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5fs4.pdb
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5fs4.pdb
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HEADER VIRAL PROTEIN 29-DEC-15 5FS4
TITLE BACTERIOPHAGE AP205 COAT PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AP205 BACTERIOPHAGE COAT PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER PHAGE AP205;
SOURCE 3 ORGANISM_TAXID: 154784;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSF-TEVDUET
KEYWDS VIRAL PROTEIN, SMALL RNA PHAGE, COAT PROTEIN, AP205
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHISHOVS,K.TARS
REVDAT 3 17-JAN-18 5FS4 1 REMARK
REVDAT 2 09-NOV-16 5FS4 1 JRNL
REVDAT 1 21-SEP-16 5FS4 0
JRNL AUTH M.SHISHOVS,J.RUMNIEKS,C.DIEBOLDER,K.JAUDZEMS,L.B.ANDREAS,
JRNL AUTH 2 J.STANEK,A.KAZAKS,S.KOTELOVICA,I.AKOPJANA,G.PINTACUDA,
JRNL AUTH 3 R.I.KONING,K.TARS
JRNL TITL STRUCTURE OF AP205 COAT PROTEIN REVEALS CIRCULAR PERMUTATION
JRNL TITL 2 IN SSRNA BACTERIOPHAGES.
JRNL REF J.MOL.BIOL. V. 428 4267 2016
JRNL REFN ISSN 0022-2836
JRNL PMID 27591890
JRNL DOI 10.1016/J.JMB.2016.08.025
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1416
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2009
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.87000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.133
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.263
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.891
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.822
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1866 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1780 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2537 ; 1.832 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4094 ; 0.982 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 240 ; 6.907 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;38.645 ;24.521
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 305 ;11.965 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.107 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 301 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2113 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 403 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 975 ; 1.408 ; 1.343
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 974 ; 1.352 ; 1.340
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1210 ; 2.272 ; 1.993
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 891 ; 1.528 ; 1.474
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U
REMARK 3 VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5FS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1290065906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28660
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 57.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.63000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: BUCCANEER
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % ETHYLENE GLYCOL AQUEOUS SOLUTION,
REMARK 280 7 MG/ML PROTEIN IN 40 MM TRIS-HCL PH 8,0, 300 MM NACL, VAPOR
REMARK 280 DIFFUSION SITTING DROP METHOR, 0.7 MIKROL PRECIPITANT PLUS 1
REMARK 280 MIKROL PROTEIN,TEMPERATURE 294 K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 57.46500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 ILE A 40
REMARK 465 ALA A 41
REMARK 465 LYS A 60
REMARK 465 PRO A 61
REMARK 465 GLU A 62
REMARK 465 GLY A 63
REMARK 465 GLY A 64
REMARK 465 ALA A 65
REMARK 465 ASP A 66
REMARK 465 ALA A 67
REMARK 465 GLY A 68
REMARK 465 VAL A 69
REMARK 465 ILE A 70
REMARK 465 ALA A 130
REMARK 465 LYS B 37
REMARK 465 VAL B 38
REMARK 465 GLY B 39
REMARK 465 ILE B 40
REMARK 465 ALA B 41
REMARK 465 ALA B 130
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 GLU A 42 CG CD OE1 OE2
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 OG SER A -1 O ASP B 66 2657 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 19 CB - CG - OD1 ANGL. DEV. = 5.8 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 ARG A 22 81.73 -152.01
REMARK 500 ARG B 22 81.95 -159.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2036 DISTANCE = 6.01 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL SERINE AS A RESULT OF RECOMBINANT CONSTRUCT
REMARK 999 INSERTION IN A PLASMID
DBREF 5FS4 A 0 130 UNP Q9AZ42 Q9AZ42_9VIRU 1 131
DBREF 5FS4 B 0 130 UNP Q9AZ42 Q9AZ42_9VIRU 1 131
SEQADV 5FS4 GLY A -2 UNP Q9AZ42 EXPRESSION TAG
SEQADV 5FS4 SER A -1 UNP Q9AZ42 EXPRESSION TAG
SEQADV 5FS4 GLY A 64 UNP Q9AZ42 CYS 65 ENGINEERED MUTATION
SEQADV 5FS4 GLY A 68 UNP Q9AZ42 CYS 69 ENGINEERED MUTATION
SEQADV 5FS4 GLY B -2 UNP Q9AZ42 EXPRESSION TAG
SEQADV 5FS4 SER B -1 UNP Q9AZ42 EXPRESSION TAG
SEQADV 5FS4 GLY B 64 UNP Q9AZ42 CYS 65 ENGINEERED MUTATION
SEQADV 5FS4 GLY B 68 UNP Q9AZ42 CYS 69 ENGINEERED MUTATION
