HEADER TOXIN 27-APR-07 2POS

TITLE CRYSTAL STRUCTURE OF SYLVATICIN, A NEW SECRETED PROTEIN

TITLE 2 FROM PYTHIUM SYLVATICUM

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: SYLVATICIN;

COMPND 3 CHAIN: A, B, C, D

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: PYTHIUM SYLVATICUM;

SOURCE 3 STRAIN: STRAIN 37

KEYWDS SYLVATICIN, ELICITIN, TOXIN

EXPDTA X-RAY DIFFRACTION

AUTHOR M.B.LASCOMBE,T.PRANGE

REVDAT 1 18-MAR-08 2POS 0

JRNL AUTH M.B.LASCOMBE,P.RETAILLEAU,M.PONCHET,B.INDUSTRI,

JRNL AUTH 2 J.P.BLEIN,T.PRANGE

JRNL TITL STRUCTURE OF SYLVATICIN, A NEW ALPHA-ELICITIN-LIKE

JRNL TITL 2 PROTEIN FROM PYTHIUM SYLVATICUM.

JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 1102 2007

JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449

REMARK 1

REMARK 1 REFERENCE 1

REMARK 1 AUTH M.B.LASCOMBE,M.PONCHET,L.CARDIN,M.L.MILAT,

REMARK 1 AUTH 2 J.P.BLEIN,T.PRANGE

REMARK 1 TITL PURIFICATION,CRYSTALLISATION AND PRELIMINARY X-RAY

REMARK 1 TITL 2 STUDIES OF SYLVATICIN, AN ELICITIN-LIKE PROTEIN

REMARK 1 TITL 3 FROM PYTHIUM SYLVATICUM

REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. D60 362 2004

REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449

REMARK 2

REMARK 2 RESOLUTION. 1.60 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) : 1.60

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.06

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

REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9

REMARK 3 NUMBER OF REFLECTIONS : 40262

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) : 0.152

REMARK 3 R VALUE (WORKING SET) : 0.150

REMARK 3 FREE R VALUE : 0.187

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

REMARK 3 FREE R VALUE TEST SET COUNT : 2024

REMARK 3

REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.

REMARK 3 TOTAL NUMBER OF BINS USED : 20

REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60

REMARK 3 BIN RESOLUTION RANGE LOW : 1.64

REMARK 3 REFLECTION IN BIN (WORKING SET) : 2875

REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.67

REMARK 3 BIN R VALUE (WORKING SET) : 0.1640

REMARK 3 BIN FREE R VALUE SET COUNT : 146

REMARK 3 BIN FREE R VALUE : 0.2000

REMARK 3

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

REMARK 3 ALL ATOMS : 3701

REMARK 3

REMARK 3 B VALUES.

REMARK 3 FROM WILSON PLOT (A**2) : 17.30

REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.77

REMARK 3 OVERALL ANISOTROPIC B VALUE.

REMARK 3 B11 (A**2) : -0.01000

REMARK 3 B22 (A**2) : 0.00000

REMARK 3 B33 (A**2) : 0.00000

REMARK 3 B12 (A**2) : 0.00000

REMARK 3 B13 (A**2) : 0.01000

REMARK 3 B23 (A**2) : 0.00000

REMARK 3

REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.

REMARK 3 ESU BASED ON R VALUE (A): 0.100

REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097

REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058

REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.630

REMARK 3

REMARK 3 CORRELATION COEFFICIENTS.

REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965

REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT

REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3057 ; 0.007 ; 0.022

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

REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4176 ; 1.110 ; 1.993

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

REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 4.767 ; 5.000

REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;27.403 ;26.033

REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 494 ;11.806 ;15.000

REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ; 6.956 ;15.000

REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.070 ; 0.200

REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2296 ; 0.003 ; 0.020

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

REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1580 ; 0.205 ; 0.200

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

REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2181 ; 0.307 ; 0.200

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

REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 578 ; 0.151 ; 0.200

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

REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.007 ; 0.200

REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL

REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 129 ; 0.169 ; 0.200

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

REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 93 ; 0.109 ; 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): 1970 ; 0.497 ; 1.500

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

REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3120 ; 0.897 ; 2.000

REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1223 ; 1.610 ; 3.000

REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1056 ; 2.647 ; 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 : 0

REMARK 3

REMARK 3 BULK SOLVENT MODELLING.

REMARK 3 METHOD USED : BABINET MODEL WITH MASK

REMARK 3 PARAMETERS FOR MASK CALCULATION

REMARK 3 VDW PROBE RADIUS : 1.40

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 2POS 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 RCSB042614.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION : 03-MAR-2007

REMARK 200 TEMPERATURE (KELVIN) : 100.0

REMARK 200 PH : 8.50

REMARK 200 NUMBER OF CRYSTALS USED : 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) : Y

REMARK 200 RADIATION SOURCE : ESRF

REMARK 200 BEAMLINE : ID14-3

REMARK 200 X-RAY GENERATOR MODEL : NULL

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

REMARK 200 WAVELENGTH OR RANGE (A) : 0.931

REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)

REMARK 200 OPTICS : NULL

REMARK 200

REMARK 200 DETECTOR TYPE : AREA DETECTOR

REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4

REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS

REMARK 200 DATA SCALING SOFTWARE : XDS

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40560

REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600

REMARK 200 RESOLUTION RANGE LOW (A) : 33.000

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

REMARK 200

REMARK 200 OVERALL.

REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0

REMARK 200 DATA REDUNDANCY : 2.000

REMARK 200 R MERGE (I) : 0.04800

REMARK 200 R SYM (I) : 0.04100

REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69

REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3

REMARK 200 DATA REDUNDANCY IN SHELL : 2.00

REMARK 200 R MERGE FOR SHELL (I) : 0.12000

REMARK 200 R SYM FOR SHELL (I) : 0.10000

REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.220

REMARK 200

REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH

REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT

REMARK 200 SOFTWARE USED: PHASER

REMARK 200 STARTING MODEL: SYLVATICIN C2

REMARK 200

REMARK 200 REMARK: NULL

REMARK 280

REMARK 280 CRYSTAL

REMARK 280 SOLVENT CONTENT, VS (%): 39.54

REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03

REMARK 280

REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 2000MME, 10MM NICL2, 0.1M

REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1

REMARK 290

REMARK 290 SYMOP SYMMETRY

REMARK 290 NNNMMM OPERATOR

REMARK 290 1555 X,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

REMARK 290 REMARK: NULL

REMARK 300

REMARK 300 BIOMOLECULE: 1, 2, 3, 4

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

REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN

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

REMARK 300 BURIED SURFACE AREA.

REMARK 300

REMARK 300 REMARK: MONOMER

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 APPLY THE FOLLOWING TO CHAINS: A

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 350

REMARK 350 BIOMOLECULE: 2

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: B

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 350

REMARK 350 BIOMOLECULE: 3

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: C

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 350

REMARK 350 BIOMOLECULE: 4

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: D

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000

REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000

REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT

REMARK 500

REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.

REMARK 500

REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI

REMARK 500 OD1 ASP A 77 CL CL A 3000 2.09

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 B 4 -33.09 -134.27

REMARK 500

REMARK 500 REMARK: NULL

REMARK 620

REMARK 620 METAL COORDINATION

REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;

REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NI A 100 NI

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 TRP A 1 N

REMARK 620 2 TRP A 1 O 81.0

REMARK 620 3 PHE B 94 OXT 88.3 94.6

REMARK 620 4 TRS A2003 N 102.0 173.1 91.7

REMARK 620 5 TRS A2003 O1 95.0 92.6 172.5 81.1

REMARK 620 6 TRS A2003 O2 176.0 95.6 94.0 81.1 83.1

REMARK 620 N 1 2 3 4 5

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NI B 100 NI

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 PHE A 94 OXT

REMARK 620 2 TRP B 1 N 86.3

REMARK 620 3 TRP B 1 O 99.0 80.2

REMARK 620 4 HOH A3173 O 88.4 167.9 90.0

REMARK 620 5 TRS B2000 O3 164.5 96.1 96.6 91.9

REMARK 620 6 TRS B2000 N 85.6 101.0 175.4 89.4 78.9

REMARK 620 N 1 2 3 4 5

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NI C 100 NI

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 TRP C 1 N

REMARK 620 2 TRP C 1 O 81.2

REMARK 620 3 HOH C2018 O 167.0 88.2

REMARK 620 4 TRS C2001 O2 96.5 97.4 92.3

REMARK 620 5 TRS C2001 N 103.1 175.6 87.6 81.3

REMARK 620 N 1 2 3 4

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NI D 100 NI

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 TRP D 1 N

REMARK 620 2 TRP D 1 O 79.9

REMARK 620 3 TRS D2002 O1 94.7 93.3

REMARK 620 4 TRS D2002 N 96.6 168.9 76.4

REMARK 620 N 1 2 3

REMARK 800

REMARK 800 SITE

REMARK 800 SITE_IDENTIFIER: AC1

REMARK 800 SITE_DESCRIPTION: NI BINDING SITE FOR RESIDUE B 100

REMARK 800 SITE_IDENTIFIER: AC2

REMARK 800 SITE_DESCRIPTION: NI BINDING SITE FOR RESIDUE C 100

REMARK 800 SITE_IDENTIFIER: AC3

REMARK 800 SITE_DESCRIPTION: NI BINDING SITE FOR RESIDUE D 100

REMARK 800 SITE_IDENTIFIER: AC4

REMARK 800 SITE_DESCRIPTION: NI BINDING SITE FOR RESIDUE A 100

REMARK 800 SITE_IDENTIFIER: AC5

REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE A 3000

REMARK 800 SITE_IDENTIFIER: AC6

REMARK 800 SITE_DESCRIPTION: TRS BINDING SITE FOR RESIDUE B 2000

REMARK 800 SITE_IDENTIFIER: AC7

REMARK 800 SITE_DESCRIPTION: TRS BINDING SITE FOR RESIDUE C 2001

REMARK 800 SITE_IDENTIFIER: AC8

REMARK 800 SITE_DESCRIPTION: TRS BINDING SITE FOR RESIDUE D 2002

REMARK 800 SITE_IDENTIFIER: AC9

REMARK 800 SITE_DESCRIPTION: TRS BINDING SITE FOR RESIDUE A 2003

SEQRES 1 A 94 TRP GLU GLU THR LYS GLU CYS ALA PHE THR GLU PHE PHE

SEQRES 2 A 94 LYS LEU ALA PRO LEU ALA SER ASN PRO ALA LEU SER VAL

SEQRES 3 A 94 CYS GLN ASP ALA SER GLY TRP GLN MET LEU PRO PRO ALA

SEQRES 4 A 94 GLY TYR PRO THR PRO GLU GLN LEU LYS LEU MET CYS GLY

SEQRES 5 A 94 THR ALA GLU CYS PHE THR LEU ILE ASP ALA ILE LYS ALA

SEQRES 6 A 94 LEU ASN PRO ASN ASP CYS ILE LEU VAL PHE GLY ASP VAL

SEQRES 7 A 94 ARG LEU ASN VAL LYS LYS LEU VAL THR GLU PHE GLU PRO

SEQRES 8 A 94 SER CYS PHE

SEQRES 1 B 94 TRP GLU GLU THR LYS GLU CYS ALA PHE THR GLU PHE PHE

SEQRES 2 B 94 LYS LEU ALA PRO LEU ALA SER ASN PRO ALA LEU SER VAL

SEQRES 3 B 94 CYS GLN ASP ALA SER GLY TRP GLN MET LEU PRO PRO ALA

SEQRES 4 B 94 GLY TYR PRO THR PRO GLU GLN LEU LYS LEU MET CYS GLY

SEQRES 5 B 94 THR ALA GLU CYS PHE THR LEU ILE ASP ALA ILE LYS ALA

SEQRES 6 B 94 LEU ASN PRO ASN ASP CYS ILE LEU VAL PHE GLY ASP VAL

SEQRES 7 B 94 ARG LEU ASN VAL LYS LYS LEU VAL THR GLU PHE GLU PRO

SEQRES 8 B 94 SER CYS PHE

SEQRES 1 C 94 TRP GLU GLU THR LYS GLU CYS ALA PHE THR GLU PHE PHE

SEQRES 2 C 94 LYS LEU ALA PRO LEU ALA SER ASN PRO ALA LEU SER VAL

SEQRES 3 C 94 CYS GLN ASP ALA SER GLY TRP GLN MET LEU PRO PRO ALA

SEQRES 4 C 94 GLY TYR PRO THR PRO GLU GLN LEU LYS LEU MET CYS GLY

SEQRES 5 C 94 THR ALA GLU CYS PHE THR LEU ILE ASP ALA ILE LYS ALA

SEQRES 6 C 94 LEU ASN PRO ASN ASP CYS ILE LEU VAL PHE GLY ASP VAL

SEQRES 7 C 94 ARG LEU ASN VAL LYS LYS LEU VAL THR GLU PHE GLU PRO

SEQRES 8 C 94 SER CYS PHE

SEQRES 1 D 94 TRP GLU GLU THR LYS GLU CYS ALA PHE THR GLU PHE PHE

SEQRES 2 D 94 LYS LEU ALA PRO LEU ALA SER ASN PRO ALA LEU SER VAL

SEQRES 3 D 94 CYS GLN ASP ALA SER GLY TRP GLN MET LEU PRO PRO ALA

SEQRES 4 D 94 GLY TYR PRO THR PRO GLU GLN LEU LYS LEU MET CYS GLY

SEQRES 5 D 94 THR ALA GLU CYS PHE THR LEU ILE ASP ALA ILE LYS ALA

SEQRES 6 D 94 LEU ASN PRO ASN ASP CYS ILE LEU VAL PHE GLY ASP VAL

SEQRES 7 D 94 ARG LEU ASN VAL LYS LYS LEU VAL THR GLU PHE GLU PRO

SEQRES 8 D 94 SER CYS PHE

HET NI A 100 1

HET CL A3000 1

HET NI B 100 1

HET NI C 100 1

HET NI D 100 1

HET TRS A2003 8

HET TRS B2000 8

HET TRS C2001 8

HET TRS D2002 8

HETNAM NI NICKEL (II) ION

HETNAM CL CHLORIDE ION

HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL

HETSYN TRS TRIS BUFFER

FORMUL 5 NI 4(NI 2+)

FORMUL 6 CL CL 1-

FORMUL 10 TRS 4(C4 H12 N O3 1+)

FORMUL 14 HOH *734(H2 O)

