HEADER COMPLEX (SERINE PROTEASE/INHIBITORS) 06-FEB-98 1A4W

TITLE CRYSTAL STRUCTURES OF THROMBIN WITH THIAZOLE-CONTAINING

TITLE 2 INHIBITORS: PROBES OF THE S1' BINDING SITE

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: ALPHA-THROMBIN (SMALL SUBUNIT);

COMPND 3 CHAIN: L;

COMPND 4 EC: 3.4.21.5;

COMPND 5 MOL_ID: 2;

COMPND 6 MOLECULE: ALPHA-THROMBIN (LARGE SUBUNIT);

COMPND 7 CHAIN: H;

COMPND 8 EC: 3.4.21.5;

COMPND 9 MOL_ID: 3;

COMPND 10 MOLECULE: HIRUGEN;

COMPND 11 CHAIN: I;

COMPND 12 ENGINEERED: YES

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;

SOURCE 3 ORGANISM_COMMON: HUMAN;

SOURCE 4 ORGANISM_TAXID: 9606;

SOURCE 5 ORGAN: BLOOD;

SOURCE 6 TISSUE: BLOOD;

SOURCE 7 MOL_ID: 2;

SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;

SOURCE 9 ORGANISM_COMMON: HUMAN;

SOURCE 10 ORGANISM_TAXID: 9606;

SOURCE 11 ORGAN: BLOOD;

SOURCE 12 TISSUE: BLOOD;

SOURCE 13 MOL_ID: 3

KEYWDS COMPLEX (SERINE PROTEASE/INHIBITORS), BLOOD COAGULATION

EXPDTA X-RAY DIFFRACTION

AUTHOR J.H.MATTHEWS,R.KRISHNAN,M.J.COSTANZO,B.E.MARYANOFF,

AUTHOR 2 A.TULINSKY

REVDAT 2 24-FEB-09 1A4W 1 VERSN

REVDAT 1 29-APR-98 1A4W 0

JRNL AUTH J.H.MATTHEWS,R.KRISHNAN,M.J.COSTANZO,B.E.MARYANOFF,

JRNL AUTH 2 A.TULINSKY

JRNL TITL CRYSTAL STRUCTURES OF THROMBIN WITH

JRNL TITL 2 THIAZOLE-CONTAINING INHIBITORS: PROBES OF THE S1'

JRNL TITL 3 BINDING SITE.

JRNL REF BIOPHYS.J. V. 71 2830 1996

JRNL REFN ISSN 0006-3495

JRNL PMID 8913620

REMARK 1

REMARK 1 REFERENCE 1

REMARK 1 AUTH J.VIJAYALAKSHMI,K.P.PADMANABHAN,K.G.MANN,A.TULINSKY

REMARK 1 TITL THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2,

REMARK 1 TITL 2 HIRUGEN-, AND PPACK-THROMBIN: CHANGES ACCOMPANYING

REMARK 1 TITL 3 ACTIVATION AND EXOSITE BINDING TO THROMBIN

REMARK 1 REF PROTEIN SCI. V. 3 2254 1994

REMARK 1 REFN ISSN 0961-8368

REMARK 1 REFERENCE 2

REMARK 1 AUTH A.TULINSKY,X.QIU

REMARK 1 TITL ACTIVE SITE AND EXOSITE BINDING OF ALPHA-THROMBIN

REMARK 1 REF BLOOD COAGULATION V. 4 305 1993

REMARK 1 REF 2 FIBRINOLYSIS

REMARK 1 REFN ISSN 0957-5235

REMARK 1 REFERENCE 3

REMARK 1 AUTH X.QIU,K.P.PADMANABHAN,V.E.CARPEROS,A.TULINSKY,

REMARK 1 AUTH 2 T.KLINE,J.M.MARAGANORE,J.W.FENTON II

REMARK 1 TITL STRUCTURE OF THE HIRULOG 3-THROMBIN COMPLEX AND

REMARK 1 TITL 2 NATURE OF THE S' SUBSITES OF SUBSTRATES AND

REMARK 1 TITL 3 INHIBITORS

REMARK 1 REF BIOCHEMISTRY V. 31 11689 1992

REMARK 1 REFN ISSN 0006-2960

REMARK 2

REMARK 2 RESOLUTION. 1.80 ANGSTROMS.

REMARK 3

REMARK 3 REFINEMENT.

REMARK 3 PROGRAM : PROFFT

REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL

REMARK 3

REMARK 3 DATA USED IN REFINEMENT.

REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80

REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00

REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000

REMARK 3 COMPLETENESS FOR RANGE (%) : 65.0

REMARK 3 NUMBER OF REFLECTIONS : 19906

REMARK 3

REMARK 3 FIT TO DATA USED IN REFINEMENT.

REMARK 3 CROSS-VALIDATION METHOD : NULL

REMARK 3 FREE R VALUE TEST SET SELECTION : NULL

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

REMARK 3 R VALUE (WORKING SET) : 0.155

REMARK 3 FREE R VALUE : NULL

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

REMARK 3 FREE R VALUE TEST SET COUNT : NULL

REMARK 3

REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.

REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL

REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL

REMARK 3 FREE R VALUE (NO CUTOFF) : NULL

REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL

REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL

REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL

REMARK 3

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

REMARK 3 PROTEIN ATOMS : 2080

REMARK 3 NUCLEIC ACID ATOMS : 0

REMARK 3 HETEROGEN ATOMS : 198

REMARK 3 SOLVENT ATOMS : 157

REMARK 3

REMARK 3 B VALUES.

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

REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.00

REMARK 3 OVERALL ANISOTROPIC B VALUE.

REMARK 3 B11 (A**2) : NULL

REMARK 3 B22 (A**2) : NULL

REMARK 3 B33 (A**2) : NULL

REMARK 3 B12 (A**2) : NULL

REMARK 3 B13 (A**2) : NULL

REMARK 3 B23 (A**2) : NULL

REMARK 3

REMARK 3 ESTIMATED COORDINATE ERROR.

REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL

REMARK 3 ESD FROM SIGMAA (A) : NULL

REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL

REMARK 3

REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.

REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA

REMARK 3 BOND LENGTH (A) : 0.016 ; 0.015

REMARK 3 ANGLE DISTANCE (A) : 0.042 ; 0.030

REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.051 ; 0.045

REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL

REMARK 3

REMARK 3 PLANE RESTRAINT (A) : 0.032 ; 0.030

REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.210 ; 0.150

REMARK 3

REMARK 3 NON-BONDED CONTACT RESTRAINTS.

REMARK 3 SINGLE TORSION (A) : 0.190 ; 0.600

REMARK 3 MULTIPLE TORSION (A) : 0.210 ; 0.600

REMARK 3 H-BOND (X...Y) (A) : 0.250 ; 0.600

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

REMARK 3

REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.

REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL

REMARK 3 PLANAR (DEGREES) : 4.000 ; 3.000

REMARK 3 STAGGERED (DEGREES) : 20.000; 15.000

REMARK 3 TRANSVERSE (DEGREES) : 30.000; 20.000

REMARK 3

REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA

REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 1.000

REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.800 ; 1.500

REMARK 3 SIDE-CHAIN BOND (A**2) : 2.800 ; 2.000

REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.100 ; 2.500

REMARK 3

REMARK 3 OTHER REFINEMENT REMARKS: NULL

REMARK 4

REMARK 4 1A4W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08

REMARK 100

REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION : 15-MAR-94

REMARK 200 TEMPERATURE (KELVIN) : 298

REMARK 200 PH : 7.3

REMARK 200 NUMBER OF CRYSTALS USED : 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) : N

REMARK 200 RADIATION SOURCE : ROTATING ANODE

REMARK 200 BEAMLINE : NULL

REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R

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

REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418

REMARK 200 MONOCHROMATOR : GRAPHITE(002)

REMARK 200 OPTICS : COLLIMATOR

REMARK 200

REMARK 200 DETECTOR TYPE : IMAGE PLATE

REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II

REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS

REMARK 200 DATA SCALING SOFTWARE : R-AXIS

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23968

REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800

REMARK 200 RESOLUTION RANGE LOW (A) : 44.200

REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000

REMARK 200

REMARK 200 OVERALL.

