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HEADER INTEGRAL MEMBRANE PROTEIN PORIN 24-APR-92 2POR
TITLE STRUCTURE OF PORIN REFINED AT 1.8 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PORIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER CAPSULATUS;
SOURCE 3 ORGANISM_TAXID: 1061
KEYWDS INTEGRAL MEMBRANE PROTEIN PORIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.WEISS,G.E.SCHULZ
REVDAT 7 21-FEB-24 2POR 1 REMARK LINK
REVDAT 6 29-NOV-17 2POR 1 HELIX
REVDAT 5 16-NOV-11 2POR 1 HETATM
REVDAT 4 13-JUL-11 2POR 1 VERSN
REVDAT 3 24-FEB-09 2POR 1 VERSN
REVDAT 2 01-APR-03 2POR 1 JRNL
REVDAT 1 15-JUL-93 2POR 0
JRNL AUTH M.S.WEISS,G.E.SCHULZ
JRNL TITL STRUCTURE OF PORIN REFINED AT 1.8 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 227 493 1992
JRNL REFN ISSN 0022-2836
JRNL PMID 1328651
JRNL DOI 10.1016/0022-2836(92)90903-W
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.S.WEISS,U.ABELE,J.WECKESSER,W.WELTE,E.SCHILTZ,G.E.SCHULZ
REMARK 1 TITL MOLECULAR ARCHITECTURE AND ELECTROSTATIC PROPERTIES OF A
REMARK 1 TITL 2 BACTERIAL PORIN
REMARK 1 REF SCIENCE V. 254 1627 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.SCHILTZ,A.KREUSCH,U.NESTEL,G.E.SCHULZ
REMARK 1 TITL PRIMARY STRUCTURE OF PORIN FROM RHODOBACTER CAPSULATUS
REMARK 1 REF EUR.J.BIOCHEM. V. 199 587 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.S.WEISS,A.KREUSCH,E.SCHILTZ,U.NESTEL,W.WELTE,J.WECKESSER,
REMARK 1 AUTH 2 G.E.SCHULZ
REMARK 1 TITL THE STRUCTURE OF PORIN FROM RHODOBACTER CAPSULATUS AT 1.8
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF FEBS LETT. V. 280 379 1991
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 4
REMARK 1 AUTH A.KREUSCH,M.S.WEISS,W.WELTE,J.WECKESSER,G.E.SCHULZ
REMARK 1 TITL CRYSTALS OF AN INTEGRAL MEMBRANE PROTEIN DIFFRACTING TO 1.8
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 217 9 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.S.WEISS,T.WACKER,J.WECKESSER,W.WELTE,G.E.SCHULZ
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF PORIN FROM RHODOBACTER
REMARK 1 TITL 2 CAPSULATUS AT 3 ANGSTROMS RESOLUTION
REMARK 1 REF FEBS LETT. V. 267 268 1990
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.S.WEISS,T.WACKER,U.NESTEL,D.WOITZIK,J.WECKESSER,W.KREUTZ,
REMARK 1 AUTH 2 W.WELTE,G.E.SCHULZ
REMARK 1 TITL THE STRUCTURE OF PORIN FROM RHODOBACTER CAPSULATUS AT 0.6 NM
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF FEBS LETT. V. 256 143 1989
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 7
REMARK 1 AUTH U.NESTEL,T.WACKER,D.WOITZIK,J.WECKESSER,W.KREUTZ,W.WELTE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF PORIN FROM
REMARK 1 TITL 2 RHODOBACTER CAPSULATUS
REMARK 1 REF FEBS LETT. V. 242 405 1989
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 42851
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 SET) : 0.186
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2219
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 2.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE CRYSTALS HAVE FORM *B* AS DESCRIBED IN THE *JRNL*
REMARK 3 REFERENCE.
REMARK 3
REMARK 3 RESIDUE 545 HAS NOT BEEN UNAMBIGUOUSLY IDENTIFIED. IT HAS BEEN
REMARK 3 MODELED AS A DETERGENT N-OCTYLTETRAOXYETHYLENE
REMARK 4
REMARK 4 2POR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.15000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.64471
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.73333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 46.15000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 26.64471
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.73333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 46.15000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 26.64471
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.73333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.28943
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 97.46667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 53.28943
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 97.46667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 53.28943
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 97.46667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 17300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 361 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 229 NE2 HIS A 229 CD2 -0.067