SEQRES 1 A 133 GLY SER MET ALA ASN LYS PRO MET GLN PRO ILE THR SER
SEQRES 2 A 133 THR ALA ASN LYS ILE VAL TRP SER ASP PRO THR ARG LEU
SEQRES 3 A 133 SER THR THR PHE SER ALA SER LEU LEU ARG GLN ARG VAL
SEQRES 4 A 133 LYS VAL GLY ILE ALA GLU LEU ASN ASN VAL SER GLY GLN
SEQRES 5 A 133 TYR VAL SER VAL TYR LYS ARG PRO ALA PRO LYS PRO GLU
SEQRES 6 A 133 GLY GLY ALA ASP ALA GLY VAL ILE MET PRO ASN GLU ASN
SEQRES 7 A 133 GLN SER ILE ARG THR VAL ILE SER GLY SER ALA GLU ASN
SEQRES 8 A 133 LEU ALA THR LEU LYS ALA GLU TRP GLU THR HIS LYS ARG
SEQRES 9 A 133 ASN VAL ASP THR LEU PHE ALA SER GLY ASN ALA GLY LEU
SEQRES 10 A 133 GLY PHE LEU ASP PRO THR ALA ALA ILE VAL SER SER ASP
SEQRES 11 A 133 THR THR ALA
SEQRES 1 B 133 GLY SER MET ALA ASN LYS PRO MET GLN PRO ILE THR SER
SEQRES 2 B 133 THR ALA ASN LYS ILE VAL TRP SER ASP PRO THR ARG LEU
SEQRES 3 B 133 SER THR THR PHE SER ALA SER LEU LEU ARG GLN ARG VAL
SEQRES 4 B 133 LYS VAL GLY ILE ALA GLU LEU ASN ASN VAL SER GLY GLN
SEQRES 5 B 133 TYR VAL SER VAL TYR LYS ARG PRO ALA PRO LYS PRO GLU
SEQRES 6 B 133 GLY GLY ALA ASP ALA GLY VAL ILE MET PRO ASN GLU ASN
SEQRES 7 B 133 GLN SER ILE ARG THR VAL ILE SER GLY SER ALA GLU ASN
SEQRES 8 B 133 LEU ALA THR LEU LYS ALA GLU TRP GLU THR HIS LYS ARG
SEQRES 9 B 133 ASN VAL ASP THR LEU PHE ALA SER GLY ASN ALA GLY LEU
SEQRES 10 B 133 GLY PHE LEU ASP PRO THR ALA ALA ILE VAL SER SER ASP
SEQRES 11 B 133 THR THR ALA
FORMUL 3 HOH *208(H2 O)
HELIX 1 1 ASN A 88 PHE A 107 1 20
HELIX 2 2 ASN A 111 GLY A 115 5 5
HELIX 3 3 ASN B 88 ALA B 108 1 21
HELIX 4 4 ASN B 111 GLY B 115 5 5
SHEET 1 AA 2 ASN A 2 PRO A 4 0
SHEET 2 AA 2 VAL B 124 THR B 128 -1 N SER B 125 O LYS A 3
SHEET 1 AB10 GLN A 6 THR A 11 0
SHEET 2 AB10 LYS A 14 ASP A 19 -1 O LYS A 14 N THR A 11
SHEET 3 AB10 ARG A 22 VAL A 36 -1 N ARG A 22 O ASP A 19
SHEET 4 AB10 LEU A 43 PRO A 57 -1 O LEU A 43 N VAL A 36
SHEET 5 AB10 ASN A 73 SER A 85 -1 O GLU A 74 N ARG A 56
SHEET 6 AB10 ASN B 73 SER B 85 -1 O SER B 77 N SER A 83
SHEET 7 AB10 ASN B 44 PRO B 57 -1 O VAL B 46 N GLY B 84
SHEET 8 AB10 ARG B 22 ARG B 35 -1 O THR B 26 N VAL B 53
SHEET 9 AB10 LYS B 14 ASP B 19 -1 O ILE B 15 N ALA B 29
SHEET 10 AB10 GLN B 6 THR B 11 -1 O GLN B 6 N SER B 18
SHEET 1 AC 2 VAL A 124 THR A 128 0
SHEET 2 AC 2 ASN B 2 PRO B 4 -1 O LYS B 3 N SER A 125
CRYST1 28.600 114.930 42.800 90.00 98.14 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.034965 0.000000 0.005001 0.00000
SCALE2 0.000000 0.008701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023602 0.00000
MTRIX1 1 0.875400 0.402600 0.267700 -23.01000 1
MTRIX2 1 0.402800 -0.913500 0.056790 62.91000 1
MTRIX3 1 0.267400 0.058110 -0.961800 66.86000 1
ATOM 1 N SER A -1 12.235 52.824 39.664 1.00 43.38 N
ATOM 2 CA SER A -1 10.972 53.424 39.199 1.00 47.25 C
ATOM 3 C SER A -1 9.840 53.083 40.169 1.00 50.25 C
ATOM 4 O SER A -1 10.076 52.469 41.217 1.00 55.69 O
ATOM 5 CB SER A -1 10.656 52.921 37.801 1.00 51.75 C
ATOM 6 OG SER A -1 11.846 52.832 37.046 1.00 59.85 O
ATOM 7 N MET A 0 8.611 53.441 39.814 1.00 46.94 N
ATOM 8 CA MET A 0 7.532 53.470 40.795 1.00 46.14 C
ATOM 9 C MET A 0 6.886 52.104 41.125 1.00 40.19 C
ATOM 10 O MET A 0 6.728 51.214 40.258 1.00 41.76 O
ATOM 11 CB MET A 0 6.467 54.489 40.352 1.00 50.35 C
ATOM 12 CG MET A 0 7.010 55.901 40.166 1.00 54.61 C
ATOM 13 SD MET A 0 7.813 56.558 41.651 1.00 60.01 S
ATOM 14 CE MET A 0 6.458 57.494 42.380 1.00 60.57 C
ATOM 15 N ALA A 1 6.532 51.955 42.400 1.00 31.99 N
ATOM 16 CA ALA A 1 5.634 50.889 42.854 1.00 26.79 C
ATOM 17 C ALA A 1 4.232 50.970 42.274 1.00 22.54 C
ATOM 18 O ALA A 1 3.653 52.051 41.975 1.00 20.79 O
ATOM 19 CB ALA A 1 5.493 50.881 44.364 1.00 26.30 C
ATOM 20 N ASN A 2 3.655 49.790 42.208 1.00 18.96 N
ATOM 21 CA ASN A 2 2.330 49.628 41.676 1.00 17.95 C
ATOM 22 C ASN A 2 1.381 50.139 42.765 1.00 15.94 C
ATOM 23 O ASN A 2 1.674 49.993 43.972 1.00 15.24 O
ATOM 24 CB ASN A 2 2.117 48.152 41.367 1.00 17.01 C
ATOM 25 CG ASN A 2 2.841 47.729 40.124 1.00 17.39 C
ATOM 26 OD1 ASN A 2 2.283 47.815 39.019 1.00 16.08 O
ATOM 27 ND2 ASN A 2 4.093 47.341 40.265 1.00 16.47 N
ATOM 28 N LYS A 3 0.257 50.707 42.340 1.00 16.21 N
ATOM 29 CA LYS A 3 -0.709 51.313 43.275 1.00 16.47 C
ATOM 30 C LYS A 3 -1.361 50.225 44.129 1.00 14.93 C
ATOM 31 O LYS A 3 -1.798 49.213 43.582 1.00 13.79 O
ATOM 32 CB LYS A 3 -1.777 52.123 42.538 1.00 16.92 C
ATOM 33 CG LYS A 3 -1.233 53.321 41.760 1.00 17.57 C
ATOM 34 CD LYS A 3 -2.319 54.123 41.076 1.00 18.43 C
ATOM 35 CE LYS A 3 -3.386 54.776 41.948 1.00 19.84 C
ATOM 36 NZ LYS A 3 -4.616 55.125 41.147 1.00 21.56 N
ATOM 37 N PRO A 4 -1.446 50.420 45.456 1.00 13.50 N
ATOM 38 CA PRO A 4 -2.070 49.383 46.322 1.00 13.40 C
ATOM 39 C PRO A 4 -3.560 49.434 46.196 1.00 13.28 C
ATOM 40 O PRO A 4 -4.145 50.511 45.977 1.00 13.60 O
ATOM 41 CB PRO A 4 -1.667 49.787 47.741 1.00 14.00 C
ATOM 42 CG PRO A 4 -1.422 51.249 47.672 1.00 14.67 C
