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pdb1g8p.ent
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HEADER PHOTOSYNTHESIS, METAL TRANSPORT 20-NOV-00 1G8P
TITLE CRYSTAL STRUCTURE OF BCHI SUBUNIT OF MAGNESIUM CHELATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAGNESIUM-CHELATASE 38 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BCHI SUBUNIT;
COMPND 5 SYNONYM: MG-PROTOPORPHYRIN IX CHELATASE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER CAPSULATUS;
SOURCE 3 ORGANISM_TAXID: 1061;
SOURCE 4 GENE: BCHI_RHOCA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PARALLEL BETA SHEET, P-LOOP, ROSSMANN FOLD, AAA+, PHOTOSYNTHESIS,
KEYWDS 2 METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.N.FODJE,A.HANSSON,M.HANSSON,J.G.OLSEN,S.GOUGH,R.D.WILLOWS,S.AL-
AUTHOR 2 KARADAGHI
REVDAT 3 12-NOV-14 1G8P 1 KEYWDS
REVDAT 2 24-FEB-09 1G8P 1 VERSN
REVDAT 1 03-AUG-01 1G8P 0
JRNL AUTH M.N.FODJE,A.HANSSON,M.HANSSON,J.G.OLSEN,S.GOUGH,R.D.WILLOWS,
JRNL AUTH 2 S.AL-KARADAGHI
JRNL TITL INTERPLAY BETWEEN AN AAA MODULE AND AN INTEGRIN I DOMAIN MAY
JRNL TITL 2 REGULATE THE FUNCTION OF MAGNESIUM CHELATASE.
JRNL REF J.MOL.BIOL. V. 311 111 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11469861
JRNL DOI 10.1006/JMBI.2001.4834
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 312841.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 22179
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 SET) : 0.214
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2207
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3229
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 370
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2457
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.35000
REMARK 3 B22 (A**2) : -1.35000
REMARK 3 B33 (A**2) : 2.69000
REMARK 3 B12 (A**2) : 1.52000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.700
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.660 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.830 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.150 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.350 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 50.33
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET
REMARK 4
REMARK 4 1G8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-00.
REMARK 100 THE RCSB ID CODE IS RCSB012372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.958
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 14.000
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.24600
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: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, TRIS , MGCL2, PH 7.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP AT 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.81067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.90533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.85800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.95267
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.76333