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TRP A 19 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP A 19 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 101 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TYR A 123 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 136 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TYR A 167 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 263 CB - CG - CD1 ANGL. DEV. = -4.4 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 ASP A 17 -37.35 -132.37
REMARK 500 ASP A 93 83.99 64.70
REMARK 500 THR A 256 -7.57 73.01
REMARK 500 ILE A 257 -77.43 -108.97
REMARK 500 SER A 289 112.52 -34.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THIRTY FOUR DETERGENT FRAGMENTS HAVE BEEN MODELED AS WATERS
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 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 20 OD1
REMARK 620 2 ASN A 116 OD1 174.7
REMARK 620 3 ASP A 136 OD2 81.5 103.7
REMARK 620 4 ASP A 136 OD1 93.2 89.8 52.3
REMARK 620 5 LYS A 138 O 94.8 81.6 128.0 76.4
REMARK 620 6 GLY A 140 O 79.9 95.7 145.2 157.5 82.9
REMARK 620 7 HOH A 314 O 97.2 84.5 78.0 126.9 152.9 75.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 80 OE2
REMARK 620 2 GLU A 80 OE1 50.2
REMARK 620 3 ASP A 108 OD2 97.7 90.6
REMARK 620 4 HOH A 305 O 128.6 80.9 97.5
REMARK 620 5 HOH A 307 O 75.3 125.5 95.8 150.3
REMARK 620 6 HOH A 312 O 80.9 92.0 175.3 86.9 79.4
REMARK 620 7 HOH A 339 O 148.9 159.5 92.3 78.6 74.4 86.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 93 OD2 52.3
REMARK 620 3 ASP A 95 OD1 77.7 113.9
REMARK 620 4 ASP A 95 OD2 87.3 84.2 49.5
REMARK 620 5 ASN A 100 OD1 77.7 122.8 73.7 123.2
REMARK 620 6 ASP A 101 OD1 155.8 151.9 85.1 94.3 81.2
REMARK 620 7 HOH A 327 O 128.6 76.5 126.7 82.6 146.6 75.5
REMARK 620 8 HOH A 331 O 93.5 80.1 150.5 159.4 76.9 93.2 80.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY A SIXTEEN-STRANDED BETA-BARREL. THIS IS
REMARK 700 REPRESENTED AS A SEVENTEEN-STRANDED SHEET IN WHICH THE
REMARK 700 FIRST AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 548
DBREF 2POR A 1 301 UNP P31243 PORI_RHOCA 1 301
SEQRES 1 A 301 GLU VAL LYS LEU SER GLY ASP ALA ARG MET GLY VAL MET
SEQRES 2 A 301 TYR ASN GLY ASP ASP TRP ASN PHE SER SER ARG SER ARG
SEQRES 3 A 301 VAL LEU PHE THR MET SER GLY THR THR ASP SER GLY LEU
SEQRES 4 A 301 GLU PHE GLY ALA SER PHE LYS ALA HIS GLU SER VAL GLY
SEQRES 5 A 301 ALA GLU THR GLY GLU ASP GLY THR VAL PHE LEU SER GLY
SEQRES 6 A 301 ALA PHE GLY LYS ILE GLU MET GLY ASP ALA LEU GLY ALA
SEQRES 7 A 301 SER GLU ALA LEU PHE GLY ASP LEU TYR GLU VAL GLY TYR
SEQRES 8 A 301 THR ASP LEU ASP ASP ARG GLY GLY ASN ASP ILE PRO TYR
SEQRES 9 A 301 LEU THR GLY ASP GLU ARG LEU THR ALA GLU ASP ASN PRO
SEQRES 10 A 301 VAL LEU LEU TYR THR TYR SER ALA GLY ALA PHE SER VAL
SEQRES 11 A 301 ALA ALA SER MET SER ASP GLY LYS VAL GLY GLU THR SER
SEQRES 12 A 301 GLU ASP ASP ALA GLN GLU MET ALA VAL ALA ALA ALA TYR
SEQRES 13 A 301 THR PHE GLY ASN TYR THR VAL GLY LEU GLY TYR GLU LYS
SEQRES 14 A 301 ILE ASP SER PRO ASP THR ALA LEU MET ALA ASP MET GLU
SEQRES 15 A 301 GLN LEU GLU LEU ALA ALA ILE ALA LYS PHE GLY ALA THR
SEQRES 16 A 301 ASN VAL LYS ALA TYR TYR ALA ASP GLY GLU LEU ASP ARG
SEQRES 17 A 301 ASP PHE ALA ARG ALA VAL PHE ASP LEU THR PRO VAL ALA
SEQRES 18 A 301 ALA ALA ALA THR ALA VAL ASP HIS LYS ALA TYR GLY LEU
SEQRES 19 A 301 SER VAL ASP SER THR PHE GLY ALA THR THR VAL GLY GLY
SEQRES 20 A 301 TYR VAL GLN VAL LEU ASP ILE ASP THR ILE ASP ASP VAL
SEQRES 21 A 301 THR TYR TYR GLY LEU GLY ALA SER TYR ASP LEU GLY GLY
SEQRES 22 A 301 GLY ALA SER ILE VAL GLY GLY ILE ALA ASP ASN ASP LEU
SEQRES 23 A 301 PRO ASN SER ASP MET VAL ALA ASP LEU GLY VAL LYS PHE
SEQRES 24 A 301 LYS PHE
HET CA A 302 1
HET CA A 303 1
HET CA A 304 1
HET C8E A 545 21
HET C8E A 546 21
HET C8E A 547 21
HET C8E A 548 21
HETNAM CA CALCIUM ION
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
FORMUL 2 CA 3(CA 2+)
FORMUL 5 C8E 4(C16 H34 O5)
FORMUL 9 HOH *274(H2 O)
HELIX 1 H1 SER A 50 GLU A 54 1 5
HELIX 2 H2 GLY A 77 PHE A 83 1 7
HELIX 3 H3 ARG A 208 VAL A 214 1 7
SHEET 1 S117 GLU A 1 ASN A 15 0
SHEET 2 S117 ASP A 18 THR A 35 -1 O ASP A 18 N ASN A 15
SHEET 3 S117 LEU A 39 LYS A 46 -1 O LEU A 39 N THR A 35
SHEET 4 S117 GLY A 59 GLY A 65 -1 N THR A 60 O SER A 44
SHEET 5 S117 GLY A 68 ASP A 74 -1 N GLY A 68 O GLY A 65
SHEET 6 S117 VAL A 118 ALA A 125 -1 N VAL A 118 O GLY A 73
SHEET 7 S117 PHE A 128 SER A 135 -1 N PHE A 128 O ALA A 125
SHEET 8 S117 GLN A 148 PHE A 158 -1 O GLU A 149 N SER A 135
SHEET 9 S117 TYR A 161 ASP A 171 -1 N TYR A 161 O PHE A 158