HELIX 1 1 PHE A 9 LYS A 14 1 6

HELIX 2 2 LEU A 15 SER A 20 5 6

HELIX 3 3 ASN A 21 GLY A 32 1 12

HELIX 4 4 THR A 43 GLY A 52 1 10

HELIX 5 5 THR A 53 ALA A 65 1 13

HELIX 6 6 ASN A 81 CYS A 93 1 13

HELIX 7 7 PHE B 9 LYS B 14 1 6

HELIX 8 8 LEU B 15 SER B 20 5 6

HELIX 9 9 ASN B 21 GLY B 32 1 12

HELIX 10 10 THR B 43 GLY B 52 1 10

HELIX 11 11 THR B 53 LEU B 66 1 14

HELIX 12 12 VAL B 82 CYS B 93 1 12

HELIX 13 13 PHE C 9 LYS C 14 1 6

HELIX 14 14 LEU C 15 SER C 20 5 6

HELIX 15 15 ASN C 21 GLY C 32 1 12

HELIX 16 16 THR C 43 GLY C 52 1 10

HELIX 17 17 THR C 53 ALA C 65 1 13

HELIX 18 18 VAL C 82 CYS C 93 1 12

HELIX 19 19 ALA D 8 SER D 20 5 13

HELIX 20 20 ASN D 21 GLY D 32 1 12

HELIX 21 21 THR D 43 GLY D 52 1 10

HELIX 22 22 THR D 53 ALA D 65 1 13

HELIX 23 23 ASN D 81 CYS D 93 1 13

SHEET 1 A 2 LEU A 73 PHE A 75 0

SHEET 2 A 2 VAL A 78 LEU A 80 -1 O LEU A 80 N LEU A 73

SHEET 1 B 2 ILE B 72 PHE B 75 0

SHEET 2 B 2 VAL B 78 ASN B 81 -1 O LEU B 80 N LEU B 73

SHEET 1 C 2 ILE C 72 PHE C 75 0

SHEET 2 C 2 VAL C 78 ASN C 81 -1 O LEU C 80 N LEU C 73

SHEET 1 D 2 LEU D 73 PHE D 75 0

SHEET 2 D 2 VAL D 78 LEU D 80 -1 O LEU D 80 N LEU D 73

SSBOND 1 CYS A 7 CYS A 71 1555 1555 2.03

SSBOND 2 CYS A 27 CYS A 56 1555 1555 2.05

SSBOND 3 CYS A 51 CYS A 93 1555 1555 2.02

SSBOND 4 CYS B 7 CYS B 71 1555 1555 2.05

SSBOND 5 CYS B 27 CYS B 56 1555 1555 2.05

SSBOND 6 CYS B 51 CYS B 93 1555 1555 2.03

SSBOND 7 CYS C 7 CYS C 71 1555 1555 2.04

SSBOND 8 CYS C 27 CYS C 56 1555 1555 2.06

SSBOND 9 CYS C 51 CYS C 93 1555 1555 2.02

SSBOND 10 CYS D 7 CYS D 71 1555 1555 2.03

SSBOND 11 CYS D 27 CYS D 56 1555 1555 2.05

SSBOND 12 CYS D 51 CYS D 93 1555 1555 2.02

LINK N TRP A 1 NI NI A 100 1555 1555 2.10

LINK O TRP A 1 NI NI A 100 1555 1555 2.05

LINK OXT PHE A 94 NI NI B 100 1555 1555 2.01

LINK N TRP B 1 NI NI B 100 1555 1555 2.14

LINK O TRP B 1 NI NI B 100 1555 1555 2.15

LINK OXT PHE B 94 NI NI A 100 1555 1555 1.94

LINK N TRP C 1 NI NI C 100 1555 1555 2.19

LINK O TRP C 1 NI NI C 100 1555 1555 2.04

LINK N TRP D 1 NI NI D 100 1555 1555 2.23

LINK O TRP D 1 NI NI D 100 1555 1555 2.03

LINK NI NI B 100 O HOH A3173 1555 1555 2.11

LINK NI NI B 100 O3 TRS B2000 1555 1555 2.03

LINK NI NI B 100 N TRS B2000 1555 1555 2.23

LINK NI NI C 100 O HOH C2018 1555 1555 2.12

LINK NI NI C 100 O2 TRS C2001 1555 1555 2.13

LINK NI NI C 100 N TRS C2001 1555 1555 2.11

LINK NI NI D 100 O1 TRS D2002 1555 1555 1.90

LINK NI NI D 100 N TRS D2002 1555 1555 2.18

LINK NI NI A 100 N TRS A2003 1555 1555 2.16

LINK NI NI A 100 O1 TRS A2003 1555 1555 2.07

LINK NI NI A 100 O2 TRS A2003 1555 1555 2.09

CISPEP 1 LEU A 36 PRO A 37 0 -6.09

CISPEP 2 LEU B 36 PRO B 37 0 -5.00

CISPEP 3 LEU C 36 PRO C 37 0 -8.11

CISPEP 4 LEU D 36 PRO D 37 0 -3.19

SITE 1 AC1 4 PRO A 91 PHE A 94 HOH A3173 TRP B 1

SITE 1 AC2 3 TRP C 1 HOH C2018 PHE D 94

SITE 1 AC3 3 PHE C 94 HOH C2062 TRP D 1

SITE 1 AC4 3 TRP A 1 PRO B 91 PHE B 94

SITE 1 AC5 6 ASP A 77 HOH A3052 HOH A3084 HOH A3170

SITE 2 AC5 6 HOH A3179 HOH A3182

SITE 1 AC6 10 PRO A 91 SER A 92 PHE A 94 HOH A3173

SITE 2 AC6 10 TRP B 1 GLU B 3 HOH B2026 HOH B2058

SITE 3 AC6 10 HOH B2175 ALA C 65

SITE 1 AC7 9 ALA B 65 HOH B2141 TRP C 1 GLU C 3

SITE 2 AC7 9 HOH C2018 PRO D 91 SER D 92 PHE D 94

SITE 3 AC7 9 HOH D2023

SITE 1 AC8 8 PRO C 91 SER C 92 PHE C 94 HOH C2046

SITE 2 AC8 8 HOH C2062 HOH C2091 TRP D 1 GLU D 3

SITE 1 AC9 7 TRP A 1 GLU A 3 HOH A3062 HOH A3172

SITE 2 AC9 7 PRO B 91 PHE B 94 HOH B2064

CRYST1 36.220 46.000 55.730 85.20 71.27 74.63 P 1 4

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 0.027609 -0.007589 -0.009373 0.00000

