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1lda.pdb
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1lda.pdb
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HEADER TRANSPORT PROTEIN 08-APR-02 1LDA
TITLE CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF)
TITLE 2 WITHOUT SUBSTRATE GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROL UPTAKE FACILITATOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AQUAGLYCEROPORIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K12
KEYWDS GLYCEROL-CONDUCTING MEMBRANE CHANNEL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.NOLLERT,L.J.W.MIERCKE,J.O'CONNELL,R.M.STROUD
REVDAT 1 08-MAY-02 1LDA 0
JRNL AUTH E.TAJKHORSHID,P.NOLLERT,M.O.JENSEN,J.O'CONNELL,
JRNL AUTH 2 R.M.STROUD,K.SCHULTEN
JRNL TITL CONTROL OF THE SELECTIVITY OF THE AQUAPORIN WATER
JRNL TITL 2 CHANNEL FAMILY BY GLOBAL ORIENTATIONAL TUNING
JRNL REF SCIENCE V. 296 525 2002
JRNL REFN ASTM SCIEAS US ISSN 0036-8075
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.FU,A.LIBSON,L.J.MIERCKE,C.WEITZMAN,P.NOLLERT,
REMARK 1 AUTH 2 J.KRUCINSKI,R.M.STROUD
REMARK 1 TITL STRUCTURE OF A GLYCEROL-CONDUCTING CHANNEL AND THE
REMARK 1 TITL 2 BASIS FOR ITS SELECTIVITY
REMARK 1 REF SCIENCE V. 290 481 2000
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.6
REMARK 3 NUMBER OF REFLECTIONS : 8698
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 929
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 : 1895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 62
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.11
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1LDA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-2002.
REMARK 100 THE RCSB ID CODE IS RCSB015855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8698
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.6
REMARK 200 DATA REDUNDANCY : 5.918
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1FX8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: GLPF AT 15-20 MG/ML, 28% (W/V) PEG
REMARK 280 2000, 100 MM BICINE PH 9.5, 15 % (V/V) GLYCEROL, 35 MM, N-
REMARK 280 OCTYL-BETA-D-GLUCOSIDE, MGCL2, 5 MM DTT
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1/2-X,1/2-Y,1/2+Z
REMARK 290 11555 1/2-Y,1/2+X,1/2+Z
REMARK 290 12555 1/2+Y,1/2-X,1/2+Z
REMARK 290 13555 1/2-X,1/2+Y,1/2-Z
REMARK 290 14555 1/2+X,1/2-Y,1/2-Z
REMARK 290 15555 1/2+Y,1/2+X,1/2-Z
REMARK 290 16555 1/2-Y,1/2-X,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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 48.37929
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 92.16590
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 48.37929
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 92.16590
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 48.37929
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 92.16590
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 48.37929
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 92.16590
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 48.37929
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 92.16590
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 48.37929
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 92.16590
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 48.37929
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 92.16590
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 48.37929
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 48.37929
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 92.16590
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 -1.000000 0.000000 0.000000 96.75859
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 96.75859
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 96.75859
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 96.75859
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 PRO A 260
REMARK 465 CYS A 261
REMARK 465 ASP A 262
REMARK 465 ILE A 263
REMARK 465 CYS A 264
REMARK 465 VAL A 265
REMARK 465 VAL A 266
REMARK 465 GLU A 267
REMARK 465 GLU A 268
REMARK 465 LYS A 269
REMARK 465 GLU A 270
REMARK 465 THR A 271
REMARK 465 THR A 272
REMARK 465 THR A 273
REMARK 465 PRO A 274
REMARK 465 SER A 275
REMARK 465 GLU A 276
REMARK 465 GLN A 277
REMARK 465 LYS A 278
REMARK 465 ALA A 279
REMARK 465 SER A 280
REMARK 465 LEU A 281
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 ARG A 257 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 347 O HOH 347 15456 0.44
REMARK 500 O HOH 55 O HOH 55 15456 0.45
REMARK 500 O HOH 1 O HOH 1 3655 0.55
REMARK 500 O HOH 37 O HOH 37 3655 0.55
REMARK 500 O HOH 348 O HOH 348 3655 0.55
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 6 CB THR A 6 CA 0.060