ATOM 43 CD PRO A 4 -0.969 51.572 46.251 1.00 14.17 C
ATOM 44 N MET A 5 -4.169 48.263 46.287 1.00 11.25 N
ATOM 45 CA MET A 5 -5.611 48.144 46.249 1.00 10.88 C
ATOM 46 C MET A 5 -6.095 47.706 47.611 1.00 11.88 C
ATOM 47 O MET A 5 -5.399 46.988 48.328 1.00 12.20 O
ATOM 48 CB MET A 5 -6.015 47.140 45.134 1.00 9.48 C
ATOM 49 CG MET A 5 -5.624 47.638 43.726 1.00 8.66 C
ATOM 50 SD MET A 5 -5.721 46.488 42.325 1.00 5.83 S
ATOM 51 CE MET A 5 -7.476 46.403 42.320 1.00 6.88 C
ATOM 52 N GLN A 6 -7.300 48.129 47.961 1.00 13.99 N
ATOM 53 CA GLN A 6 -7.851 47.878 49.292 1.00 16.31 C
ATOM 54 C GLN A 6 -9.078 46.968 49.208 1.00 15.96 C
ATOM 55 O GLN A 6 -9.870 47.158 48.305 1.00 12.95 O
ATOM 56 CB GLN A 6 -8.273 49.222 49.914 1.00 18.58 C
ATOM 57 CG GLN A 6 -7.147 50.266 50.061 1.00 21.31 C
ATOM 58 CD GLN A 6 -5.980 49.872 50.966 1.00 24.03 C
ATOM 59 OE1 GLN A 6 -4.834 50.288 50.755 1.00 25.53 O
ATOM 60 NE2 GLN A 6 -6.262 49.062 51.981 1.00 27.79 N
ATOM 61 N PRO A 7 -9.261 46.030 50.159 1.00 17.30 N
ATOM 62 CA PRO A 7 -10.458 45.213 50.143 1.00 19.83 C
ATOM 63 C PRO A 7 -11.717 46.043 50.463 1.00 25.43 C
ATOM 64 O PRO A 7 -11.756 46.734 51.472 1.00 27.38 O
ATOM 65 CB PRO A 7 -10.218 44.151 51.215 1.00 20.48 C
ATOM 66 CG PRO A 7 -8.919 44.493 51.857 1.00 19.90 C
ATOM 67 CD PRO A 7 -8.507 45.849 51.392 1.00 18.89 C
ATOM 68 N ILE A 8 -12.696 45.999 49.565 1.00 25.22 N
ATOM 69 CA ILE A 8 -13.904 46.810 49.630 1.00 25.27 C
ATOM 70 C ILE A 8 -15.126 45.967 50.001 1.00 25.92 C
ATOM 71 O ILE A 8 -16.009 46.451 50.681 1.00 27.08 O
ATOM 72 CB ILE A 8 -14.099 47.629 48.311 1.00 27.00 C
ATOM 73 CG1 ILE A 8 -14.256 46.745 47.034 1.00 26.56 C
ATOM 74 CG2 ILE A 8 -12.882 48.540 48.086 1.00 27.10 C
ATOM 75 CD1 ILE A 8 -15.686 46.510 46.586 1.00 26.14 C
ATOM 76 N THR A 9 -15.170 44.720 49.566 1.00 26.47 N
ATOM 77 CA THR A 9 -16.106 43.706 50.099 1.00 31.64 C
ATOM 78 C THR A 9 -15.194 42.587 50.587 1.00 30.89 C
ATOM 79 O THR A 9 -14.216 42.302 49.884 1.00 19.89 O
ATOM 80 CB THR A 9 -17.039 43.030 49.045 1.00 35.55 C
ATOM 81 OG1 THR A 9 -17.500 43.966 48.066 1.00 37.51 O
ATOM 82 CG2 THR A 9 -18.242 42.376 49.761 1.00 39.13 C
ATOM 83 N SER A 10 -15.563 41.973 51.731 1.00 32.73 N
ATOM 84 CA SER A 10 -14.778 40.948 52.457 1.00 36.68 C
ATOM 85 C SER A 10 -15.638 39.909 53.140 1.00 39.29 C
ATOM 86 O SER A 10 -16.084 40.130 54.278 1.00 39.13 O
ATOM 87 CB SER A 10 -13.933 41.566 53.571 1.00 36.33 C
ATOM 88 OG SER A 10 -12.759 42.138 53.048 1.00 37.89 O
ATOM 89 N THR A 11 -15.818 38.769 52.469 1.00 40.26 N
ATOM 90 CA THR A 11 -16.543 37.588 53.007 1.00 39.11 C
ATOM 91 C THR A 11 -15.569 36.415 53.160 1.00 37.05 C
ATOM 92 O THR A 11 -14.533 36.385 52.476 1.00 36.53 O
ATOM 93 CB THR A 11 -17.696 37.233 52.060 1.00 39.08 C
ATOM 94 OG1 THR A 11 -18.501 38.412 51.898 1.00 44.45 O
ATOM 95 CG2 THR A 11 -18.554 36.082 52.593 1.00 39.76 C
ATOM 96 N ALA A 12 -15.869 35.449 54.039 1.00 31.70 N
ATOM 97 CA ALA A 12 -15.007 34.235 54.189 1.00 28.99 C
ATOM 98 C ALA A 12 -14.442 33.714 52.875 1.00 28.01 C
ATOM 99 O ALA A 12 -13.249 33.373 52.778 1.00 28.53 O
ATOM 100 CB ALA A 12 -15.778 33.108 54.854 1.00 28.36 C
ATOM 101 N ASN A 13 -15.338 33.633 51.884 1.00 25.07 N
ATOM 102 CA ASN A 13 -15.074 32.984 50.615 1.00 24.10 C
ATOM 103 C ASN A 13 -14.781 33.891 49.465 1.00 18.35 C
ATOM 104 O ASN A 13 -14.402 33.389 48.416 1.00 16.69 O
ATOM 105 CB ASN A 13 -16.252 32.102 50.255 1.00 27.69 C
ATOM 106 CG ASN A 13 -16.394 30.944 51.225 1.00 34.00 C
ATOM 107 OD1 ASN A 13 -15.444 30.168 51.409 1.00 36.29 O
ATOM 108 ND2 ASN A 13 -17.560 30.833 51.878 1.00 37.23 N
ATOM 109 N LYS A 14 -14.937 35.198 49.620 1.00 14.75 N
ATOM 110 CA LYS A 14 -14.714 36.071 48.468 1.00 12.69 C
ATOM 111 C LYS A 14 -14.343 37.485 48.903 1.00 11.47 C
ATOM 112 O LYS A 14 -15.041 38.098 49.704 1.00 9.28 O
ATOM 113 CB LYS A 14 -15.955 36.110 47.627 1.00 13.43 C
ATOM 114 CG LYS A 14 -15.861 37.139 46.521 1.00 14.34 C
ATOM 115 CD LYS A 14 -16.808 36.955 45.373 1.00 15.91 C
ATOM 116 CE LYS A 14 -16.405 37.912 44.241 1.00 17.25 C
ATOM 117 NZ LYS A 14 -17.518 38.197 43.294 1.00 19.14 N
ATOM 118 N ILE A 15 -13.239 37.981 48.377 1.00 9.34 N
ATOM 119 CA ILE A 15 -12.845 39.370 48.627 1.00 8.84 C
ATOM 120 C ILE A 15 -12.699 40.102 47.298 1.00 8.71 C
ATOM 121 O ILE A 15 -12.198 39.525 46.347 1.00 8.63 O
ATOM 122 CB ILE A 15 -11.507 39.362 49.347 1.00 9.12 C
ATOM 123 CG1 ILE A 15 -11.672 38.667 50.728 1.00 9.49 C
ATOM 124 CG2 ILE A 15 -10.966 40.775 49.547 1.00 9.01 C
ATOM 125 CD1 ILE A 15 -10.446 38.623 51.562 1.00 9.83 C
ATOM 126 N VAL A 16 -13.103 41.374 47.283 1.00 9.23 N
ATOM 127 CA VAL A 16 -12.950 42.247 46.114 1.00 9.48 C
ATOM 128 C VAL A 16 -12.037 43.368 46.588 1.00 9.46 C
ATOM 129 O VAL A 16 -12.336 44.042 47.563 1.00 9.48 O
ATOM 130 CB VAL A 16 -14.325 42.778 45.603 1.00 10.11 C