SCALE2 0.000000 0.022545 0.000035 0.00000

SCALE3 0.000000 0.000000 0.018947 0.00000

ATOM 1 N TRP A 1 23.058 -21.590 -5.956 1.00 12.57 N

ATOM 2 CA TRP A 1 22.963 -20.113 -5.769 1.00 12.70 C

ATOM 3 C TRP A 1 23.952 -19.691 -4.716 1.00 12.88 C

ATOM 4 O TRP A 1 24.333 -20.491 -3.851 1.00 12.46 O

ATOM 5 CB TRP A 1 21.550 -19.710 -5.330 1.00 12.97 C

ATOM 6 CG TRP A 1 20.530 -20.056 -6.350 1.00 13.12 C

ATOM 7 CD1 TRP A 1 19.675 -21.125 -6.327 1.00 14.55 C

ATOM 8 CD2 TRP A 1 20.279 -19.363 -7.575 1.00 13.78 C

ATOM 9 NE1 TRP A 1 18.904 -21.134 -7.465 1.00 15.23 N

ATOM 10 CE2 TRP A 1 19.242 -20.057 -8.241 1.00 13.86 C

ATOM 11 CE3 TRP A 1 20.825 -18.221 -8.177 1.00 14.21 C

ATOM 12 CZ2 TRP A 1 18.746 -19.647 -9.480 1.00 13.78 C

ATOM 13 CZ3 TRP A 1 20.328 -17.809 -9.410 1.00 14.99 C

ATOM 14 CH2 TRP A 1 19.295 -18.522 -10.045 1.00 14.67 C

ATOM 15 N GLU A 2 24.353 -18.427 -4.781 1.00 13.35 N

ATOM 16 CA GLU A 2 25.248 -17.863 -3.789 1.00 13.95 C

ATOM 17 C GLU A 2 24.570 -17.763 -2.429 1.00 14.59 C

ATOM 18 O GLU A 2 23.508 -17.159 -2.299 1.00 14.62 O

ATOM 19 CB GLU A 2 25.742 -16.485 -4.241 1.00 14.23 C

ATOM 20 CG GLU A 2 26.789 -15.908 -3.315 1.00 14.90 C

ATOM 21 CD GLU A 2 27.984 -16.837 -3.173 1.00 16.67 C

ATOM 22 OE1 GLU A 2 28.565 -17.202 -4.223 1.00 17.32 O

ATOM 23 OE2 GLU A 2 28.334 -17.205 -2.019 1.00 16.58 O

ATOM 24 N GLU A 3 25.201 -18.356 -1.419 1.00 14.72 N

ATOM 25 CA GLU A 3 24.646 -18.373 -0.066 1.00 15.53 C

ATOM 26 C GLU A 3 25.554 -17.701 0.972 1.00 16.18 C

ATOM 27 O GLU A 3 25.163 -17.563 2.132 1.00 16.17 O

ATOM 28 CB GLU A 3 24.320 -19.806 0.362 1.00 15.80 C

ATOM 29 CG GLU A 3 23.344 -20.567 -0.555 1.00 17.88 C

ATOM 30 CD GLU A 3 21.901 -20.043 -0.516 1.00 19.73 C

ATOM 31 OE1 GLU A 3 21.550 -19.275 0.409 1.00 20.59 O

ATOM 32 OE2 GLU A 3 21.110 -20.417 -1.412 1.00 21.93 O

ATOM 33 N THR A 4 26.746 -17.275 0.558 1.00 16.63 N

ATOM 34 CA THR A 4 27.711 -16.689 1.494 1.00 17.61 C

ATOM 35 C THR A 4 28.069 -15.254 1.129 1.00 17.52 C

ATOM 36 O THR A 4 28.014 -14.353 1.973 1.00 17.76 O

ATOM 37 CB THR A 4 28.999 -17.537 1.583 1.00 17.89 C

ATOM 38 OG1 THR A 4 28.663 -18.861 2.013 1.00 19.49 O

ATOM 39 CG2 THR A 4 29.989 -16.917 2.572 1.00 18.60 C

ATOM 40 N LYS A 5 28.444 -15.050 -0.128 1.00 17.29 N

ATOM 41 CA LYS A 5 28.842 -13.732 -0.604 1.00 17.81 C

ATOM 42 C LYS A 5 27.679 -12.756 -0.492 1.00 18.07 C

ATOM 43 O LYS A 5 26.585 -13.014 -1.002 1.00 16.96 O

ATOM 44 CB LYS A 5 29.340 -13.841 -2.040 1.00 18.31 C

ATOM 45 CG LYS A 5 29.924 -12.579 -2.639 1.00 19.90 C

ATOM 46 CD LYS A 5 30.735 -12.915 -3.898 1.00 22.68 C

ATOM 47 CE LYS A 5 29.862 -13.483 -5.011 1.00 24.01 C

ATOM 48 NZ LYS A 5 30.645 -13.827 -6.240 1.00 26.44 N

ATOM 49 N GLU A 6 27.927 -11.637 0.180 1.00 18.67 N

ATOM 50 CA GLU A 6 26.900 -10.617 0.398 1.00 19.28 C

ATOM 51 C GLU A 6 26.928 -9.536 -0.680 1.00 19.19 C

ATOM 52 O GLU A 6 27.997 -9.173 -1.185 1.00 19.94 O

ATOM 53 CB GLU A 6 27.016 -10.026 1.811 1.00 19.46 C

ATOM 54 CG GLU A 6 26.622 -11.048 2.876 1.00 20.52 C

ATOM 55 CD GLU A 6 27.012 -10.681 4.299 1.00 21.02 C

ATOM 56 OE1 GLU A 6 27.361 -9.515 4.567 1.00 23.87 O

ATOM 57 OE2 GLU A 6 26.957 -11.588 5.153 1.00 25.34 O

ATOM 58 N CYS A 7 25.741 -9.050 -1.044 1.00 18.79 N

ATOM 59 CA CYS A 7 25.598 -7.971 -2.005 1.00 18.72 C

ATOM 60 C CYS A 7 26.101 -6.682 -1.383 1.00 18.67 C

ATOM 61 O CYS A 7 25.922 -6.452 -0.184 1.00 18.88 O

ATOM 62 CB CYS A 7 24.127 -7.750 -2.381 1.00 18.73 C

ATOM 63 SG CYS A 7 23.209 -9.204 -2.910 1.00 19.30 S

ATOM 64 N ALA A 8 26.717 -5.849 -2.209 1.00 18.51 N

ATOM 65 CA ALA A 8 26.988 -4.461 -1.846 1.00 18.47 C

ATOM 66 C ALA A 8 25.654 -3.765 -1.591 1.00 18.60 C

ATOM 67 O ALA A 8 24.629 -4.142 -2.166 1.00 17.81 O

ATOM 68 CB ALA A 8 27.740 -3.771 -2.961 1.00 18.79 C

ATOM 69 N PHE A 9 25.657 -2.748 -0.734 1.00 18.56 N

ATOM 70 CA PHE A 9 24.410 -2.057 -0.413 1.00 18.64 C

ATOM 71 C PHE A 9 23.749 -1.473 -1.663 1.00 18.53 C

ATOM 72 O PHE A 9 22.521 -1.364 -1.724 1.00 18.80 O

ATOM 73 CB PHE A 9 24.624 -0.967 0.649 1.00 18.77 C

ATOM 74 CG PHE A 9 23.344 -0.363 1.155 1.00 19.17 C

ATOM 75 CD1 PHE A 9 22.610 -0.992 2.151 1.00 20.34 C

ATOM 76 CD2 PHE A 9 22.863 0.830 0.625 1.00 19.51 C

ATOM 77 CE1 PHE A 9 21.421 -0.442 2.615 1.00 21.05 C

ATOM 78 CE2 PHE A 9 21.673 1.385 1.079 1.00 19.72 C

ATOM 79 CZ PHE A 9 20.952 0.750 2.072 1.00 19.44 C

ATOM 80 N THR A 10 24.566 -1.115 -2.657 1.00 18.53 N

ATOM 81 CA THR A 10 24.079 -0.547 -3.917 1.00 18.61 C

ATOM 82 C THR A 10 23.070 -1.452 -4.625 1.00 17.95 C

ATOM 83 O THR A 10 22.257 -0.989 -5.424 1.00 17.99 O

ATOM 84 CB THR A 10 25.239 -0.184 -4.882 1.00 18.74 C

ATOM 85 OG1 THR A 10 26.115 -1.306 -5.039 1.00 19.39 O

ATOM 86 CG2 THR A 10 26.032 1.009 -4.353 1.00 20.34 C

ATOM 87 N GLU A 11 23.108 -2.747 -4.314 1.00 17.65 N

ATOM 88 CA GLU A 11 22.132 -3.680 -4.851 1.00 17.11 C

ATOM 89 C GLU A 11 20.707 -3.255 -4.487 1.00 16.68 C

ATOM 90 O GLU A 11 19.800 -3.428 -5.293 1.00 17.20 O

ATOM 91 CB GLU A 11 22.425 -5.100 -4.365 1.00 17.60 C

ATOM 92 CG GLU A 11 21.580 -6.198 -5.003 1.00 17.42 C

ATOM 93 CD GLU A 11 21.985 -6.554 -6.428 1.00 17.86 C

ATOM 94 OE1 GLU A 11 23.042 -6.104 -6.915 1.00 20.12 O

ATOM 95 OE2 GLU A 11 21.230 -7.312 -7.065 1.00 17.55 O

ATOM 96 N PHE A 12 20.507 -2.699 -3.288 1.00 16.20 N

ATOM 97 CA PHE A 12 19.179 -2.216 -2.887 1.00 15.78 C

ATOM 98 C PHE A 12 18.663 -1.186 -3.879 1.00 15.10 C

ATOM 99 O PHE A 12 17.478 -1.183 -4.221 1.00 15.06 O

ATOM 100 CB PHE A 12 19.187 -1.568 -1.493 1.00 16.45 C

ATOM 101 CG PHE A 12 19.183 -2.544 -0.353 1.00 16.84 C