SHEET 10 S117 MET A 181 PHE A 192 -1 N MET A 181 O ILE A 170
SHEET 11 S117 THR A 195 LEU A 206 -1 N THR A 195 O PHE A 192
SHEET 12 S117 VAL A 227 PHE A 240 -1 N VAL A 227 O LEU A 206
SHEET 13 S117 THR A 243 ILE A 254 -1 N THR A 243 O PHE A 240
SHEET 14 S117 ASP A 258 LEU A 271 -1 N ASP A 258 O ILE A 254
SHEET 15 S117 ALA A 275 ASP A 285 -1 O ALA A 275 N LEU A 271
SHEET 16 S117 VAL A 292 PHE A 301 -1 N VAL A 292 O ALA A 282
SHEET 17 S117 GLU A 1 ASN A 15 1 N GLY A 6 O PHE A 301
LINK OD1 ASN A 20 CA CA A 304 2555 1555 2.18
LINK OE2 GLU A 80 CA CA A 302 1555 1555 2.48
LINK OE1 GLU A 80 CA CA A 302 1555 1555 2.53
LINK OD1 ASP A 93 CA CA A 303 1555 1555 2.33
LINK OD2 ASP A 93 CA CA A 303 1555 1555 2.45
LINK OD1 ASP A 95 CA CA A 303 1555 1555 2.63
LINK OD2 ASP A 95 CA CA A 303 1555 1555 2.40
LINK OD1 ASN A 100 CA CA A 303 1555 1555 2.31
LINK OD1 ASP A 101 CA CA A 303 1555 1555 2.25
LINK OD2 ASP A 108 CA CA A 302 1555 1555 2.24
LINK OD1 ASN A 116 CA CA A 304 1555 1555 2.16
LINK OD2 ASP A 136 CA CA A 304 1555 1555 2.39
LINK OD1 ASP A 136 CA CA A 304 1555 1555 2.35
LINK O LYS A 138 CA CA A 304 1555 1555 2.55
LINK O GLY A 140 CA CA A 304 1555 1555 2.18
LINK CA CA A 302 O HOH A 305 1555 1555 2.43
LINK CA CA A 302 O HOH A 307 1555 1555 2.32
LINK CA CA A 302 O HOH A 312 1555 1555 2.28
LINK CA CA A 302 O HOH A 339 1555 1555 2.38
LINK CA CA A 303 O HOH A 327 1555 1555 2.24
LINK CA CA A 303 O HOH A 331 1555 1555 2.39
LINK CA CA A 304 O HOH A 314 1555 1555 2.35
SITE 1 AC1 6 GLU A 80 ASP A 108 HOH A 305 HOH A 307
SITE 2 AC1 6 HOH A 312 HOH A 339
SITE 1 AC2 6 ASP A 93 ASP A 95 ASN A 100 ASP A 101
SITE 2 AC2 6 HOH A 327 HOH A 331
SITE 1 AC3 6 ASN A 20 ASN A 116 ASP A 136 LYS A 138
SITE 2 AC3 6 GLY A 140 HOH A 314
SITE 1 AC4 4 GLN A 183 VAL A 214 LEU A 286 ASN A 288
SITE 1 AC5 4 TRP A 19 MET A 134 GLN A 148 GLY A 280
SITE 1 AC6 4 TYR A 200 TYR A 232 VAL A 249 THR A 261
CRYST1 92.300 92.300 146.200 90.00 90.00 120.00 H 3 9
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 0.010834 0.006255 0.000000 0.00000
SCALE2 0.000000 0.012510 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006840 0.00000
ATOM 1 N GLU A 1 10.975 -2.428 6.735 1.00 27.59 N
ATOM 2 CA GLU A 1 9.566 -2.578 6.405 1.00 36.06 C
ATOM 3 C GLU A 1 8.689 -3.034 7.601 1.00 22.34 C
ATOM 4 O GLU A 1 9.156 -3.908 8.335 1.00 23.38 O
ATOM 5 CB GLU A 1 9.513 -3.583 5.273 1.00 27.56 C
ATOM 6 CG GLU A 1 8.120 -3.932 4.767 1.00 46.76 C
ATOM 7 CD GLU A 1 8.059 -5.151 3.839 1.00 78.17 C
ATOM 8 OE1 GLU A 1 8.986 -5.978 3.838 1.00 83.62 O
ATOM 9 OE2 GLU A 1 7.059 -5.270 3.122 1.00 88.58 O
ATOM 10 N VAL A 2 7.445 -2.564 7.760 1.00 24.91 N
ATOM 11 CA VAL A 2 6.554 -2.916 8.868 1.00 26.19 C
ATOM 12 C VAL A 2 5.235 -3.431 8.314 1.00 21.63 C
ATOM 13 O VAL A 2 4.554 -2.685 7.614 1.00 25.05 O
ATOM 14 CB VAL A 2 6.258 -1.672 9.795 1.00 21.80 C
ATOM 15 CG1 VAL A 2 5.414 -2.151 10.975 1.00 21.14 C
ATOM 16 CG2 VAL A 2 7.526 -1.022 10.328 1.00 21.61 C
ATOM 17 N LYS A 3 4.811 -4.658 8.584 1.00 17.35 N
ATOM 18 CA LYS A 3 3.536 -5.187 8.138 1.00 16.93 C
ATOM 19 C LYS A 3 2.611 -5.431 9.336 1.00 22.75 C
ATOM 20 O LYS A 3 3.086 -5.703 10.440 1.00 24.29 O
ATOM 21 CB LYS A 3 3.712 -6.524 7.421 1.00 20.86 C
ATOM 22 CG LYS A 3 4.477 -6.434 6.116 1.00 49.31 C
ATOM 23 CD LYS A 3 4.137 -7.645 5.248 1.00 66.30 C
ATOM 24 CE LYS A 3 4.389 -7.309 3.763 1.00 91.35 C
ATOM 25 NZ LYS A 3 3.660 -6.128 3.288 1.00 86.70 N
ATOM 26 N LEU A 4 1.317 -5.393 9.102 1.00 18.28 N
ATOM 27 CA LEU A 4 0.307 -5.586 10.089 1.00 17.20 C
ATOM 28 C LEU A 4 -0.511 -6.790 9.822 1.00 25.71 C
ATOM 29 O LEU A 4 -0.857 -7.096 8.688 1.00 22.60 O
ATOM 30 CB LEU A 4 -0.658 -4.425 10.135 1.00 17.62 C
ATOM 31 CG LEU A 4 -0.154 -3.047 10.591 1.00 25.02 C
ATOM 32 CD1 LEU A 4 -1.260 -2.032 10.663 1.00 27.49 C
ATOM 33 CD2 LEU A 4 0.342 -3.158 12.001 1.00 28.78 C
ATOM 34 N SER A 5 -0.858 -7.520 10.854 1.00 18.09 N
ATOM 35 CA SER A 5 -1.843 -8.581 10.759 1.00 16.56 C
ATOM 36 C SER A 5 -2.590 -8.569 12.107 1.00 21.22 C
ATOM 37 O SER A 5 -2.231 -7.755 12.976 1.00 17.63 O
ATOM 38 CB SER A 5 -1.182 -9.918 10.543 1.00 15.90 C
ATOM 39 OG SER A 5 -0.206 -10.289 11.503 1.00 22.45 O
ATOM 40 N GLY A 6 -3.582 -9.404 12.337 1.00 22.36 N
ATOM 41 CA GLY A 6 -4.313 -9.399 13.598 1.00 18.52 C
ATOM 42 C GLY A 6 -5.194 -10.590 13.711 1.00 20.43 C
ATOM 43 O GLY A 6 -5.272 -11.470 12.839 1.00 19.89 O
ATOM 44 N ASP A 7 -5.858 -10.676 14.845 1.00 17.75 N
ATOM 45 CA ASP A 7 -6.828 -11.730 15.071 1.00 14.63 C