REMARK 500 MET A 54 CE MET A 54 SD 0.094
REMARK 500 MET A 153 CE MET A 153 SD 0.098
REMARK 500 MET A 202 CE MET A 202 SD 0.066
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 21 CA - CB - CG ANGL. DEV. = 7.8 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 35 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH 63 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH 423 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH 382 DISTANCE = 7.69 ANGSTROMS
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LDF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR
REMARK 900 (GLPF) MUTATION W48F, F200T
REMARK 900 RELATED ID: 1LDI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR
REMARK 900 (GLPF) WITHOUT SUBSTRATE GLYCEROL
DBREF 1LDA A 1 281 SWS P11244 GLPF_ECOLI 1 281
SEQRES 1 A 281 MET SER GLN THR SER THR LEU LYS GLY GLN CYS ILE ALA
SEQRES 2 A 281 GLU PHE LEU GLY THR GLY LEU LEU ILE PHE PHE GLY VAL
SEQRES 3 A 281 GLY CYS VAL ALA ALA LEU LYS VAL ALA GLY ALA SER PHE
SEQRES 4 A 281 GLY GLN TRP GLU ILE SER VAL ILE TRP GLY LEU GLY VAL
SEQRES 5 A 281 ALA MET ALA ILE TYR LEU THR ALA GLY VAL SER GLY ALA
SEQRES 6 A 281 HIS LEU ASN PRO ALA VAL THR ILE ALA LEU TRP LEU PHE
SEQRES 7 A 281 ALA CYS PHE ASP LYS ARG LYS VAL ILE PRO PHE ILE VAL
SEQRES 8 A 281 SER GLN VAL ALA GLY ALA PHE CYS ALA ALA ALA LEU VAL
SEQRES 9 A 281 TYR GLY LEU TYR TYR ASN LEU PHE PHE ASP PHE GLU GLN
SEQRES 10 A 281 THR HIS HIS ILE VAL ARG GLY SER VAL GLU SER VAL ASP
SEQRES 11 A 281 LEU ALA GLY THR PHE SER THR TYR PRO ASN PRO HIS ILE
SEQRES 12 A 281 ASN PHE VAL GLN ALA PHE ALA VAL GLU MET VAL ILE THR
SEQRES 13 A 281 ALA ILE LEU MET GLY LEU ILE LEU ALA LEU THR ASP ASP
SEQRES 14 A 281 GLY ASN GLY VAL PRO ARG GLY PRO LEU ALA PRO LEU LEU
SEQRES 15 A 281 ILE GLY LEU LEU ILE ALA VAL ILE GLY ALA SER MET GLY
SEQRES 16 A 281 PRO LEU THR GLY PHE ALA MET ASN PRO ALA ARG ASP PHE
SEQRES 17 A 281 GLY PRO LYS VAL PHE ALA TRP LEU ALA GLY TRP GLY ASN
SEQRES 18 A 281 VAL ALA PHE THR GLY GLY ARG ASP ILE PRO TYR PHE LEU
SEQRES 19 A 281 VAL PRO LEU PHE GLY PRO ILE VAL GLY ALA ILE VAL GLY
SEQRES 20 A 281 ALA PHE ALA TYR ARG LYS LEU ILE GLY ARG HIS LEU PRO
SEQRES 21 A 281 CYS ASP ILE CYS VAL VAL GLU GLU LYS GLU THR THR THR
SEQRES 22 A 281 PRO SER GLU GLN LYS ALA SER LEU
HET BOG 473 20
HET BOG 474 20
HETNAM BOG B-OCTYLGLUCOSIDE
FORMUL 2 BOG 2(C14 H28 O6)
FORMUL 4 HOH *62(H2 O1)
HELIX 1 1 THR A 6 ALA A 35 1 30
HELIX 2 2 GLY A 40 GLY A 64 1 25
HELIX 3 3 ASN A 68 ALA A 79 1 12
HELIX 4 4 ASP A 82 ARG A 84 5 3
HELIX 5 5 LYS A 85 TYR A 109 1 25
HELIX 6 6 TYR A 108 HIS A 119 1 12
HELIX 7 7 SER A 125 GLU A 127 5 3
HELIX 8 8 SER A 128 GLY A 133 1 6
HELIX 9 9 ASN A 144 ASP A 168 1 25
HELIX 10 10 ARG A 175 PRO A 177 5 3
HELIX 11 11 LEU A 178 GLY A 199 1 22
HELIX 12 12 ASN A 203 ALA A 217 1 15
HELIX 13 13 ASN A 221 GLY A 226 1 6
HELIX 14 14 PHE A 233 GLY A 239 1 7
HELIX 15 15 PRO A 240 ILE A 255 1 16
HELIX 16 16 GLY A 256 LEU A 259 5 4
CRYST1 96.230 96.230 184.370 90.00 90.00 90.00 I 4 2 2 16
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 0.010335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005425 0.00000
ATOM 1 N THR A 6 30.252 70.723 179.736 1.00 62.78 N
ATOM 2 CA THR A 6 29.511 71.883 179.140 1.00 63.84 C
ATOM 3 C THR A 6 29.064 71.592 177.713 1.00 63.62 C
ATOM 4 O THR A 6 29.886 71.373 176.823 1.00 63.87 O
ATOM 5 CB THR A 6 30.363 73.237 179.155 1.00 64.26 C
ATOM 6 OG1 THR A 6 29.723 74.231 178.344 1.00 64.07 O
ATOM 7 CG2 THR A 6 31.774 73.027 178.628 1.00 63.66 C
ATOM 8 N LEU A 7 27.747 71.598 177.511 1.00 63.04 N
ATOM 9 CA LEU A 7 27.152 71.336 176.204 1.00 61.60 C
ATOM 10 C LEU A 7 27.764 72.138 175.051 1.00 60.88 C
ATOM 11 O LEU A 7 27.814 71.643 173.932 1.00 62.30 O
ATOM 12 CB LEU A 7 25.640 71.580 176.249 1.00 59.98 C
ATOM 13 CG LEU A 7 24.867 71.259 174.966 1.00 58.20 C
ATOM 14 CD1 LEU A 7 25.050 69.818 174.578 1.00 58.62 C
ATOM 15 CD2 LEU A 7 23.413 71.514 175.192 1.00 56.44 C
ATOM 16 N LYS A 8 28.220 73.362 175.306 1.00 60.48 N
ATOM 17 CA LYS A 8 28.824 74.167 174.246 1.00 60.39 C
ATOM 18 C LYS A 8 30.177 73.581 173.822 1.00 60.05 C
ATOM 19 O LYS A 8 30.535 73.583 172.642 1.00 58.35 O
ATOM 20 CB LYS A 8 29.023 75.607 174.705 1.00 61.92 C
ATOM 21 CG LYS A 8 29.671 76.472 173.651 1.00 64.99 C
ATOM 22 CD LYS A 8 29.872 77.886 174.152 1.00 68.45 C
ATOM 23 CE LYS A 8 30.371 78.806 173.042 1.00 71.83 C
ATOM 24 NZ LYS A 8 30.430 80.251 173.438 1.00 73.68 N
ATOM 25 N GLY A 9 30.926 73.086 174.803 1.00 58.56 N
ATOM 26 CA GLY A 9 32.223 72.493 174.525 1.00 57.49 C
ATOM 27 C GLY A 9 32.128 71.131 173.850 1.00 57.05 C
ATOM 28 O GLY A 9 33.077 70.665 173.206 1.00 56.64 O
ATOM 29 N GLN A 10 30.972 70.492 174.007 1.00 55.25 N