ATOM 131 CG1 VAL A 16 -14.154 43.818 44.473 1.00 9.70 C
ATOM 132 CG2 VAL A 16 -15.265 41.645 45.192 1.00 10.31 C
ATOM 133 N TRP A 17 -10.882 43.514 45.944 1.00 9.15 N
ATOM 134 CA TRP A 17 -9.995 44.636 46.143 1.00 9.88 C
ATOM 135 C TRP A 17 -10.293 45.660 45.026 1.00 10.41 C
ATOM 136 O TRP A 17 -10.618 45.258 43.927 1.00 10.06 O
ATOM 137 CB TRP A 17 -8.544 44.151 45.990 1.00 9.68 C
ATOM 138 CG TRP A 17 -7.972 43.432 47.146 1.00 9.98 C
ATOM 139 CD1 TRP A 17 -7.229 43.982 48.159 1.00 10.51 C
ATOM 140 CD2 TRP A 17 -8.040 42.028 47.419 1.00 10.72 C
ATOM 141 NE1 TRP A 17 -6.816 42.996 49.047 1.00 10.99 N
ATOM 142 CE2 TRP A 17 -7.314 41.795 48.632 1.00 10.74 C
ATOM 143 CE3 TRP A 17 -8.629 40.936 46.771 1.00 11.11 C
ATOM 144 CZ2 TRP A 17 -7.175 40.513 49.191 1.00 11.27 C
ATOM 145 CZ3 TRP A 17 -8.493 39.672 47.328 1.00 11.28 C
ATOM 146 CH2 TRP A 17 -7.773 39.470 48.536 1.00 11.75 C
ATOM 147 N SER A 18 -10.235 46.964 45.327 1.00 10.32 N
ATOM 148 CA SER A 18 -10.237 47.986 44.331 1.00 11.56 C
ATOM 149 C SER A 18 -9.209 49.054 44.646 1.00 11.53 C
ATOM 150 O SER A 18 -8.827 49.212 45.777 1.00 10.84 O
ATOM 151 CB SER A 18 -11.612 48.621 44.211 1.00 12.49 C
ATOM 152 OG SER A 18 -11.903 49.363 45.367 1.00 14.52 O
ATOM 153 N ASP A 19 -8.733 49.729 43.582 1.00 13.24 N
ATOM 154 CA ASP A 19 -7.919 50.932 43.680 1.00 12.05 C
ATOM 155 C ASP A 19 -8.760 52.065 44.276 1.00 11.93 C
ATOM 156 O ASP A 19 -9.709 52.527 43.650 1.00 9.98 O
ATOM 157 CB ASP A 19 -7.418 51.290 42.282 1.00 11.55 C
ATOM 158 CG ASP A 19 -6.453 52.443 42.260 1.00 11.76 C
ATOM 159 OD1 ASP A 19 -6.338 53.161 43.275 1.00 12.26 O
ATOM 160 OD2 ASP A 19 -5.860 52.654 41.204 1.00 12.27 O
ATOM 161 N PRO A 20 -8.423 52.519 45.487 1.00 12.01 N
ATOM 162 CA PRO A 20 -9.250 53.602 46.069 1.00 13.44 C
ATOM 163 C PRO A 20 -9.261 54.926 45.293 1.00 14.70 C
ATOM 164 O PRO A 20 -10.116 55.781 45.508 1.00 15.66 O
ATOM 165 CB PRO A 20 -8.687 53.786 47.481 1.00 13.55 C
ATOM 166 CG PRO A 20 -7.395 53.038 47.532 1.00 12.78 C
ATOM 167 CD PRO A 20 -7.282 52.141 46.332 1.00 12.93 C
ATOM 168 N THR A 21 -8.336 55.118 44.395 1.00 14.11 N
ATOM 169 CA THR A 21 -8.429 56.304 43.536 1.00 14.27 C
ATOM 170 C THR A 21 -8.772 55.981 42.096 1.00 13.42 C
ATOM 171 O THR A 21 -8.680 56.853 41.263 1.00 12.95 O
ATOM 172 CB THR A 21 -7.108 57.125 43.572 1.00 14.96 C
ATOM 173 OG1 THR A 21 -6.000 56.348 43.106 1.00 16.85 O
ATOM 174 CG2 THR A 21 -6.831 57.636 45.000 1.00 15.71 C
ATOM 175 N ARG A 22 -9.127 54.727 41.793 1.00 12.59 N
ATOM 176 CA ARG A 22 -9.730 54.399 40.491 1.00 12.08 C
ATOM 177 C ARG A 22 -10.613 53.178 40.709 1.00 11.73 C
ATOM 178 O ARG A 22 -10.229 52.021 40.431 1.00 13.52 O
ATOM 179 CB ARG A 22 -8.668 54.200 39.400 1.00 11.44 C
ATOM 180 CG ARG A 22 -9.228 54.172 37.990 1.00 12.20 C
ATOM 181 CD ARG A 22 -8.189 53.752 36.974 1.00 12.61 C
ATOM 182 NE ARG A 22 -8.760 53.664 35.624 1.00 12.93 N
ATOM 183 CZ ARG A 22 -8.857 54.690 34.775 1.00 13.60 C
ATOM 184 NH1 ARG A 22 -8.456 55.932 35.126 1.00 13.26 N
ATOM 185 NH2 ARG A 22 -9.370 54.491 33.570 1.00 14.06 N
ATOM 186 N LEU A 23 -11.808 53.454 41.203 1.00 12.02 N
ATOM 187 CA LEU A 23 -12.654 52.436 41.796 1.00 11.84 C
ATOM 188 C LEU A 23 -13.144 51.401 40.795 1.00 10.67 C
ATOM 189 O LEU A 23 -13.488 50.294 41.206 1.00 10.23 O
ATOM 190 CB LEU A 23 -13.835 53.068 42.539 1.00 12.53 C
ATOM 191 CG LEU A 23 -13.341 53.904 43.740 1.00 13.84 C
ATOM 192 CD1 LEU A 23 -14.355 54.957 44.085 1.00 15.32 C
ATOM 193 CD2 LEU A 23 -13.011 53.041 44.946 1.00 13.92 C
ATOM 194 N SER A 24 -13.078 51.682 39.493 1.00 9.97 N
ATOM 195 CA SER A 24 -13.355 50.673 38.474 1.00 9.41 C
ATOM 196 C SER A 24 -12.255 49.588 38.348 1.00 9.54 C
ATOM 197 O SER A 24 -12.494 48.516 37.730 1.00 9.24 O
ATOM 198 CB SER A 24 -13.591 51.359 37.095 1.00 9.18 C
ATOM 199 OG SER A 24 -12.401 52.005 36.603 1.00 9.03 O
ATOM 200 N THR A 25 -11.053 49.835 38.900 1.00 9.32 N
ATOM 201 CA THR A 25 -9.977 48.865 38.861 1.00 9.01 C
ATOM 202 C THR A 25 -10.209 47.855 39.977 1.00 9.20 C
ATOM 203 O THR A 25 -10.241 48.217 41.155 1.00 8.84 O
ATOM 204 CB THR A 25 -8.586 49.515 38.960 1.00 8.94 C
ATOM 205 OG1 THR A 25 -8.327 50.362 37.828 1.00 9.11 O
ATOM 206 CG2 THR A 25 -7.528 48.415 38.970 1.00 8.69 C
ATOM 207 N THR A 26 -10.429 46.582 39.618 1.00 9.11 N
ATOM 208 CA THR A 26 -10.794 45.598 40.646 1.00 9.26 C
ATOM 209 C THR A 26 -10.036 44.318 40.441 1.00 9.26 C
ATOM 210 O THR A 26 -9.672 43.999 39.327 1.00 9.37 O
ATOM 211 CB THR A 26 -12.320 45.283 40.765 1.00 9.46 C
ATOM 212 OG1 THR A 26 -12.853 44.652 39.562 1.00 9.56 O
ATOM 213 CG2 THR A 26 -13.083 46.571 41.104 1.00 9.78 C
ATOM 214 N PHE A 27 -9.760 43.665 41.566 1.00 8.64 N
ATOM 215 CA PHE A 27 -9.288 42.272 41.574 1.00 8.57 C
ATOM 216 C PHE A 27 -10.062 41.526 42.614 1.00 8.58 C
ATOM 217 O PHE A 27 -10.092 41.925 43.770 1.00 8.13 O
ATOM 218 CB PHE A 27 -7.795 42.194 41.886 1.00 8.28 C