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 VAL A 5
REMARK 465 ALA A 6
REMARK 465 ARG A 7
REMARK 465 LEU A 8
REMARK 465 GLN A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 ALA A 12
REMARK 465 SER A 13
REMARK 465 GLY A 14
REMARK 465 ALA A 15
REMARK 465 LYS A 16
REMARK 465 THR A 17
REMARK 465 ARG A 329
REMARK 465 ASP A 330
REMARK 465 PRO A 331
REMARK 465 LEU A 332
REMARK 465 ASP A 333
REMARK 465 GLU A 334
REMARK 465 ALA A 335
REMARK 465 GLY A 336
REMARK 465 SER A 337
REMARK 465 THR A 338
REMARK 465 ALA A 339
REMARK 465 ARG A 340
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 GLY A 131 N - CA - C ANGL. DEV. = 15.9 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 SER A 129 -74.46 -58.90
REMARK 500 GLU A 132 -42.81 -17.04
REMARK 500 LYS A 133 0.03 -66.24
REMARK 500 GLU A 176 49.66 -94.68
REMARK 500 ASN A 195 173.07 -50.77
REMARK 500 PRO A 196 -80.29 -40.59
REMARK 500 ASP A 200 52.21 31.13
REMARK 500 LEU A 201 177.05 -38.21
REMARK 500 ARG A 202 107.79 -22.81
REMARK 500 ASP A 237 85.05 -166.80
REMARK 500 LEU A 263 -61.36 -28.84
REMARK 500 ASP A 286 -90.74 -35.64
REMARK 500 LEU A 288 -75.31 -0.82
REMARK 500 LEU A 349 67.15 -113.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G8P A 1 350 UNP P26239 BCHI_RHOCA 1 350
SEQRES 1 A 350 MET THR THR ALA VAL ALA ARG LEU GLN PRO SER ALA SER
SEQRES 2 A 350 GLY ALA LYS THR ARG PRO VAL PHE PRO PHE SER ALA ILE
SEQRES 3 A 350 VAL GLY GLN GLU ASP MET LYS LEU ALA LEU LEU LEU THR
SEQRES 4 A 350 ALA VAL ASP PRO GLY ILE GLY GLY VAL LEU VAL PHE GLY
SEQRES 5 A 350 ASP ARG GLY THR GLY LYS SER THR ALA VAL ARG ALA LEU
SEQRES 6 A 350 ALA ALA LEU LEU PRO GLU ILE GLU ALA VAL GLU GLY CYS
SEQRES 7 A 350 PRO VAL SER SER PRO ASN VAL GLU MET ILE PRO ASP TRP
SEQRES 8 A 350 ALA THR VAL LEU SER THR ASN VAL ILE ARG LYS PRO THR
SEQRES 9 A 350 PRO VAL VAL ASP LEU PRO LEU GLY VAL SER GLU ASP ARG
SEQRES 10 A 350 VAL VAL GLY ALA LEU ASP ILE GLU ARG ALA ILE SER LYS
SEQRES 11 A 350 GLY GLU LYS ALA PHE GLU PRO GLY LEU LEU ALA ARG ALA
SEQRES 12 A 350 ASN ARG GLY TYR LEU TYR ILE ASP GLU CYS ASN LEU LEU
SEQRES 13 A 350 GLU ASP HIS ILE VAL ASP LEU LEU LEU ASP VAL ALA GLN
SEQRES 14 A 350 SER GLY GLU ASN VAL VAL GLU ARG ASP GLY LEU SER ILE
SEQRES 15 A 350 ARG HIS PRO ALA ARG PHE VAL LEU VAL GLY SER GLY ASN
SEQRES 16 A 350 PRO GLU GLU GLY ASP LEU ARG PRO GLN LEU LEU ASP ARG
SEQRES 17 A 350 PHE GLY LEU SER VAL GLU VAL LEU SER PRO ARG ASP VAL
SEQRES 18 A 350 GLU THR ARG VAL GLU VAL ILE ARG ARG ARG ASP THR TYR
SEQRES 19 A 350 ASP ALA ASP PRO LYS ALA PHE LEU GLU GLU TRP ARG PRO
SEQRES 20 A 350 LYS ASP MET ASP ILE ARG ASN GLN ILE LEU GLU ALA ARG
SEQRES 21 A 350 GLU ARG LEU PRO LYS VAL GLU ALA PRO ASN THR ALA LEU
SEQRES 22 A 350 TYR ASP CYS ALA ALA LEU CYS ILE ALA LEU GLY SER ASP
SEQRES 23 A 350 GLY LEU ARG GLY GLU LEU THR LEU LEU ARG SER ALA ARG
SEQRES 24 A 350 ALA LEU ALA ALA LEU GLU GLY ALA THR ALA VAL GLY ARG
SEQRES 25 A 350 ASP HIS LEU LYS ARG VAL ALA THR MET ALA LEU SER HIS