ATOM 30 CA GLN A 10 30.719 69.189 173.423 1.00 52.89 C
ATOM 31 C GLN A 10 30.317 69.348 171.972 1.00 53.50 C
ATOM 32 O GLN A 10 30.692 68.541 171.124 1.00 54.23 O
ATOM 33 CB GLN A 10 29.615 68.480 174.184 1.00 51.88 C
ATOM 34 CG GLN A 10 29.972 68.213 175.607 1.00 50.53 C
ATOM 35 CD GLN A 10 29.009 67.256 176.228 1.00 50.76 C
ATOM 36 OE1 GLN A 10 27.801 67.505 176.242 1.00 52.58 O
ATOM 37 NE2 GLN A 10 29.519 66.146 176.735 1.00 49.56 N
ATOM 38 N CYS A 11 29.550 70.393 171.683 1.00 52.89 N
ATOM 39 CA CYS A 11 29.127 70.655 170.317 1.00 52.98 C
ATOM 40 C CYS A 11 30.324 71.091 169.487 1.00 51.38 C
ATOM 41 O CYS A 11 30.396 70.824 168.290 1.00 52.28 O
ATOM 42 CB CYS A 11 28.052 71.733 170.296 1.00 51.99 C
ATOM 43 SG CYS A 11 26.510 71.127 170.983 1.00 53.42 S
ATOM 44 N ILE A 12 31.265 71.767 170.125 1.00 49.12 N
ATOM 45 CA ILE A 12 32.456 72.199 169.420 1.00 48.65 C
ATOM 46 C ILE A 12 33.286 70.969 169.039 1.00 48.56 C
ATOM 47 O ILE A 12 33.724 70.833 167.897 1.00 48.11 O
ATOM 48 CB ILE A 12 33.297 73.154 170.299 1.00 47.52 C
ATOM 49 CG1 ILE A 12 32.616 74.520 170.357 1.00 46.29 C
ATOM 50 CG2 ILE A 12 34.720 73.284 169.755 1.00 48.94 C
ATOM 51 CD1 ILE A 12 33.371 75.545 171.174 1.00 42.58 C
ATOM 52 N ALA A 13 33.485 70.072 170.001 1.00 48.38 N
ATOM 53 CA ALA A 13 34.260 68.854 169.785 1.00 48.02 C
ATOM 54 C ALA A 13 33.632 68.039 168.654 1.00 48.25 C
ATOM 55 O ALA A 13 34.319 67.561 167.746 1.00 48.57 O
ATOM 56 CB ALA A 13 34.310 68.031 171.074 1.00 47.48 C
ATOM 57 N GLU A 14 32.320 67.884 168.718 1.00 49.26 N
ATOM 58 CA GLU A 14 31.598 67.159 167.693 1.00 49.48 C
ATOM 59 C GLU A 14 31.782 67.831 166.327 1.00 49.26 C
ATOM 60 O GLU A 14 31.853 67.157 165.302 1.00 51.09 O
ATOM 61 CB GLU A 14 30.116 67.094 168.055 1.00 48.86 C
ATOM 62 CG GLU A 14 29.803 66.078 169.164 1.00 48.28 C
ATOM 63 CD GLU A 14 30.068 64.615 168.762 1.00 49.32 C
ATOM 64 OE1 GLU A 14 29.512 64.156 167.743 1.00 47.60 O
ATOM 65 OE2 GLU A 14 30.822 63.910 169.477 1.00 49.63 O
ATOM 66 N PHE A 15 31.865 69.157 166.319 1.00 48.32 N
ATOM 67 CA PHE A 15 32.055 69.926 165.090 1.00 46.14 C
ATOM 68 C PHE A 15 33.466 69.672 164.528 1.00 46.55 C
ATOM 69 O PHE A 15 33.659 69.482 163.326 1.00 44.88 O
ATOM 70 CB PHE A 15 31.879 71.412 165.398 1.00 44.07 C
ATOM 71 CG PHE A 15 31.993 72.296 164.200 1.00 42.19 C
ATOM 72 CD1 PHE A 15 30.885 72.549 163.410 1.00 41.30 C
ATOM 73 CD2 PHE A 15 33.219 72.855 163.842 1.00 40.42 C
ATOM 74 CE1 PHE A 15 30.983 73.340 162.274 1.00 40.24 C
ATOM 75 CE2 PHE A 15 33.333 73.650 162.701 1.00 40.17 C
ATOM 76 CZ PHE A 15 32.211 73.893 161.917 1.00 39.60 C
ATOM 77 N LEU A 16 34.452 69.675 165.411 1.00 45.89 N
ATOM 78 CA LEU A 16 35.822 69.435 165.004 1.00 46.24 C
ATOM 79 C LEU A 16 36.057 67.954 164.671 1.00 47.20 C
ATOM 80 O LEU A 16 36.777 67.616 163.728 1.00 49.32 O
ATOM 81 CB LEU A 16 36.770 69.851 166.123 1.00 44.03 C
ATOM 82 CG LEU A 16 36.782 71.315 166.534 1.00 42.76 C
ATOM 83 CD1 LEU A 16 37.683 71.481 167.747 1.00 43.44 C
ATOM 84 CD2 LEU A 16 37.263 72.162 165.374 1.00 39.29 C
ATOM 85 N GLY A 17 35.453 67.070 165.452 1.00 46.46 N
ATOM 86 CA GLY A 17 35.623 65.659 165.210 1.00 46.26 C
ATOM 87 C GLY A 17 35.060 65.248 163.864 1.00 46.72 C
ATOM 88 O GLY A 17 35.762 64.667 163.039 1.00 47.95 O
ATOM 89 N THR A 18 33.793 65.558 163.626 1.00 45.45 N
ATOM 90 CA THR A 18 33.164 65.191 162.370 1.00 44.92 C
ATOM 91 C THR A 18 33.878 65.830 161.195 1.00 43.16 C
ATOM 92 O THR A 18 34.020 65.215 160.135 1.00 44.07 O
ATOM 93 CB THR A 18 31.679 65.611 162.355 1.00 45.75 C
ATOM 94 OG1 THR A 18 31.019 64.983 163.456 1.00 47.08 O
ATOM 95 CG2 THR A 18 30.990 65.174 161.064 1.00 45.18 C
ATOM 96 N GLY A 19 34.340 67.055 161.389 1.00 41.31 N
ATOM 97 CA GLY A 19 35.023 67.741 160.322 1.00 39.20 C
ATOM 98 C GLY A 19 36.343 67.077 160.046 1.00 39.35 C
ATOM 99 O GLY A 19 36.690 66.828 158.890 1.00 40.80 O
ATOM 100 N LEU A 20 37.079 66.766 161.106 1.00 39.28 N
ATOM 101 CA LEU A 20 38.387 66.131 160.969 1.00 40.78 C
ATOM 102 C LEU A 20 38.206 64.838 160.196 1.00 41.23 C
ATOM 103 O LEU A 20 38.926 64.550 159.233 1.00 41.73 O
ATOM 104 CB LEU A 20 38.986 65.900 162.363 1.00 41.45 C
ATOM 105 CG LEU A 20 40.419 65.371 162.551 1.00 42.66 C
ATOM 106 CD1 LEU A 20 40.402 63.864 162.590 1.00 45.70 C
ATOM 107 CD2 LEU A 20 41.324 65.871 161.441 1.00 44.81 C
ATOM 108 N LEU A 21 37.214 64.076 160.623 1.00 43.54 N
ATOM 109 CA LEU A 21 36.841 62.821 160.000 1.00 43.32 C
ATOM 110 C LEU A 21 36.656 63.012 158.494 1.00 44.51 C
ATOM 111 O LEU A 21 37.283 62.303 157.714 1.00 45.95 O
ATOM 112 CB LEU A 21 35.547 62.358 160.645 1.00 44.69 C
ATOM 113 CG LEU A 21 34.803 61.113 160.245 1.00 46.79 C
ATOM 114 CD1 LEU A 21 33.807 60.833 161.362 1.00 45.66 C