ATOM 219 CG PHE A 27 -7.249 40.790 41.950 1.00 8.59 C
ATOM 220 CD1 PHE A 27 -6.936 40.117 40.806 1.00 8.12 C
ATOM 221 CD2 PHE A 27 -6.980 40.167 43.213 1.00 8.27 C
ATOM 222 CE1 PHE A 27 -6.363 38.853 40.869 1.00 8.01 C
ATOM 223 CE2 PHE A 27 -6.457 38.866 43.258 1.00 8.45 C
ATOM 224 CZ PHE A 27 -6.162 38.228 42.083 1.00 8.33 C
ATOM 225 N SER A 28 -10.668 40.410 42.233 1.00 8.89 N
ATOM 226 CA SER A 28 -11.462 39.674 43.186 1.00 9.86 C
ATOM 227 C SER A 28 -11.016 38.213 43.261 1.00 9.84 C
ATOM 228 O SER A 28 -10.580 37.630 42.241 1.00 10.27 O
ATOM 229 CB SER A 28 -12.941 39.743 42.800 1.00 10.20 C
ATOM 230 OG SER A 28 -13.201 38.919 41.696 1.00 12.29 O
ATOM 231 N ALA A 29 -11.152 37.618 44.463 1.00 8.54 N
ATOM 232 CA ALA A 29 -10.765 36.206 44.621 1.00 8.84 C
ATOM 233 C ALA A 29 -11.925 35.475 45.304 1.00 9.19 C
ATOM 234 O ALA A 29 -12.399 35.969 46.264 1.00 8.91 O
ATOM 235 CB ALA A 29 -9.458 36.120 45.397 1.00 8.59 C
ATOM 236 N SER A 30 -12.424 34.362 44.716 1.00 10.53 N
ATOM 237 CA SER A 30 -13.544 33.669 45.282 1.00 10.55 C
ATOM 238 C SER A 30 -13.206 32.203 45.275 1.00 10.47 C
ATOM 239 O SER A 30 -12.769 31.689 44.272 1.00 9.54 O
ATOM 240 CB SER A 30 -14.769 33.910 44.456 1.00 11.79 C
ATOM 241 OG SER A 30 -15.852 33.145 45.022 1.00 13.12 O
ATOM 242 N LEU A 31 -13.405 31.538 46.396 1.00 10.28 N
ATOM 243 CA LEU A 31 -12.877 30.197 46.580 1.00 11.15 C
ATOM 244 C LEU A 31 -14.024 29.283 46.922 1.00 13.02 C
ATOM 245 O LEU A 31 -14.940 29.670 47.642 1.00 12.33 O
ATOM 246 CB LEU A 31 -11.840 30.220 47.738 1.00 10.90 C
ATOM 247 CG LEU A 31 -10.626 31.178 47.655 1.00 10.66 C
ATOM 248 CD1 LEU A 31 -9.704 30.893 48.811 1.00 10.40 C
ATOM 249 CD2 LEU A 31 -9.867 31.117 46.356 1.00 10.99 C
ATOM 250 N LEU A 32 -13.997 28.072 46.424 1.00 14.81 N
ATOM 251 CA LEU A 32 -15.064 27.091 46.658 1.00 17.77 C
ATOM 252 C LEU A 32 -14.349 25.806 46.979 1.00 19.34 C
ATOM 253 O LEU A 32 -13.700 25.279 46.112 1.00 17.08 O
ATOM 254 CB LEU A 32 -15.913 26.921 45.398 1.00 20.46 C
ATOM 255 CG LEU A 32 -17.022 25.835 45.369 1.00 23.04 C
ATOM 256 CD1 LEU A 32 -18.178 26.190 46.291 1.00 23.89 C
ATOM 257 CD2 LEU A 32 -17.511 25.562 43.959 1.00 23.67 C
ATOM 258 N ARG A 33 -14.465 25.323 48.214 1.00 21.95 N
ATOM 259 CA ARG A 33 -13.860 24.062 48.632 1.00 25.78 C
ATOM 260 C ARG A 33 -14.956 23.011 48.622 1.00 26.21 C
ATOM 261 O ARG A 33 -16.058 23.292 49.073 1.00 26.69 O
ATOM 262 CB ARG A 33 -13.239 24.198 50.011 1.00 28.12 C
ATOM 263 CG ARG A 33 -12.263 23.069 50.344 1.00 31.55 C
ATOM 264 CD ARG A 33 -11.385 23.433 51.531 1.00 33.43 C
ATOM 265 NE ARG A 33 -10.911 22.233 52.249 1.00 36.94 N
ATOM 266 CZ ARG A 33 -9.634 21.870 52.486 1.00 36.45 C
ATOM 267 NH1 ARG A 33 -8.592 22.592 52.070 1.00 36.40 N
ATOM 268 NH2 ARG A 33 -9.390 20.742 53.166 1.00 34.37 N
ATOM 269 N GLN A 34 -14.679 21.831 48.074 1.00 25.65 N
ATOM 270 CA GLN A 34 -15.700 20.782 47.885 1.00 26.73 C
ATOM 271 C GLN A 34 -15.059 19.402 48.002 1.00 29.17 C
ATOM 272 O GLN A 34 -14.007 19.150 47.368 1.00 23.89 O
ATOM 273 CB GLN A 34 -16.316 20.856 46.497 1.00 29.19 C
ATOM 274 CG GLN A 34 -17.302 21.980 46.247 1.00 33.25 C
ATOM 275 CD GLN A 34 -17.619 22.185 44.757 1.00 34.11 C
ATOM 276 OE1 GLN A 34 -16.728 22.340 43.903 1.00 34.65 O
ATOM 277 NE2 GLN A 34 -18.893 22.243 44.455 1.00 35.86 N
ATOM 278 N ARG A 35 -15.693 18.515 48.783 1.00 29.70 N
ATOM 279 CA ARG A 35 -15.331 17.094 48.837 1.00 31.30 C
ATOM 280 C ARG A 35 -15.525 16.490 47.468 1.00 29.35 C
ATOM 281 O ARG A 35 -16.525 16.771 46.837 1.00 28.92 O
ATOM 282 CB ARG A 35 -16.230 16.319 49.812 1.00 35.89 C
ATOM 283 CG ARG A 35 -16.113 16.639 51.296 1.00 41.70 C
ATOM 284 CD ARG A 35 -14.707 16.441 51.849 1.00 46.02 C
ATOM 285 NE ARG A 35 -14.187 15.083 51.668 1.00 51.65 N
ATOM 286 CZ ARG A 35 -14.422 14.032 52.468 1.00 56.33 C
ATOM 287 NH1 ARG A 35 -15.195 14.121 53.555 1.00 57.65 N
ATOM 288 NH2 ARG A 35 -13.874 12.854 52.169 1.00 58.17 N
ATOM 289 N VAL A 36 -14.556 15.708 46.981 1.00 28.86 N
ATOM 290 CA VAL A 36 -14.714 14.951 45.730 1.00 29.37 C
ATOM 291 C VAL A 36 -14.177 13.538 45.963 1.00 27.14 C
ATOM 292 O VAL A 36 -13.166 13.355 46.620 1.00 25.67 O
ATOM 293 CB VAL A 36 -14.007 15.601 44.512 1.00 30.56 C
ATOM 294 CG1 VAL A 36 -14.330 14.836 43.226 1.00 33.15 C
ATOM 295 CG2 VAL A 36 -14.471 17.043 44.316 1.00 32.24 C
ATOM 296 N LYS A 37 -14.881 12.534 45.464 1.00 27.61 N
ATOM 297 CA LYS A 37 -14.350 11.166 45.538 1.00 26.61 C
ATOM 298 C LYS A 37 -13.690 10.952 44.187 1.00 26.69 C
ATOM 299 O LYS A 37 -14.254 11.295 43.140 1.00 30.00 O
ATOM 300 CB LYS A 37 -15.415 10.116 45.828 1.00 27.52 C
ATOM 301 N VAL A 38 -12.468 10.452 44.252 1.00 26.53 N
ATOM 302 CA VAL A 38 -11.656 10.077 43.107 1.00 27.34 C
ATOM 303 C VAL A 38 -11.432 8.554 43.291 1.00 27.74 C
ATOM 304 O VAL A 38 -10.602 8.137 44.116 1.00 27.22 O