ATOM 102 CD1 PHE A 12 20.352 -2.800 0.357 1.00 18.02 C

ATOM 103 CD2 PHE A 12 18.011 -3.195 0.026 1.00 19.39 C

ATOM 104 CE1 PHE A 12 20.359 -3.692 1.428 1.00 18.29 C

ATOM 105 CE2 PHE A 12 18.011 -4.105 1.093 1.00 19.59 C

ATOM 106 CZ PHE A 12 19.182 -4.347 1.792 1.00 18.70 C

ATOM 107 N PHE A 13 19.552 -0.315 -4.352 1.00 14.21 N

ATOM 108 CA PHE A 13 19.124 0.781 -5.222 1.00 13.46 C

ATOM 109 C PHE A 13 18.554 0.290 -6.544 1.00 13.25 C

ATOM 110 O PHE A 13 17.734 0.971 -7.166 1.00 12.96 O

ATOM 111 CB PHE A 13 20.250 1.794 -5.456 1.00 13.61 C

ATOM 112 CG PHE A 13 20.781 2.432 -4.187 1.00 12.99 C

ATOM 113 CD1 PHE A 13 22.145 2.676 -4.047 1.00 13.42 C

ATOM 114 CD2 PHE A 13 19.925 2.807 -3.152 1.00 13.28 C

ATOM 115 CE1 PHE A 13 22.649 3.264 -2.891 1.00 14.61 C

ATOM 116 CE2 PHE A 13 20.426 3.406 -1.993 1.00 14.72 C

ATOM 117 CZ PHE A 13 21.795 3.634 -1.873 1.00 14.11 C

ATOM 118 N LYS A 14 18.969 -0.908 -6.969 1.00 12.89 N

ATOM 119 CA LYS A 14 18.416 -1.521 -8.179 1.00 13.42 C

ATOM 120 C LYS A 14 16.910 -1.742 -8.092 1.00 12.91 C

ATOM 121 O LYS A 14 16.237 -1.798 -9.121 1.00 13.43 O

ATOM 122 CB LYS A 14 19.053 -2.886 -8.440 1.00 13.77 C

ATOM 123 CG LYS A 14 20.462 -2.876 -8.960 1.00 16.12 C

ATOM 124 CD LYS A 14 20.829 -4.327 -9.247 1.00 18.70 C

ATOM 125 CE LYS A 14 22.271 -4.475 -9.622 1.00 21.30 C

ATOM 126 NZ LYS A 14 22.562 -5.925 -9.815 1.00 20.28 N

ATOM 127 N LEU A 15 16.402 -1.902 -6.874 1.00 12.62 N

ATOM 128 CA LEU A 15 14.989 -2.203 -6.655 1.00 12.83 C

ATOM 129 C LEU A 15 14.065 -0.991 -6.804 1.00 12.52 C

ATOM 130 O LEU A 15 12.847 -1.146 -6.773 1.00 12.87 O

ATOM 131 CB LEU A 15 14.795 -2.829 -5.270 1.00 13.08 C

ATOM 132 CG LEU A 15 15.623 -4.074 -4.941 1.00 15.23 C

ATOM 133 CD1 LEU A 15 15.383 -4.457 -3.485 1.00 16.96 C

ATOM 134 CD2 LEU A 15 15.288 -5.222 -5.870 1.00 16.87 C

ATOM 135 N ALA A 16 14.637 0.201 -6.978 1.00 12.55 N

ATOM 136 CA ALA A 16 13.848 1.450 -6.963 1.00 11.96 C

ATOM 137 C ALA A 16 12.636 1.466 -7.909 1.00 12.02 C

ATOM 138 O ALA A 16 11.553 1.906 -7.514 1.00 11.89 O

ATOM 139 CB ALA A 16 14.749 2.663 -7.209 1.00 11.98 C

ATOM 140 N PRO A 17 12.797 0.965 -9.149 1.00 11.81 N

ATOM 141 CA PRO A 17 11.630 0.963 -10.054 1.00 12.27 C

ATOM 142 C PRO A 17 10.392 0.249 -9.500 1.00 12.38 C

ATOM 143 O PRO A 17 9.263 0.567 -9.897 1.00 12.96 O

ATOM 144 CB PRO A 17 12.158 0.223 -11.287 1.00 12.43 C

ATOM 145 CG PRO A 17 13.606 0.494 -11.279 1.00 12.28 C

ATOM 146 CD PRO A 17 13.989 0.420 -9.824 1.00 12.07 C

ATOM 147 N LEU A 18 10.583 -0.709 -8.593 1.00 12.48 N

ATOM 148 CA LEU A 18 9.442 -1.463 -8.078 1.00 12.52 C

ATOM 149 C LEU A 18 8.432 -0.577 -7.354 1.00 12.58 C

ATOM 150 O LEU A 18 7.240 -0.863 -7.380 1.00 12.51 O

ATOM 151 CB LEU A 18 9.890 -2.601 -7.162 1.00 12.71 C

ATOM 152 CG LEU A 18 10.857 -3.628 -7.753 1.00 12.24 C

ATOM 153 CD1 LEU A 18 11.136 -4.644 -6.682 1.00 13.66 C

ATOM 154 CD2 LEU A 18 10.273 -4.291 -9.000 1.00 11.74 C

ATOM 155 N ALA A 19 8.905 0.503 -6.732 1.00 12.74 N

ATOM 156 CA ALA A 19 8.012 1.353 -5.929 1.00 13.02 C

ATOM 157 C ALA A 19 6.965 2.083 -6.761 1.00 13.26 C

ATOM 158 O ALA A 19 5.932 2.493 -6.238 1.00 13.80 O

ATOM 159 CB ALA A 19 8.814 2.352 -5.095 1.00 13.38 C

ATOM 160 N SER A 20 7.251 2.251 -8.047 1.00 12.79 N

ATOM 161 CA SER A 20 6.329 2.905 -8.973 1.00 13.29 C

ATOM 162 C SER A 20 5.663 1.879 -9.896 1.00 13.31 C

ATOM 163 O SER A 20 5.043 2.236 -10.896 1.00 12.99 O

ATOM 164 CB SER A 20 7.065 3.981 -9.779 1.00 13.11 C

ATOM 165 OG SER A 20 8.240 3.461 -10.368 1.00 14.27 O

ATOM 166 N ASN A 21 5.775 0.606 -9.534 1.00 13.52 N

ATOM 167 CA ASN A 21 5.127 -0.457 -10.285 1.00 13.62 C

ATOM 168 C ASN A 21 3.917 -0.961 -9.499 1.00 13.98 C

ATOM 169 O ASN A 21 4.074 -1.487 -8.402 1.00 14.14 O

ATOM 170 CB ASN A 21 6.111 -1.598 -10.563 1.00 13.47 C

ATOM 171 CG ASN A 21 5.543 -2.647 -11.506 1.00 13.18 C

ATOM 172 OD1 ASN A 21 4.341 -2.921 -11.508 1.00 13.47 O

ATOM 173 ND2 ASN A 21 6.417 -3.245 -12.315 1.00 14.23 N

ATOM 174 N PRO A 22 2.698 -0.780 -10.044 1.00 14.22 N

ATOM 175 CA PRO A 22 1.493 -1.159 -9.296 1.00 14.56 C

ATOM 176 C PRO A 22 1.454 -2.630 -8.869 1.00 14.57 C

ATOM 177 O PRO A 22 0.800 -2.954 -7.877 1.00 15.28 O

ATOM 178 CB PRO A 22 0.352 -0.854 -10.284 1.00 14.77 C

ATOM 179 CG PRO A 22 0.912 0.186 -11.188 1.00 15.59 C

ATOM 180 CD PRO A 22 2.363 -0.194 -11.356 1.00 14.02 C

ATOM 181 N ALA A 23 2.157 -3.498 -9.599 1.00 14.48 N

ATOM 182 CA ALA A 23 2.150 -4.936 -9.307 1.00 14.88 C

ATOM 183 C ALA A 23 2.747 -5.223 -7.932 1.00 14.73 C

ATOM 184 O ALA A 23 2.385 -6.218 -7.295 1.00 15.24 O

ATOM 185 CB ALA A 23 2.889 -5.712 -10.388 1.00 14.86 C

ATOM 186 N LEU A 24 3.654 -4.356 -7.475 1.00 14.82 N

ATOM 187 CA LEU A 24 4.275 -4.530 -6.154 1.00 14.66 C

ATOM 188 C LEU A 24 3.217 -4.525 -5.053 1.00 15.05 C

ATOM 189 O LEU A 24 3.119 -5.475 -4.280 1.00 14.87 O

ATOM 190 CB LEU A 24 5.350 -3.467 -5.872 1.00 14.88 C

ATOM 191 CG LEU A 24 6.019 -3.543 -4.489 1.00 14.25 C

ATOM 192 CD1 LEU A 24 6.935 -4.761 -4.371 1.00 15.78 C

ATOM 193 CD2 LEU A 24 6.786 -2.259 -4.170 1.00 14.64 C

ATOM 194 N SER A 25 2.427 -3.453 -4.994 1.00 15.62 N

ATOM 195 CA SER A 25 1.392 -3.306 -3.982 1.00 16.87 C

ATOM 196 C SER A 25 0.346 -4.420 -4.061 1.00 16.29 C

ATOM 197 O SER A 25 -0.049 -4.978 -3.035 1.00 16.28 O

ATOM 198 CB SER A 25 0.731 -1.929 -4.103 1.00 17.32 C

ATOM 199 OG SER A 25 -0.389 -1.820 -3.243 1.00 21.39 O

ATOM 200 N VAL A 26 -0.102 -4.748 -5.272 1.00 16.34 N

ATOM 201 CA VAL A 26 -1.129 -5.782 -5.441 1.00 16.38 C

ATOM 202 C VAL A 26 -0.638 -7.141 -4.951 1.00 16.31 C

ATOM 203 O VAL A 26 -1.354 -7.845 -4.240 1.00 16.91 O