REMARK 200 COMPLETENESS FOR RANGE (%) : 69.5

REMARK 200 DATA REDUNDANCY : 2.200

REMARK 200 R MERGE (I) : 0.05200

REMARK 200 R SYM (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00

REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0

REMARK 200 DATA REDUNDANCY IN SHELL : NULL

REMARK 200 R MERGE FOR SHELL (I) : 0.16500

REMARK 200 R SYM FOR SHELL (I) : NULL

REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.610

REMARK 200

REMARK 200 DIFFRACTION PROTOCOL: NULL

REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PREVIOUS STRUCTURE

REMARK 200 SOFTWARE USED: NULL

REMARK 200 STARTING MODEL: PDB ENTRY 1FPC

REMARK 200

REMARK 200 REMARK: NULL

REMARK 280

REMARK 280 CRYSTAL

REMARK 280 SOLVENT CONTENT, VS (%): 51.00

REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40

REMARK 280

REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM PHOSPHATE BUFFER AT PH

REMARK 280 7.3, 27-28% PEG 8000; HANGING DROPS WITH MACROSEEDING, VAPOR

REMARK 280 DIFFUSION - HANGING DROP AND MACROSEEDING

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY

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

REMARK 290

REMARK 290 SYMOP SYMMETRY

REMARK 290 NNNMMM OPERATOR

REMARK 290 1555 X,Y,Z

REMARK 290 2555 -X,Y,-Z

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

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

REMARK 290

REMARK 290 WHERE NNN -> OPERATOR NUMBER

REMARK 290 MMM -> TRANSLATION VECTOR

REMARK 290

REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

REMARK 290 RELATED MOLECULES.

REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000

REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000

REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000

REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000

REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.73500

REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.00000

REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000

REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.73500

REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.00000

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: TRIMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I

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 400

REMARK 400 COMPOUND

REMARK 400

REMARK 400 THROMBIN IS CLEAVED BETWEEN RESIDUES 15 AND 16. CHAIN

REMARK 400 IDENTIFIER *L* IS USED FOR RESIDUES 1H - 15 AND CHAIN

REMARK 400 IDENTIFIER *H* IS USED FOR RESIDUES 16 - 247. CHAIN

REMARK 400 IDENTIFIER *I* IS USED FOR HIRUGEN, THE CARBOXYL.

REMARK 400 RESIDUES DAN R 373, ARG R 350, PIP R 375, AND TZL R 377

REMARK 400 CONSTITUTE THE ACTIVE SITE INHIBITOR.

REMARK 465

REMARK 465 MISSING RESIDUES

REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE

REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN

REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)

REMARK 465

REMARK 465 M RES C SSSEQI

REMARK 465 THR L 1H

REMARK 465 PHE L 1G

REMARK 465 GLY L 1F

REMARK 465 SER L 1E

REMARK 465 GLY L 1D

REMARK 465 GLU L 1C

REMARK 465 ALA L 1B

REMARK 465 ASP L 14L

REMARK 465 GLY L 14M

REMARK 465 ARG L 14N

REMARK 465 THR H 146A

REMARK 465 TRP H 146B

REMARK 465 THR H 146C

REMARK 465 ALA H 146D

REMARK 465 ASN H 146E

REMARK 465 VAL H 146F

REMARK 465 GLY H 146G

REMARK 465 LYS H 146H

REMARK 465 PHE H 245

REMARK 465 GLY H 246

REMARK 465 GLU H 247

REMARK 465 ASN I 353

REMARK 465 GLY I 354

REMARK 465 LEU I 364

REMARK 470

REMARK 470 MISSING ATOM

REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;

REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;

REMARK 470 I=INSERTION CODE):

REMARK 470 M RES CSSEQI ATOMS

REMARK 470 LYS L 14A CG CD CE NZ

REMARK 470 ARG L 14D CG CD NE CZ NH1 NH2

REMARK 470 ILE L 14K CB CG1 CG2 CD1

REMARK 470 ASN H 62 CB CG OD1 ND2

REMARK 470 ARG H 75 CB CG CD NE CZ NH1 NH2

REMARK 470 ARG H 77A CB CG CD NE CZ NH1 NH2

REMARK 470 LYS H 110 CG CD CE NZ

REMARK 470 ASP H 125 CG OD1 OD2

REMARK 470 LYS H 145 CG CD CE NZ

REMARK 470 ASP H 186A CB CG OD1 OD2

REMARK 470 LYS H 240 CD CE NZ

REMARK 470 GLN H 244 CB CG CD OE1 NE2

REMARK 470 ASP I 355 CB CG OD1 OD2

REMARK 470 GLU I 358 CB CG CD OE1 OE2

REMARK 470 GLU I 361 CG CD OE1 OE2

REMARK 470 GLU I 362 CG CD OE1 OE2

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT

REMARK 500

REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.

REMARK 500

REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE

REMARK 500 NH1 ARG H 50 O LEU H 108 1.96

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: COVALENT BOND ANGLES

REMARK 500

REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES

REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE

REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN

REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).

REMARK 500

REMARK 500 STANDARD TABLE:

REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)

REMARK 500

REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999

REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996

REMARK 500

REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3

REMARK 500 ASP L 1A CB - CG - OD1 ANGL. DEV. = -8.5 DEGREES

REMARK 500 ARG L 4 NE - CZ - NH2 ANGL. DEV. = 5.5 DEGREES

REMARK 500 SER L 11 N - CA - CB ANGL. DEV. = 16.1 DEGREES

REMARK 500 LEU L 14G CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES

REMARK 500 ASP H 21 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES

REMARK 500 ASP H 21 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES

REMARK 500 ARG H 35 NH1 - CZ - NH2 ANGL. DEV. = 8.3 DEGREES

REMARK 500 ARG H 35 NE - CZ - NH2 ANGL. DEV. = -8.4 DEGREES

REMARK 500 ASP H 49 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES

REMARK 500 ARG H 50 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES

REMARK 500 ARG H 50 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES

REMARK 500 TYR H 60A CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES

REMARK 500 LYS H 60F CA - CB - CG ANGL. DEV. = 17.9 DEGREES

REMARK 500 LEU H 64 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES

REMARK 500 ARG H 73 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES

REMARK 500 ARG H 73 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES

REMARK 500 THR H 74 N - CA - CB ANGL. DEV. = -17.7 DEGREES

REMARK 500 THR H 74 OG1 - CB - CG2 ANGL. DEV. = 18.9 DEGREES

REMARK 500 SER H 83 N - CA - CB ANGL. DEV. = 9.2 DEGREES

REMARK 500 ARG H 93 CD - NE - CZ ANGL. DEV. = 20.6 DEGREES

REMARK 500 ARG H 93 NE - CZ - NH1 ANGL. DEV. = 8.4 DEGREES

REMARK 500 ARG H 93 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES

REMARK 500 TYR H 94 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES

REMARK 500 ASP H 100 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES

REMARK 500 ARG H 101 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES

REMARK 500 ARG H 101 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES

REMARK 500 ASP H 102 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES

REMARK 500 ARG H 137 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES

REMARK 500 VAL H 138 O - C - N ANGL. DEV. = 11.8 DEGREES

REMARK 500 VAL H 154 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES

REMARK 500 ARG H 165 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES

REMARK 500 ARG H 165 NE - CZ - NH1 ANGL. DEV. = 9.7 DEGREES

REMARK 500 ARG H 165 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES

REMARK 500 ASP H 170 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES

REMARK 500 ARG H 173 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES

REMARK 500 TYR H 184A CB - CG - CD1 ANGL. DEV. = -6.2 DEGREES

REMARK 500 GLU H 186B CG - CD - OE1 ANGL. DEV. = 14.4 DEGREES

REMARK 500 ARG H 206 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES

REMARK 500 TYR H 208 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES

REMARK 500 TYR H 228 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES

REMARK 500 PHE H 232 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES

REMARK 500 ARG H 233 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES

REMARK 500 ARG H 233 NE - CZ - NH2 ANGL. DEV. = -9.4 DEGREES

REMARK 500 VAL H 241 CA - CB - CG1 ANGL. DEV. = 12.4 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 PHE L 7 -78.63 -128.28