ATOM 305 CB VAL A 38 -10.330 10.887 43.119 1.00 28.04 C
ATOM 306 CG1 VAL A 38 -9.471 10.571 41.890 1.00 27.89 C
ATOM 307 CG2 VAL A 38 -10.633 12.383 43.217 1.00 27.89 C
ATOM 308 N GLY A 39 -12.213 7.742 42.567 1.00 28.66 N
ATOM 309 CA GLY A 39 -12.392 6.341 42.908 1.00 29.07 C
ATOM 310 C GLY A 39 -13.036 6.236 44.282 1.00 29.60 C
ATOM 311 O GLY A 39 -12.345 6.108 45.292 1.00 30.40 O
ATOM 312 N GLU A 42 -11.007 10.144 47.953 1.00 18.46 N
ATOM 313 CA GLU A 42 -11.540 11.132 48.925 1.00 19.78 C
ATOM 314 C GLU A 42 -10.780 12.473 49.171 1.00 19.11 C
ATOM 315 O GLU A 42 -10.174 12.622 50.201 1.00 19.66 O
ATOM 316 CB GLU A 42 -11.691 10.446 50.294 1.00 20.76 C
ATOM 317 N LEU A 43 -10.906 13.465 48.278 1.00 18.19 N
ATOM 318 CA LEU A 43 -10.059 14.694 48.279 1.00 16.39 C
ATOM 319 C LEU A 43 -10.880 15.936 48.565 1.00 15.28 C
ATOM 320 O LEU A 43 -12.093 15.879 48.535 1.00 20.40 O
ATOM 321 CB LEU A 43 -9.405 14.846 46.896 1.00 15.21 C
ATOM 322 CG LEU A 43 -8.496 13.665 46.439 1.00 15.16 C
ATOM 323 CD1 LEU A 43 -7.953 13.854 45.039 1.00 15.48 C
ATOM 324 CD2 LEU A 43 -7.319 13.394 47.365 1.00 15.88 C
ATOM 325 N ASN A 44 -10.225 17.070 48.809 1.00 14.67 N
ATOM 326 CA ASN A 44 -10.911 18.335 48.922 1.00 13.41 C
ATOM 327 C ASN A 44 -10.505 19.241 47.777 1.00 12.33 C
ATOM 328 O ASN A 44 -9.421 19.864 47.815 1.00 14.19 O
ATOM 329 CB ASN A 44 -10.573 18.971 50.242 1.00 15.14 C
ATOM 330 CG ASN A 44 -10.974 18.104 51.416 1.00 15.47 C
ATOM 331 OD1 ASN A 44 -12.091 18.187 51.889 1.00 17.39 O
ATOM 332 ND2 ASN A 44 -10.054 17.261 51.878 1.00 15.74 N
ATOM 333 N ASN A 45 -11.381 19.317 46.770 1.00 11.30 N
ATOM 334 CA ASN A 45 -11.170 20.181 45.644 1.00 10.47 C
ATOM 335 C ASN A 45 -11.338 21.641 46.122 1.00 9.87 C
ATOM 336 O ASN A 45 -12.175 21.950 46.955 1.00 9.87 O
ATOM 337 CB ASN A 45 -12.120 19.940 44.482 1.00 10.53 C
ATOM 338 CG ASN A 45 -11.574 20.503 43.160 1.00 10.62 C
ATOM 339 OD1 ASN A 45 -10.737 19.904 42.518 1.00 10.12 O
ATOM 340 ND2 ASN A 45 -11.995 21.716 42.809 1.00 10.54 N
ATOM 341 N VAL A 46 -10.502 22.502 45.584 1.00 9.29 N
ATOM 342 CA VAL A 46 -10.632 23.906 45.796 1.00 9.20 C
ATOM 343 C VAL A 46 -10.652 24.459 44.396 1.00 9.19 C
ATOM 344 O VAL A 46 -9.690 24.170 43.615 1.00 8.92 O
ATOM 345 CB VAL A 46 -9.438 24.516 46.559 1.00 8.84 C
ATOM 346 CG1 VAL A 46 -9.575 26.059 46.548 1.00 8.78 C
ATOM 347 CG2 VAL A 46 -9.343 23.956 47.980 1.00 9.05 C
ATOM 348 N SER A 47 -11.676 25.262 44.096 1.00 9.16 N
ATOM 349 CA SER A 47 -11.742 25.974 42.810 1.00 9.49 C
ATOM 350 C SER A 47 -11.580 27.431 43.153 1.00 9.17 C
ATOM 351 O SER A 47 -12.400 27.948 43.932 1.00 10.08 O
ATOM 352 CB SER A 47 -13.074 25.724 42.140 1.00 9.80 C
ATOM 353 OG SER A 47 -13.140 26.358 40.878 1.00 10.84 O
ATOM 354 N GLY A 48 -10.509 28.061 42.652 1.00 7.79 N
ATOM 355 CA GLY A 48 -10.184 29.474 42.980 1.00 7.79 C
ATOM 356 C GLY A 48 -10.437 30.320 41.758 1.00 7.65 C
ATOM 357 O GLY A 48 -9.907 30.028 40.719 1.00 7.39 O
ATOM 358 N GLN A 49 -11.294 31.333 41.860 1.00 8.35 N
ATOM 359 CA GLN A 49 -11.659 32.180 40.718 1.00 8.80 C
ATOM 360 C GLN A 49 -11.111 33.582 40.952 1.00 7.89 C
ATOM 361 O GLN A 49 -11.429 34.196 41.975 1.00 6.44 O
ATOM 362 CB GLN A 49 -13.163 32.254 40.568 1.00 10.76 C
ATOM 363 CG GLN A 49 -13.607 33.005 39.330 1.00 14.61 C
ATOM 364 CD GLN A 49 -15.135 33.194 39.306 1.00 18.62 C
ATOM 365 OE1 GLN A 49 -15.847 32.667 38.451 1.00 22.93 O
ATOM 366 NE2 GLN A 49 -15.621 33.931 40.269 1.00 22.16 N
ATOM 367 N TYR A 50 -10.231 34.020 40.060 1.00 6.93 N
ATOM 368 CA TYR A 50 -9.455 35.254 40.223 1.00 6.55 C
ATOM 369 C TYR A 50 -9.780 36.155 39.006 1.00 6.25 C
ATOM 370 O TYR A 50 -9.508 35.773 37.911 1.00 5.98 O
ATOM 371 CB TYR A 50 -7.967 34.903 40.252 1.00 6.56 C
ATOM 372 CG TYR A 50 -7.573 33.892 41.385 1.00 6.69 C
ATOM 373 CD1 TYR A 50 -7.292 34.346 42.663 1.00 6.98 C
ATOM 374 CD2 TYR A 50 -7.504 32.548 41.149 1.00 6.71 C
ATOM 375 CE1 TYR A 50 -6.854 33.478 43.690 1.00 6.88 C
ATOM 376 CE2 TYR A 50 -7.144 31.644 42.161 1.00 6.73 C
ATOM 377 CZ TYR A 50 -6.848 32.099 43.452 1.00 7.08 C
ATOM 378 OH TYR A 50 -6.493 31.215 44.456 1.00 7.19 O
ATOM 379 N VAL A 51 -10.252 37.395 39.233 1.00 6.40 N
ATOM 380 CA VAL A 51 -10.777 38.230 38.165 1.00 6.26 C
ATOM 381 C VAL A 51 -10.233 39.632 38.334 1.00 6.28 C
ATOM 382 O VAL A 51 -10.410 40.232 39.380 1.00 6.05 O
ATOM 383 CB VAL A 51 -12.317 38.341 38.132 1.00 6.60 C
ATOM 384 CG1 VAL A 51 -12.800 39.143 36.909 1.00 6.47 C
ATOM 385 CG2 VAL A 51 -12.937 36.950 38.151 1.00 6.34 C
ATOM 386 N SER A 52 -9.601 40.085 37.269 1.00 6.73 N
ATOM 387 CA SER A 52 -9.019 41.408 37.163 1.00 6.87 C
ATOM 388 C SER A 52 -9.843 42.193 36.192 1.00 7.04 C
ATOM 389 O SER A 52 -10.138 41.709 35.118 1.00 6.33 O
ATOM 390 CB SER A 52 -7.605 41.297 36.622 1.00 6.95 C
ATOM 391 OG SER A 52 -6.820 40.632 37.571 1.00 7.43 O