ATOM 46 C ASP A 7 -7.839 -11.230 16.099 1.00 17.50 C
ATOM 47 O ASP A 7 -7.656 -10.162 16.698 1.00 17.10 O
ATOM 48 CB ASP A 7 -6.157 -13.038 15.557 1.00 15.83 C
ATOM 49 CG ASP A 7 -5.230 -12.906 16.760 1.00 23.05 C
ATOM 50 OD1 ASP A 7 -5.656 -12.431 17.801 1.00 20.15 O
ATOM 51 OD2 ASP A 7 -4.071 -13.234 16.640 1.00 25.78 O
ATOM 52 N ALA A 8 -8.944 -11.946 16.224 1.00 19.52 N
ATOM 53 CA ALA A 8 -10.035 -11.603 17.141 1.00 15.71 C
ATOM 54 C ALA A 8 -10.861 -12.858 17.357 1.00 19.05 C
ATOM 55 O ALA A 8 -10.682 -13.866 16.641 1.00 18.32 O
ATOM 56 CB ALA A 8 -10.945 -10.502 16.587 1.00 14.05 C
ATOM 57 N ARG A 9 -11.662 -12.914 18.432 1.00 16.33 N
ATOM 58 CA ARG A 9 -12.501 -14.065 18.709 1.00 13.95 C
ATOM 59 C ARG A 9 -13.651 -13.601 19.567 1.00 17.40 C
ATOM 60 O ARG A 9 -13.553 -12.536 20.208 1.00 18.39 O
ATOM 61 CB ARG A 9 -11.687 -15.156 19.410 1.00 15.94 C
ATOM 62 CG ARG A 9 -11.320 -14.825 20.843 1.00 16.00 C
ATOM 63 CD ARG A 9 -10.256 -15.772 21.276 1.00 19.18 C
ATOM 64 NE ARG A 9 -10.038 -15.564 22.699 1.00 20.39 N
ATOM 65 CZ ARG A 9 -8.998 -16.081 23.374 1.00 23.61 C
ATOM 66 NH1 ARG A 9 -8.039 -16.818 22.792 1.00 19.92 N
ATOM 67 NH2 ARG A 9 -8.922 -15.805 24.689 1.00 23.34 N
ATOM 68 N MET A 10 -14.789 -14.262 19.531 1.00 15.77 N
ATOM 69 CA MET A 10 -15.931 -13.891 20.365 1.00 19.06 C
ATOM 70 C MET A 10 -16.832 -15.099 20.499 1.00 24.44 C
ATOM 71 O MET A 10 -16.838 -15.965 19.620 1.00 18.02 O
ATOM 72 CB MET A 10 -16.723 -12.707 19.809 1.00 18.72 C
ATOM 73 CG MET A 10 -17.489 -12.938 18.541 1.00 25.28 C
ATOM 74 SD MET A 10 -18.482 -11.490 18.191 1.00 30.85 S
ATOM 75 CE MET A 10 -18.740 -12.010 16.541 1.00 33.80 C
ATOM 76 N GLY A 11 -17.502 -15.304 21.642 1.00 17.85 N
ATOM 77 CA GLY A 11 -18.325 -16.491 21.829 1.00 18.79 C
ATOM 78 C GLY A 11 -18.676 -16.572 23.288 1.00 25.94 C
ATOM 79 O GLY A 11 -18.702 -15.531 23.959 1.00 21.22 O
ATOM 80 N VAL A 12 -18.929 -17.776 23.769 1.00 22.43 N
ATOM 81 CA VAL A 12 -19.310 -18.051 25.177 1.00 22.84 C
ATOM 82 C VAL A 12 -18.421 -19.118 25.753 1.00 21.81 C
ATOM 83 O VAL A 12 -18.005 -20.034 25.037 1.00 20.69 O
ATOM 84 CB VAL A 12 -20.786 -18.518 25.319 1.00 23.09 C
ATOM 85 CG1 VAL A 12 -21.639 -17.287 25.071 1.00 21.02 C
ATOM 86 CG2 VAL A 12 -21.167 -19.632 24.355 1.00 22.56 C
ATOM 87 N MET A 13 -18.010 -18.982 27.018 1.00 16.86 N
ATOM 88 CA MET A 13 -17.066 -19.909 27.604 1.00 18.95 C
ATOM 89 C MET A 13 -17.695 -20.359 28.938 1.00 26.49 C
ATOM 90 O MET A 13 -18.277 -19.533 29.649 1.00 22.68 O
ATOM 91 CB MET A 13 -15.725 -19.176 27.821 1.00 19.57 C
ATOM 92 CG AMET A 13 -14.661 -20.018 28.553 0.51 33.28 C
ATOM 93 CG BMET A 13 -14.564 -19.969 28.448 0.49 31.07 C
ATOM 94 SD AMET A 13 -14.864 -20.093 30.362 0.51 18.59 S
ATOM 95 SD BMET A 13 -14.047 -19.495 30.135 0.49 33.60 S
ATOM 96 CE AMET A 13 -14.637 -18.365 30.663 0.51 14.41 C
ATOM 97 CE BMET A 13 -13.423 -21.075 30.594 0.49 12.77 C
ATOM 98 N TYR A 14 -17.572 -21.615 29.305 1.00 23.01 N
ATOM 99 CA TYR A 14 -18.178 -22.199 30.497 1.00 25.16 C
ATOM 100 C TYR A 14 -17.029 -22.485 31.428 1.00 23.22 C
ATOM 101 O TYR A 14 -16.171 -23.295 31.063 1.00 23.70 O
ATOM 102 CB TYR A 14 -18.841 -23.482 30.133 1.00 24.00 C
ATOM 103 CG TYR A 14 -19.541 -24.129 31.300 1.00 28.72 C
ATOM 104 CD1 TYR A 14 -20.727 -23.561 31.734 1.00 29.42 C
ATOM 105 CD2 TYR A 14 -19.017 -25.283 31.856 1.00 27.77 C
ATOM 106 CE1 TYR A 14 -21.430 -24.167 32.750 1.00 32.13 C
ATOM 107 CE2 TYR A 14 -19.717 -25.895 32.876 1.00 30.23 C
ATOM 108 CZ TYR A 14 -20.915 -25.329 33.305 1.00 32.81 C
ATOM 109 OH TYR A 14 -21.626 -25.944 34.326 1.00 50.72 O
ATOM 110 N ASN A 15 -17.000 -21.905 32.638 1.00 22.01 N
ATOM 111 CA ASN A 15 -15.841 -22.047 33.535 1.00 22.52 C
ATOM 112 C ASN A 15 -15.889 -23.250 34.484 1.00 31.39 C
ATOM 113 O ASN A 15 -15.038 -23.447 35.359 1.00 32.32 O
ATOM 114 CB ASN A 15 -15.660 -20.755 34.380 1.00 24.87 C
ATOM 115 CG ASN A 15 -16.856 -20.434 35.271 1.00 23.96 C
ATOM 116 OD1 ASN A 15 -17.708 -21.291 35.515 1.00 23.91 O
ATOM 117 ND2 ASN A 15 -17.090 -19.204 35.695 1.00 26.01 N
ATOM 118 N GLY A 16 -16.865 -24.119 34.303 1.00 26.28 N
ATOM 119 CA GLY A 16 -17.013 -25.246 35.198 1.00 33.32 C
ATOM 120 C GLY A 16 -18.353 -25.113 35.878 1.00 30.42 C
ATOM 121 O GLY A 16 -18.975 -26.124 36.199 1.00 36.69 O
ATOM 122 N ASP A 17 -18.860 -23.882 36.047 1.00 29.56 N
ATOM 123 CA ASP A 17 -20.141 -23.614 36.727 1.00 29.65 C
ATOM 124 C ASP A 17 -21.077 -22.659 35.981 1.00 32.17 C
ATOM 125 O ASP A 17 -22.304 -22.831 35.929 1.00 30.83 O