REMARK 500 SER H 36A 117.15 -163.62

REMARK 500 ALA H 44 -175.78 -171.19

REMARK 500 TYR H 60A 79.88 -154.74

REMARK 500 ASN H 60G 83.28 -160.79

REMARK 500 HIS H 71 -56.01 -134.72

REMARK 500 ASN H 78 -0.86 71.84

REMARK 500 GLU H 97A -63.15 -131.02

REMARK 500 LYS H 186D 143.14 179.93

REMARK 500 SER H 214 -98.33 -112.77

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: PLANAR GROUPS

REMARK 500

REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL

REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE

REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN

REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS

REMARK 500 AN RMSD GREATER THAN THIS VALUE

REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;

REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).

REMARK 500

REMARK 500 M RES CSSEQI RMS TYPE

REMARK 500 ARG H 73 0.12 SIDE_CHAIN

REMARK 500 PHE H 232 0.08 SIDE_CHAIN

REMARK 500

REMARK 500 REMARK: NULL

REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY

REMARK 500

REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY

REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER

REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;

REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;

REMARK 500 I=INSERTION CODE).

REMARK 500

REMARK 500 M RES CSSEQI ANGLE

REMARK 500 SER H 20 11.04

REMARK 500 GLN H 151 10.60

REMARK 500

REMARK 500 REMARK: NULL

REMARK 525

REMARK 525 SOLVENT

REMARK 525

REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT

REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST

REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT

REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE

REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;

REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE

REMARK 525 NUMBER; I=INSERTION CODE):

REMARK 525

REMARK 525 M RES CSSEQI

REMARK 525 HOH H 537 DISTANCE = 5.46 ANGSTROMS

REMARK 620

REMARK 620 METAL COORDINATION

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

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

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NA H 541 NA

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 LYS H 224 O

REMARK 620 2 HOH H 497 O 92.4

REMARK 620 3 ARG H 221A O 95.7 104.9

REMARK 620 4 HOH H 464 O 165.3 87.9 98.3

REMARK 620 5 HOH H 460 O 71.0 89.9 160.8 94.3

REMARK 620 6 HOH H 403 O 90.7 167.3 87.1 86.0 79.4

REMARK 620 N 1 2 3 4 5

REMARK 620

REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL

REMARK 620 NA H 542 NA

REMARK 620 N RES CSSEQI ATOM

REMARK 620 1 LYS H 169 O

REMARK 620 2 THR H 172 O 85.2

REMARK 620 3 HOH H 518 O 84.9 166.5

REMARK 620 4 HOH H 467 O 171.9 94.2 96.9

REMARK 620 5 PHE H 204A O 97.8 93.6 78.7 90.3

REMARK 620 6 HOH H 515 O 74.9 84.0 102.2 97.0 172.5

REMARK 620 N 1 2 3 4 5

REMARK 800

REMARK 800 SITE

REMARK 800 SITE_IDENTIFIER: CAT

REMARK 800 EVIDENCE_CODE: UNKNOWN

REMARK 800 SITE_DESCRIPTION: ACTIVE SITE

REMARK 800 SITE_IDENTIFIER: AC1

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 541

REMARK 800 SITE_IDENTIFIER: AC2

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 542

REMARK 800 SITE_IDENTIFIER: AC3

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANS H 373

REMARK 800 SITE_IDENTIFIER: AC4

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAR H 350

REMARK 800 SITE_IDENTIFIER: AC5

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2EP H 375

REMARK 800 SITE_IDENTIFIER: AC6

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KTH H 377

DBREF 1A4W L 1H 14N UNP P00734 THRB_HUMAN 328 363

DBREF 1A4W H 16 247 UNP P00734 THRB_HUMAN 364 622

DBREF 1A4W I 353 364 UNP P09945 ITH3_HIRME 60 71

SEQADV 1A4W TYS I 363 UNP P09945 TYR 70 CONFLICT

SEQRES 1 L 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO

SEQRES 2 L 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG

SEQRES 3 L 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG

SEQRES 1 H 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO

SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU

SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU

SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS

SEQRES 5 H 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS

SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE

SEQRES 7 H 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN

SEQRES 8 H 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS

SEQRES 9 H 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO

SEQRES 10 H 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU

SEQRES 11 H 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN

SEQRES 12 H 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN

SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU

SEQRES 14 H 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR

SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY

SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO

SEQRES 17 H 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN

SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP

SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS

SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU

SEQRES 1 I 12 ASN GLY ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU

MODRES 1A4W TYS I 363 TYR O-SULFO-L-TYROSINE

HET TYS I 363 16

HET NA H 541 1

HET NA H 542 1

HET ANS H 373 16

HET DAR H 350 11

HET 2EP H 375 8

HET KTH H 377 7

HETNAM TYS O-SULFO-L-TYROSINE

HETNAM NA SODIUM ION

HETNAM ANS 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL

HETNAM 2 ANS ACID)

HETNAM DAR D-ARGININE

HETNAM 2EP 2-ETHYLPIPERIDINE

HETNAM KTH 2-KETOTHIAZOLE

HETSYN ANS DANSYL ACID

FORMUL 3 TYS C9 H11 N O6 S

FORMUL 4 NA 2(NA 1+)

FORMUL 6 ANS C12 H13 N O3 S

FORMUL 6 DAR C6 H15 N4 O2 1+

FORMUL 6 2EP C7 H15 N

FORMUL 7 KTH C4 H3 N O S

FORMUL 8 HOH *157(H2 O)