ATOM 115 CD2 LEU A 21 34.092 61.280 158.901 1.00 47.48 C
ATOM 116 N ILE A 22 35.796 63.954 158.079 1.00 45.14 N
ATOM 117 CA ILE A 22 35.539 64.216 156.638 1.00 45.89 C
ATOM 118 C ILE A 22 36.773 64.769 155.898 1.00 45.13 C
ATOM 119 O ILE A 22 36.968 64.523 154.700 1.00 44.17 O
ATOM 120 CB ILE A 22 34.324 65.223 156.411 1.00 45.66 C
ATOM 121 CG1 ILE A 22 32.988 64.464 156.313 1.00 45.49 C
ATOM 122 CG2 ILE A 22 34.514 66.013 155.126 1.00 44.69 C
ATOM 123 CD1 ILE A 22 32.533 63.867 157.624 1.00 49.11 C
ATOM 124 N PHE A 23 37.602 65.524 156.620 1.00 44.14 N
ATOM 125 CA PHE A 23 38.809 66.099 156.043 1.00 41.77 C
ATOM 126 C PHE A 23 39.642 64.980 155.404 1.00 42.21 C
ATOM 127 O PHE A 23 40.006 65.058 154.233 1.00 42.28 O
ATOM 128 CB PHE A 23 39.626 66.816 157.127 1.00 41.89 C
ATOM 129 CG PHE A 23 40.846 67.520 156.599 1.00 42.46 C
ATOM 130 CD1 PHE A 23 40.742 68.777 156.009 1.00 42.40 C
ATOM 131 CD2 PHE A 23 42.098 66.884 156.607 1.00 42.36 C
ATOM 132 CE1 PHE A 23 41.861 69.399 155.435 1.00 42.11 C
ATOM 133 CE2 PHE A 23 43.233 67.488 156.033 1.00 40.88 C
ATOM 134 CZ PHE A 23 43.115 68.747 155.443 1.00 41.91 C
ATOM 135 N PHE A 24 39.933 63.933 156.167 1.00 40.73 N
ATOM 136 CA PHE A 24 40.706 62.805 155.655 1.00 41.33 C
ATOM 137 C PHE A 24 39.934 61.993 154.600 1.00 41.34 C
ATOM 138 O PHE A 24 40.467 61.660 153.538 1.00 42.02 O
ATOM 139 CB PHE A 24 41.089 61.885 156.811 1.00 40.62 C
ATOM 140 CG PHE A 24 41.932 62.549 157.854 1.00 41.75 C
ATOM 141 CD1 PHE A 24 41.670 62.358 159.208 1.00 41.59 C
ATOM 142 CD2 PHE A 24 43.020 63.340 157.485 1.00 42.53 C
ATOM 143 CE1 PHE A 24 42.480 62.936 160.187 1.00 41.40 C
ATOM 144 CE2 PHE A 24 43.840 63.922 158.447 1.00 42.22 C
ATOM 145 CZ PHE A 24 43.572 63.722 159.804 1.00 42.56 C
ATOM 146 N GLY A 25 38.685 61.665 154.899 1.00 41.60 N
ATOM 147 CA GLY A 25 37.893 60.910 153.954 1.00 42.25 C
ATOM 148 C GLY A 25 37.727 61.574 152.589 1.00 43.54 C
ATOM 149 O GLY A 25 38.127 61.008 151.573 1.00 44.16 O
ATOM 150 N VAL A 26 37.137 62.768 152.553 1.00 42.76 N
ATOM 151 CA VAL A 26 36.920 63.485 151.288 1.00 42.39 C
ATOM 152 C VAL A 26 38.268 63.861 150.661 1.00 41.75 C
ATOM 153 O VAL A 26 38.419 63.955 149.435 1.00 40.65 O
ATOM 154 CB VAL A 26 36.049 64.778 151.516 1.00 43.12 C
ATOM 155 CG1 VAL A 26 35.965 65.599 150.243 1.00 42.46 C
ATOM 156 CG2 VAL A 26 34.630 64.390 151.946 1.00 41.91 C
ATOM 157 N GLY A 27 39.254 64.042 151.525 1.00 41.04 N
ATOM 158 CA GLY A 27 40.572 64.399 151.061 1.00 40.88 C
ATOM 159 C GLY A 27 41.239 63.319 150.238 1.00 41.86 C
ATOM 160 O GLY A 27 41.695 63.598 149.134 1.00 43.14 O
ATOM 161 N CYS A 28 41.299 62.091 150.766 1.00 42.31 N
ATOM 162 CA CYS A 28 41.944 60.984 150.059 1.00 42.70 C
ATOM 163 C CYS A 28 41.152 60.593 148.821 1.00 42.65 C
ATOM 164 O CYS A 28 41.712 60.104 147.841 1.00 43.65 O
ATOM 165 CB CYS A 28 42.144 59.770 150.988 1.00 42.37 C
ATOM 166 SG CYS A 28 40.688 58.710 151.364 1.00 45.22 S
ATOM 167 N VAL A 29 39.842 60.819 148.862 1.00 42.77 N
ATOM 168 CA VAL A 29 38.995 60.501 147.726 1.00 40.82 C
ATOM 169 C VAL A 29 39.123 61.548 146.627 1.00 41.37 C
ATOM 170 O VAL A 29 38.882 61.251 145.460 1.00 41.48 O
ATOM 171 CB VAL A 29 37.539 60.411 148.124 1.00 40.51 C
ATOM 172 CG1 VAL A 29 36.683 60.078 146.903 1.00 36.33 C
ATOM 173 CG2 VAL A 29 37.389 59.388 149.222 1.00 39.15 C
ATOM 174 N ALA A 30 39.475 62.778 147.002 1.00 40.46 N
ATOM 175 CA ALA A 30 39.663 63.849 146.023 1.00 39.65 C
ATOM 176 C ALA A 30 40.985 63.622 145.303 1.00 40.44 C
ATOM 177 O ALA A 30 41.123 63.947 144.123 1.00 40.04 O
ATOM 178 CB ALA A 30 39.692 65.195 146.712 1.00 38.25 C
ATOM 179 N ALA A 31 41.965 63.076 146.033 1.00 39.70 N
ATOM 180 CA ALA A 31 43.290 62.781 145.488 1.00 39.54 C
ATOM 181 C ALA A 31 43.185 61.634 144.503 1.00 40.23 C
ATOM 182 O ALA A 31 43.926 61.569 143.519 1.00 41.53 O
ATOM 183 CB ALA A 31 44.256 62.411 146.611 1.00 38.82 C
ATOM 184 N LEU A 32 42.263 60.719 144.785 1.00 39.97 N
ATOM 185 CA LEU A 32 42.005 59.571 143.924 1.00 37.77 C
ATOM 186 C LEU A 32 41.277 60.008 142.649 1.00 38.08 C
ATOM 187 O LEU A 32 41.635 59.584 141.552 1.00 38.07 O
ATOM 188 CB LEU A 32 41.129 58.554 144.656 1.00 34.71 C
ATOM 189 CG LEU A 32 40.461 57.464 143.797 1.00 31.89 C
ATOM 190 CD1 LEU A 32 41.500 56.487 143.334 1.00 29.63 C
ATOM 191 CD2 LEU A 32 39.416 56.739 144.605 1.00 29.37 C
ATOM 192 N LYS A 33 40.262 60.850 142.808 1.00 37.14 N
ATOM 193 CA LYS A 33 39.455 61.302 141.678 1.00 39.26 C
ATOM 194 C LYS A 33 40.074 62.379 140.797 1.00 40.94 C
ATOM 195 O LYS A 33 40.100 62.228 139.578 1.00 41.67 O
ATOM 196 CB LYS A 33 38.090 61.823 142.151 1.00 37.92 C
ATOM 197 CG LYS A 33 37.271 60.901 143.032 1.00 37.14 C
