45 C

ATOM 283 O SER A 39 69.794 -5.795 -44.788 1.00 56.42 O

ATOM 284 CB SER A 39 71.069 -7.811 -47.109 1.00 55.81 C

ATOM 285 OG SER A 39 70.162 -7.612 -48.180 1.00 56.17 O

ATOM 286 N LYS A 40 69.606 -4.962 -46.879 1.00 57.48 N

ATOM 287 CA LYS A 40 68.365 -4.231 -46.610 1.00 58.36 C

ATOM 288 C LYS A 40 67.205 -5.199 -46.309 1.00 58.96 C

ATOM 289 O LYS A 40 66.394 -4.943 -45.417 1.00 59.08 O

ATOM 290 CB LYS A 40 68.025 -3.311 -47.788 1.00 58.41 C

ATOM 291 CG LYS A 40 66.966 -2.230 -47.517 1.00 58.26 C

ATOM 292 CD LYS A 40 66.533 -1.596 -48.839 1.00 58.73 C

ATOM 293 CE LYS A 40 65.816 -0.266 -48.665 1.00 58.95 C

ATOM 294 NZ LYS A 40 65.193 0.158 -49.961 1.00 59.03 N

ATOM 295 N ARG A 41 67.158 -6.337 -46.973 1.00 59.55 N

ATOM 296 CA ARG A 41 66.108 -7.280 -46.673 1.00 60.23 C

ATOM 297 C ARG A 41 66.350 -7.875 -45.307 1.00 60.60 C

ATOM 298 O ARG A 41 65.422 -8.205 -44.598 1.00 60.80 O

ATOM 299 CB ARG A 41 66.044 -8.358 -47.736 1.00 60.22 C

ATOM 300 CG ARG A 41 65.153 -8.009 -48.915 1.00 60.68 C

ATOM 301 CD ARG A 41 65.702 -8.564 -50.222 1.00 61.37 C

ATOM 302 NE ARG A 41 65.070 -7.969 -51.398 1.00 60.58 N

ATOM 303 CZ ARG A 41 65.264 -6.722 -51.807 1.00 60.22 C

ATOM 304 NH1 ARG A 41 66.078 -5.920 -51.129 1.00 59.51 N

ATOM 305 NH2 ARG A 41 64.644 -6.276 -52.887 1.00 59.67 N

ATOM 306 N THR A 42 67.605 -7.986 -44.925 1.00 60.84 N

ATOM 307 CA THR A 42 67.951 -8.551 -43.616 1.00 60.91 C

ATOM 308 C THR A 42 67.371 -7.679 -42.490 1.00 61.29 C

ATOM 309 O THR A 42 66.886 -8.193 -41.473 1.00 60.96 O

ATOM 310 CB THR A 42 69.486 -8.733 -43.460 1.00 60.85 C

ATOM 311 OG1 THR A 42 70.013 -9.426 -44.603 1.00 59.93 O

ATOM 312 CG2 THR A 42 69.818 -9.527 -42.200 1.00 60.59 C

ATOM 313 N VAL A 43 67.424 -6.362 -42.697 1.00 61.78 N

ATOM 314 CA VAL A 43 66.772 -5.378 -41.833 1.00 62.27 C

ATOM 315 C VAL A 43 65.249 -5.460 -41.993 1.00 62.62 C

ATOM 316 O VAL A 43 64.503 -5.372 -41.008 1.00 62.89 O

ATOM 317 CB VAL A 43 67.244 -3.927 -42.172 1.00 62.41 C

ATOM 318 CG1 VAL A 43 66.364 -2.877 -41.496 1.00 62.55 C

ATOM 319 CG2 VAL A 43 68.701 -3.715 -41.786 1.00 62.11 C

ATOM 320 N TYR A 44 64.803 -5.640 -43.239 1.00 62.72 N

ATOM 321 CA TYR A 44 63.390 -5.498 -43.586 1.00 62.58 C

ATOM 322 C TYR A 44 62.530 -6.651 -43.098 1.00 61.86 C

ATOM 323 O TYR A 44 61.307 -6.530 -43.055 1.00 62.00 O

ATOM 324 CB TYR A 44 63.190 -5.268 -45.095 1.00 63.29 C

ATOM 325 CG TYR A 44 62.764 -3.850 -45.471 1.00 64.31 C

ATOM 326 CD1 TYR A 44 63.602 -3.023 -46.221 1.00 65.60 C

ATOM 327 CD2 TYR A 44 61.516 -3.340 -45.082 1.00 64.96 C

ATOM 328 CE1 TYR A 44 63.217 -1.714 -46.572 1.00 65.73 C

ATOM 329 CE2 TYR A 44 61.119 -2.035 -45.432 1.00 65.40 C