ATOM 126 CB ASP A 17 -19.849 -23.042 38.165 1.00 35.32 C
ATOM 127 CG ASP A 17 -18.950 -23.913 39.090 1.00 51.32 C
ATOM 128 OD1 ASP A 17 -19.361 -25.019 39.486 1.00 59.35 O
ATOM 129 OD2 ASP A 17 -17.822 -23.488 39.391 1.00 65.43 O
ATOM 130 N ASP A 18 -20.505 -21.638 35.336 1.00 24.80 N
ATOM 131 CA ASP A 18 -21.301 -20.661 34.621 1.00 23.22 C
ATOM 132 C ASP A 18 -20.689 -20.330 33.261 1.00 26.47 C
ATOM 133 O ASP A 18 -19.485 -20.520 33.049 1.00 25.52 O
ATOM 134 CB ASP A 18 -21.381 -19.351 35.370 1.00 25.98 C
ATOM 135 CG ASP A 18 -22.210 -19.562 36.608 1.00 43.16 C
ATOM 136 OD1 ASP A 18 -23.428 -19.634 36.500 1.00 41.16 O
ATOM 137 OD2 ASP A 18 -21.610 -19.689 37.666 1.00 33.11 O
ATOM 138 N TRP A 19 -21.570 -19.845 32.394 1.00 24.02 N
ATOM 139 CA TRP A 19 -21.228 -19.334 31.074 1.00 29.52 C
ATOM 140 C TRP A 19 -20.887 -17.850 31.201 1.00 34.72 C
ATOM 141 O TRP A 19 -21.489 -17.150 32.023 1.00 26.95 O
ATOM 142 CB TRP A 19 -22.413 -19.489 30.099 1.00 20.45 C
ATOM 143 CG TRP A 19 -22.600 -20.931 29.671 1.00 34.12 C
ATOM 144 CD1 TRP A 19 -23.521 -21.735 30.283 1.00 38.42 C
ATOM 145 CD2 TRP A 19 -21.879 -21.586 28.704 1.00 43.20 C
ATOM 146 NE1 TRP A 19 -23.378 -22.907 29.705 1.00 28.98 N
ATOM 147 CE2 TRP A 19 -22.416 -22.861 28.769 1.00 43.13 C
ATOM 148 CE3 TRP A 19 -20.869 -21.291 27.804 1.00 27.67 C
ATOM 149 CZ2 TRP A 19 -21.955 -23.858 27.942 1.00 37.29 C
ATOM 150 CZ3 TRP A 19 -20.404 -22.293 26.974 1.00 26.31 C
ATOM 151 CH2 TRP A 19 -20.947 -23.560 27.045 1.00 34.35 C
ATOM 152 N ASN A 20 -19.915 -17.345 30.439 1.00 20.14 N
ATOM 153 CA ASN A 20 -19.610 -15.934 30.363 1.00 20.63 C
ATOM 154 C ASN A 20 -19.325 -15.585 28.909 1.00 21.59 C
ATOM 155 O ASN A 20 -18.824 -16.452 28.179 1.00 20.91 O
ATOM 156 CB ASN A 20 -18.358 -15.571 31.135 1.00 19.26 C
ATOM 157 CG ASN A 20 -18.632 -15.209 32.594 1.00 16.94 C
ATOM 158 OD1 ASN A 20 -18.981 -14.061 32.912 1.00 19.32 O
ATOM 159 ND2 ASN A 20 -18.356 -16.193 33.429 1.00 18.90 N
ATOM 160 N PHE A 21 -19.579 -14.348 28.511 1.00 20.31 N
ATOM 161 CA PHE A 21 -19.123 -13.839 27.208 1.00 18.80 C
ATOM 162 C PHE A 21 -17.596 -13.740 27.273 1.00 29.01 C
ATOM 163 O PHE A 21 -17.046 -13.375 28.323 1.00 18.59 O
ATOM 164 CB PHE A 21 -19.693 -12.434 26.920 1.00 15.96 C
ATOM 165 CG PHE A 21 -21.210 -12.260 26.798 1.00 16.47 C
ATOM 166 CD1 PHE A 21 -22.038 -13.317 26.450 1.00 18.25 C
ATOM 167 CD2 PHE A 21 -21.730 -11.004 27.047 1.00 17.20 C
ATOM 168 CE1 PHE A 21 -23.387 -13.081 26.366 1.00 20.58 C
ATOM 169 CE2 PHE A 21 -23.088 -10.789 26.954 1.00 18.95 C
ATOM 170 CZ PHE A 21 -23.906 -11.831 26.615 1.00 18.40 C
ATOM 171 N SER A 22 -16.849 -14.072 26.211 1.00 16.37 N
ATOM 172 CA SER A 22 -15.406 -13.978 26.201 1.00 15.71 C
ATOM 173 C SER A 22 -14.989 -13.518 24.795 1.00 27.98 C
ATOM 174 O SER A 22 -15.346 -14.160 23.810 1.00 18.52 O
ATOM 175 CB SER A 22 -14.824 -15.314 26.508 1.00 13.95 C
ATOM 176 OG SER A 22 -13.431 -15.173 26.702 1.00 17.49 O
ATOM 177 N SER A 23 -14.273 -12.416 24.652 1.00 17.53 N
ATOM 178 CA SER A 23 -13.869 -11.906 23.350 1.00 21.71 C
ATOM 179 C SER A 23 -12.546 -11.168 23.448 1.00 27.30 C
ATOM 180 O SER A 23 -12.101 -10.859 24.561 1.00 18.45 O
ATOM 181 CB SER A 23 -14.984 -11.006 22.851 1.00 13.04 C
ATOM 182 OG SER A 23 -15.192 -9.821 23.590 1.00 17.20 O
ATOM 183 N ARG A 24 -11.805 -10.927 22.371 1.00 16.47 N
ATOM 184 CA ARG A 24 -10.586 -10.139 22.390 1.00 18.28 C
ATOM 185 C ARG A 24 -10.232 -9.787 20.944 1.00 21.67 C
ATOM 186 O ARG A 24 -10.765 -10.417 20.032 1.00 17.72 O
ATOM 187 CB ARG A 24 -9.384 -10.889 22.934 1.00 14.39 C
ATOM 188 CG ARG A 24 -8.805 -12.022 22.187 1.00 17.95 C
ATOM 189 CD ARG A 24 -7.506 -12.385 22.785 1.00 18.22 C
ATOM 190 NE ARG A 24 -6.965 -13.447 21.943 1.00 16.16 N
ATOM 191 CZ ARG A 24 -5.984 -14.286 22.251 1.00 22.92 C
ATOM 192 NH1 ARG A 24 -5.364 -14.285 23.426 1.00 23.47 N
ATOM 193 NH2 ARG A 24 -5.544 -15.105 21.299 1.00 24.06 N
ATOM 194 N SER A 25 -9.355 -8.836 20.719 1.00 19.57 N
ATOM 195 CA SER A 25 -8.788 -8.593 19.406 1.00 19.55 C
ATOM 196 C SER A 25 -7.354 -8.200 19.668 1.00 22.34 C
ATOM 197 O SER A 25 -7.009 -7.632 20.724 1.00 18.07 O
ATOM 198 CB SER A 25 -9.563 -7.488 18.650 1.00 15.96 C
ATOM 199 OG SER A 25 -9.822 -6.295 19.331 1.00 31.90 O
ATOM 200 N ARG A 26 -6.442 -8.524 18.741 1.00 16.42 N
ATOM 201 CA ARG A 26 -5.006 -8.261 18.856 1.00 14.69 C
ATOM 202 C ARG A 26 -4.472 -7.806 17.479 1.00 18.06 C
ATOM 203 O ARG A 26 -5.093 -8.135 16.455 1.00 16.70 O
ATOM 204 CB ARG A 26 -4.249 -9.528 19.261 1.00 15.19 C