SEQRES 26 A 350 ARG LEU ARG ARG ASP PRO LEU ASP GLU ALA GLY SER THR
SEQRES 27 A 350 ALA ARG VAL ALA ARG THR VAL GLU GLU THR LEU PRO
FORMUL 2 HOH *218(H2 O)
HELIX 1 1 PRO A 22 ILE A 26 5 5
HELIX 2 2 GLN A 29 ASP A 42 1 14
HELIX 3 3 PRO A 43 GLY A 46 5 4
HELIX 4 4 ASP A 53 GLY A 57 5 5
HELIX 5 5 SER A 59 LEU A 69 1 11
HELIX 6 6 ASN A 84 ILE A 88 5 5
HELIX 7 7 SER A 114 GLY A 120 1 7
HELIX 8 8 ASP A 123 GLY A 131 1 9
HELIX 9 9 GLY A 138 ASN A 144 1 7
HELIX 10 10 GLU A 152 LEU A 156 5 5
HELIX 11 11 GLU A 157 GLY A 171 1 15
HELIX 12 12 ARG A 202 ASP A 207 1 6
HELIX 13 13 ASP A 220 ASP A 237 1 18
HELIX 14 14 ASP A 237 LEU A 263 1 27
HELIX 15 15 PRO A 264 VAL A 266 5 3
HELIX 16 16 PRO A 269 LEU A 283 1 15
HELIX 17 17 GLY A 287 GLU A 305 1 19
HELIX 18 18 GLY A 311 SER A 324 1 14
HELIX 19 19 HIS A 325 LEU A 327 5 3
HELIX 20 20 VAL A 341 LEU A 349 1 9
SHEET 1 A 5 VAL A 106 LEU A 109 0
SHEET 2 A 5 GLY A 146 ILE A 150 1 O TYR A 147 N VAL A 107
SHEET 3 A 5 PHE A 188 GLY A 194 1 O VAL A 189 N LEU A 148
SHEET 4 A 5 VAL A 48 PHE A 51 1 N VAL A 48 O LEU A 190
SHEET 5 A 5 LEU A 211 GLU A 214 1 O LEU A 211 N LEU A 49
SHEET 1 B 2 ILE A 72 VAL A 75 0
SHEET 2 B 2 VAL A 99 LYS A 102 -1 N ILE A 100 O ALA A 74
SHEET 1 C 2 ALA A 121 LEU A 122 0
SHEET 2 C 2 PHE A 135 GLU A 136 -1 N GLU A 136 O ALA A 121
SHEET 1 D 2 GLU A 172 VAL A 175 0
SHEET 2 D 2 ILE A 182 PRO A 185 -1 O ILE A 182 N VAL A 175
CRYST1 90.259 90.259 83.716 90.00 90.00 120.00 P 65 6
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 0.011079 0.006397 0.000000 0.00000
SCALE2 0.000000 0.012793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011945 0.00000
ATOM 1 N ARG A 18 14.699 61.369 62.050 1.00 39.19 N
ATOM 2 CA ARG A 18 14.500 62.241 60.856 1.00 38.35 C
ATOM 3 C ARG A 18 13.762 61.516 59.729 1.00 36.05 C
ATOM 4 O ARG A 18 14.354 60.740 58.982 1.00 34.91 O
ATOM 5 CB ARG A 18 15.850 62.753 60.334 1.00 42.36 C
ATOM 6 CG ARG A 18 16.537 63.770 61.247 1.00 46.92 C
ATOM 7 CD ARG A 18 17.825 64.314 60.629 1.00 51.24 C
ATOM 8 NE ARG A 18 18.442 65.347 61.462 1.00 54.15 N
ATOM 9 CZ ARG A 18 19.527 66.040 61.124 1.00 55.44 C
ATOM 10 NH1 ARG A 18 20.127 65.816 59.964 1.00 56.86 N
ATOM 11 NH2 ARG A 18 20.012 66.964 61.944 1.00 56.41 N
ATOM 12 N PRO A 19 12.448 61.750 59.608 1.00 32.25 N
ATOM 13 CA PRO A 19 11.622 61.128 58.568 1.00 29.63 C
ATOM 14 C PRO A 19 12.058 61.532 57.159 1.00 25.81 C
ATOM 15 O PRO A 19 12.501 62.658 56.929 1.00 23.20 O
ATOM 16 CB PRO A 19 10.223 61.634 58.898 1.00 31.09 C
ATOM 17 CG PRO A 19 10.267 61.757 60.392 1.00 33.58 C
ATOM 18 CD PRO A 19 11.602 62.425 60.608 1.00 33.78 C
ATOM 19 N VAL A 20 11.930 60.606 56.217 1.00 23.29 N
ATOM 20 CA VAL A 20 12.305 60.867 54.832 1.00 21.08 C
ATOM 21 C VAL A 20 11.144 60.448 53.915 1.00 20.63 C
ATOM 22 O VAL A 20 10.487 59.425 54.164 1.00 18.63 O
ATOM 23 CB VAL A 20 13.598 60.076 54.470 1.00 22.62 C
ATOM 24 CG1 VAL A 20 13.931 60.230 53.000 1.00 22.29 C
ATOM 25 CG2 VAL A 20 14.764 60.568 55.334 1.00 23.10 C
ATOM 26 N PHE A 21 10.868 61.243 52.878 1.00 17.65 N