ATOM 330 CZ TYR A 44 61.977 -1.230 -46.179 1.00 65.23 C

ATOM 331 OH TYR A 44 61.604 0.051 -46.535 1.00 64.94 O

ATOM 332 N ASN A 45 63.165 -7.762 -42.731 1.00 60.94 N

ATOM 333 CA ASN A 45 62.440 -8.891 -42.148 1.00 59.60 C

ATOM 334 C ASN A 45 62.559 -8.966 -40.618 1.00 59.07 C

ATOM 335 O ASN A 45 61.908 -9.802 -39.978 1.00 59.19 O

ATOM 336 CB ASN A 45 62.811 -10.219 -42.841 1.00 59.51 C

ATOM 337 CG ASN A 45 64.241 -10.674 -42.558 1.00 58.46 C

ATOM 338 OD1 ASN A 45 64.821 -11.454 -43.355 1.00 56.66 O

ATOM 339 ND2 ASN A 45 64.806 -10.201 -41.427 1.00 58.08 N

ATOM 340 N HIS A 46 63.390 -8.087 -40.045 1.00 58.34 N

ATOM 341 CA HIS A 46 63.471 -7.932 -38.593 1.00 57.43 C

ATOM 342 C HIS A 46 62.512 -6.830 -38.160 1.00 56.88 C

ATOM 343 O HIS A 46 61.692 -7.030 -37.256 1.00 56.89 O

ATOM 344 CB HIS A 46 64.906 -7.638 -38.129 1.00 57.49 C

ATOM 345 CG HIS A 46 65.667 -8.855 -37.700 1.00 57.35 C

ATOM 346 ND1 HIS A 46 65.208 -9.718 -36.726 1.00 58.40 N

ATOM 347 CD2 HIS A 46 66.860 -9.351 -38.106 1.00 57.74 C

ATOM 348 CE1 HIS A 46 66.079 -10.697 -36.557 1.00 58.42 C

ATOM 349 NE2 HIS A 46 67.093 -10.496 -37.381 1.00 58.45 N

ATOM 350 N PHE A 47 62.617 -5.677 -38.826 1.00 56.03 N

ATOM 351 CA PHE A 47 61.646 -4.606 -38.673 1.00 55.02 C

ATOM 352 C PHE A 47 60.906 -4.384 -39.992 1.00 54.30 C

ATOM 353 O PHE A 47 61.352 -3.598 -40.827 1.00 54.01 O

ATOM 354 CB PHE A 47 62.335 -3.321 -38.222 1.00 54.92 C

ATOM 355 CG PHE A 47 62.913 -3.397 -36.829 1.00 55.40 C

ATOM 356 CD1 PHE A 47 62.129 -3.103 -35.704 1.00 55.18 C

ATOM 357 CD2 PHE A 47 64.247 -3.761 -36.637 1.00 55.95 C

ATOM 358 CE1 PHE A 47 62.666 -3.208 -34.421 1.00 54.84 C

ATOM 359 CE2 PHE A 47 64.790 -3.826 -35.342 1.00 55.16 C

ATOM 360 CZ PHE A 47 63.996 -3.581 -34.237 1.00 54.61 C

ATOM 361 N PRO A 48 59.766 -5.085 -40.176 1.00 53.76 N

ATOM 362 CA PRO A 48 58.926 -5.104 -41.379 1.00 53.30 C

ATOM 363 C PRO A 48 58.620 -3.724 -41.950 1.00 53.21 C

ATOM 364 O PRO A 48 58.214 -3.618 -43.145 1.00 52.80 O

ATOM 365 CB PRO A 48 57.629 -5.741 -40.883 1.00 53.60 C

ATOM 366 CG PRO A 48 58.056 -6.644 -39.795 1.00 53.74 C

ATOM 367 CD PRO A 48 59.211 -5.947 -39.116 1.00 53.70 C

ATOM 368 N SER A 49 58.820 -2.692 -41.093 1.00 52.91 N

ATOM 369 CA SER A 49 58.545 -1.293 -41.424 1.00 52.73 C

ATOM 370 C SER A 49 59.400 -0.349 -40.560 1.00 52.46 C

ATOM 371 O SER A 49 59.888 -0.737 -39.494 1.00 52.05 O

ATOM 372 CB SER A 49 57.058 -0.986 -41.184 1.00 52.83 C

ATOM 373 OG SER A 49 56.693 -1.280 -39.830 1.00 53.58 O

ATOM 374 N LYS A 50 59.581 0.887 -41.027 1.00 52.33 N

ATOM 375 CA LYS A 50 60.230 1.927 -40.225 1.00 52.42 C

ATOM 376 C LYS A 50 59.436 2.209 -38.964 1.00 52.68 C

ATOM 377 O LYS A 50 59.991 2.607 -37.943 1.00 52.72 O