HELIX 1 H1 ALA H 55 LEU H 60 1 6

HELIX 2 H2 GLU H 164 SER H 171 1 8

HELIX 3 H3 ASP H 125 LEU H 129C 1 8

HELIX 4 H4 VAL H 231 GLN H 244 1 14

SHEET 1 B1 7 PRO H 28 ARG H 35 0

SHEET 2 B1 7 CYS H 42 ASP H 49 -1

SHEET 3 B1 7 ARG H 50 ALA H 56 -1

SHEET 4 B1 7 ARG H 101 LYS H 110 -1

SHEET 5 B1 7 LYS H 81 PRO H 92 -1

SHEET 6 B1 7 ASP H 63 GLY H 69 -1

SHEET 7 B1 7 PRO H 28 ARG H 35 -1

SHEET 1 B2 7 GLY H 133 TRP H 141 0

SHEET 2 B2 7 LEU H 155 ILE H 162 -1

SHEET 3 B2 7 ASN H 179 PRO H 186 -1

SHEET 4 B2 7 GLY H 223 THR H 229 -1

SHEET 5 B2 7 ILE H 212 GLU H 217 -1

SHEET 6 B2 7 GLY H 193 MET H 201 -1

SHEET 7 B2 7 GLY H 133 TRP H 141 -1

SSBOND 1 CYS L 1 CYS H 122 1555 1555 1.97

SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.06

SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.06

SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.09

LINK N TYS I 363 C GLU I 362 1555 1555 1.33

LINK S ANS H 373 N DAR H 350 1555 1555 1.91

LINK N1 2EP H 375 C DAR H 350 1555 1555 1.42

LINK C2' 2EP H 375 C2' KTH H 377 1555 1555 1.48

LINK NA NA H 541 O LYS H 224 1555 1555 2.32

LINK NA NA H 542 O LYS H 169 1555 1555 2.36

LINK NA NA H 542 O THR H 172 1555 1555 2.33

LINK NA NA H 541 O HOH H 497 1555 1555 2.21

LINK NA NA H 541 O ARG H 221A 1555 1555 2.44

LINK NA NA H 541 O HOH H 464 1555 1555 2.37

LINK NA NA H 541 O HOH H 460 1555 1555 2.41

LINK NA NA H 542 O HOH H 518 1555 1555 2.54

LINK NA NA H 542 O HOH H 467 1555 1555 2.39

LINK NA NA H 542 O PHE H 204A 1555 4546 2.43

LINK NA NA H 541 O HOH H 403 1555 1555 2.91

LINK NA NA H 542 O HOH H 515 1555 1555 2.84

CISPEP 1 SER H 36A PRO H 37 0 -2.26

SITE 1 CAT 3 HIS H 57 ASP H 102 SER H 195

SITE 1 AC1 6 ARG H 221A LYS H 224 HOH H 403 HOH H 460

SITE 2 AC1 6 HOH H 464 HOH H 497

SITE 1 AC2 6 LYS H 169 THR H 172 PHE H 204A HOH H 467

SITE 2 AC2 6 HOH H 515 HOH H 518

SITE 1 AC3 8 TYR H 60A GLU H 97A LEU H 99 TRP H 215

SITE 2 AC3 8 GLY H 216 GLY H 219 DAR H 350 HOH H 448

SITE 1 AC4 8 ASP H 189 ALA H 190 TRP H 215 GLY H 216

SITE 2 AC4 8 GLY H 219 ANS H 373 2EP H 375 HOH H 471

SITE 1 AC5 4 TRP H 60D LEU H 99 DAR H 350 KTH H 377

SITE 1 AC6 5 HIS H 57 TRP H 60D LYS H 60F 2EP H 375

SITE 2 AC6 5 HOH H 532

CRYST1 71.470 72.000 73.390 90.00 101.13 90.00 C 1 2 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 0.013992 0.000000 0.002753 0.00000