ATOM 392 N VAL A 53 -10.219 43.434 36.560 1.00 7.78 N
ATOM 393 CA VAL A 53 -10.990 44.299 35.682 1.00 8.83 C
ATOM 394 C VAL A 53 -10.322 45.688 35.678 1.00 9.25 C
ATOM 395 O VAL A 53 -9.873 46.184 36.726 1.00 9.05 O
ATOM 396 CB VAL A 53 -12.513 44.414 36.043 1.00 9.37 C
ATOM 397 CG1 VAL A 53 -13.194 45.431 35.121 1.00 10.01 C
ATOM 398 CG2 VAL A 53 -13.254 43.069 35.979 1.00 9.59 C
ATOM 399 N TYR A 54 -10.168 46.249 34.466 1.00 9.68 N
ATOM 400 CA TYR A 54 -9.654 47.616 34.313 1.00 9.94 C
ATOM 401 C TYR A 54 -10.489 48.305 33.240 1.00 10.60 C
ATOM 402 O TYR A 54 -10.794 47.702 32.223 1.00 10.31 O
ATOM 403 CB TYR A 54 -8.156 47.652 33.960 1.00 10.01 C
ATOM 404 CG TYR A 54 -7.507 49.027 34.124 1.00 10.60 C
ATOM 405 CD1 TYR A 54 -7.732 50.039 33.216 1.00 10.45 C
ATOM 406 CD2 TYR A 54 -6.650 49.298 35.219 1.00 9.94 C
ATOM 407 CE1 TYR A 54 -7.153 51.294 33.384 1.00 10.80 C
ATOM 408 CE2 TYR A 54 -6.124 50.556 35.420 1.00 10.02 C
ATOM 409 CZ TYR A 54 -6.350 51.555 34.498 1.00 10.47 C
ATOM 410 OH TYR A 54 -5.765 52.815 34.675 1.00 11.53 O
ATOM 411 N LYS A 55 -10.857 49.567 33.475 1.00 11.52 N
ATOM 412 CA LYS A 55 -11.632 50.324 32.501 1.00 13.67 C
ATOM 413 C LYS A 55 -10.701 51.176 31.683 1.00 13.26 C
ATOM 414 O LYS A 55 -10.088 52.100 32.223 1.00 11.56 O
ATOM 415 CB LYS A 55 -12.685 51.198 33.169 1.00 15.47 C
ATOM 416 CG LYS A 55 -13.965 50.483 33.464 1.00 17.02 C
ATOM 417 CD LYS A 55 -15.039 51.488 33.804 1.00 18.62 C
ATOM 418 CE LYS A 55 -16.291 50.772 34.283 1.00 21.45 C
ATOM 419 NZ LYS A 55 -17.393 51.759 34.488 1.00 24.23 N
ATOM 420 N ARG A 56 -10.580 50.867 30.374 1.00 13.88 N
ATOM 421 CA ARG A 56 -9.536 51.475 29.533 1.00 14.29 C
ATOM 422 C ARG A 56 -10.138 52.330 28.417 1.00 13.41 C
ATOM 423 O ARG A 56 -10.941 51.844 27.672 1.00 10.98 O
ATOM 424 CB ARG A 56 -8.661 50.386 28.886 1.00 15.05 C
ATOM 425 CG ARG A 56 -7.323 50.890 28.311 1.00 16.27 C
ATOM 426 CD ARG A 56 -6.301 51.364 29.349 1.00 15.71 C
ATOM 427 NE ARG A 56 -5.886 50.290 30.238 1.00 15.44 N
ATOM 428 CZ ARG A 56 -5.023 50.414 31.241 1.00 16.43 C
ATOM 429 NH1 ARG A 56 -4.478 51.576 31.521 1.00 19.25 N
ATOM 430 NH2 ARG A 56 -4.759 49.378 32.012 1.00 17.91 N
ATOM 431 N PRO A 57 -9.718 53.605 28.304 1.00 15.35 N
ATOM 432 CA PRO A 57 -10.212 54.432 27.228 1.00 16.26 C
ATOM 433 C PRO A 57 -9.929 53.790 25.885 1.00 17.14 C
ATOM 434 O PRO A 57 -8.819 53.273 25.654 1.00 16.83 O
ATOM 435 CB PRO A 57 -9.395 55.739 27.358 1.00 16.33 C
ATOM 436 CG PRO A 57 -9.015 55.795 28.754 1.00 15.48 C
ATOM 437 CD PRO A 57 -8.749 54.344 29.129 1.00 16.38 C
ATOM 438 N ALA A 58 -10.944 53.776 25.043 1.00 18.20 N
ATOM 439 CA ALA A 58 -10.736 53.529 23.610 1.00 20.47 C
ATOM 440 C ALA A 58 -9.860 54.661 23.042 1.00 24.20 C
ATOM 441 O ALA A 58 -10.089 55.799 23.386 1.00 24.17 O
ATOM 442 CB ALA A 58 -12.081 53.488 22.901 1.00 21.67 C
ATOM 443 N PRO A 59 -8.855 54.369 22.186 1.00 26.85 N
ATOM 444 CA PRO A 59 -7.990 55.478 21.679 1.00 28.94 C
ATOM 445 C PRO A 59 -8.700 56.622 20.918 1.00 28.03 C
ATOM 446 O PRO A 59 -9.578 56.367 20.090 1.00 27.00 O
ATOM 447 CB PRO A 59 -7.000 54.762 20.736 1.00 28.93 C
ATOM 448 CG PRO A 59 -7.016 53.344 21.172 1.00 29.19 C
ATOM 449 CD PRO A 59 -8.424 53.073 21.646 1.00 28.74 C
ATOM 450 N MET A 71 -15.128 60.211 24.905 1.00 27.75 N
ATOM 451 CA MET A 71 -14.908 58.850 24.455 1.00 28.29 C
ATOM 452 C MET A 71 -14.924 57.745 25.515 1.00 25.80 C
ATOM 453 O MET A 71 -14.372 57.932 26.594 1.00 25.86 O
ATOM 454 CB MET A 71 -13.629 58.758 23.660 1.00 28.03 C
ATOM 455 CG MET A 71 -13.884 59.136 22.195 1.00 30.21 C
ATOM 456 SD MET A 71 -12.566 58.439 21.272 1.00 29.30 S
ATOM 457 CE MET A 71 -13.289 56.984 20.569 1.00 27.21 C
ATOM 458 N PRO A 72 -15.545 56.586 25.174 1.00 24.29 N
ATOM 459 CA PRO A 72 -15.863 55.526 26.125 1.00 22.90 C
ATOM 460 C PRO A 72 -14.686 54.664 26.631 1.00 19.58 C
ATOM 461 O PRO A 72 -13.636 54.600 26.023 1.00 19.41 O
ATOM 462 CB PRO A 72 -16.869 54.658 25.336 1.00 24.18 C
ATOM 463 CG PRO A 72 -16.469 54.824 23.918 1.00 25.03 C
ATOM 464 CD PRO A 72 -16.001 56.245 23.807 1.00 23.09 C
ATOM 465 N ASN A 73 -14.884 54.043 27.783 1.00 17.44 N
ATOM 466 CA ASN A 73 -13.951 53.063 28.322 1.00 15.59 C
ATOM 467 C ASN A 73 -14.419 51.683 27.949 1.00 15.10 C
ATOM 468 O ASN A 73 -15.595 51.456 27.896 1.00 15.81 O
ATOM 469 CB ASN A 73 -13.923 53.144 29.835 1.00 15.74 C
ATOM 470 CG ASN A 73 -13.485 54.493 30.342 1.00 14.70 C
ATOM 471 OD1 ASN A 73 -14.042 54.990 31.321 1.00 15.95 O
ATOM 472 ND2 ASN A 73 -12.444 55.053 29.742 1.00 13.92 N
ATOM 473 N GLU A 74 -13.493 50.764 27.736 1.00 14.32 N
ATOM 474 CA GLU A 74 -13.845 49.322 27.545 1.00 13.81 C
ATOM 475 C GLU A 74 -13.485 48.650 28.879 1.00 14.32 C
ATOM 476 O GLU A 74 -12.732 49.248 29.677 1.00 14.79 O
ATOM 477 CB GLU A 74 -13.057 48.710 26.379 1.00 13.51 C
ATOM 478 CG GLU A 74 -11.544 48.651 26.594 1.00 13.58 C