ATOM 205 CG ARG A 26 -4.855 -10.136 20.527 1.00 18.12 C
ATOM 206 CD ARG A 26 -3.970 -11.208 21.079 1.00 19.43 C
ATOM 207 NE ARG A 26 -3.803 -12.232 20.097 1.00 17.77 N
ATOM 208 CZ ARG A 26 -2.963 -13.245 20.234 1.00 29.11 C
ATOM 209 NH1 ARG A 26 -2.202 -13.413 21.297 1.00 20.54 N
ATOM 210 NH2 ARG A 26 -2.829 -14.114 19.235 1.00 23.76 N
ATOM 211 N VAL A 27 -3.371 -7.074 17.436 1.00 18.18 N
ATOM 212 CA VAL A 27 -2.700 -6.649 16.202 1.00 17.02 C
ATOM 213 C VAL A 27 -1.254 -7.078 16.396 1.00 20.98 C
ATOM 214 O VAL A 27 -0.700 -6.935 17.506 1.00 18.90 O
ATOM 215 CB VAL A 27 -2.810 -5.120 16.021 1.00 13.14 C
ATOM 216 CG1 VAL A 27 -1.844 -4.555 14.983 1.00 20.80 C
ATOM 217 CG2 VAL A 27 -4.232 -4.852 15.560 1.00 18.48 C
ATOM 218 N LEU A 28 -0.669 -7.658 15.334 1.00 13.21 N
ATOM 219 CA LEU A 28 0.727 -8.028 15.294 1.00 12.34 C
ATOM 220 C LEU A 28 1.508 -7.115 14.333 1.00 16.60 C
ATOM 221 O LEU A 28 1.087 -6.828 13.211 1.00 19.12 O
ATOM 222 CB LEU A 28 0.834 -9.503 14.877 1.00 15.44 C
ATOM 223 CG LEU A 28 2.234 -10.063 14.618 1.00 17.29 C
ATOM 224 CD1 LEU A 28 3.075 -10.180 15.886 1.00 19.53 C
ATOM 225 CD2 LEU A 28 2.062 -11.434 14.044 1.00 18.79 C
ATOM 226 N PHE A 29 2.623 -6.562 14.779 1.00 14.46 N
ATOM 227 CA PHE A 29 3.533 -5.760 13.971 1.00 19.10 C
ATOM 228 C PHE A 29 4.627 -6.700 13.519 1.00 28.14 C
ATOM 229 O PHE A 29 5.273 -7.290 14.396 1.00 19.55 O
ATOM 230 CB PHE A 29 4.201 -4.663 14.773 1.00 14.05 C
ATOM 231 CG PHE A 29 3.203 -3.682 15.339 1.00 21.24 C
ATOM 232 CD1 PHE A 29 2.576 -2.776 14.523 1.00 17.81 C
ATOM 233 CD2 PHE A 29 2.900 -3.706 16.696 1.00 23.31 C
ATOM 234 CE1 PHE A 29 1.646 -1.902 15.054 1.00 26.27 C
ATOM 235 CE2 PHE A 29 1.972 -2.831 17.226 1.00 20.41 C
ATOM 236 CZ PHE A 29 1.340 -1.928 16.407 1.00 22.27 C
ATOM 237 N THR A 30 4.879 -6.914 12.210 1.00 18.98 N
ATOM 238 CA THR A 30 6.001 -7.751 11.761 1.00 17.37 C
ATOM 239 C THR A 30 6.950 -6.853 11.010 1.00 18.66 C
ATOM 240 O THR A 30 6.537 -6.160 10.078 1.00 21.64 O
ATOM 241 CB THR A 30 5.535 -8.820 10.853 1.00 16.98 C
ATOM 242 OG1 THR A 30 4.602 -9.605 11.567 1.00 23.49 O
ATOM 243 CG2 THR A 30 6.660 -9.675 10.412 1.00 20.20 C
ATOM 244 N MET A 31 8.199 -6.782 11.425 1.00 16.66 N
ATOM 245 CA MET A 31 9.149 -5.864 10.838 1.00 17.95 C
ATOM 246 C MET A 31 10.236 -6.670 10.197 1.00 20.41 C
ATOM 247 O MET A 31 10.633 -7.704 10.743 1.00 16.53 O
ATOM 248 CB MET A 31 9.738 -4.957 11.902 1.00 18.36 C
ATOM 249 CG MET A 31 8.614 -4.154 12.542 1.00 28.91 C
ATOM 250 SD MET A 31 9.221 -2.829 13.578 1.00 29.44 S
ATOM 251 CE MET A 31 9.642 -3.773 14.989 1.00 24.49 C
ATOM 252 N SER A 32 10.719 -6.278 9.007 1.00 18.58 N
ATOM 253 CA SER A 32 11.747 -7.076 8.317 1.00 18.25 C
ATOM 254 C SER A 32 12.663 -6.231 7.441 1.00 17.77 C
ATOM 255 O SER A 32 12.309 -5.074 7.116 1.00 21.99 O
ATOM 256 CB SER A 32 11.084 -8.169 7.454 1.00 21.16 C
ATOM 257 OG SER A 32 10.036 -7.595 6.687 1.00 36.32 O
ATOM 258 N GLY A 33 13.846 -6.810 7.214 1.00 18.75 N
ATOM 259 CA GLY A 33 14.879 -6.169 6.423 1.00 19.45 C
ATOM 260 C GLY A 33 15.928 -7.193 5.988 1.00 19.89 C
ATOM 261 O GLY A 33 15.912 -8.349 6.429 1.00 18.98 O
ATOM 262 N THR A 34 16.861 -6.765 5.111 1.00 20.70 N
ATOM 263 CA THR A 34 17.891 -7.609 4.533 1.00 18.70 C
ATOM 264 C THR A 34 19.122 -6.741 4.408 1.00 15.56 C
ATOM 265 O THR A 34 19.002 -5.588 3.989 1.00 22.55 O
ATOM 266 CB THR A 34 17.516 -8.091 3.111 1.00 23.51 C
ATOM 267 OG1 THR A 34 16.253 -8.696 3.212 1.00 25.34 O
ATOM 268 CG2 THR A 34 18.429 -9.157 2.563 1.00 21.14 C
ATOM 269 N THR A 35 20.302 -7.237 4.741 1.00 16.89 N
ATOM 270 CA THR A 35 21.478 -6.410 4.639 1.00 19.04 C
ATOM 271 C THR A 35 21.964 -6.602 3.189 1.00 31.99 C
ATOM 272 O THR A 35 21.482 -7.478 2.459 1.00 22.91 O
ATOM 273 CB THR A 35 22.529 -6.898 5.632 1.00 21.23 C
ATOM 274 OG1 THR A 35 22.879 -8.235 5.245 1.00 19.46 O
ATOM 275 CG2 THR A 35 21.993 -6.888 7.090 1.00 20.86 C
ATOM 276 N ASP A 36 22.997 -5.869 2.796 1.00 26.13 N
ATOM 277 CA ASP A 36 23.590 -5.924 1.463 1.00 25.73 C
ATOM 278 C ASP A 36 24.060 -7.327 1.137 1.00 25.09 C
ATOM 279 O ASP A 36 23.867 -7.777 0.000 1.00 31.82 O
ATOM 280 CB ASP A 36 24.735 -4.929 1.425 1.00 23.29 C
ATOM 281 CG ASP A 36 24.297 -3.456 1.398 1.00 29.35 C
ATOM 282 OD1 ASP A 36 23.086 -3.192 1.251 1.00 32.92 O
ATOM 283 OD2 ASP A 36 25.180 -2.587 1.538 1.00 36.59 O
ATOM 284 N SER A 37 24.590 -8.117 2.070 1.00 25.70 N
ATOM 285 CA SER A 37 24.981 -9.467 1.714 1.00 23.90 C
ATOM 286 C SER A 37 23.883 -10.508 1.852 1.00 22.34 C