SCALE2 0.000000 0.013889 0.000000 0.00000

SCALE3 0.000000 0.000000 0.013887 0.00000

ATOM 1 N ASP L 1A 11.095 19.341 20.188 1.00 30.14 N

ATOM 2 CA ASP L 1A 10.070 18.634 19.379 1.00 28.34 C

ATOM 3 C ASP L 1A 9.846 17.102 19.503 1.00 26.08 C

ATOM 4 O ASP L 1A 8.744 16.584 19.162 1.00 23.47 O

ATOM 5 CB ASP L 1A 10.255 18.858 17.853 1.00 37.55 C

ATOM 6 CG ASP L 1A 8.836 19.264 17.401 1.00 42.76 C

ATOM 7 OD1 ASP L 1A 8.058 19.292 18.400 1.00 44.03 O

ATOM 8 OD2 ASP L 1A 8.616 19.668 16.244 1.00 46.88 O

ATOM 9 N CYS L 1 10.835 16.440 20.113 1.00 23.72 N

ATOM 10 CA CYS L 1 10.769 14.970 20.210 1.00 20.89 C

ATOM 11 C CYS L 1 9.580 14.524 21.006 1.00 18.64 C

ATOM 12 O CYS L 1 9.110 15.220 21.912 1.00 19.03 O

ATOM 13 CB CYS L 1 12.117 14.468 20.771 1.00 21.77 C

ATOM 14 SG CYS L 1 12.247 14.885 22.538 1.00 20.55 S

ATOM 15 N GLY L 2 9.089 13.336 20.667 1.00 17.86 N

ATOM 16 CA GLY L 2 8.063 12.669 21.474 1.00 16.86 C

ATOM 17 C GLY L 2 6.676 13.272 21.469 1.00 17.77 C

ATOM 18 O GLY L 2 5.817 12.697 22.177 1.00 18.41 O

ATOM 19 N LEU L 3 6.402 14.258 20.605 1.00 17.18 N

ATOM 20 CA LEU L 3 5.020 14.820 20.506 1.00 17.45 C

ATOM 21 C LEU L 3 4.475 14.399 19.121 1.00 18.01 C

ATOM 22 O LEU L 3 5.050 14.872 18.152 1.00 17.71 O

ATOM 23 CB LEU L 3 5.153 16.362 20.592 1.00 18.74 C

ATOM 24 CG LEU L 3 5.596 16.876 21.959 1.00 19.10 C

ATOM 25 CD1 LEU L 3 5.857 18.363 21.889 1.00 24.28 C

ATOM 26 CD2 LEU L 3 4.508 16.554 22.974 1.00 18.04 C

ATOM 27 N ARG L 4 3.440 13.556 19.122 1.00 18.12 N

ATOM 28 CA ARG L 4 3.071 12.990 17.788 1.00 17.89 C

ATOM 29 C ARG L 4 2.134 13.988 17.068 1.00 17.92 C

ATOM 30 O ARG L 4 1.174 14.450 17.660 1.00 17.08 O

ATOM 31 CB ARG L 4 2.467 11.627 18.029 1.00 16.85 C

ATOM 32 CG ARG L 4 3.367 10.563 18.782 1.00 16.70 C

ATOM 33 CD ARG L 4 2.419 9.446 19.142 1.00 13.02 C

ATOM 34 NE ARG L 4 1.484 9.747 20.203 1.00 15.17 N

ATOM 35 CZ ARG L 4 0.562 8.963 20.751 1.00 13.48 C

ATOM 36 NH1 ARG L 4 0.443 7.685 20.335 1.00 17.03 N

ATOM 37 NH2 ARG L 4 -0.275 9.310 21.731 1.00 13.89 N

ATOM 38 N PRO L 5 2.364 14.134 15.770 1.00 18.55 N

ATOM 39 CA PRO L 5 1.539 15.061 14.927 1.00 19.37 C

ATOM 40 C PRO L 5 0.083 14.714 14.917 1.00 20.23 C

ATOM 41 O PRO L 5 -0.823 15.558 15.077 1.00 22.67 O

ATOM 42 CB PRO L 5 2.174 15.030 13.563 1.00 18.78 C

ATOM 43 CG PRO L 5 3.508 14.382 13.705 1.00 20.38 C

ATOM 44 CD PRO L 5 3.525 13.664 15.054 1.00 18.50 C

ATOM 45 N LEU L 6 -0.219 13.406 15.013 1.00 20.42 N

ATOM 46 CA LEU L 6 -1.617 12.995 14.949 1.00 19.27 C

ATOM 47 C LEU L 6 -2.214 12.854 16.308 1.00 19.13 C

ATOM 48 O LEU L 6 -3.421 12.472 16.320 1.00 18.99 O

ATOM 49 CB LEU L 6 -1.771 11.753 14.052 1.00 16.88 C

ATOM 50 CG LEU L 6 -1.303 11.960 12.608 1.00 20.87 C

ATOM 51 CD1 LEU L 6 -1.485 10.637 11.829 1.00 18.53 C

ATOM 52 CD2 LEU L 6 -2.202 13.079 12.077 1.00 23.77 C

ATOM 53 N PHE L 7 -1.435 13.030 17.371 1.00 18.39 N

ATOM 54 CA PHE L 7 -2.108 12.832 18.688 1.00 19.38 C

ATOM 55 C PHE L 7 -1.848 14.061 19.592 1.00 19.71 C

ATOM 56 O PHE L 7 -2.605 15.044 19.526 1.00 21.49 O

ATOM 57 CB PHE L 7 -1.595 11.495 19.287 1.00 19.65 C

ATOM 58 CG PHE L 7 -2.202 10.288 18.617 1.00 19.95 C

ATOM 59 CD1 PHE L 7 -3.522 9.915 18.973 1.00 19.04 C

ATOM 60 CD2 PHE L 7 -1.516 9.686 17.561 1.00 17.87 C

ATOM 61 CE1 PHE L 7 -4.109 8.849 18.260 1.00 17.67 C

ATOM 62 CE2 PHE L 7 -2.101 8.627 16.834 1.00 16.67 C

ATOM 63 CZ PHE L 7 -3.367 8.222 17.221 1.00 16.37 C

ATOM 64 N GLU L 8 -0.649 14.133 20.195 1.00 18.01 N

ATOM 65 CA GLU L 8 -0.356 15.200 21.140 1.00 16.75 C

ATOM 66 C GLU L 8 -0.499 16.586 20.484 1.00 17.59 C

ATOM 67 O GLU L 8 -1.173 17.450 21.090 1.00 17.01 O

ATOM 68 CB GLU L 8 1.118 15.113 21.640 1.00 17.14 C

ATOM 69 CG GLU L 8 1.159 14.046 22.770 1.00 15.66 C

ATOM 70 CD GLU L 8 1.202 12.632 22.265 1.00 15.06 C

ATOM 71 OE1 GLU L 8 1.728 12.484 21.134 1.00 17.16 O

ATOM 72 OE2 GLU L 8 0.840 11.717 23.033 1.00 19.50 O

ATOM 73 N LYS L 9 -0.044 16.610 19.273 1.00 18.40 N

ATOM 74 CA LYS L 9 -0.065 17.898 18.545 1.00 20.91 C

ATOM 75 C LYS L 9 -1.500 18.323 18.259 1.00 21.80 C

ATOM 76 O LYS L 9 -1.601 19.532 18.107 1.00 21.53 O

ATOM 77 CB LYS L 9 0.767 17.946 17.282 1.00 24.39 C

ATOM 78 CG LYS L 9 2.260 17.710 17.521 1.00 29.43 C

ATOM 79 CD LYS L 9 2.957 18.892 18.149 1.00 35.29 C

ATOM 80 CE LYS L 9 4.341 19.214 17.604 1.00 38.83 C

ATOM 81 NZ LYS L 9 4.724 20.558 18.197 1.00 41.45 N

ATOM 82 N LYS L 10 -2.499 17.479 18.376 1.00 21.52 N

ATOM 83 CA LYS L 10 -3.896 17.811 18.056 1.00 23.02 C

ATOM 84 C LYS L 10 -4.754 17.625 19.273 1.00 22.04 C

ATOM 85 O LYS L 10 -5.984 17.776 19.242 1.00 22.20 O

ATOM 86 CB LYS L 10 -4.470 16.864 16.955 1.00 24.25 C

ATOM 87 CG LYS L 10 -3.944 17.220 15.567 1.00 28.75 C

ATOM 88 CD LYS L 10 -3.842 16.029 14.632 1.00 33.60 C

ATOM 89 CE LYS L 10 -4.561 16.212 13.305 1.00 36.09 C

ATOM 90 NZ LYS L 10 -6.027 16.109 13.685 1.00 38.97 N

ATOM 91 N SER L 11 -4.027 17.312 20.349 1.00 22.33 N

ATOM 92 CA SER L 11 -4.667 16.965 21.604 1.00 22.03 C

ATOM 93 C SER L 11 -5.592 15.760 21.359 1.00 22.61 C

ATOM 94 O SER L 11 -6.532 15.724 22.174 1.00 24.34 O

ATOM 95 CB SER L 11 -5.458 17.901 22.510 1.00 25.62 C

ATOM 96 OG SER L 11 -5.424 19.222 22.024 1.00 35.68 O