ATOM 198 CD LYS A 33 36.337 60.084 142.195 1.00 36.13 C
ATOM 199 CE LYS A 33 35.173 59.576 143.004 1.00 34.98 C
ATOM 200 NZ LYS A 33 34.219 58.857 142.114 1.00 37.13 N
ATOM 201 N VAL A 34 40.560 63.462 141.404 1.00 41.80 N
ATOM 202 CA VAL A 34 41.127 64.573 140.637 1.00 41.50 C
ATOM 203 C VAL A 34 42.628 64.786 140.759 1.00 41.42 C
ATOM 204 O VAL A 34 43.166 65.720 140.167 1.00 43.50 O
ATOM 205 CB VAL A 34 40.434 65.917 141.000 1.00 41.81 C
ATOM 206 CG1 VAL A 34 38.940 65.795 140.805 1.00 43.05 C
ATOM 207 CG2 VAL A 34 40.745 66.311 142.437 1.00 42.13 C
ATOM 208 N ALA A 35 43.311 63.938 141.520 1.00 41.80 N
ATOM 209 CA ALA A 35 44.760 64.098 141.663 1.00 40.45 C
ATOM 210 C ALA A 35 45.507 62.925 141.036 1.00 40.17 C
ATOM 211 O ALA A 35 46.738 62.906 141.010 1.00 43.02 O
ATOM 212 CB ALA A 35 45.145 64.264 143.145 1.00 39.04 C
ATOM 213 N GLY A 36 44.762 61.955 140.529 1.00 40.54 N
ATOM 214 CA GLY A 36 45.391 60.805 139.909 1.00 42.60 C
ATOM 215 C GLY A 36 46.214 59.934 140.841 1.00 43.74 C
ATOM 216 O GLY A 36 47.127 59.238 140.398 1.00 44.38 O
ATOM 217 N ALA A 37 45.892 59.958 142.130 1.00 43.41 N
ATOM 218 CA ALA A 37 46.603 59.161 143.126 1.00 43.69 C
ATOM 219 C ALA A 37 46.129 57.706 143.077 1.00 44.42 C
ATOM 220 O ALA A 37 44.950 57.447 142.826 1.00 46.29 O
ATOM 221 CB ALA A 37 46.369 59.754 144.509 1.00 42.11 C
ATOM 222 N SER A 38 47.038 56.755 143.298 1.00 43.50 N
ATOM 223 CA SER A 38 46.695 55.327 143.282 1.00 42.86 C
ATOM 224 C SER A 38 46.177 54.858 144.601 1.00 41.95 C
ATOM 225 O SER A 38 46.913 54.841 145.590 1.00 42.14 O
ATOM 226 CB SER A 38 47.896 54.473 142.937 1.00 43.19 C
ATOM 227 OG SER A 38 48.220 54.673 141.587 1.00 48.13 O
ATOM 228 N PHE A 39 44.911 54.449 144.598 1.00 42.44 N
ATOM 229 CA PHE A 39 44.228 53.947 145.785 1.00 42.29 C
ATOM 230 C PHE A 39 43.363 52.742 145.442 1.00 42.32 C
ATOM 231 O PHE A 39 42.665 52.730 144.429 1.00 43.15 O
ATOM 232 CB PHE A 39 43.328 55.023 146.375 1.00 42.70 C
ATOM 233 CG PHE A 39 44.064 56.136 147.041 1.00 44.66 C
ATOM 234 CD1 PHE A 39 43.983 57.437 146.550 1.00 45.61 C
ATOM 235 CD2 PHE A 39 44.787 55.903 148.199 1.00 46.54 C
ATOM 236 CE1 PHE A 39 44.603 58.490 147.213 1.00 46.17 C
ATOM 237 CE2 PHE A 39 45.410 56.941 148.872 1.00 46.37 C
ATOM 238 CZ PHE A 39 45.316 58.240 148.378 1.00 46.15 C
ATOM 239 N GLY A 40 43.402 51.728 146.293 1.00 41.55 N
ATOM 240 CA GLY A 40 42.578 50.562 146.050 1.00 40.95 C
ATOM 241 C GLY A 40 41.357 50.663 146.945 1.00 41.06 C
ATOM 242 O GLY A 40 41.235 51.616 147.707 1.00 40.08 O
ATOM 243 N GLN A 41 40.443 49.699 146.847 1.00 41.19 N
ATOM 244 CA GLN A 41 39.245 49.697 147.688 1.00 40.39 C
ATOM 245 C GLN A 41 39.600 49.619 149.184 1.00 39.79 C
ATOM 246 O GLN A 41 38.902 50.189 150.027 1.00 39.83 O
ATOM 247 CB GLN A 41 38.339 48.520 147.318 1.00 40.83 C
ATOM 248 CG GLN A 41 37.020 48.477 148.084 1.00 41.98 C
ATOM 249 CD GLN A 41 36.265 49.776 147.952 1.00 42.05 C
ATOM 250 OE1 GLN A 41 36.236 50.360 146.870 1.00 43.92 O
ATOM 251 NE2 GLN A 41 35.661 50.241 149.036 1.00 39.66 N
ATOM 252 N TRP A 42 40.673 48.907 149.513 1.00 38.95 N
ATOM 253 CA TRP A 42 41.100 48.759 150.899 1.00 39.09 C
ATOM 254 C TRP A 42 41.824 50.002 151.412 1.00 40.72 C
ATOM 255 O TRP A 42 41.685 50.377 152.577 1.00 40.73 O
ATOM 256 CB TRP A 42 42.008 47.535 151.055 1.00 37.66 C
ATOM 257 CG TRP A 42 42.854 47.571 152.296 1.00 37.38 C
ATOM 258 CD1 TRP A 42 44.196 47.814 152.361 1.00 36.37 C
ATOM 259 CD2 TRP A 42 42.409 47.421 153.651 1.00 36.54 C
ATOM 260 NE1 TRP A 42 44.614 47.825 153.670 1.00 37.37 N
ATOM 261 CE2 TRP A 42 43.535 47.582 154.486 1.00 36.71 C
ATOM 262 CE3 TRP A 42 41.166 47.156 154.243 1.00 36.74 C
ATOM 263 CZ2 TRP A 42 43.462 47.501 155.882 1.00 35.40 C
ATOM 264 CZ3 TRP A 42 41.087 47.074 155.637 1.00 36.64 C
ATOM 265 CH2 TRP A 42 42.232 47.244 156.436 1.00 36.74 C
ATOM 266 N GLU A 43 42.609 50.638 150.546 1.00 40.20 N
ATOM 267 CA GLU A 43 43.333 51.845 150.932 1.00 40.28 C
ATOM 268 C GLU A 43 42.360 52.968 151.305 1.00 40.69 C
ATOM 269 O GLU A 43 42.493 53.586 152.365 1.00 41.60 O
ATOM 270 CB GLU A 43 44.244 52.315 149.795 1.00 41.20 C
ATOM 271 CG GLU A 43 45.439 51.423 149.533 1.00 42.14 C
ATOM 272 CD GLU A 43 45.040 50.050 149.058 1.00 43.58 C
ATOM 273 OE1 GLU A 43 43.977 49.926 148.410 1.00 42.97 O
ATOM 274 OE2 GLU A 43 45.797 49.092 149.319 1.00 45.41 O
ATOM 275 N ILE A 44 41.391 53.234 150.426 1.00 39.40 N
ATOM 276 CA ILE A 44 40.382 54.264 150.674 1.00 38.31 C
ATOM 277 C ILE A 44 39.633 53.957 151.967 1.00 37.15 C
ATOM 278 O ILE A 44 39.358 54.849 152.762 1.00 35.98 O
ATOM 279 CB ILE A 44 39.356 54.349 149.513 1.00 38.31 C
ATOM 280 CG1 ILE A 44 40.064 54.856 148.248 1.00 39.37 C
ATOM 281 CG2 ILE A 44 38.199 55.286 149.886 1.00 38.11 C