ATOM 287 O SER A 37 24.157 -11.702 1.670 1.00 24.38 O
ATOM 288 CB SER A 37 26.190 -9.852 2.557 1.00 30.09 C
ATOM 289 OG SER A 37 25.867 -9.979 3.940 1.00 48.00 O
ATOM 290 N GLY A 38 22.646 -10.103 2.203 1.00 21.78 N
ATOM 291 CA GLY A 38 21.563 -11.054 2.307 1.00 18.40 C
ATOM 292 C GLY A 38 21.344 -11.680 3.691 1.00 21.34 C
ATOM 293 O GLY A 38 20.692 -12.732 3.780 1.00 22.81 O
ATOM 294 N LEU A 39 21.905 -11.117 4.777 1.00 21.84 N
ATOM 295 CA LEU A 39 21.498 -11.566 6.115 1.00 23.27 C
ATOM 296 C LEU A 39 20.097 -10.977 6.290 1.00 19.54 C
ATOM 297 O LEU A 39 19.805 -9.851 5.869 1.00 23.50 O
ATOM 298 CB LEU A 39 22.375 -10.994 7.207 1.00 22.31 C
ATOM 299 CG LEU A 39 23.816 -11.396 7.138 1.00 21.30 C
ATOM 300 CD1 LEU A 39 24.572 -10.776 8.272 1.00 28.69 C
ATOM 301 CD2 LEU A 39 23.898 -12.869 7.179 1.00 25.27 C
ATOM 302 N GLU A 40 19.151 -11.696 6.862 1.00 18.39 N
ATOM 303 CA GLU A 40 17.800 -11.215 7.032 1.00 18.96 C
ATOM 304 C GLU A 40 17.670 -10.825 8.514 1.00 26.64 C
ATOM 305 O GLU A 40 18.276 -11.448 9.393 1.00 22.66 O
ATOM 306 CB GLU A 40 16.815 -12.318 6.729 1.00 21.71 C
ATOM 307 CG GLU A 40 16.895 -12.947 5.330 1.00 36.43 C
ATOM 308 CD GLU A 40 16.532 -11.980 4.209 1.00 58.73 C
ATOM 309 OE1 GLU A 40 15.614 -11.176 4.367 1.00 52.82 O
ATOM 310 OE2 GLU A 40 17.172 -12.043 3.163 1.00 61.13 O
ATOM 311 N PHE A 41 16.903 -9.813 8.825 1.00 23.28 N
ATOM 312 CA PHE A 41 16.729 -9.397 10.204 1.00 20.43 C
ATOM 313 C PHE A 41 15.288 -9.003 10.392 1.00 33.11 C
ATOM 314 O PHE A 41 14.563 -8.770 9.407 1.00 17.55 O
ATOM 315 CB PHE A 41 17.694 -8.252 10.489 1.00 17.40 C
ATOM 316 CG PHE A 41 17.603 -6.962 9.670 1.00 19.97 C
ATOM 317 CD1 PHE A 41 16.752 -5.938 10.031 1.00 18.79 C
ATOM 318 CD2 PHE A 41 18.455 -6.794 8.582 1.00 24.90 C
ATOM 319 CE1 PHE A 41 16.740 -4.744 9.333 1.00 18.42 C
ATOM 320 CE2 PHE A 41 18.444 -5.600 7.882 1.00 18.53 C
ATOM 321 CZ PHE A 41 17.594 -4.583 8.257 1.00 20.56 C
ATOM 322 N GLY A 42 14.810 -8.936 11.626 1.00 16.60 N
ATOM 323 CA GLY A 42 13.432 -8.570 11.827 1.00 15.94 C
ATOM 324 C GLY A 42 13.130 -8.441 13.326 1.00 18.51 C
ATOM 325 O GLY A 42 14.038 -8.612 14.142 1.00 17.74 O
ATOM 326 N ALA A 43 11.882 -8.141 13.619 1.00 19.68 N
ATOM 327 CA ALA A 43 11.393 -8.009 14.983 1.00 19.54 C
ATOM 328 C ALA A 43 9.876 -8.122 14.929 1.00 25.22 C
ATOM 329 O ALA A 43 9.252 -7.819 13.898 1.00 20.81 O
ATOM 330 CB ALA A 43 11.797 -6.646 15.537 1.00 16.52 C
ATOM 331 N SER A 44 9.180 -8.631 15.949 1.00 17.32 N
ATOM 332 CA SER A 44 7.736 -8.545 15.971 1.00 13.95 C
ATOM 333 C SER A 44 7.250 -8.527 17.428 1.00 17.36 C
ATOM 334 O SER A 44 7.963 -9.025 18.307 1.00 16.29 O
ATOM 335 CB SER A 44 7.093 -9.733 15.268 1.00 18.32 C
ATOM 336 OG SER A 44 7.556 -10.959 15.751 1.00 28.70 O
ATOM 337 N PHE A 45 6.076 -7.971 17.629 1.00 18.21 N
ATOM 338 CA PHE A 45 5.403 -7.974 18.916 1.00 19.59 C
ATOM 339 C PHE A 45 3.972 -7.562 18.664 1.00 21.25 C
ATOM 340 O PHE A 45 3.681 -7.002 17.593 1.00 19.84 O
ATOM 341 CB PHE A 45 6.102 -6.994 19.881 1.00 12.80 C
ATOM 342 CG PHE A 45 6.124 -5.522 19.533 1.00 16.76 C
ATOM 343 CD1 PHE A 45 5.086 -4.685 19.910 1.00 13.03 C
ATOM 344 CD2 PHE A 45 7.207 -4.996 18.829 1.00 15.77 C
ATOM 345 CE1 PHE A 45 5.134 -3.325 19.575 1.00 18.11 C
ATOM 346 CE2 PHE A 45 7.242 -3.644 18.503 1.00 14.29 C
ATOM 347 CZ PHE A 45 6.208 -2.799 18.869 1.00 18.49 C
ATOM 348 N LYS A 46 3.049 -7.825 19.601 1.00 14.65 N
ATOM 349 CA LYS A 46 1.661 -7.465 19.434 1.00 13.19 C
ATOM 350 C LYS A 46 1.393 -6.162 20.108 1.00 16.83 C
ATOM 351 O LYS A 46 2.154 -5.743 20.989 1.00 18.21 O
ATOM 352 CB LYS A 46 0.738 -8.518 20.001 1.00 14.48 C
ATOM 353 CG LYS A 46 1.038 -9.835 19.322 1.00 19.35 C
ATOM 354 CD LYS A 46 -0.003 -10.886 19.568 1.00 22.07 C
ATOM 355 CE LYS A 46 0.414 -12.179 18.892 1.00 29.45 C
ATOM 356 NZ LYS A 46 1.569 -12.753 19.553 1.00 30.58 N
ATOM 357 N ALA A 47 0.308 -5.501 19.763 1.00 13.74 N
ATOM 358 CA ALA A 47 0.078 -4.159 20.218 1.00 14.51 C
ATOM 359 C ALA A 47 -0.066 -4.148 21.761 1.00 17.84 C
ATOM 360 O ALA A 47 0.398 -3.213 22.427 1.00 16.71 O
ATOM 361 CB ALA A 47 -1.210 -3.622 19.625 1.00 13.21 C
ATOM 362 N HIS A 48 -0.708 -5.145 22.361 1.00 18.81 N
ATOM 363 CA HIS A 48 -0.891 -5.162 23.828 1.00 17.50 C
ATOM 364 C HIS A 48 0.419 -5.424 24.553 1.00 22.24 C
ATOM 365 O HIS A 48 0.466 -5.259 25.766 1.00 17.89 O
ATOM 366 CB HIS A 48 -1.945 -6.227 24.217 1.00 11.96 C
ATOM 367 CG HIS A 48 -1.534 -7.665 24.011 1.00 19.24 C
ATOM 368 ND1 HIS A 48 -1.497 -8.384 22.895 1.00 19.50 N