ATOM 479 CD GLU A 74 -10.791 47.699 25.659 1.00 13.33 C
ATOM 480 OE1 GLU A 74 -11.263 46.626 25.312 1.00 13.93 O
ATOM 481 OE2 GLU A 74 -9.652 47.980 25.315 1.00 15.14 O
ATOM 482 N ASN A 75 -14.010 47.445 29.130 1.00 15.08 N
ATOM 483 CA ASN A 75 -13.600 46.608 30.275 1.00 15.50 C
ATOM 484 C ASN A 75 -12.572 45.584 29.795 1.00 14.25 C
ATOM 485 O ASN A 75 -12.909 44.620 29.051 1.00 16.18 O
ATOM 486 CB ASN A 75 -14.795 45.892 30.886 1.00 16.02 C
ATOM 487 CG ASN A 75 -15.880 46.860 31.328 1.00 19.01 C
ATOM 488 OD1 ASN A 75 -17.031 46.718 30.943 1.00 22.27 O
ATOM 489 ND2 ASN A 75 -15.511 47.870 32.075 1.00 17.88 N
ATOM 490 N GLN A 76 -11.320 45.817 30.139 1.00 12.33 N
ATOM 491 CA GLN A 76 -10.280 44.818 30.013 1.00 11.36 C
ATOM 492 C GLN A 76 -10.430 43.832 31.214 1.00 11.32 C
ATOM 493 O GLN A 76 -10.412 44.231 32.373 1.00 10.35 O
ATOM 494 CB GLN A 76 -8.913 45.491 30.054 1.00 12.42 C
ATOM 495 CG GLN A 76 -8.638 46.418 28.851 1.00 12.50 C
ATOM 496 CD GLN A 76 -7.301 47.065 28.979 1.00 12.89 C
ATOM 497 OE1 GLN A 76 -6.961 47.579 30.053 1.00 14.69 O
ATOM 498 NE2 GLN A 76 -6.523 47.060 27.901 1.00 14.05 N
ATOM 499 N SER A 77 -10.570 42.547 30.940 1.00 11.33 N
ATOM 500 CA SER A 77 -10.813 41.620 32.030 1.00 10.54 C
ATOM 501 C SER A 77 -10.021 40.374 31.807 1.00 9.60 C
ATOM 502 O SER A 77 -9.830 39.908 30.670 1.00 8.74 O
ATOM 503 CB SER A 77 -12.293 41.326 32.271 1.00 12.02 C
ATOM 504 OG SER A 77 -12.891 40.562 31.255 1.00 13.67 O
ATOM 505 N ILE A 78 -9.541 39.854 32.931 1.00 8.53 N
ATOM 506 CA ILE A 78 -8.785 38.616 32.915 1.00 8.67 C
ATOM 507 C ILE A 78 -9.380 37.742 34.036 1.00 9.47 C
ATOM 508 O ILE A 78 -9.434 38.205 35.134 1.00 8.52 O
ATOM 509 CB ILE A 78 -7.282 38.787 33.090 1.00 8.31 C
ATOM 510 CG1 ILE A 78 -6.781 39.792 32.050 1.00 8.61 C
ATOM 511 CG2 ILE A 78 -6.634 37.367 33.042 1.00 8.67 C
ATOM 512 CD1 ILE A 78 -5.301 40.020 31.951 1.00 8.73 C
ATOM 513 N ARG A 79 -9.845 36.521 33.705 1.00 9.88 N
ATOM 514 CA ARG A 79 -10.468 35.608 34.685 1.00 10.70 C
ATOM 515 C ARG A 79 -9.729 34.293 34.663 1.00 9.55 C
ATOM 516 O ARG A 79 -9.607 33.673 33.599 1.00 9.39 O
ATOM 517 CB ARG A 79 -11.918 35.349 34.366 1.00 13.47 C
ATOM 518 CG ARG A 79 -12.727 36.597 34.109 1.00 17.28 C
ATOM 519 CD ARG A 79 -14.146 36.244 33.656 1.00 22.07 C
ATOM 520 NE ARG A 79 -14.727 35.376 34.695 1.00 25.77 N
ATOM 521 CZ ARG A 79 -15.431 35.767 35.764 1.00 29.44 C
ATOM 522 NH1 ARG A 79 -15.752 37.052 35.968 1.00 32.33 N
ATOM 523 NH2 ARG A 79 -15.838 34.835 36.646 1.00 32.72 N
ATOM 524 N THR A 80 -9.212 33.892 35.832 1.00 7.70 N
ATOM 525 CA THR A 80 -8.493 32.654 35.941 1.00 7.38 C
ATOM 526 C THR A 80 -9.217 31.803 36.962 1.00 7.55 C
ATOM 527 O THR A 80 -9.481 32.245 38.074 1.00 7.15 O
ATOM 528 CB THR A 80 -7.037 32.836 36.416 1.00 6.78 C
ATOM 529 OG1 THR A 80 -6.267 33.438 35.396 1.00 6.32 O
ATOM 530 CG2 THR A 80 -6.424 31.468 36.689 1.00 6.58 C
ATOM 531 N VAL A 81 -9.421 30.542 36.609 1.00 7.81 N
ATOM 532 CA VAL A 81 -9.931 29.593 37.565 1.00 8.47 C
ATOM 533 C VAL A 81 -8.917 28.522 37.729 1.00 8.04 C
ATOM 534 O VAL A 81 -8.558 27.907 36.720 1.00 8.93 O
ATOM 535 CB VAL A 81 -11.286 28.985 37.121 1.00 9.34 C
ATOM 536 CG1 VAL A 81 -11.761 27.946 38.107 1.00 9.36 C
ATOM 537 CG2 VAL A 81 -12.326 30.073 36.977 1.00 9.89 C
ATOM 538 N ILE A 82 -8.534 28.258 38.982 1.00 7.03 N
ATOM 539 CA ILE A 82 -7.580 27.153 39.302 1.00 6.88 C
ATOM 540 C ILE A 82 -8.329 26.140 40.114 1.00 6.68 C
ATOM 541 O ILE A 82 -8.930 26.481 41.122 1.00 6.10 O
ATOM 542 CB ILE A 82 -6.410 27.662 40.122 1.00 6.91 C
ATOM 543 CG1 ILE A 82 -5.538 28.532 39.231 1.00 6.56 C
ATOM 544 CG2 ILE A 82 -5.572 26.527 40.690 1.00 6.68 C
ATOM 545 CD1 ILE A 82 -4.536 29.398 39.987 1.00 6.50 C
ATOM 546 N SER A 83 -8.300 24.879 39.687 1.00 6.52 N
ATOM 547 CA SER A 83 -9.164 23.883 40.316 1.00 6.59 C
ATOM 548 C SER A 83 -8.399 22.574 40.490 1.00 7.20 C
ATOM 549 O SER A 83 -8.011 21.883 39.538 1.00 7.47 O
ATOM 550 CB SER A 83 -10.510 23.732 39.589 1.00 6.69 C
ATOM 551 OG SER A 83 -11.341 22.707 40.128 1.00 6.18 O
ATOM 552 N GLY A 84 -8.240 22.195 41.744 1.00 6.95 N
ATOM 553 CA GLY A 84 -7.613 20.905 42.014 1.00 7.43 C
ATOM 554 C GLY A 84 -7.613 20.695 43.529 1.00 7.65 C
ATOM 555 O GLY A 84 -7.835 21.640 44.311 1.00 7.69 O
ATOM 556 N SER A 85 -7.410 19.446 43.932 1.00 7.81 N
ATOM 557 CA SER A 85 -7.377 19.114 45.344 1.00 8.49 C
ATOM 558 C SER A 85 -6.294 19.872 46.117 1.00 9.27 C
ATOM 559 O SER A 85 -5.170 20.094 45.623 1.00 10.61 O
ATOM 560 CB SER A 85 -7.121 17.632 45.524 1.00 8.28 C
ATOM 561 OG SER A 85 -5.775 17.345 45.271 1.00 8.95 O
ATOM 562 N ALA A 86 -6.633 20.265 47.347 1.00 9.92 N
ATOM 563 CA ALA A 86 -5.642 20.778 48.265 1.00 9.58 C
ATOM 564 C ALA A 86 -4.505 19.773 48.490 1.00 10.11 C
ATOM 565 O ALA A 86 -3.331 20.142 48.660 1.00 9.73 O
ATOM 566 CB ALA A 86 -6.315 21.165 49.587 1.00 9.36 C