ATOM 27 CA PHE A 21 9.788 60.893 51.958 1.00 18.96 C
ATOM 28 C PHE A 21 10.049 59.441 51.554 1.00 16.92 C
ATOM 29 O PHE A 21 11.133 59.112 51.079 1.00 16.51 O
ATOM 30 CB PHE A 21 9.787 61.785 50.719 1.00 17.62 C
ATOM 31 CG PHE A 21 8.587 61.568 49.840 1.00 18.84 C
ATOM 32 CD1 PHE A 21 7.329 62.013 50.242 1.00 18.21 C
ATOM 33 CD2 PHE A 21 8.703 60.882 48.641 1.00 16.79 C
ATOM 34 CE1 PHE A 21 6.193 61.778 49.457 1.00 18.44 C
ATOM 35 CE2 PHE A 21 7.577 60.637 47.843 1.00 21.95 C
ATOM 36 CZ PHE A 21 6.317 61.088 48.255 1.00 19.02 C
ATOM 37 N PRO A 22 9.055 58.558 51.732 1.00 16.84 N
ATOM 38 CA PRO A 22 9.215 57.137 51.400 1.00 16.25 C
ATOM 39 C PRO A 22 9.344 56.719 49.934 1.00 17.25 C
ATOM 40 O PRO A 22 8.668 57.241 49.048 1.00 15.98 O
ATOM 41 CB PRO A 22 8.024 56.495 52.110 1.00 18.02 C
ATOM 42 CG PRO A 22 6.954 57.540 51.956 1.00 15.35 C
ATOM 43 CD PRO A 22 7.692 58.840 52.224 1.00 16.08 C
ATOM 44 N PHE A 23 10.245 55.760 49.715 1.00 15.99 N
ATOM 45 CA PHE A 23 10.570 55.194 48.409 1.00 15.18 C
ATOM 46 C PHE A 23 9.347 54.719 47.631 1.00 16.41 C
ATOM 47 O PHE A 23 9.177 55.049 46.454 1.00 14.94 O
ATOM 48 CB PHE A 23 11.516 54.005 48.618 1.00 15.39 C
ATOM 49 CG PHE A 23 12.155 53.485 47.361 1.00 17.57 C
ATOM 50 CD1 PHE A 23 13.309 54.077 46.856 1.00 18.12 C
ATOM 51 CD2 PHE A 23 11.642 52.365 46.717 1.00 17.94 C
ATOM 52 CE1 PHE A 23 13.949 53.551 45.725 1.00 17.35 C
ATOM 53 CE2 PHE A 23 12.273 51.832 45.589 1.00 16.67 C
ATOM 54 CZ PHE A 23 13.431 52.428 45.096 1.00 17.87 C
ATOM 55 N SER A 24 8.505 53.932 48.290 1.00 16.34 N
ATOM 56 CA SER A 24 7.319 53.374 47.647 1.00 20.32 C
ATOM 57 C SER A 24 6.281 54.408 47.220 1.00 21.23 C
ATOM 58 O SER A 24 5.450 54.125 46.355 1.00 21.52 O
ATOM 59 CB SER A 24 6.665 52.334 48.567 1.00 22.63 C
ATOM 60 OG SER A 24 6.321 52.910 49.821 1.00 27.10 O
ATOM 61 N ALA A 25 6.331 55.601 47.810 1.00 19.69 N
ATOM 62 CA ALA A 25 5.368 56.651 47.464 1.00 20.38 C
ATOM 63 C ALA A 25 5.842 57.546 46.315 1.00 19.99 C
ATOM 64 O ALA A 25 5.102 58.414 45.858 1.00 20.26 O
ATOM 65 CB ALA A 25 5.052 57.501 48.697 1.00 18.64 C
ATOM 66 N ILE A 26 7.072 57.339 45.856 1.00 19.85 N
ATOM 67 CA ILE A 26 7.619 58.122 44.751 1.00 20.00 C
ATOM 68 C ILE A 26 6.886 57.700 43.479 1.00 21.96 C
ATOM 69 O ILE A 26 6.742 56.506 43.217 1.00 21.92 O
ATOM 70 CB ILE A 26 9.131 57.853 44.580 1.00 19.42 C
ATOM 71 CG1 ILE A 26 9.911 58.465 45.750 1.00 18.93 C
ATOM 72 CG2 ILE A 26 9.621 58.429 43.266 1.00 19.22 C
ATOM 73 CD1 ILE A 26 11.413 58.164 45.709 1.00 20.30 C
ATOM 74 N VAL A 27 6.424 58.675 42.698 1.00 21.85 N
ATOM 75 CA VAL A 27 5.688 58.395 41.462 1.00 23.27 C
ATOM 76 C VAL A 27 6.593 58.143 40.261 1.00 23.59 C
ATOM 77 O VAL A 27 7.525 58.907 39.993 1.00 24.36 O
ATOM 78 CB VAL A 27 4.726 59.556 41.117 1.00 22.89 C
ATOM 79 CG1 VAL A 27 4.087 59.322 39.752 1.00 21.75 C
ATOM 80 CG2 VAL A 27 3.651 59.671 42.201 1.00 24.07 C
ATOM 81 N GLY A 28 6.309 57.069 39.534 1.00 24.25 N
ATOM 82 CA GLY A 28 7.112 56.735 38.369 1.00 25.26 C