ATOM 369 CD2 HIS A 48 -1.086 -8.486 25.013 1.00 18.37 C
ATOM 370 CE1 HIS A 48 -1.055 -9.584 23.167 1.00 20.35 C
ATOM 371 NE2 HIS A 48 -0.808 -9.640 24.459 1.00 20.64 N
ATOM 372 N GLU A 49 1.498 -5.770 23.833 1.00 14.70 N
ATOM 373 CA GLU A 49 2.792 -6.076 24.377 1.00 14.46 C
ATOM 374 C GLU A 49 3.721 -4.937 24.115 1.00 14.22 C
ATOM 375 O GLU A 49 4.926 -5.114 24.355 1.00 15.82 O
ATOM 376 CB GLU A 49 3.502 -7.231 23.733 1.00 15.73 C
ATOM 377 CG GLU A 49 2.678 -8.470 23.628 1.00 24.60 C
ATOM 378 CD GLU A 49 3.401 -9.595 22.894 1.00 32.30 C
ATOM 379 OE1 GLU A 49 3.947 -9.415 21.802 1.00 21.35 O
ATOM 380 OE2 GLU A 49 3.405 -10.693 23.434 1.00 21.91 O
ATOM 381 N SER A 50 3.267 -3.778 23.639 1.00 14.73 N
ATOM 382 CA SER A 50 4.225 -2.763 23.249 1.00 13.74 C
ATOM 383 C SER A 50 5.102 -2.232 24.381 1.00 20.29 C
ATOM 384 O SER A 50 6.283 -1.952 24.134 1.00 16.11 O
ATOM 385 CB ASER A 50 3.509 -1.575 22.648 0.60 12.78 C
ATOM 386 CB BSER A 50 3.508 -1.603 22.576 0.40 12.35 C
ATOM 387 OG ASER A 50 2.591 -1.903 21.621 0.60 15.12 O
ATOM 388 OG BSER A 50 2.465 -1.023 23.337 0.40 13.87 O
ATOM 389 N VAL A 51 4.593 -2.082 25.643 1.00 15.56 N
ATOM 390 CA VAL A 51 5.457 -1.647 26.754 1.00 16.90 C
ATOM 391 C VAL A 51 6.573 -2.640 27.042 1.00 10.27 C
ATOM 392 O VAL A 51 7.741 -2.242 27.190 1.00 17.77 O
ATOM 393 CB VAL A 51 4.552 -1.433 27.990 1.00 16.34 C
ATOM 394 CG1 VAL A 51 5.421 -1.112 29.187 1.00 18.56 C
ATOM 395 CG2 VAL A 51 3.614 -0.273 27.756 1.00 16.82 C
ATOM 396 N GLY A 52 6.229 -3.936 27.076 1.00 12.24 N
ATOM 397 CA GLY A 52 7.179 -4.995 27.308 1.00 13.64 C
ATOM 398 C GLY A 52 8.163 -5.141 26.173 1.00 15.14 C
ATOM 399 O GLY A 52 9.333 -5.412 26.407 1.00 15.99 O
ATOM 400 N ALA A 53 7.731 -4.935 24.916 1.00 18.76 N
ATOM 401 CA ALA A 53 8.646 -5.080 23.781 1.00 14.32 C
ATOM 402 C ALA A 53 9.731 -4.043 23.846 1.00 10.54 C
ATOM 403 O ALA A 53 10.860 -4.300 23.428 1.00 15.30 O
ATOM 404 CB ALA A 53 7.858 -4.926 22.504 1.00 14.72 C
ATOM 405 N GLU A 54 9.478 -2.845 24.408 1.00 13.35 N
ATOM 406 CA GLU A 54 10.494 -1.846 24.572 1.00 13.86 C
ATOM 407 C GLU A 54 11.561 -2.194 25.631 1.00 17.54 C
ATOM 408 O GLU A 54 12.581 -1.509 25.658 1.00 17.99 O
ATOM 409 CB GLU A 54 9.754 -0.556 24.867 1.00 16.36 C
ATOM 410 CG GLU A 54 10.604 0.728 24.700 1.00 19.98 C
ATOM 411 CD GLU A 54 11.242 1.324 25.973 1.00 33.77 C
ATOM 412 OE1 GLU A 54 10.752 1.040 27.063 1.00 26.33 O
ATOM 413 OE2 GLU A 54 12.220 2.070 25.890 1.00 28.75 O
ATOM 414 N THR A 55 11.475 -3.220 26.506 1.00 19.05 N
ATOM 415 CA THR A 55 12.551 -3.557 27.444 1.00 15.96 C
ATOM 416 C THR A 55 13.110 -4.947 27.155 1.00 17.46 C
ATOM 417 O THR A 55 14.042 -5.381 27.817 1.00 21.17 O
ATOM 418 CB THR A 55 12.005 -3.513 28.919 1.00 13.94 C
ATOM 419 OG1 THR A 55 11.287 -4.727 29.108 1.00 16.77 O
ATOM 420 CG2 THR A 55 11.073 -2.348 29.195 1.00 18.93 C
ATOM 421 N GLY A 56 12.570 -5.748 26.218 1.00 18.11 N
ATOM 422 CA GLY A 56 13.084 -7.088 25.925 1.00 14.36 C
ATOM 423 C GLY A 56 12.237 -8.176 26.524 1.00 14.53 C
ATOM 424 O GLY A 56 12.434 -9.374 26.329 1.00 19.77 O
ATOM 425 N GLU A 57 11.236 -7.772 27.302 1.00 17.95 N
ATOM 426 CA GLU A 57 10.388 -8.714 28.003 1.00 14.56 C
ATOM 427 C GLU A 57 9.399 -9.429 27.094 1.00 19.55 C
ATOM 428 O GLU A 57 8.985 -10.570 27.364 1.00 18.74 O
ATOM 429 CB GLU A 57 9.647 -7.937 29.080 1.00 15.25 C
ATOM 430 CG GLU A 57 8.695 -8.852 29.844 1.00 25.44 C
ATOM 431 CD GLU A 57 7.968 -8.238 31.032 1.00 32.41 C
ATOM 432 OE1 GLU A 57 7.965 -7.015 31.165 1.00 25.94 O
ATOM 433 OE2 GLU A 57 7.404 -9.005 31.819 1.00 40.55 O
ATOM 434 N ASP A 58 8.907 -8.711 26.061 1.00 16.20 N
ATOM 435 CA ASP A 58 7.928 -9.271 25.141 1.00 12.73 C
ATOM 436 C ASP A 58 8.437 -9.040 23.703 1.00 13.30 C
ATOM 437 O ASP A 58 9.261 -8.155 23.492 1.00 14.77 O
ATOM 438 CB ASP A 58 6.608 -8.577 25.263 1.00 14.67 C
ATOM 439 CG ASP A 58 5.857 -8.919 26.553 1.00 21.34 C
ATOM 440 OD1 ASP A 58 5.853 -10.077 26.968 1.00 21.30 O
ATOM 441 OD2 ASP A 58 5.266 -8.004 27.106 1.00 23.15 O
ATOM 442 N GLY A 59 7.926 -9.816 22.763 1.00 19.15 N
ATOM 443 CA GLY A 59 8.326 -9.704 21.358 1.00 17.18 C
ATOM 444 C GLY A 59 9.697 -10.284 21.149 1.00 19.54 C
ATOM 445 O GLY A 59 10.389 -10.660 22.106 1.00 19.80 O
ATOM 446 N THR A 60 10.154 -10.452 19.904 1.00 16.10 N
ATOM 447 CA THR A 60 11.516 -10.939 19.634 1.00 16.20 C
ATOM 448 C THR A 60 12.208 -10.120 18.533 1.00 19.22 C
ATOM 449 O THR A 60 11.492 -9.446 17.781 1.00 17.59 O
ATOM 450 CB THR A 60 11.550 -12.410 19.180 1.00 22.89 C