ATOM 378 CB LYS A 50 60.375 3.219 -41.013 1.00 52.10 C

ATOM 379 CG LYS A 50 61.704 3.365 -41.711 1.00 52.26 C

ATOM 380 CD LYS A 50 61.956 4.796 -42.182 1.00 52.79 C

ATOM 381 CE LYS A 50 62.346 5.721 -41.022 1.00 50.91 C

ATOM 382 NZ LYS A 50 62.435 7.107 -41.518 1.00 50.48 N

ATOM 383 N GLU A 51 58.127 1.999 -39.043 1.00 53.18 N

ATOM 384 CA GLU A 51 57.251 2.184 -37.893 1.00 53.61 C

ATOM 385 C GLU A 51 57.488 1.177 -36.774 1.00 53.60 C

ATOM 386 O GLU A 51 57.292 1.502 -35.603 1.00 53.79 O

ATOM 387 CB GLU A 51 55.783 2.213 -38.327 1.00 53.83 C

ATOM 388 CG GLU A 51 55.456 3.429 -39.190 1.00 54.16 C

ATOM 389 CD GLU A 51 55.766 4.757 -38.506 1.00 53.49 C

ATOM 390 OE1 GLU A 51 56.831 4.899 -37.865 1.00 54.04 O

ATOM 391 OE2 GLU A 51 54.935 5.674 -38.615 1.00 53.46 O

ATOM 392 N GLU A 52 57.920 -0.034 -37.125 1.00 53.27 N

ATOM 393 CA GLU A 52 58.331 -0.992 -36.101 1.00 53.15 C

ATOM 394 C GLU A 52 59.661 -0.583 -35.441 1.00 52.47 C

ATOM 395 O GLU A 52 59.932 -0.962 -34.303 1.00 52.74 O

ATOM 396 CB GLU A 52 58.388 -2.425 -36.650 1.00 53.14 C

ATOM 397 CG GLU A 52 57.734 -3.457 -35.711 1.00 53.58 C

ATOM 398 CD GLU A 52 58.389 -4.869 -35.842 1.00 53.97 C

ATOM 399 OE1 GLU A 52 57.631 -5.883 -36.031 1.00 54.86 O

ATOM 400 OE2 GLU A 52 59.668 -4.969 -35.753 1.00 54.54 O

ATOM 401 N LEU A 53 60.479 0.192 -36.149 1.00 51.79 N

ATOM 402 CA LEU A 53 61.674 0.788 -35.553 1.00 51.09 C

ATOM 403 C LEU A 53 61.297 1.814 -34.491 1.00 50.80 C

ATOM 404 O LEU A 53 61.851 1.799 -33.388 1.00 51.40 O

ATOM 405 CB LEU A 53 62.579 1.455 -36.605 1.00 50.84 C

ATOM 406 CG LEU A 53 63.759 0.756 -37.312 1.00 50.20 C

ATOM 407 CD1 LEU A 53 64.578 -0.170 -36.414 1.00 49.00 C

ATOM 408 CD2 LEU A 53 63.264 0.005 -38.517 1.00 51.68 C

ATOM 409 N PHE A 54 60.371 2.713 -34.825 1.00 50.14 N

ATOM 410 CA PHE A 54 59.926 3.759 -33.891 1.00 49.44 C

ATOM 411 C PHE A 54 59.354 3.167 -32.608 1.00 49.52 C

ATOM 412 O PHE A 54 59.630 3.666 -31.509 1.00 49.41 O

ATOM 413 CB PHE A 54 58.890 4.670 -34.545 1.00 49.31 C

ATOM 414 CG PHE A 54 58.294 5.671 -33.607 1.00 49.49 C

ATOM 415 CD1 PHE A 54 58.985 6.843 -33.286 1.00 49.33 C

ATOM 416 CD2 PHE A 54 57.054 5.445 -33.030 1.00 48.67 C

ATOM 417 CE1 PHE A 54 58.443 7.771 -32.424 1.00 49.61 C

ATOM 418 CE2 PHE A 54 56.514 6.371 -32.154 1.00 49.59 C

ATOM 419 CZ PHE A 54 57.206 7.537 -31.853 1.00 48.89 C

ATOM 420 N ALA A 55 58.553 2.109 -32.763 1.00 49.16 N

ATOM 421 CA ALA A 55 58.031 1.356 -31.643 1.00 49.32 C

ATOM 422 C ALA A 55 59.166 0.873 -30.746 1.00 49.74 C

ATOM 423 O ALA A 55 59.086 1.008 -29.521 1.00 49.44 O

ATOM 424 CB ALA A 55 57.199 0.171 -32.140 1.00 49.10 C

ATOM 425 N GLU A 56 60.226 0.331 -31.360 1.00 50.40 N