ATOM 83 C GLY A 28 8.560 56.409 38.717 1.00 24.97 C
ATOM 84 O GLY A 28 8.824 55.698 39.685 1.00 24.12 O
ATOM 85 N GLN A 29 9.492 56.939 37.928 1.00 24.86 N
ATOM 86 CA GLN A 29 10.919 56.707 38.132 1.00 25.31 C
ATOM 87 C GLN A 29 11.251 55.218 38.219 1.00 24.38 C
ATOM 88 O GLN A 29 12.126 54.823 38.984 1.00 23.18 O
ATOM 89 CB GLN A 29 11.400 57.414 39.405 1.00 25.65 C
ATOM 90 CG GLN A 29 11.403 58.933 39.309 1.00 30.42 C
ATOM 91 CD GLN A 29 12.009 59.603 40.541 1.00 32.27 C
ATOM 92 OE1 GLN A 29 13.072 59.200 41.024 1.00 32.18 O
ATOM 93 NE2 GLN A 29 11.341 60.638 41.042 1.00 31.70 N
ATOM 94 N GLU A 30 10.563 54.400 37.424 1.00 24.21 N
ATOM 95 CA GLU A 30 10.781 52.956 37.430 1.00 25.29 C
ATOM 96 C GLU A 30 12.239 52.526 37.273 1.00 23.96 C
ATOM 97 O GLU A 30 12.742 51.736 38.069 1.00 23.39 O
ATOM 98 CB GLU A 30 9.968 52.278 36.324 1.00 27.88 C
ATOM 99 CG GLU A 30 8.477 52.195 36.567 1.00 32.77 C
ATOM 100 CD GLU A 30 7.785 53.536 36.474 1.00 36.80 C
ATOM 101 OE1 GLU A 30 8.304 54.441 35.773 1.00 40.45 O
ATOM 102 OE2 GLU A 30 6.707 53.678 37.090 1.00 38.79 O
ATOM 103 N ASP A 31 12.906 53.023 36.238 1.00 22.14 N
ATOM 104 CA ASP A 31 14.294 52.652 35.997 1.00 23.40 C
ATOM 105 C ASP A 31 15.214 53.123 37.101 1.00 22.35 C
ATOM 106 O ASP A 31 16.141 52.411 37.488 1.00 19.76 O
ATOM 107 CB ASP A 31 14.771 53.196 34.652 1.00 24.67 C
ATOM 108 CG ASP A 31 14.293 52.351 33.487 1.00 29.24 C
ATOM 109 OD1 ASP A 31 13.595 51.347 33.738 1.00 28.51 O
ATOM 110 OD2 ASP A 31 14.621 52.684 32.324 1.00 32.26 O
ATOM 111 N MET A 32 14.969 54.331 37.595 1.00 21.20 N
ATOM 112 CA MET A 32 15.775 54.865 38.682 1.00 22.01 C
ATOM 113 C MET A 32 15.635 53.936 39.885 1.00 20.68 C
ATOM 114 O MET A 32 16.627 53.566 40.515 1.00 22.92 O
ATOM 115 CB MET A 32 15.294 56.265 39.069 1.00 24.88 C
ATOM 116 CG MET A 32 15.913 56.798 40.357 1.00 29.25 C
ATOM 117 SD MET A 32 17.603 57.417 40.166 1.00 34.92 S
ATOM 118 CE MET A 32 17.290 59.189 40.342 1.00 34.90 C
ATOM 119 N LYS A 33 14.401 53.559 40.202 1.00 19.59 N
ATOM 120 CA LYS A 33 14.158 52.684 41.343 1.00 20.49 C
ATOM 121 C LYS A 33 14.829 51.322 41.169 1.00 19.55 C
ATOM 122 O LYS A 33 15.451 50.813 42.097 1.00 19.34 O
ATOM 123 CB LYS A 33 12.657 52.494 41.569 1.00 19.82 C
ATOM 124 CG LYS A 33 11.923 53.723 42.099 1.00 21.28 C
ATOM 125 CD LYS A 33 10.490 53.347 42.452 1.00 22.49 C
ATOM 126 CE LYS A 33 9.723 54.492 43.089 1.00 23.29 C
ATOM 127 NZ LYS A 33 8.362 54.034 43.506 1.00 24.12 N
ATOM 128 N LEU A 34 14.710 50.734 39.984 1.00 18.44 N
ATOM 129 CA LEU A 34 15.333 49.438 39.745 1.00 18.87 C
ATOM 130 C LEU A 34 16.849 49.532 39.893 1.00 17.73 C
ATOM 131 O LEU A 34 17.467 48.670 40.511 1.00 18.68 O
ATOM 132 CB LEU A 34 14.987 48.913 38.344 1.00 18.32 C
ATOM 133 CG LEU A 34 15.564 47.519 38.037 1.00 21.49 C
ATOM 134 CD1 LEU A 34 15.099 46.524 39.096 1.00 18.23 C
ATOM 135 CD2 LEU A 34 15.133 47.071 36.637 1.00 20.68 C
ATOM 136 N ALA A 35 17.445 50.581 39.331 1.00 16.96 N
ATOM 137 CA ALA A 35 18.896 50.765 39.407 1.00 17.98 C
ATOM 138 C ALA A 35 19.363 50.810 40.857 1.00 16.81 C