ATOM 204 CB VAL A 26 -1.633 -5.895 -6.899 1.00 16.76 C

ATOM 205 CG1 VAL A 26 -2.664 -7.028 -7.027 1.00 17.56 C

ATOM 206 CG2 VAL A 26 -2.227 -4.580 -7.357 1.00 17.15 C

ATOM 207 N CYS A 27 0.593 -7.495 -5.317 1.00 15.33 N

ATOM 208 CA CYS A 27 1.164 -8.778 -4.921 1.00 15.37 C

ATOM 209 C CYS A 27 1.367 -8.858 -3.410 1.00 15.36 C

ATOM 210 O CYS A 27 0.995 -9.857 -2.789 1.00 15.59 O

ATOM 211 CB CYS A 27 2.483 -9.027 -5.656 1.00 15.44 C

ATOM 212 SG CYS A 27 3.257 -10.614 -5.260 1.00 15.65 S

ATOM 213 N GLN A 28 1.930 -7.801 -2.824 1.00 15.26 N

ATOM 214 CA GLN A 28 2.193 -7.756 -1.386 1.00 15.25 C

ATOM 215 C GLN A 28 0.900 -7.807 -0.577 1.00 16.17 C

ATOM 216 O GLN A 28 0.793 -8.583 0.381 1.00 16.38 O

ATOM 217 CB GLN A 28 3.012 -6.510 -1.019 1.00 15.37 C

ATOM 218 CG GLN A 28 4.445 -6.538 -1.571 1.00 13.98 C

ATOM 219 CD GLN A 28 5.273 -5.345 -1.129 1.00 14.83 C

ATOM 220 OE1 GLN A 28 6.497 -5.431 -1.042 1.00 14.99 O

ATOM 221 NE2 GLN A 28 4.609 -4.221 -0.853 1.00 14.68 N

ATOM 222 N ASP A 29 -0.091 -7.019 -0.985 1.00 17.35 N

ATOM 223 CA ASP A 29 -1.380 -7.006 -0.288 1.00 18.30 C

ATOM 224 C ASP A 29 -2.131 -8.327 -0.408 1.00 18.43 C

ATOM 225 O ASP A 29 -2.771 -8.762 0.547 1.00 19.07 O

ATOM 226 CB ASP A 29 -2.263 -5.861 -0.791 1.00 18.77 C

ATOM 227 CG ASP A 29 -1.739 -4.488 -0.387 1.00 20.59 C

ATOM 228 OD1 ASP A 29 -0.750 -4.409 0.372 1.00 22.32 O

ATOM 229 OD2 ASP A 29 -2.325 -3.480 -0.831 1.00 23.24 O

ATOM 230 N ALA A 30 -2.042 -8.967 -1.574 1.00 17.89 N

ATOM 231 CA ALA A 30 -2.730 -10.237 -1.812 1.00 17.98 C

ATOM 232 C ALA A 30 -2.122 -11.380 -1.010 1.00 17.67 C

ATOM 233 O ALA A 30 -2.841 -12.247 -0.508 1.00 18.48 O

ATOM 234 CB ALA A 30 -2.728 -10.579 -3.297 1.00 18.14 C

ATOM 235 N SER A 31 -0.795 -11.376 -0.888 1.00 16.86 N

ATOM 236 CA SER A 31 -0.082 -12.527 -0.335 1.00 16.60 C

ATOM 237 C SER A 31 0.397 -12.357 1.102 1.00 16.45 C

ATOM 238 O SER A 31 0.608 -13.351 1.798 1.00 16.73 O

ATOM 239 CB SER A 31 1.116 -12.870 -1.225 1.00 16.47 C

ATOM 240 OG SER A 31 2.090 -11.851 -1.163 1.00 15.80 O

ATOM 241 N GLY A 32 0.593 -11.109 1.531 1.00 16.28 N

ATOM 242 CA GLY A 32 1.196 -10.840 2.832 1.00 16.59 C

ATOM 243 C GLY A 32 2.717 -10.914 2.816 1.00 16.72 C

ATOM 244 O GLY A 32 3.361 -10.648 3.840 1.00 17.43 O

ATOM 245 N TRP A 33 3.287 -11.308 1.672 1.00 16.43 N

ATOM 246 CA TRP A 33 4.745 -11.303 1.481 1.00 16.19 C

ATOM 247 C TRP A 33 5.217 -9.921 1.067 1.00 16.56 C

ATOM 248 O TRP A 33 4.633 -9.304 0.175 1.00 16.62 O

ATOM 249 CB TRP A 33 5.171 -12.320 0.418 1.00 15.76 C

ATOM 250 CG TRP A 33 6.619 -12.213 0.021 1.00 15.04 C

ATOM 251 CD1 TRP A 33 7.697 -12.618 0.750 1.00 14.27 C

ATOM 252 CD2 TRP A 33 7.143 -11.669 -1.199 1.00 14.59 C

ATOM 253 NE1 TRP A 33 8.864 -12.365 0.062 1.00 14.69 N

ATOM 254 CE2 TRP A 33 8.551 -11.781 -1.137 1.00 14.77 C

ATOM 255 CE3 TRP A 33 6.559 -11.099 -2.336 1.00 13.24 C

ATOM 256 CZ2 TRP A 33 9.385 -11.343 -2.172 1.00 14.32 C

ATOM 257 CZ3 TRP A 33 7.389 -10.661 -3.369 1.00 14.65 C

ATOM 258 CH2 TRP A 33 8.783 -10.792 -3.281 1.00 14.17 C

ATOM 259 N GLN A 34 6.290 -9.448 1.695 1.00 16.59 N

ATOM 260 CA GLN A 34 6.822 -8.125 1.388 1.00 17.01 C

ATOM 261 C GLN A 34 8.177 -8.195 0.694 1.00 16.43 C

ATOM 262 O GLN A 34 9.073 -8.919 1.134 1.00 15.73 O

ATOM 263 CB GLN A 34 6.922 -7.266 2.654 1.00 17.60 C

ATOM 264 CG GLN A 34 5.657 -7.265 3.539 1.00 20.08 C

ATOM 265 CD GLN A 34 4.388 -6.825 2.804 1.00 23.92 C

ATOM 266 OE1 GLN A 34 3.329 -7.461 2.922 1.00 26.56 O

ATOM 267 NE2 GLN A 34 4.486 -5.735 2.051 1.00 24.14 N

ATOM 268 N MET A 35 8.305 -7.425 -0.387 1.00 16.14 N

ATOM 269 CA MET A 35 9.566 -7.240 -1.101 1.00 16.11 C

ATOM 270 C MET A 35 10.218 -5.927 -0.654 1.00 15.87 C

ATOM 271 O MET A 35 11.434 -5.862 -0.514 1.00 15.85 O

ATOM 272 CB MET A 35 9.331 -7.241 -2.618 1.00 15.70 C

ATOM 273 CG MET A 35 10.585 -7.058 -3.487 1.00 16.95 C

ATOM 274 SD MET A 35 11.717 -8.477 -3.442 1.00 21.05 S

ATOM 275 CE MET A 35 13.120 -7.810 -2.535 1.00 21.82 C

ATOM 276 N LEU A 36 9.411 -4.889 -0.442 1.00 16.05 N

ATOM 277 CA LEU A 36 9.919 -3.602 0.046 1.00 16.38 C

ATOM 278 C LEU A 36 9.136 -3.121 1.276 1.00 16.66 C

ATOM 279 O LEU A 36 7.966 -2.756 1.160 1.00 17.36 O

ATOM 280 CB LEU A 36 9.860 -2.525 -1.046 1.00 16.29 C

ATOM 281 CG LEU A 36 10.618 -2.724 -2.360 1.00 16.45 C

ATOM 282 CD1 LEU A 36 10.387 -1.532 -3.271 1.00 16.87 C

ATOM 283 CD2 LEU A 36 12.097 -2.933 -2.121 1.00 16.79 C

ATOM 284 N PRO A 37 9.764 -3.136 2.465 1.00 16.99 N

ATOM 285 CA PRO A 37 11.085 -3.669 2.787 1.00 16.70 C

ATOM 286 C PRO A 37 11.070 -5.192 2.680 1.00 16.51 C

ATOM 287 O PRO A 37 10.022 -5.804 2.874 1.00 16.52 O

ATOM 288 CB PRO A 37 11.295 -3.262 4.256 1.00 16.85 C

ATOM 289 CG PRO A 37 10.202 -2.338 4.595 1.00 17.78 C

ATOM 290 CD PRO A 37 9.085 -2.583 3.650 1.00 16.71 C

ATOM 291 N PRO A 38 12.224 -5.807 2.385 1.00 16.72 N

ATOM 292 CA PRO A 38 12.210 -7.260 2.175 1.00 17.13 C

ATOM 293 C PRO A 38 11.974 -8.068 3.451 1.00 17.53 C

ATOM 294 O PRO A 38 12.691 -7.887 4.446 1.00 18.27 O

ATOM 295 CB PRO A 38 13.600 -7.544 1.598 1.00 17.22 C

ATOM 296 CG PRO A 38 14.456 -6.448 2.126 1.00 17.19 C

ATOM 297 CD PRO A 38 13.566 -5.230 2.204 1.00 16.98 C

ATOM 298 N ALA A 39 10.975 -8.952 3.411 1.00 17.41 N

ATOM 299 CA ALA A 39 10.721 -9.901 4.496 1.00 17.41 C

ATOM 300 C ALA A 39 11.545 -11.178 4.358 1.00 17.32 C

ATOM 301 O ALA A 39 11.657 -11.952 5.318 1.00 18.00 O

ATOM 302 CB ALA A 39 9.248 -10.243 4.562 1.00 17.42 C

ATOM 303 N GLY A 40 12.105 -11.399 3.168 1.00 16.88 N

ATOM 304 CA GLY A 40 12.831 -12.635 2.876 1.00 17.21 C