ATOM 97 N LEU L 12 -5.210 14.737 20.606 1.00 21.81 N

ATOM 98 CA LEU L 12 -6.064 13.530 20.587 1.00 21.97 C

ATOM 99 C LEU L 12 -5.275 12.448 21.363 1.00 22.30 C

ATOM 100 O LEU L 12 -4.034 12.473 21.307 1.00 21.13 O

ATOM 101 CB LEU L 12 -6.209 13.152 19.106 1.00 19.02 C

ATOM 102 CG LEU L 12 -6.935 14.257 18.307 1.00 23.88 C

ATOM 103 CD1 LEU L 12 -6.996 13.845 16.861 1.00 23.12 C

ATOM 104 CD2 LEU L 12 -8.339 14.345 18.891 1.00 22.97 C

ATOM 105 N GLU L 13 -5.997 11.588 22.006 1.00 22.34 N

ATOM 106 CA GLU L 13 -5.303 10.472 22.709 1.00 24.14 C

ATOM 107 C GLU L 13 -5.380 9.199 21.913 1.00 23.81 C

ATOM 108 O GLU L 13 -6.470 8.998 21.302 1.00 25.39 O

ATOM 109 CB GLU L 13 -6.150 10.222 23.967 1.00 26.06 C

ATOM 110 CG GLU L 13 -5.978 11.320 24.994 1.00 36.69 C

ATOM 111 CD GLU L 13 -6.421 11.003 26.391 1.00 42.27 C

ATOM 112 OE1 GLU L 13 -6.995 9.892 26.528 1.00 46.63 O

ATOM 113 OE2 GLU L 13 -6.208 11.780 27.305 1.00 46.31 O

ATOM 114 N ASP L 14 -4.407 8.330 21.972 1.00 22.45 N

ATOM 115 CA ASP L 14 -4.526 6.972 21.347 1.00 21.73 C

ATOM 116 C ASP L 14 -5.408 6.153 22.306 1.00 20.49 C

ATOM 117 O ASP L 14 -5.818 6.528 23.416 1.00 19.90 O

ATOM 118 CB ASP L 14 -3.184 6.429 20.919 1.00 20.07 C

ATOM 119 CG ASP L 14 -2.229 6.045 22.052 1.00 17.98 C

ATOM 120 OD1 ASP L 14 -2.698 5.227 22.871 1.00 21.20 O

ATOM 121 OD2 ASP L 14 -1.046 6.434 21.950 1.00 20.58 O

ATOM 122 N LYS L 14A -5.864 5.031 21.805 1.00 21.06 N

ATOM 123 CA LYS L 14A -6.839 4.178 22.443 1.00 21.93 C

ATOM 124 C LYS L 14A -6.366 3.509 23.720 1.00 23.19 C

ATOM 125 O LYS L 14A -7.278 3.215 24.547 1.00 24.43 O

ATOM 126 CB LYS L 14A -7.402 3.138 21.440 1.00 26.01 C

ATOM 127 N THR L 14B -5.057 3.419 23.938 1.00 22.46 N

ATOM 128 CA THR L 14B -4.630 2.812 25.224 1.00 22.68 C

ATOM 129 C THR L 14B -3.665 3.661 26.015 1.00 22.44 C

ATOM 130 O THR L 14B -3.189 3.038 27.011 1.00 23.82 O

ATOM 131 CB THR L 14B -3.981 1.384 25.060 1.00 21.88 C

ATOM 132 OG1 THR L 14B -2.778 1.473 24.244 1.00 20.69 O

ATOM 133 CG2 THR L 14B -4.993 0.404 24.463 1.00 24.38 C

ATOM 134 N GLU L 14C -3.262 4.834 25.632 1.00 21.92 N

ATOM 135 CA GLU L 14C -2.281 5.549 26.481 1.00 22.63 C

ATOM 136 C GLU L 14C -2.784 5.838 27.885 1.00 24.40 C

ATOM 137 O GLU L 14C -1.920 5.853 28.810 1.00 24.63 O

ATOM 138 CB GLU L 14C -1.728 6.812 25.841 1.00 21.93 C

ATOM 139 CG GLU L 14C -2.887 7.759 25.512 1.00 20.89 C

ATOM 140 CD GLU L 14C -2.373 9.016 24.883 1.00 22.13 C

ATOM 141 OE1 GLU L 14C -2.275 9.186 23.690 1.00 23.94 O

ATOM 142 OE2 GLU L 14C -2.186 9.887 25.756 1.00 23.30 O

ATOM 143 N ARG L 14D -4.072 5.948 28.168 1.00 24.26 N

ATOM 144 CA ARG L 14D -4.641 6.122 29.488 1.00 25.80 C

ATOM 145 C ARG L 14D -4.150 5.006 30.459 1.00 25.99 C

ATOM 146 O ARG L 14D -4.045 5.215 31.686 1.00 25.42 O

ATOM 147 CB ARG L 14D -6.179 5.984 29.466 1.00 31.17 C

ATOM 148 N GLU L 14E -4.103 3.807 29.891 1.00 26.36 N

ATOM 149 CA GLU L 14E -3.631 2.631 30.658 1.00 26.18 C

ATOM 150 C GLU L 14E -2.226 2.906 31.156 1.00 25.41 C

ATOM 151 O GLU L 14E -1.892 2.470 32.261 1.00 26.18 O

ATOM 152 CB GLU L 14E -3.681 1.336 29.867 1.00 28.05 C

ATOM 153 CG GLU L 14E -3.070 0.083 30.459 1.00 33.29 C

ATOM 154 CD GLU L 14E -2.969 -1.192 29.667 1.00 34.03 C

ATOM 155 OE1 GLU L 14E -3.332 -1.074 28.479 1.00 34.13 O

ATOM 156 OE2 GLU L 14E -2.630 -2.275 30.156 1.00 35.06 O

ATOM 157 N LEU L 14F -1.348 3.524 30.386 1.00 24.50 N

ATOM 158 CA LEU L 14F -0.006 3.833 30.879 1.00 23.99 C

ATOM 159 C LEU L 14F -0.091 4.854 32.041 1.00 24.26 C

ATOM 160 O LEU L 14F 0.422 4.617 33.153 1.00 22.84 O

ATOM 161 CB LEU L 14F 0.781 4.375 29.700 1.00 21.42 C

ATOM 162 CG LEU L 14F 1.475 3.337 28.808 1.00 23.24 C

ATOM 163 CD1 LEU L 14F 0.628 2.112 28.674 1.00 22.76 C

ATOM 164 CD2 LEU L 14F 1.842 4.008 27.493 1.00 21.79 C

ATOM 165 N LEU L 14G -0.729 5.971 31.715 1.00 23.55 N

ATOM 166 CA LEU L 14G -0.851 7.043 32.726 1.00 23.72 C

ATOM 167 C LEU L 14G -1.432 6.536 34.017 1.00 23.57 C

ATOM 168 O LEU L 14G -1.013 6.946 35.128 1.00 23.28 O

ATOM 169 CB LEU L 14G -1.556 8.261 32.130 1.00 25.86 C

ATOM 170 CG LEU L 14G -0.858 9.125 31.096 1.00 28.42 C

ATOM 171 CD1 LEU L 14G 0.556 9.649 31.304 1.00 25.61 C

ATOM 172 CD2 LEU L 14G -0.874 8.435 29.722 1.00 31.26 C

ATOM 173 N GLU L 14H -2.424 5.694 33.935 1.00 24.11 N

ATOM 174 CA GLU L 14H -3.043 5.235 35.174 1.00 25.85 C

ATOM 175 C GLU L 14H -2.074 4.373 35.958 1.00 26.07 C

ATOM 176 O GLU L 14H -2.451 4.176 37.131 1.00 26.57 O

ATOM 177 CB GLU L 14H -4.323 4.401 35.011 1.00 27.91 C

ATOM 178 CG GLU L 14H -5.419 5.211 34.318 1.00 35.96 C

ATOM 179 CD GLU L 14H -6.718 4.479 34.136 1.00 39.04 C

ATOM 180 OE1 GLU L 14H -6.593 3.234 34.231 1.00 42.07 O

ATOM 181 OE2 GLU L 14H -7.734 5.163 33.995 1.00 43.42 O

ATOM 182 N SER L 14I -1.012 3.894 35.412 1.00 26.64 N

ATOM 183 CA SER L 14I -0.118 2.994 36.205 1.00 28.38 C

ATOM 184 C SER L 14I 0.953 3.784 36.970 1.00 29.21 C

ATOM 185 O SER L 14I 1.685 3.205 37.785 1.00 30.32 O

ATOM 186 CB SER L 14I 0.546 1.995 35.273 1.00 26.76 C

ATOM 187 OG SER L 14I 1.527 2.626 34.440 1.00 26.27 O

ATOM 188 N TYR L 14J 1.134 5.021 36.595 1.00 29.71 N

ATOM 189 CA TYR L 14J 2.164 5.937 37.054 1.00 31.38 C