ATOM 139 O ALA A 35 20.388 50.221 41.206 1.00 16.38 O
ATOM 140 CB ALA A 35 19.313 52.054 38.671 1.00 17.12 C
ATOM 141 N LEU A 36 18.603 51.503 41.700 1.00 15.10 N
ATOM 142 CA LEU A 36 18.936 51.609 43.115 1.00 16.95 C
ATOM 143 C LEU A 36 18.742 50.249 43.799 1.00 15.84 C
ATOM 144 O LEU A 36 19.506 49.882 44.686 1.00 16.65 O
ATOM 145 CB LEU A 36 18.064 52.686 43.791 1.00 15.89 C
ATOM 146 CG LEU A 36 18.374 54.132 43.365 1.00 17.84 C
ATOM 147 CD1 LEU A 36 17.394 55.124 44.020 1.00 17.35 C
ATOM 148 CD2 LEU A 36 19.805 54.475 43.769 1.00 18.67 C
ATOM 149 N LEU A 37 17.724 49.496 43.393 1.00 16.58 N
ATOM 150 CA LEU A 37 17.517 48.178 43.996 1.00 17.93 C
ATOM 151 C LEU A 37 18.631 47.227 43.558 1.00 16.78 C
ATOM 152 O LEU A 37 19.149 46.452 44.361 1.00 20.28 O
ATOM 153 CB LEU A 37 16.155 47.585 43.607 1.00 19.85 C
ATOM 154 CG LEU A 37 14.878 48.251 44.118 1.00 21.64 C
ATOM 155 CD1 LEU A 37 13.715 47.253 44.006 1.00 24.31 C
ATOM 156 CD2 LEU A 37 15.053 48.686 45.567 1.00 22.85 C
ATOM 157 N LEU A 38 19.007 47.299 42.285 1.00 17.12 N
ATOM 158 CA LEU A 38 20.064 46.445 41.751 1.00 17.84 C
ATOM 159 C LEU A 38 21.402 46.660 42.441 1.00 16.92 C
ATOM 160 O LEU A 38 22.083 45.694 42.795 1.00 17.42 O
ATOM 161 CB LEU A 38 20.239 46.683 40.249 1.00 15.79 C
ATOM 162 CG LEU A 38 19.065 46.331 39.335 1.00 18.10 C
ATOM 163 CD1 LEU A 38 19.409 46.785 37.926 1.00 16.43 C
ATOM 164 CD2 LEU A 38 18.775 44.827 39.367 1.00 18.87 C
ATOM 165 N THR A 39 21.792 47.923 42.612 1.00 16.79 N
ATOM 166 CA THR A 39 23.056 48.233 43.260 1.00 17.27 C
ATOM 167 C THR A 39 22.971 48.058 44.774 1.00 17.49 C
ATOM 168 O THR A 39 23.994 47.981 45.450 1.00 17.06 O
ATOM 169 CB THR A 39 23.561 49.667 42.893 1.00 17.42 C
ATOM 170 OG1 THR A 39 22.593 50.658 43.277 1.00 16.37 O
ATOM 171 CG2 THR A 39 23.801 49.754 41.390 1.00 16.86 C
ATOM 172 N ALA A 40 21.754 48.001 45.308 1.00 17.63 N
ATOM 173 CA ALA A 40 21.579 47.771 46.738 1.00 17.52 C
ATOM 174 C ALA A 40 21.861 46.283 46.949 1.00 17.58 C
ATOM 175 O ALA A 40 22.390 45.878 47.978 1.00 18.87 O
ATOM 176 CB ALA A 40 20.147 48.101 47.168 1.00 17.29 C
ATOM 177 N VAL A 41 21.502 45.476 45.953 1.00 19.72 N
ATOM 178 CA VAL A 41 21.713 44.029 45.996 1.00 20.48 C
ATOM 179 C VAL A 41 23.166 43.674 45.650 1.00 20.87 C
ATOM 180 O VAL A 41 23.790 42.849 46.316 1.00 22.57 O
ATOM 181 CB VAL A 41 20.742 43.306 45.017 1.00 21.04 C
ATOM 182 CG1 VAL A 41 21.078 41.818 44.923 1.00 23.31 C
ATOM 183 CG2 VAL A 41 19.311 43.479 45.496 1.00 19.23 C
ATOM 184 N ASP A 42 23.705 44.304 44.613 1.00 20.79 N
ATOM 185 CA ASP A 42 25.085 44.051 44.199 1.00 20.13 C
ATOM 186 C ASP A 42 25.808 45.355 43.899 1.00 19.42 C
ATOM 187 O ASP A 42 25.794 45.826 42.769 1.00 18.38 O
ATOM 188 CB ASP A 42 25.116 43.173 42.947 1.00 20.25 C
ATOM 189 CG ASP A 42 26.532 42.809 42.526 1.00 22.64 C
ATOM 190 OD1 ASP A 42 27.490 43.309 43.157 1.00 21.72 O
ATOM 191 OD2 ASP A 42 26.685 42.023 41.568 1.00 23.81 O
ATOM 192 N PRO A 43 26.458 45.956 44.905 1.00 19.40 N