ATOM 282 CD1 ILE A 44 40.764 56.222 148.417 1.00 36.16 C
ATOM 283 N SER A 45 39.321 52.683 152.173 1.00 38.47 N
ATOM 284 CA SER A 45 38.625 52.245 153.373 1.00 39.40 C
ATOM 285 C SER A 45 39.457 52.425 154.647 1.00 39.48 C
ATOM 286 O SER A 45 38.957 52.911 155.667 1.00 40.09 O
ATOM 287 CB SER A 45 38.242 50.780 153.228 1.00 37.86 C
ATOM 288 OG SER A 45 37.423 50.605 152.084 1.00 39.10 O
ATOM 289 N VAL A 46 40.725 52.036 154.592 1.00 40.09 N
ATOM 290 CA VAL A 46 41.583 52.139 155.765 1.00 40.95 C
ATOM 291 C VAL A 46 41.849 53.591 156.115 1.00 40.76 C
ATOM 292 O VAL A 46 41.989 53.945 157.287 1.00 42.11 O
ATOM 293 CB VAL A 46 42.917 51.393 155.564 1.00 39.37 C
ATOM 294 CG1 VAL A 46 43.759 52.098 154.546 1.00 39.15 C
ATOM 295 CG2 VAL A 46 43.659 51.302 156.879 1.00 39.32 C
ATOM 296 N ILE A 47 41.902 54.439 155.103 1.00 39.29 N
ATOM 297 CA ILE A 47 42.138 55.854 155.347 1.00 38.85 C
ATOM 298 C ILE A 47 40.897 56.462 156.008 1.00 38.94 C
ATOM 299 O ILE A 47 41.009 57.305 156.901 1.00 39.54 O
ATOM 300 CB ILE A 47 42.469 56.589 154.025 1.00 35.83 C
ATOM 301 CG1 ILE A 47 43.789 56.054 153.467 1.00 33.49 C
ATOM 302 CG2 ILE A 47 42.556 58.098 154.260 1.00 33.30 C
ATOM 303 CD1 ILE A 47 44.024 56.422 152.037 1.00 33.00 C
ATOM 304 N TRP A 48 39.714 56.029 155.575 1.00 38.07 N
ATOM 305 CA TRP A 48 38.483 56.541 156.153 1.00 37.31 C
ATOM 306 C TRP A 48 38.417 56.070 157.593 1.00 38.51 C
ATOM 307 O TRP A 48 38.118 56.848 158.497 1.00 38.99 O
ATOM 308 CB TRP A 48 37.261 56.045 155.390 1.00 35.49 C
ATOM 309 CG TRP A 48 36.784 56.986 154.344 1.00 37.19 C
ATOM 310 CD1 TRP A 48 37.097 56.970 153.015 1.00 39.10 C
ATOM 311 CD2 TRP A 48 35.924 58.125 154.537 1.00 38.38 C
ATOM 312 NE1 TRP A 48 36.490 58.021 152.369 1.00 38.39 N
ATOM 313 CE2 TRP A 48 35.764 58.745 153.275 1.00 38.52 C
ATOM 314 CE3 TRP A 48 35.278 58.680 155.653 1.00 38.60 C
ATOM 315 CZ2 TRP A 48 34.979 59.901 153.101 1.00 37.22 C
ATOM 316 CZ3 TRP A 48 34.494 59.835 155.478 1.00 37.47 C
ATOM 317 CH2 TRP A 48 34.355 60.428 154.209 1.00 37.35 C
ATOM 318 N GLY A 49 38.713 54.788 157.795 1.00 37.78 N
ATOM 319 CA GLY A 49 38.696 54.201 159.120 1.00 38.11 C
ATOM 320 C GLY A 49 39.631 54.887 160.097 1.00 38.91 C
ATOM 321 O GLY A 49 39.218 55.265 161.199 1.00 39.78 O
ATOM 322 N LEU A 50 40.892 55.051 159.705 1.00 40.39 N
ATOM 323 CA LEU A 50 41.879 55.709 160.566 1.00 40.53 C
ATOM 324 C LEU A 50 41.556 57.180 160.763 1.00 40.32 C
ATOM 325 O LEU A 50 41.952 57.766 161.764 1.00 41.68 O
ATOM 326 CB LEU A 50 43.288 55.581 159.992 1.00 40.49 C
ATOM 327 CG LEU A 50 43.818 54.148 159.929 1.00 43.27 C
ATOM 328 CD1 LEU A 50 45.221 54.140 159.320 1.00 43.51 C
ATOM 329 CD2 LEU A 50 43.801 53.539 161.335 1.00 42.84 C
ATOM 330 N GLY A 51 40.856 57.792 159.815 1.00 39.68 N
ATOM 331 CA GLY A 51 40.526 59.189 159.986 1.00 38.74 C
ATOM 332 C GLY A 51 39.531 59.335 161.120 1.00 38.69 C
ATOM 333 O GLY A 51 39.613 60.253 161.945 1.00 37.49 O
ATOM 334 N VAL A 52 38.579 58.408 161.153 1.00 39.70 N
ATOM 335 CA VAL A 52 37.549 58.399 162.177 1.00 39.31 C
ATOM 336 C VAL A 52 38.211 58.067 163.507 1.00 39.86 C
ATOM 337 O VAL A 52 37.850 58.635 164.538 1.00 40.74 O
ATOM 338 CB VAL A 52 36.442 57.353 161.859 1.00 38.31 C
ATOM 339 CG1 VAL A 52 35.416 57.321 162.970 1.00 36.48 C
ATOM 340 CG2 VAL A 52 35.744 57.722 160.570 1.00 35.46 C
ATOM 341 N ALA A 53 39.192 57.166 163.469 1.00 39.16 N
ATOM 342 CA ALA A 53 39.919 56.762 164.670 1.00 38.96 C
ATOM 343 C ALA A 53 40.574 57.963 165.335 1.00 38.93 C
ATOM 344 O ALA A 53 40.578 58.065 166.556 1.00 39.04 O
ATOM 345 CB ALA A 53 40.971 55.724 164.321 1.00 37.39 C
ATOM 346 N MET A 54 41.136 58.854 164.518 1.00 40.50 N
ATOM 347 CA MET A 54 41.781 60.078 164.990 1.00 40.88 C
ATOM 348 C MET A 54 40.722 61.052 165.485 1.00 40.27 C
ATOM 349 O MET A 54 40.924 61.747 166.476 1.00 39.01 O
ATOM 350 CB MET A 54 42.563 60.733 163.862 1.00 42.39 C
ATOM 351 CG MET A 54 43.730 59.913 163.373 1.00 47.33 C
ATOM 352 SD MET A 54 45.023 59.698 164.626 1.00 52.76 S
ATOM 353 CE MET A 54 45.280 57.832 164.552 1.00 50.17 C
ATOM 354 N ALA A 55 39.599 61.108 164.766 1.00 41.37 N
ATOM 355 CA ALA A 55 38.494 61.998 165.132 1.00 42.59 C
ATOM 356 C ALA A 55 37.982 61.656 166.525 1.00 42.41 C
ATOM 357 O ALA A 55 37.547 62.537 167.259 1.00 42.67 O
ATOM 358 CB ALA A 55 37.357 61.884 164.125 1.00 41.90 C
ATOM 359 N ILE A 56 38.022 60.371 166.868 1.00 43.88 N
ATOM 360 CA ILE A 56 37.586 59.880 168.171 1.00 43.52 C
ATOM 361 C ILE A 56 38.606 60.249 169.256 1.00 43.96 C
ATOM 362 O ILE A 56 38.254 60.838 170.277 1.00 45.97 O
ATOM 363 CB ILE A 56 37.407 58.338 168.144 1.00 42.82 C
ATOM 364 CG1 ILE A 56 36.223 57.986 167.246 1.00 42.50 C
ATOM 365 CG2 ILE A 56 37.204 57.779 169.558 1.00 41.58 C