ATOM 190 C TYR L 14J 1.671 6.599 38.322 1.00 34.51 C

ATOM 191 O TYR L 14J 1.146 7.709 38.192 1.00 35.41 O

ATOM 192 CB TYR L 14J 2.497 6.986 35.993 1.00 26.63 C

ATOM 193 CG TYR L 14J 2.996 6.541 34.653 1.00 27.22 C

ATOM 194 CD1 TYR L 14J 3.543 5.261 34.480 1.00 25.01 C

ATOM 195 CD2 TYR L 14J 2.930 7.388 33.520 1.00 26.08 C

ATOM 196 CE1 TYR L 14J 3.866 4.827 33.193 1.00 27.70 C

ATOM 197 CE2 TYR L 14J 3.412 6.992 32.279 1.00 24.84 C

ATOM 198 CZ TYR L 14J 3.856 5.702 32.087 1.00 27.55 C

ATOM 199 OH TYR L 14J 4.260 5.239 30.842 1.00 24.38 O

ATOM 200 N ILE L 14K 1.794 5.927 39.444 1.00 36.84 N

ATOM 201 CA ILE L 14K 1.345 6.506 40.743 1.00 39.69 C

ATOM 202 C ILE L 14K 0.014 5.755 41.031 1.00 41.10 C

ATOM 203 O ILE L 14K 0.229 4.528 41.260 1.00 43.24 O

TER 204 ILE L 14K

ATOM 205 N ILE H 16 5.006 -9.272 18.209 1.00 18.00 N

ATOM 206 CA ILE H 16 4.289 -8.948 19.452 1.00 18.46 C

ATOM 207 C ILE H 16 3.264 -10.040 19.684 1.00 21.62 C

ATOM 208 O ILE H 16 2.401 -10.298 18.813 1.00 22.36 O

ATOM 209 CB ILE H 16 3.649 -7.510 19.422 1.00 20.13 C

ATOM 210 CG1 ILE H 16 4.598 -6.342 19.038 1.00 16.87 C

ATOM 211 CG2 ILE H 16 2.823 -7.212 20.706 1.00 17.00 C

ATOM 212 CD1 ILE H 16 5.740 -6.135 20.083 1.00 17.05 C

ATOM 213 N VAL H 17 3.196 -10.623 20.870 1.00 22.67 N

ATOM 214 CA VAL H 17 2.251 -11.640 21.335 1.00 24.14 C

ATOM 215 C VAL H 17 1.213 -11.007 22.252 1.00 25.33 C

ATOM 216 O VAL H 17 1.390 -10.263 23.236 1.00 26.75 O

ATOM 217 CB VAL H 17 2.941 -12.886 21.985 1.00 22.11 C

ATOM 218 CG1 VAL H 17 1.887 -13.875 22.432 1.00 21.21 C

ATOM 219 CG2 VAL H 17 4.016 -13.485 21.128 1.00 18.47 C

ATOM 220 N GLU H 18 -0.064 -11.226 21.872 1.00 26.46 N

ATOM 221 CA GLU H 18 -1.235 -10.713 22.558 1.00 25.57 C

ATOM 222 C GLU H 18 -1.369 -9.196 22.525 1.00 25.17 C

ATOM 223 O GLU H 18 -1.849 -8.686 23.568 1.00 25.14 O

ATOM 224 CB GLU H 18 -1.302 -11.052 24.049 1.00 31.69 C

ATOM 225 CG GLU H 18 -1.463 -12.554 24.287 1.00 41.45 C

ATOM 226 CD GLU H 18 -2.891 -13.036 24.336 1.00 46.71 C

ATOM 227 OE1 GLU H 18 -3.557 -12.394 25.199 1.00 50.00 O

ATOM 228 OE2 GLU H 18 -3.297 -13.991 23.683 1.00 50.00 O

ATOM 229 N GLY H 19 -0.915 -8.626 21.436 1.00 25.00 N

ATOM 230 CA GLY H 19 -0.948 -7.187 21.202 1.00 24.77 C

ATOM 231 C GLY H 19 -2.218 -6.886 20.368 1.00 26.81 C

ATOM 232 O GLY H 19 -3.161 -7.694 20.297 1.00 26.00 O

ATOM 233 N SER H 20 -2.192 -5.666 19.818 1.00 26.26 N

ATOM 234 CA SER H 20 -3.365 -5.232 19.010 1.00 25.89 C

ATOM 235 C SER H 20 -2.775 -4.289 17.987 1.00 24.83 C

ATOM 236 O SER H 20 -1.557 -4.036 17.966 1.00 23.59 O

ATOM 237 CB SER H 20 -4.468 -4.736 19.894 1.00 29.18 C

ATOM 238 OG SER H 20 -4.155 -3.462 20.424 1.00 33.92 O

ATOM 239 N ASP H 21 -3.574 -4.169 16.917 1.00 24.63 N

ATOM 240 CA ASP H 21 -3.168 -3.338 15.769 1.00 24.12 C

ATOM 241 C ASP H 21 -2.978 -1.886 16.253 1.00 23.22 C

ATOM 242 O ASP H 21 -3.817 -1.383 17.002 1.00 23.09 O

ATOM 243 CB ASP H 21 -4.275 -3.390 14.720 1.00 26.77 C

ATOM 244 CG ASP H 21 -4.272 -4.691 13.931 1.00 31.32 C

ATOM 245 OD1 ASP H 21 -3.741 -5.715 14.319 1.00 29.36 O

ATOM 246 OD2 ASP H 21 -4.773 -4.559 12.770 1.00 38.88 O

ATOM 247 N ALA H 22 -1.871 -1.345 15.828 1.00 23.52 N

ATOM 248 CA ALA H 22 -1.634 0.072 16.185 1.00 23.33 C

ATOM 249 C ALA H 22 -2.573 0.943 15.325 1.00 24.24 C

ATOM 250 O ALA H 22 -3.031 0.541 14.231 1.00 24.34 O

ATOM 251 CB ALA H 22 -0.197 0.344 15.841 1.00 20.32 C

ATOM 252 N GLU H 23 -2.837 2.123 15.860 1.00 23.82 N

ATOM 253 CA GLU H 23 -3.546 3.191 15.143 1.00 22.74 C

ATOM 254 C GLU H 23 -2.580 3.859 14.204 1.00 21.74 C

ATOM 255 O GLU H 23 -1.354 3.888 14.437 1.00 20.95 O

ATOM 256 CB GLU H 23 -4.019 4.278 16.112 1.00 19.49 C

ATOM 257 CG GLU H 23 -5.054 3.759 17.092 1.00 24.35 C

ATOM 258 CD GLU H 23 -5.538 4.709 18.159 1.00 28.76 C

ATOM 259 OE1 GLU H 23 -6.316 5.609 17.843 1.00 31.88 O

ATOM 260 OE2 GLU H 23 -5.321 4.329 19.331 1.00 29.89 O

ATOM 261 N ILE H 24 -3.091 4.510 13.166 1.00 21.43 N

ATOM 262 CA ILE H 24 -2.175 5.193 12.217 1.00 20.74 C

ATOM 263 C ILE H 24 -1.479 6.323 13.016 1.00 20.50 C

ATOM 264 O ILE H 24 -2.195 6.988 13.751 1.00 20.47 O

ATOM 265 CB ILE H 24 -2.992 5.702 10.974 1.00 19.53 C

ATOM 266 CG1 ILE H 24 -3.661 4.500 10.253 1.00 21.84 C

ATOM 267 CG2 ILE H 24 -2.017 6.422 9.995 1.00 19.12 C

ATOM 268 CD1 ILE H 24 -2.567 3.569 9.692 1.00 24.10 C

ATOM 269 N GLY H 25 -0.222 6.519 12.778 1.00 20.93 N

ATOM 270 CA GLY H 25 0.658 7.487 13.409 1.00 21.31 C

ATOM 271 C GLY H 25 0.824 7.287 14.920 1.00 20.95 C

ATOM 272 O GLY H 25 1.237 8.274 15.562 1.00 20.35 O

ATOM 273 N MET H 26 0.477 6.146 15.493 1.00 20.22 N

ATOM 274 CA MET H 26 0.601 5.994 16.965 1.00 19.41 C

ATOM 275 C MET H 26 2.089 5.890 17.386 1.00 18.39 C

ATOM 276 O MET H 26 2.394 6.251 18.531 1.00 19.23 O

ATOM 277 CB MET H 26 -0.143 4.752 17.354 1.00 20.64 C

ATOM 278 CG MET H 26 -0.656 4.594 18.745 1.00 23.70 C

ATOM 279 SD MET H 26 -0.862 2.768 18.926 1.00 28.83 S

ATOM 280 CE MET H 26 -1.963 2.717 20.331 1.00 26.00 C

ATOM 281 N SER H 27 2.933 5.415 16.530 1.00 16.27 N

ATOM 282 CA SER H 27 4.368 5.208 16.862 1.00 17.12 C

ATOM 283 C SER H 27 5.246 5.619 15.738 1.00 14.64 C

ATOM 284 O SER H 27 5.898 4.930 14.957 1.00 14.70 O