ATOM 426 CA GLU A 56 61.336 -0.270 -30.620 1.00 51.11 C

ATOM 427 C GLU A 56 62.124 0.821 -29.965 1.00 51.52 C

ATOM 428 O GLU A 56 62.685 0.628 -28.895 1.00 51.89 O

ATOM 429 CB GLU A 56 62.261 -1.067 -31.535 1.00 51.26 C

ATOM 430 CG GLU A 56 62.564 -2.499 -31.040 1.00 53.65 C

ATOM 431 CD GLU A 56 63.204 -2.578 -29.652 1.00 55.21 C

ATOM 432 OE1 GLU A 56 62.527 -3.069 -28.720 1.00 56.54 O

ATOM 433 OE2 GLU A 56 64.377 -2.169 -29.496 1.00 55.87 O

HETATM 434 N MSE A 57 62.155 1.975 -30.624 1.00 51.81 N

HETATM 435 CA MSE A 57 62.812 3.155 -30.106 1.00 52.57 C

HETATM 436 C MSE A 57 62.172 3.573 -28.780 1.00 52.30 C

HETATM 437 O MSE A 57 62.855 4.025 -27.863 1.00 51.77 O

HETATM 438 CB MSE A 57 62.708 4.282 -31.135 1.00 53.17 C

HETATM 439 CG MSE A 57 64.019 4.926 -31.472 1.00 55.26 C

HETATM 440 SE MSE A 57 65.481 3.659 -31.838 1.00 59.58 SE

HETATM 441 CE MSE A 57 66.908 4.920 -31.459 1.00 55.82 C

ATOM 442 N LEU A 58 60.858 3.402 -28.685 1.00 52.20 N

ATOM 443 CA LEU A 58 60.141 3.698 -27.452 1.00 52.56 C

ATOM 444 C LEU A 58 60.449 2.709 -26.346 1.00 52.86 C

ATOM 445 O LEU A 58 60.742 3.102 -25.217 1.00 53.08 O

ATOM 446 CB LEU A 58 58.639 3.752 -27.701 1.00 52.38 C

ATOM 447 CG LEU A 58 58.207 5.039 -28.382 1.00 52.03 C

ATOM 448 CD1 LEU A 58 56.696 5.064 -28.505 1.00 51.91 C

ATOM 449 CD2 LEU A 58 58.715 6.234 -27.594 1.00 52.15 C

ATOM 450 N GLN A 59 60.373 1.425 -26.677 1.00 53.30 N

ATOM 451 CA GLN A 59 60.714 0.370 -25.739 1.00 53.66 C

ATOM 452 C GLN A 59 62.034 0.697 -25.027 1.00 54.02 C

ATOM 453 O GLN A 59 62.107 0.672 -23.799 1.00 54.10 O

ATOM 454 CB GLN A 59 60.793 -0.971 -26.474 1.00 53.47 C

ATOM 455 CG GLN A 59 61.262 -2.128 -25.618 1.00 53.27 C

ATOM 456 CD GLN A 59 60.213 -2.609 -24.602 1.00 52.50 C

ATOM 457 OE1 GLN A 59 59.288 -1.865 -24.200 1.00 51.49 O

ATOM 458 NE2 GLN A 59 60.367 -3.869 -24.175 1.00 52.50 N

ATOM 459 N ARG A 60 63.051 1.025 -25.820 1.00 54.47 N

ATOM 460 CA ARG A 60 64.364 1.429 -25.340 1.00 55.02 C

ATOM 461 C ARG A 60 64.294 2.625 -24.415 1.00 55.74 C

ATOM 462 O ARG A 60 64.824 2.595 -23.307 1.00 56.19 O

ATOM 463 CB ARG A 60 65.250 1.787 -26.532 1.00 54.96 C

ATOM 464 CG ARG A 60 65.530 0.641 -27.454 1.00 53.92 C

ATOM 465 CD ARG A 60 66.579 -0.220 -26.843 1.00 52.32 C

ATOM 466 NE ARG A 60 66.680 -1.503 -27.510 1.00 52.54 N

ATOM 467 CZ ARG A 60 67.766 -2.265 -27.471 1.00 51.90 C

ATOM 468 NH1 ARG A 60 68.845 -1.855 -26.807 1.00 51.65 N

ATOM 469 NH2 ARG A 60 67.780 -3.424 -28.109 1.00 51.60 N

ATOM 470 N LEU A 61 63.639 3.684 -24.873 1.00 56.68 N

ATOM 471 CA LEU A 61 63.479 4.883 -24.060 1.00 57.76 C

ATOM 472 C LEU A 61 62.855 4.544 -22.718 1.00 58.40 C

ATOM 473 O LEU A 61 63.231 5.106 -21.692 1.00 58.55 O