ATOM 366 CD1 ILE A 56 35.909 56.507 167.200 1.00 42.58 C
ATOM 367 N TYR A 57 39.869 59.914 169.049 1.00 43.90 N
ATOM 368 CA TYR A 57 40.879 60.242 170.046 1.00 45.95 C
ATOM 369 C TYR A 57 40.885 61.729 170.417 1.00 46.72 C
ATOM 370 O TYR A 57 41.223 62.105 171.544 1.00 46.70 O
ATOM 371 CB TYR A 57 42.272 59.861 169.541 1.00 44.83 C
ATOM 372 CG TYR A 57 42.577 58.382 169.594 1.00 44.51 C
ATOM 373 CD1 TYR A 57 42.548 57.682 170.802 1.00 44.13 C
ATOM 374 CD2 TYR A 57 42.911 57.682 168.436 1.00 44.56 C
ATOM 375 CE1 TYR A 57 42.846 56.322 170.851 1.00 44.79 C
ATOM 376 CE2 TYR A 57 43.208 56.328 168.477 1.00 43.84 C
ATOM 377 CZ TYR A 57 43.174 55.655 169.682 1.00 43.68 C
ATOM 378 OH TYR A 57 43.472 54.315 169.697 1.00 42.21 O
ATOM 379 N LEU A 58 40.496 62.564 169.466 1.00 46.89 N
ATOM 380 CA LEU A 58 40.496 64.002 169.658 1.00 46.94 C
ATOM 381 C LEU A 58 39.311 64.511 170.451 1.00 48.19 C
ATOM 382 O LEU A 58 39.463 65.403 171.278 1.00 49.42 O
ATOM 383 CB LEU A 58 40.495 64.701 168.296 1.00 46.63 C
ATOM 384 CG LEU A 58 41.045 66.122 168.111 1.00 46.04 C
ATOM 385 CD1 LEU A 58 40.081 66.914 167.218 1.00 42.71 C
ATOM 386 CD2 LEU A 58 41.248 66.799 169.461 1.00 46.59 C
ATOM 387 N THR A 59 38.136 63.942 170.209 1.00 48.70 N
ATOM 388 CA THR A 59 36.921 64.408 170.860 1.00 48.50 C
ATOM 389 C THR A 59 36.286 63.478 171.897 1.00 49.34 C
ATOM 390 O THR A 59 35.357 63.869 172.609 1.00 48.28 O
ATOM 391 CB THR A 59 35.843 64.725 169.787 1.00 47.98 C
ATOM 392 OG1 THR A 59 35.352 63.488 169.232 1.00 48.39 O
ATOM 393 CG2 THR A 59 36.435 65.606 168.656 1.00 45.21 C
ATOM 394 N ALA A 60 36.776 62.253 171.995 1.00 49.11 N
ATOM 395 CA ALA A 60 36.178 61.317 172.935 1.00 50.52 C
ATOM 396 C ALA A 60 36.125 61.849 174.358 1.00 51.35 C
ATOM 397 O ALA A 60 35.080 61.812 175.013 1.00 51.96 O
ATOM 398 CB ALA A 60 36.922 60.001 172.896 1.00 50.39 C
ATOM 399 N GLY A 61 37.257 62.363 174.824 1.00 52.47 N
ATOM 400 CA GLY A 61 37.344 62.883 176.178 1.00 52.00 C
ATOM 401 C GLY A 61 36.397 64.010 176.526 1.00 51.82 C
ATOM 402 O GLY A 61 36.178 64.282 177.706 1.00 54.01 O
ATOM 403 N VAL A 62 35.836 64.665 175.520 1.00 50.89 N
ATOM 404 CA VAL A 62 34.922 65.772 175.750 1.00 49.10 C
ATOM 405 C VAL A 62 33.466 65.407 175.487 1.00 49.74 C
ATOM 406 O VAL A 62 32.694 65.192 176.418 1.00 50.97 O
ATOM 407 CB VAL A 62 35.303 66.955 174.873 1.00 47.27 C
ATOM 408 CG1 VAL A 62 34.380 68.098 175.117 1.00 46.50 C
ATOM 409 CG2 VAL A 62 36.708 67.363 175.177 1.00 46.89 C
ATOM 410 N SER A 63 33.098 65.325 174.213 1.00 50.12 N
ATOM 411 CA SER A 63 31.731 65.008 173.823 1.00 48.80 C
ATOM 412 C SER A 63 31.390 63.539 173.848 1.00 49.18 C
ATOM 413 O SER A 63 30.227 63.191 173.683 1.00 51.26 O
ATOM 414 CB SER A 63 31.460 65.499 172.412 1.00 50.14 C
ATOM 415 OG SER A 63 32.341 64.846 171.507 1.00 53.35 O
ATOM 416 N GLY A 64 32.382 62.669 174.022 1.00 48.52 N
ATOM 417 CA GLY A 64 32.121 61.237 173.989 1.00 47.43 C
ATOM 418 C GLY A 64 32.354 60.717 172.574 1.00 48.18 C
ATOM 419 O GLY A 64 32.279 59.516 172.300 1.00 46.95 O
ATOM 420 N ALA A 65 32.640 61.661 171.677 1.00 49.37 N
ATOM 421 CA ALA A 65 32.912 61.415 170.261 1.00 49.22 C
ATOM 422 C ALA A 65 31.862 60.606 169.489 1.00 48.69 C
ATOM 423 O ALA A 65 32.158 59.508 169.022 1.00 48.51 O
ATOM 424 CB ALA A 65 34.301 60.758 170.103 1.00 47.97 C
ATOM 425 N HIS A 66 30.645 61.138 169.362 1.00 48.17 N
ATOM 426 CA HIS A 66 29.602 60.442 168.596 1.00 46.79 C
ATOM 427 C HIS A 66 29.999 60.603 167.135 1.00 44.02 C
ATOM 428 O HIS A 66 30.167 59.622 166.416 1.00 43.62 O
ATOM 429 CB HIS A 66 28.210 61.065 168.816 1.00 48.02 C
ATOM 430 CG HIS A 66 27.699 60.914 170.215 1.00 50.42 C
ATOM 431 ND1 HIS A 66 26.352 60.897 170.519 1.00 51.15 N
ATOM 432 CD2 HIS A 66 28.354 60.773 171.396 1.00 51.64 C
ATOM 433 CE1 HIS A 66 26.201 60.749 171.826 1.00 51.66 C
ATOM 434 NE2 HIS A 66 27.400 60.671 172.383 1.00 51.69 N
ATOM 435 N LEU A 67 30.155 61.853 166.710 1.00 43.63 N
ATOM 436 CA LEU A 67 30.569 62.152 165.345 1.00 42.77 C
ATOM 437 C LEU A 67 29.695 61.453 164.322 1.00 44.36 C
ATOM 438 O LEU A 67 30.128 61.233 163.191 1.00 44.45 O
ATOM 439 CB LEU A 67 32.013 61.715 165.145 1.00 41.63 C
ATOM 440 CG LEU A 67 32.916 62.092 166.324 1.00 39.49 C
ATOM 441 CD1 LEU A 67 34.260 61.395 166.142 1.00 39.70 C
ATOM 442 CD2 LEU A 67 33.055 63.623 166.436 1.00 37.36 C
ATOM 443 N ASN A 68 28.469 61.108 164.715 1.00 44.62 N
ATOM 444 CA ASN A 68 27.528 60.409 163.840 1.00 45.37 C
ATOM 445 C ASN A 68 26.095 60.544 164.367 1.00 45.58 C
ATOM 446 O ASN A 68 25.778 60.079 165.468 1.00 45.06 O
ATOM 447 CB ASN A 68 27.913 58.914 163.750 1.00 44.81 C
ATOM 448 CG ASN A 68 27.094 58.144 162.704 1.00 44.84 C