ATOM 193 CA PRO A 43 27.159 47.212 44.626 1.00 21.33 C
ATOM 194 C PRO A 43 28.288 47.068 43.593 1.00 21.15 C
ATOM 195 O PRO A 43 28.769 48.065 43.055 1.00 22.25 O
ATOM 196 CB PRO A 43 27.655 47.646 46.007 1.00 21.80 C
ATOM 197 CG PRO A 43 27.830 46.342 46.736 1.00 22.94 C
ATOM 198 CD PRO A 43 26.591 45.575 46.318 1.00 22.07 C
ATOM 199 N GLY A 44 28.690 45.829 43.312 1.00 21.55 N
ATOM 200 CA GLY A 44 29.743 45.576 42.336 1.00 22.19 C
ATOM 201 C GLY A 44 29.325 45.942 40.921 1.00 23.14 C
ATOM 202 O GLY A 44 30.142 45.970 40.003 1.00 24.81 O
ATOM 203 N ILE A 45 28.040 46.217 40.733 1.00 23.05 N
ATOM 204 CA ILE A 45 27.547 46.603 39.421 1.00 20.93 C
ATOM 205 C ILE A 45 28.193 47.926 39.023 1.00 21.25 C
ATOM 206 O ILE A 45 28.457 48.170 37.848 1.00 21.11 O
ATOM 207 CB ILE A 45 25.999 46.721 39.424 1.00 18.93 C
ATOM 208 CG1 ILE A 45 25.386 45.313 39.399 1.00 18.75 C
ATOM 209 CG2 ILE A 45 25.528 47.550 38.237 1.00 17.17 C
ATOM 210 CD1 ILE A 45 23.882 45.263 39.631 1.00 19.21 C
ATOM 211 N GLY A 46 28.464 48.771 40.015 1.00 21.55 N
ATOM 212 CA GLY A 46 29.095 50.053 39.750 1.00 19.10 C
ATOM 213 C GLY A 46 28.199 51.240 40.060 1.00 17.38 C
ATOM 214 O GLY A 46 27.104 51.081 40.590 1.00 16.67 O
ATOM 215 N GLY A 47 28.664 52.433 39.716 1.00 18.76 N
ATOM 216 CA GLY A 47 27.890 53.639 39.973 1.00 20.78 C
ATOM 217 C GLY A 47 26.673 53.807 39.080 1.00 21.26 C
ATOM 218 O GLY A 47 26.582 53.208 38.004 1.00 21.39 O
ATOM 219 N VAL A 48 25.729 54.625 39.534 1.00 21.17 N
ATOM 220 CA VAL A 48 24.513 54.882 38.776 1.00 21.64 C
ATOM 221 C VAL A 48 24.540 56.313 38.238 1.00 22.57 C
ATOM 222 O VAL A 48 24.801 57.263 38.980 1.00 19.90 O
ATOM 223 CB VAL A 48 23.257 54.690 39.654 1.00 20.38 C
ATOM 224 CG1 VAL A 48 22.002 55.004 38.849 1.00 19.32 C
ATOM 225 CG2 VAL A 48 23.201 53.253 40.182 1.00 18.52 C
ATOM 226 N LEU A 49 24.283 56.449 36.941 1.00 22.44 N
ATOM 227 CA LEU A 49 24.274 57.746 36.283 1.00 24.14 C
ATOM 228 C LEU A 49 22.827 58.102 35.958 1.00 23.61 C
ATOM 229 O LEU A 49 22.133 57.378 35.237 1.00 23.13 O
ATOM 230 CB LEU A 49 25.117 57.689 35.004 1.00 27.65 C
ATOM 231 CG LEU A 49 25.454 59.017 34.323 1.00 32.42 C
ATOM 232 CD1 LEU A 49 26.183 59.922 35.305 1.00 33.90 C
ATOM 233 CD2 LEU A 49 26.330 58.759 33.109 1.00 34.86 C
ATOM 234 N VAL A 50 22.374 59.218 36.512 1.00 25.27 N
ATOM 235 CA VAL A 50 21.002 59.675 36.315 1.00 28.08 C
ATOM 236 C VAL A 50 20.897 60.872 35.365 1.00 30.40 C
ATOM 237 O VAL A 50 21.344 61.965 35.695 1.00 29.96 O
ATOM 238 CB VAL A 50 20.377 60.077 37.667 1.00 26.72 C
ATOM 239 CG1 VAL A 50 18.961 60.548 37.461 1.00 26.70 C
ATOM 240 CG2 VAL A 50 20.428 58.904 38.637 1.00 24.43 C
ATOM 241 N PHE A 51 20.301 60.666 34.197 1.00 32.67 N
ATOM 242 CA PHE A 51 20.133 61.750 33.233 1.00 37.56 C
ATOM 243 C PHE A 51 18.733 62.337 33.349 1.00 41.21 C
ATOM 244 O PHE A 51 17.748 61.599 33.410 1.00 40.35 O
ATOM 245 CB PHE A 51 20.323 61.241 31.802 1.00 38.76 C
ATOM 246 CG PHE A 51 21.739 60.891 31.462 1.00 40.71 C
ATOM 247 CD1 PHE A 51 22.765 61.823 31.623 1.00 41.22 C