ATOM 285 CB SER H 27 4.464 3.761 17.397 1.00 20.90 C

ATOM 286 OG SER H 27 5.868 3.496 17.419 1.00 24.38 O

ATOM 287 N PRO H 28 5.380 6.961 15.577 1.00 15.97 N

ATOM 288 CA PRO H 28 5.996 7.545 14.389 1.00 16.31 C

ATOM 289 C PRO H 28 7.486 7.457 14.331 1.00 16.18 C

ATOM 290 O PRO H 28 8.106 7.817 13.320 1.00 14.94 O

ATOM 291 CB PRO H 28 5.573 9.028 14.357 1.00 16.23 C

ATOM 292 CG PRO H 28 5.164 9.263 15.766 1.00 15.06 C

ATOM 293 CD PRO H 28 4.752 7.993 16.418 1.00 13.91 C

ATOM 294 N TRP H 29 8.049 7.046 15.479 1.00 15.48 N

ATOM 295 CA TRP H 29 9.529 6.822 15.480 1.00 14.57 C

ATOM 296 C TRP H 29 9.834 5.360 15.196 1.00 15.24 C

ATOM 297 O TRP H 29 11.002 5.014 15.053 1.00 15.39 O

ATOM 298 CB TRP H 29 10.044 7.135 16.922 1.00 15.71 C

ATOM 299 CG TRP H 29 9.029 6.737 17.951 1.00 13.03 C

ATOM 300 CD1 TRP H 29 8.765 5.476 18.449 1.00 13.65 C

ATOM 301 CD2 TRP H 29 8.067 7.597 18.558 1.00 12.63 C

ATOM 302 NE1 TRP H 29 7.741 5.512 19.328 1.00 12.17 N

ATOM 303 CE2 TRP H 29 7.305 6.800 19.421 1.00 12.32 C

ATOM 304 CE3 TRP H 29 7.861 8.969 18.511 1.00 14.75 C

ATOM 305 CZ2 TRP H 29 6.252 7.333 20.172 1.00 15.46 C

ATOM 306 CZ3 TRP H 29 6.857 9.524 19.290 1.00 14.88 C

ATOM 307 CH2 TRP H 29 6.113 8.700 20.109 1.00 15.02 C

ATOM 308 N GLN H 30 8.838 4.531 14.959 1.00 17.28 N

ATOM 309 CA GLN H 30 9.059 3.110 14.641 1.00 17.51 C

ATOM 310 C GLN H 30 9.750 2.951 13.310 1.00 19.03 C

ATOM 311 O GLN H 30 9.366 3.598 12.280 1.00 20.01 O

ATOM 312 CB GLN H 30 7.790 2.299 14.699 1.00 19.34 C

ATOM 313 CG GLN H 30 7.929 0.823 14.436 1.00 17.15 C

ATOM 314 CD GLN H 30 8.558 0.046 15.569 1.00 17.30 C

ATOM 315 OE1 GLN H 30 8.098 0.299 16.654 1.00 20.69 O

ATOM 316 NE2 GLN H 30 9.402 -0.904 15.198 1.00 21.27 N

ATOM 317 N VAL H 31 10.838 2.190 13.332 1.00 16.74 N

ATOM 318 CA VAL H 31 11.625 1.974 12.153 1.00 17.96 C

ATOM 319 C VAL H 31 11.613 0.492 11.772 1.00 19.31 C

ATOM 320 O VAL H 31 11.628 -0.360 12.711 1.00 19.16 O

ATOM 321 CB VAL H 31 13.047 2.568 12.238 1.00 17.69 C

ATOM 322 CG1 VAL H 31 13.856 2.179 10.994 1.00 17.76 C

ATOM 323 CG2 VAL H 31 13.089 4.053 12.490 1.00 15.35 C

ATOM 324 N MET H 32 11.777 0.162 10.493 1.00 18.34 N

ATOM 325 CA MET H 32 11.830 -1.295 10.156 1.00 19.33 C

ATOM 326 C MET H 32 13.214 -1.480 9.544 1.00 19.74 C

ATOM 327 O MET H 32 13.590 -0.693 8.659 1.00 18.74 O

ATOM 328 CB MET H 32 10.746 -1.763 9.147 1.00 21.17 C

ATOM 329 CG MET H 32 11.035 -3.165 8.612 1.00 20.84 C

ATOM 330 SD MET H 32 9.755 -3.574 7.310 1.00 22.36 S

ATOM 331 CE MET H 32 8.275 -3.732 8.209 1.00 17.40 C

ATOM 332 N LEU H 33 13.971 -2.440 10.065 1.00 19.91 N

ATOM 333 CA LEU H 33 15.236 -2.888 9.516 1.00 22.36 C

ATOM 334 C LEU H 33 14.889 -3.997 8.495 1.00 22.11 C

ATOM 335 O LEU H 33 14.346 -5.055 8.835 1.00 23.62 O

ATOM 336 CB LEU H 33 16.173 -3.438 10.651 1.00 24.80 C

ATOM 337 CG LEU H 33 17.397 -2.585 10.944 1.00 25.86 C

ATOM 338 CD1 LEU H 33 16.966 -1.179 11.274 1.00 25.67 C

ATOM 339 CD2 LEU H 33 18.120 -3.179 12.150 1.00 23.89 C

ATOM 340 N PHE H 34 15.306 -3.741 7.298 1.00 23.99 N

ATOM 341 CA PHE H 34 14.858 -4.571 6.127 1.00 26.50 C

ATOM 342 C PHE H 34 16.054 -5.035 5.318 1.00 28.00 C

ATOM 343 O PHE H 34 16.911 -4.248 4.865 1.00 28.42 O

ATOM 344 CB PHE H 34 13.897 -3.679 5.287 1.00 28.04 C

ATOM 345 CG PHE H 34 13.153 -4.439 4.209 1.00 27.44 C

ATOM 346 CD1 PHE H 34 12.124 -5.321 4.595 1.00 28.85 C

ATOM 347 CD2 PHE H 34 13.656 -4.438 2.907 1.00 26.68 C

ATOM 348 CE1 PHE H 34 11.480 -6.100 3.643 1.00 28.99 C

ATOM 349 CE2 PHE H 34 13.019 -5.231 1.934 1.00 28.27 C

ATOM 350 CZ PHE H 34 11.948 -6.041 2.331 1.00 27.55 C

ATOM 351 N ARG H 35 16.132 -6.363 5.206 1.00 29.69 N

ATOM 352 CA ARG H 35 17.246 -6.951 4.425 1.00 32.22 C

ATOM 353 C ARG H 35 17.046 -6.751 2.929 1.00 34.40 C

ATOM 354 O ARG H 35 15.909 -6.820 2.402 1.00 34.90 O

ATOM 355 CB ARG H 35 17.325 -8.429 4.813 1.00 32.94 C

ATOM 356 CG ARG H 35 18.671 -8.974 4.354 1.00 35.87 C

ATOM 357 CD ARG H 35 18.821 -10.362 4.882 1.00 38.70 C

ATOM 358 NE ARG H 35 20.147 -10.783 4.379 1.00 42.64 N

ATOM 359 CZ ARG H 35 20.538 -12.024 4.740 1.00 43.83 C

ATOM 360 NH1 ARG H 35 19.755 -12.779 5.516 1.00 41.38 N

ATOM 361 NH2 ARG H 35 21.753 -12.318 4.276 1.00 45.03 N

ATOM 362 N LYS H 36 18.113 -6.415 2.214 1.00 36.59 N

ATOM 363 CA LYS H 36 18.016 -6.175 0.756 1.00 38.46 C

ATOM 364 C LYS H 36 17.787 -7.471 -0.021 1.00 39.84 C

ATOM 365 O LYS H 36 16.886 -7.496 -0.881 1.00 41.46 O

ATOM 366 CB LYS H 36 19.214 -5.526 0.144 1.00 36.13 C

ATOM 367 CG LYS H 36 19.455 -4.069 0.535 1.00 36.91 C

ATOM 368 CD LYS H 36 20.724 -3.628 -0.182 1.00 37.63 C

ATOM 369 CE LYS H 36 20.894 -2.136 -0.127 1.00 40.58 C

ATOM 370 NZ LYS H 36 22.321 -1.755 -0.335 1.00 42.58 N

ATOM 371 N SER H 36A 18.449 -8.537 0.358 1.00 40.23 N

ATOM 372 CA SER H 36A 18.338 -9.784 -0.413 1.00 41.21 C

ATOM 373 C SER H 36A 18.842 -10.957 0.405 1.00 41.02 C

ATOM 374 O SER H 36A 20.065 -10.944 0.652 1.00 41.56 O

ATOM 375 CB SER H 36A 19.280 -9.642 -1.630 1.00 43.76 C

ATOM 376 OG SER H 36A 18.866 -10.532 -2.670 1.00 48.38 O

ATOM 377 N PRO H 37 18.000 -11.921 0.721 1.00 41.12 N

ATOM 378 CA PRO H 37 16.581 -11.965 0.399 1.00 40.74 C