ATOM 449 OD1 ASN A 68 25.909 58.411 162.516 1.00 46.09 O
ATOM 450 ND2 ASN A 68 27.722 57.171 162.041 1.00 42.59 N
ATOM 451 N PRO A 69 25.213 61.197 163.589 1.00 45.87 N
ATOM 452 CA PRO A 69 23.819 61.370 164.003 1.00 44.79 C
ATOM 453 C PRO A 69 23.181 60.025 164.350 1.00 46.26 C
ATOM 454 O PRO A 69 22.532 59.895 165.380 1.00 46.27 O
ATOM 455 CB PRO A 69 23.173 62.013 162.782 1.00 43.86 C
ATOM 456 CG PRO A 69 24.280 62.811 162.199 1.00 44.35 C
ATOM 457 CD PRO A 69 25.465 61.876 162.310 1.00 44.67 C
ATOM 458 N ALA A 70 23.364 59.026 163.482 1.00 46.88 N
ATOM 459 CA ALA A 70 22.803 57.692 163.705 1.00 47.63 C
ATOM 460 C ALA A 70 23.258 57.136 165.055 1.00 48.91 C
ATOM 461 O ALA A 70 22.476 56.537 165.795 1.00 49.20 O
ATOM 462 CB ALA A 70 23.215 56.758 162.582 1.00 46.26 C
ATOM 463 N VAL A 71 24.529 57.337 165.374 1.00 50.04 N
ATOM 464 CA VAL A 71 25.072 56.895 166.651 1.00 51.32 C
ATOM 465 C VAL A 71 24.453 57.667 167.833 1.00 51.94 C
ATOM 466 O VAL A 71 24.083 57.064 168.845 1.00 52.91 O
ATOM 467 CB VAL A 71 26.595 57.092 166.682 1.00 51.51 C
ATOM 468 CG1 VAL A 71 27.138 56.790 168.073 1.00 50.96 C
ATOM 469 CG2 VAL A 71 27.240 56.201 165.634 1.00 51.94 C
ATOM 470 N THR A 72 24.350 58.993 167.697 1.00 52.28 N
ATOM 471 CA THR A 72 23.794 59.848 168.753 1.00 51.70 C
ATOM 472 C THR A 72 22.384 59.409 169.120 1.00 51.49 C
ATOM 473 O THR A 72 22.065 59.255 170.296 1.00 51.32 O
ATOM 474 CB THR A 72 23.752 61.338 168.329 1.00 51.72 C
ATOM 475 OG1 THR A 72 25.085 61.810 168.087 1.00 52.83 O
ATOM 476 CG2 THR A 72 23.123 62.183 169.428 1.00 50.39 C
ATOM 477 N ILE A 73 21.552 59.213 168.100 1.00 51.36 N
ATOM 478 CA ILE A 73 20.178 58.767 168.280 1.00 51.43 C
ATOM 479 C ILE A 73 20.150 57.391 168.963 1.00 53.38 C
ATOM 480 O ILE A 73 19.418 57.187 169.931 1.00 55.46 O
ATOM 481 CB ILE A 73 19.449 58.664 166.915 1.00 49.89 C
ATOM 482 CG1 ILE A 73 19.334 60.055 166.280 1.00 48.25 C
ATOM 483 CG2 ILE A 73 18.086 58.013 167.088 1.00 49.00 C
ATOM 484 CD1 ILE A 73 18.727 60.032 164.897 1.00 46.16 C
ATOM 485 N ALA A 74 20.946 56.448 168.466 1.00 54.41 N
ATOM 486 CA ALA A 74 20.988 55.114 169.059 1.00 53.89 C
ATOM 487 C ALA A 74 21.405 55.157 170.541 1.00 54.67 C
ATOM 488 O ALA A 74 20.801 54.481 171.371 1.00 55.46 O
ATOM 489 CB ALA A 74 21.929 54.221 168.269 1.00 54.26 C
ATOM 490 N LEU A 75 22.427 55.942 170.877 1.00 54.43 N
ATOM 491 CA LEU A 75 22.870 56.058 172.267 1.00 54.56 C
ATOM 492 C LEU A 75 21.766 56.694 173.125 1.00 56.23 C
ATOM 493 O LEU A 75 21.614 56.403 174.314 1.00 55.32 O
ATOM 494 CB LEU A 75 24.141 56.910 172.347 1.00 52.26 C
ATOM 495 CG LEU A 75 25.378 56.353 171.642 1.00 50.11 C
ATOM 496 CD1 LEU A 75 26.555 57.282 171.879 1.00 50.30 C
ATOM 497 CD2 LEU A 75 25.676 54.963 172.172 1.00 49.18 C
ATOM 498 N TRP A 76 20.994 57.574 172.512 1.00 57.45 N
ATOM 499 CA TRP A 76 19.902 58.215 173.216 1.00 59.25 C
ATOM 500 C TRP A 76 18.832 57.183 173.583 1.00 60.08 C
ATOM 501 O TRP A 76 18.343 57.148 174.710 1.00 62.20 O
ATOM 502 CB TRP A 76 19.308 59.313 172.331 1.00 59.42 C
ATOM 503 CG TRP A 76 17.925 59.751 172.699 1.00 59.64 C
ATOM 504 CD1 TRP A 76 17.500 60.203 173.915 1.00 59.03 C
ATOM 505 CD2 TRP A 76 16.783 59.798 171.831 1.00 59.71 C
ATOM 506 NE1 TRP A 76 16.167 60.530 173.856 1.00 58.83 N
ATOM 507 CE2 TRP A 76 15.703 60.297 172.592 1.00 58.49 C
ATOM 508 CE3 TRP A 76 16.572 59.479 170.481 1.00 59.99 C
ATOM 509 CZ2 TRP A 76 14.425 60.470 172.053 1.00 58.07 C
ATOM 510 CZ3 TRP A 76 15.297 59.653 169.944 1.00 59.36 C
ATOM 511 CH2 TRP A 76 14.243 60.148 170.734 1.00 59.28 C
ATOM 512 N LEU A 77 18.483 56.335 172.631 1.00 59.56 N
ATOM 513 CA LEU A 77 17.478 55.318 172.854 1.00 58.57 C
ATOM 514 C LEU A 77 17.983 54.052 173.559 1.00 60.06 C
ATOM 515 O LEU A 77 17.179 53.255 174.031 1.00 61.58 O
ATOM 516 CB LEU A 77 16.866 54.925 171.516 1.00 55.36 C
ATOM 517 CG LEU A 77 16.288 56.047 170.670 1.00 53.83 C
ATOM 518 CD1 LEU A 77 15.881 55.517 169.324 1.00 52.06 C
ATOM 519 CD2 LEU A 77 15.092 56.617 171.367 1.00 53.98 C
ATOM 520 N PHE A 78 19.295 53.845 173.631 1.00 60.92 N
ATOM 521 CA PHE A 78 19.791 52.626 174.269 1.00 61.14 C
ATOM 522 C PHE A 78 20.970 52.803 175.214 1.00 62.18 C
ATOM 523 O PHE A 78 21.361 51.850 175.885 1.00 64.00 O
ATOM 524 CB PHE A 78 20.190 51.574 173.219 1.00 58.58 C
ATOM 525 CG PHE A 78 19.102 51.235 172.243 1.00 56.65 C
ATOM 526 CD1 PHE A 78 18.915 51.998 171.098 1.00 56.37 C
ATOM 527 CD2 PHE A 78 18.255 50.160 172.481 1.00 56.22 C
ATOM 528 CE1 PHE A 78 17.896 51.691 170.205 1.00 57.02 C
ATOM 529 CE2 PHE A 78 17.235 49.845 171.598 1.00 56.00 C
ATOM 530 CZ PHE A 78 17.054 50.610 170.459 1.00 57.11 C
ATOM 531 N ALA A 79 21.553 53.991 175.272 1.00 62.85 N
ATOM 532 CA ALA A 79 22.695 54.201 176.156 1.00 63.49 C