ATOM 305 C GLY A 40 12.112 -13.490 1.852 1.00 17.06 C

ATOM 306 O GLY A 40 11.450 -12.969 0.951 1.00 17.45 O

ATOM 307 N TYR A 41 12.244 -14.807 1.978 1.00 16.36 N

ATOM 308 CA TYR A 41 11.567 -15.710 1.058 1.00 16.32 C

ATOM 309 C TYR A 41 10.128 -15.891 1.496 1.00 16.29 C

ATOM 310 O TYR A 41 9.857 -15.920 2.700 1.00 16.50 O

ATOM 311 CB TYR A 41 12.264 -17.073 0.990 1.00 16.13 C

ATOM 312 CG TYR A 41 13.689 -16.991 0.501 1.00 16.36 C

ATOM 313 CD1 TYR A 41 14.748 -17.118 1.388 1.00 16.88 C

ATOM 314 CD2 TYR A 41 13.969 -16.764 -0.845 1.00 16.83 C

ATOM 315 CE1 TYR A 41 16.060 -17.035 0.945 1.00 16.99 C

ATOM 316 CE2 TYR A 41 15.276 -16.678 -1.305 1.00 16.66 C

ATOM 317 CZ TYR A 41 16.315 -16.816 -0.403 1.00 16.16 C

ATOM 318 OH TYR A 41 17.611 -16.735 -0.845 1.00 16.57 O

ATOM 319 N PRO A 42 9.197 -16.008 0.525 1.00 16.61 N

ATOM 320 CA PRO A 42 7.799 -16.247 0.888 1.00 16.88 C

ATOM 321 C PRO A 42 7.676 -17.549 1.667 1.00 17.24 C

ATOM 322 O PRO A 42 8.359 -18.529 1.345 1.00 17.66 O

ATOM 323 CB PRO A 42 7.107 -16.395 -0.470 1.00 16.73 C

ATOM 324 CG PRO A 42 8.002 -15.713 -1.450 1.00 17.59 C

ATOM 325 CD PRO A 42 9.381 -15.915 -0.934 1.00 16.52 C

ATOM 326 N THR A 43 6.826 -17.546 2.690 1.00 17.63 N

ATOM 327 CA THR A 43 6.437 -18.775 3.381 1.00 18.18 C

ATOM 328 C THR A 43 5.563 -19.595 2.430 1.00 18.09 C

ATOM 329 O THR A 43 5.078 -19.066 1.428 1.00 18.37 O

ATOM 330 CB THR A 43 5.644 -18.464 4.669 1.00 18.23 C

ATOM 331 OG1 THR A 43 4.409 -17.819 4.327 1.00 18.84 O

ATOM 332 CG2 THR A 43 6.451 -17.572 5.602 1.00 18.74 C

ATOM 333 N PRO A 44 5.374 -20.898 2.714 1.00 18.19 N

ATOM 334 CA PRO A 44 4.497 -21.692 1.850 1.00 18.26 C

ATOM 335 C PRO A 44 3.084 -21.107 1.717 1.00 18.01 C

ATOM 336 O PRO A 44 2.519 -21.141 0.623 1.00 17.89 O

ATOM 337 CB PRO A 44 4.469 -23.055 2.546 1.00 18.27 C

ATOM 338 CG PRO A 44 5.802 -23.112 3.263 1.00 18.18 C

ATOM 339 CD PRO A 44 5.984 -21.719 3.778 1.00 18.50 C

ATOM 340 N GLU A 45 2.546 -20.554 2.808 1.00 17.82 N

ATOM 341 CA GLU A 45 1.225 -19.919 2.802 1.00 18.05 C

ATOM 342 C GLU A 45 1.213 -18.710 1.873 1.00 17.40 C

ATOM 343 O GLU A 45 0.280 -18.532 1.094 1.00 17.88 O

ATOM 344 CB GLU A 45 0.807 -19.494 4.218 1.00 18.24 C

ATOM 345 CG GLU A 45 0.466 -20.658 5.155 1.00 20.81 C

ATOM 346 CD GLU A 45 1.679 -21.324 5.812 1.00 23.63 C

ATOM 347 OE1 GLU A 45 2.821 -20.847 5.654 1.00 24.51 O

ATOM 348 OE2 GLU A 45 1.479 -22.342 6.509 1.00 26.89 O

ATOM 349 N GLN A 46 2.257 -17.890 1.968 1.00 16.94 N

ATOM 350 CA GLN A 46 2.390 -16.703 1.123 1.00 16.31 C

ATOM 351 C GLN A 46 2.583 -17.085 -0.327 1.00 16.37 C

ATOM 352 O GLN A 46 1.966 -16.490 -1.215 1.00 15.25 O

ATOM 353 CB GLN A 46 3.548 -15.828 1.600 1.00 16.13 C

ATOM 354 CG GLN A 46 3.257 -15.113 2.911 1.00 16.93 C

ATOM 355 CD GLN A 46 4.508 -14.583 3.584 1.00 18.14 C

ATOM 356 OE1 GLN A 46 5.629 -14.870 3.162 1.00 17.93 O

ATOM 357 NE2 GLN A 46 4.321 -13.810 4.649 1.00 21.06 N

ATOM 358 N LEU A 47 3.424 -18.091 -0.562 1.00 16.36 N

ATOM 359 CA LEU A 47 3.679 -18.571 -1.917 1.00 17.10 C

ATOM 360 C LEU A 47 2.398 -19.058 -2.605 1.00 17.36 C

ATOM 361 O LEU A 47 2.162 -18.758 -3.778 1.00 17.06 O

ATOM 362 CB LEU A 47 4.744 -19.675 -1.910 1.00 17.30 C

ATOM 363 CG LEU A 47 5.201 -20.190 -3.274 1.00 17.80 C

ATOM 364 CD1 LEU A 47 5.809 -19.062 -4.111 1.00 17.91 C

ATOM 365 CD2 LEU A 47 6.215 -21.318 -3.094 1.00 17.99 C

ATOM 366 N LYS A 48 1.582 -19.816 -1.868 1.00 17.74 N

ATOM 367 CA LYS A 48 0.274 -20.275 -2.337 1.00 18.21 C

ATOM 368 C LYS A 48 -0.535 -19.108 -2.889 1.00 17.86 C

ATOM 369 O LYS A 48 -1.075 -19.174 -3.996 1.00 18.19 O

ATOM 370 CB LYS A 48 -0.495 -20.917 -1.174 1.00 18.61 C

ATOM 371 CG LYS A 48 -1.848 -21.531 -1.536 1.00 22.40 C

ATOM 372 CD LYS A 48 -1.774 -23.036 -1.757 1.00 27.16 C

ATOM 373 CE LYS A 48 -1.602 -23.380 -3.233 1.00 29.32 C

ATOM 374 NZ LYS A 48 -1.626 -24.850 -3.487 1.00 30.46 N

ATOM 375 N LEU A 49 -0.615 -18.046 -2.096 1.00 17.30 N

ATOM 376 CA LEU A 49 -1.336 -16.842 -2.485 1.00 17.15 C

ATOM 377 C LEU A 49 -0.701 -16.159 -3.695 1.00 16.79 C

ATOM 378 O LEU A 49 -1.400 -15.776 -4.624 1.00 16.77 O

ATOM 379 CB LEU A 49 -1.435 -15.879 -1.303 1.00 17.49 C

ATOM 380 CG LEU A 49 -2.466 -16.269 -0.234 1.00 18.07 C

ATOM 381 CD1 LEU A 49 -2.151 -15.618 1.106 1.00 18.50 C

ATOM 382 CD2 LEU A 49 -3.873 -15.902 -0.698 1.00 20.16 C

ATOM 383 N MET A 50 0.627 -16.040 -3.688 1.00 16.35 N

ATOM 384 CA MET A 50 1.353 -15.424 -4.803 1.00 15.73 C

ATOM 385 C MET A 50 1.107 -16.166 -6.110 1.00 15.93 C

ATOM 386 O MET A 50 0.879 -15.545 -7.151 1.00 15.87 O

ATOM 387 CB MET A 50 2.856 -15.409 -4.518 1.00 15.71 C

ATOM 388 CG MET A 50 3.271 -14.429 -3.446 1.00 14.86 C

ATOM 389 SD MET A 50 5.018 -14.584 -3.041 1.00 15.96 S

ATOM 390 CE MET A 50 5.759 -13.777 -4.456 1.00 14.71 C

ATOM 391 N CYS A 51 1.147 -17.497 -6.044 1.00 16.35 N

ATOM 392 CA CYS A 51 0.997 -18.338 -7.229 1.00 16.97 C

ATOM 393 C CYS A 51 -0.385 -18.233 -7.881 1.00 17.20 C

ATOM 394 O CYS A 51 -0.541 -18.592 -9.041 1.00 17.62 O

ATOM 395 CB CYS A 51 1.344 -19.794 -6.901 1.00 17.06 C

ATOM 396 SG CYS A 51 3.105 -20.013 -6.508 1.00 18.29 S

ATOM 397 N GLY A 52 -1.371 -17.747 -7.131 1.00 17.70 N

ATOM 398 CA GLY A 52 -2.703 -17.498 -7.680 1.00 18.32 C

ATOM 399 C GLY A 52 -3.006 -16.037 -7.982 1.00 18.63 C

ATOM 400 O GLY A 52 -4.161 -15.674 -8.228 1.00 19.50 O

ATOM 401 N THR A 53 -1.970 -15.199 -7.975 1.00 18.29 N

ATOM 402 CA THR A 53 -2.121 -13.760 -8.194 1.00 17.77 C

ATOM 403 C THR A 53 -1.307 -13.360 -9.423 1.00 17.77 C

ATOM 404 O THR A 53 -0.071 -13.408 -9.403 1.00 17.08 O

ATOM 405 CB THR A 53 -1.672 -12.963 -6.942 1.00 17.40 C

ATOM 406 OG1 THR A 53 -2.392 -13.427 -5.790 1.00 18.09 O

ATOM 407 CG2 THR A 53 -1.904 -11.455 -7.112 1.00 18.27 C

ATOM 408 N ALA A 54 -1.997 -12.994 -10.502 1.00 17.35 N

ATOM 409 CA ALA A 54 -1.325 -12.628 -11.751 1.00 17.50 C

ATOM 410 C ALA A 54 -0.254 -11.568 -11.525 1.00 17.16 C

ATOM 411 O ALA A 54 0.829 -11.633 -12.109 1.00 17.51 O

ATOM 412 CB ALA A 54 -2.332 -12.144 -12.795 1.00 17.82 C

ATOM 413 N GLU A 55 -0.563 -10.603 -10.664 1.00 16.99 N

ATOM 414 CA GLU A 55 0.335 -9.478 -10.406 1.00 16.96 C

ATOM 415 C GLU A 55 1.647 -9.895 -9.749 1.00 16.29 C

ATOM 416 O GLU A 55 2.664 -9.214 -9.905 1.00 16.40 O

ATOM 417 CB GLU A 55 -0.367 -8.415 -9.570 1.00 17.05 C

ATOM 418 CG GLU A 55 -1.449 -7.656 -10.348 1.00 18.80 C

ATOM 419 CD GLU A 55 -2.824 -8.318 -10.315 1.00 22.30 C

ATOM 420 OE1 GLU A 55 -2.982 -9.442 -9.777 1.00 22.35 O

ATOM 421 OE2 GLU A 55 -3.768 -7.689 -10.838 1.00 23.91 O

ATOM 422 N CYS A 56 1.627 -11.005 -9.013 1.00 15.48 N

ATOM 423 CA CYS A 56 2.874 -11.543 -8.455 1.00 14.97 C

ATOM 424 C CYS A 56 3.818 -12.036 -9.549 1.00 14.58 C

ATOM 425 O CYS A 56 5.024 -11.829 -9.470 1.00 14.10 O

ATOM 426 CB CYS A 56 2.597 -12.629 -7.420 1.00 15.27 C

ATOM 427 SG CYS A 56 1.875 -11.978 -5.909 1.00 16.06 S

ATOM 428 N PHE A 57 3.269 -12.651 -10.591 1.00 14.69 N

ATOM 429 CA PHE A 57 4.075 -13.032 -11.757 1.00 15.10 C

ATOM 430 C PHE A 57 4.623 -11.797 -12.468 1.00 15.13 C

ATOM 431 O PHE A 57 5.781 -11.773 -12.881 1.00 14.75 O

ATOM 432 CB PHE A 57 3.265 -13.900 -12.720 1.00 15.84 C

ATOM 433 CG PHE A 57 2.932 -15.254 -12.164 1.00 16.07 C

ATOM 434 CD1 PHE A 57 1.837 -15.424 -11.320 1.00 17.47 C

ATOM 435 CD2 PHE A 57 3.722 -16.359 -12.471 1.00 18.23 C

ATOM 436 CE1 PHE A 57 1.529 -16.675 -10.789 1.00 17.10 C

ATOM 437 CE2 PHE A 57 3.413 -17.620 -11.948 1.00 17.96 C

ATOM 438 CZ PHE A 57 2.320 -17.774 -11.110 1.00 17.49 C

ATOM 439 N THR A 58 3.782 -10.772 -12.602 1.00 15.11 N

ATOM 440 CA THR A 58 4.206 -9.496 -13.170 1.00 15.15 C

ATOM 441 C THR A 58 5.334 -8.887 -12.341 1.00 14.69 C

ATOM 442 O THR A 58 6.343 -8.425 -12.892 1.00 15.23 O

ATOM 443 CB THR A 58 3.019 -8.510 -13.270 1.00 15.82 C

ATOM 444 OG1 THR A 58 1.974 -9.128 -14.035 1.00 16.75 O

ATOM 445 CG2 THR A 58 3.438 -7.197 -13.947 1.00 15.88 C

ATOM 446 N LEU A 59 5.165 -8.897 -11.023 1.00 14.14 N

ATOM 447 CA LEU A 59 6.178 -8.364 -10.129 1.00 13.65 C

ATOM 448 C LEU A 59 7.494 -9.120 -10.274 1.00 13.27 C

ATOM 449 O LEU A 59 8.556 -8.508 -10.404 1.00 13.10 O

ATOM 450 CB LEU A 59 5.706 -8.413 -8.671 1.00 13.50 C

ATOM 451 CG LEU A 59 6.760 -8.000 -7.641 1.00 14.25 C

ATOM 452 CD1 LEU A 59 7.231 -6.566 -7.858 1.00 14.01 C

ATOM 453 CD2 LEU A 59 6.218 -8.179 -6.225 1.00 13.33 C

ATOM 454 N ILE A 60 7.425 -10.448 -10.243 1.00 13.43 N

ATOM 455 CA ILE A 60 8.628 -11.269 -10.360 1.00 14.00 C

ATOM 456 C ILE A 60 9.371 -11.011 -11.673 1.00 14.16 C

ATOM 457 O ILE A 60 10.598 -10.887 -11.682 1.00 14.03 O

ATOM 458 CB ILE A 60 8.305 -12.780 -10.126 1.00 14.00 C

ATOM 459 CG1 ILE A 60 7.955 -13.020 -8.644 1.00 16.08 C

ATOM 460 CG2 ILE A 60 9.433 -13.691 -10.652 1.00 15.45 C

ATOM 461 CD1 ILE A 60 9.089 -12.873 -7.630 1.00 18.79 C

ATOM 462 N ASP A 61 8.626 -10.874 -12.769 1.00 14.30 N

ATOM 463 CA ASP A 61 9.238 -10.532 -14.051 1.00 15.28 C

ATOM 464 C ASP A 61 9.871 -9.136 -14.019 1.00 14.60 C

ATOM 465 O ASP A 61 10.935 -8.919 -14.610 1.00 14.62 O

ATOM 466 CB ASP A 61 8.225 -10.656 -15.197 1.00 16.06 C

ATOM 467 CG ASP A 61 7.852 -12.101 -15.498 1.00 20.71 C

ATOM 468 OD1 ASP A 61 8.498 -13.021 -14.955 1.00 25.67 O

ATOM 469 OD2 ASP A 61 6.904 -12.320 -16.279 1.00 25.97 O

ATOM 470 N ALA A 62 9.227 -8.197 -13.323 1.00 14.10 N

ATOM 471 CA ALA A 62 9.769 -6.842 -13.172 1.00 13.76 C

ATOM 472 C ALA A 62 11.075 -6.835 -12.363 1.00 13.64 C

ATOM 473 O ALA A 62 11.981 -6.043 -12.645 1.00 14.15 O

ATOM 474 CB ALA A 62 8.738 -5.917 -12.543 1.00 13.79 C

ATOM 475 N ILE A 63 11.178 -7.724 -11.374 1.00 13.07 N

ATOM 476 CA ILE A 63 12.427 -7.872 -10.618 1.00 13.00 C

ATOM 477 C ILE A 63 13.516 -8.498 -11.491 1.00 13.47 C

ATOM 478 O ILE A 63 14.671 -8.062 -11.462 1.00 13.84 O

ATOM 479 CB ILE A 63 12.236 -8.673 -9.294 1.00 13.12 C

ATOM 480 CG1 ILE A 63 11.197 -7.977 -8.408 1.00 12.42 C

ATOM 481 CG2 ILE A 63 13.558 -8.769 -8.538 1.00 12.66 C

ATOM 482 CD1 ILE A 63 10.599 -8.840 -7.284 1.00 13.31 C

ATOM 483 N LYS A 64 13.154 -9.513 -12.270 1.00 14.23 N

ATOM 484 CA LYS A 64 14.108 -10.114 -13.199 1.00 15.11 C

ATOM 485 C LYS A 64 14.731 -9.055 -14.106 1.00 15.42 C

ATOM 486 O LYS A 64 15.934 -9.081 -14.360 1.00 15.84 O

ATOM 487 CB LYS A 64 13.442 -11.186 -14.054 1.00 15.54 C

ATOM 488 CG LYS A 64 13.219 -12.487 -13.344 1.00 17.14 C

ATOM 489 CD LYS A 64 12.583 -13.482 -14.292 1.00 19.58 C

ATOM 490 CE LYS A 64 12.372 -14.807 -13.608 1.00 22.74 C

ATOM 491 NZ LYS A 64 11.647 -15.742 -14.503 1.00 25.72 N

ATOM 492 N ALA A 65 13.898 -8.126 -14.580 1.00 15.94 N

ATOM 493 CA ALA A 65 14.319 -7.055 -15.494 1.00 15.89 C

ATOM 494 C ALA A 65 15.347 -6.085 -14.889 1.00 16.07 C

ATOM 495 O ALA A 65 16.037 -5.360 -15.620 1.00 16.68 O

ATOM 496 CB ALA A 65 13.089 -6.287 -16.001 1.00 15.92 C

ATOM 497 N LEU A 66 15.445 -6.078 -13.560 1.00 15.66 N

ATOM 498 CA LEU A 66 16.436 -5.265 -12.848 1.00 15.43 C

ATOM 499 C LEU A 66 17.809 -5.922 -12.813 1.00 15.14 C

ATOM 500 O LEU A 66 18.770 -5.332 -12.327 1.00 14.93 O

ATOM 501 CB LEU A 66 15.998 -5.023 -11.405 1.00 15.80 C

ATOM 502 CG LEU A 66 14.566 -4.575 -11.140 1.00 17.18 C

ATOM 503 CD1 LEU A 66 14.327 -4.617 -9.645 1.00 18.91 C