ATOM 248 CD2 PHE A 51 22.048 59.628 30.971 1.00 41.02 C
ATOM 249 CE1 PHE A 51 24.082 61.499 31.300 1.00 42.14 C
ATOM 250 CE2 PHE A 51 23.357 59.291 30.644 1.00 41.89 C
ATOM 251 CZ PHE A 51 24.378 60.230 30.808 1.00 42.80 C
ATOM 252 N GLY A 52 18.644 63.663 33.361 1.00 44.56 N
ATOM 253 CA GLY A 52 17.342 64.297 33.447 1.00 50.05 C
ATOM 254 C GLY A 52 17.404 65.799 33.621 1.00 53.69 C
ATOM 255 O GLY A 52 18.481 66.382 33.780 1.00 53.34 O
ATOM 256 N ASP A 53 16.241 66.436 33.585 1.00 57.25 N
ATOM 257 CA ASP A 53 16.198 67.867 33.747 1.00 60.56 C
ATOM 258 C ASP A 53 16.171 68.226 35.219 1.00 62.39 C
ATOM 259 O ASP A 53 15.965 67.391 36.103 1.00 62.65 O
ATOM 260 CB ASP A 53 14.976 68.468 33.027 1.00 61.66 C
ATOM 261 CG ASP A 53 13.667 67.800 33.422 1.00 63.20 C
ATOM 262 OD1 ASP A 53 13.110 68.183 34.473 1.00 64.05 O
ATOM 263 OD2 ASP A 53 13.200 66.896 32.690 1.00 63.79 O
ATOM 264 N ARG A 54 16.439 69.499 35.436 1.00 64.90 N
ATOM 265 CA ARG A 54 16.455 70.177 36.718 1.00 66.87 C
ATOM 266 C ARG A 54 15.489 69.687 37.825 1.00 66.64 C
ATOM 267 O ARG A 54 15.927 69.179 38.853 1.00 66.87 O
ATOM 268 CB ARG A 54 16.196 71.647 36.405 1.00 69.85 C
ATOM 269 CG ARG A 54 15.095 71.757 35.349 1.00 73.04 C
ATOM 270 CD ARG A 54 15.336 72.780 34.251 1.00 74.85 C
ATOM 271 NE ARG A 54 14.185 72.774 33.353 1.00 76.92 N
ATOM 272 CZ ARG A 54 13.957 73.673 32.402 1.00 78.20 C
ATOM 273 NH1 ARG A 54 14.805 74.675 32.196 1.00 78.39 N
ATOM 274 NH2 ARG A 54 12.856 73.587 31.670 1.00 78.75 N
ATOM 275 N GLY A 55 14.186 69.848 37.622 1.00 66.08 N
ATOM 276 CA GLY A 55 13.233 69.473 38.652 1.00 65.02 C
ATOM 277 C GLY A 55 12.858 68.020 38.852 1.00 64.40 C
ATOM 278 O GLY A 55 11.803 67.748 39.467 1.00 65.05 O
ATOM 279 N THR A 56 13.658 67.075 38.369 1.00 63.12 N
ATOM 280 CA THR A 56 13.281 65.665 38.525 1.00 61.70 C
ATOM 281 C THR A 56 13.429 65.105 39.963 1.00 60.23 C
ATOM 282 O THR A 56 12.978 64.022 40.245 1.00 61.74 O
ATOM 283 CB THR A 56 14.157 64.767 37.550 1.00 62.53 C
ATOM 284 OG1 THR A 56 15.559 64.965 37.815 1.00 64.33 O
ATOM 285 CG2 THR A 56 13.914 65.105 36.106 1.00 62.86 C
ATOM 286 N GLY A 57 14.059 65.900 40.828 1.00 57.53 N
ATOM 287 CA GLY A 57 14.373 65.567 42.201 1.00 53.65 C
ATOM 288 C GLY A 57 15.082 64.254 42.141 1.00 51.25 C
ATOM 289 O GLY A 57 14.602 63.274 42.652 1.00 52.52 O
ATOM 290 N LYS A 58 16.253 64.221 41.529 1.00 47.73 N
ATOM 291 CA LYS A 58 16.975 62.945 41.403 1.00 44.60 C
ATOM 292 C LYS A 58 17.598 62.313 42.640 1.00 40.84 C
ATOM 293 O LYS A 58 18.009 61.165 42.584 1.00 43.11 O
ATOM 294 CB LYS A 58 18.053 63.045 40.323 1.00 45.43 C
ATOM 295 CG LYS A 58 17.506 63.504 39.005 1.00 47.37 C
ATOM 296 CD LYS A 58 18.643 63.919 38.076 1.00 49.87 C
ATOM 297 CE LYS A 58 18.090 64.382 36.718 1.00 51.85 C
ATOM 298 NZ LYS A 58 19.154 64.874 35.772 1.00 56.08 N
ATOM 299 N SER A 59 17.688 63.039 43.748 1.00 34.58 N
ATOM 300 CA SER A 59 18.271 62.462 44.958 1.00 30.16 C
ATOM 301 C SER A 59 17.200 61.993 45.942 1.00 27.19 C
ATOM 302 O SER A 59 17.504 61.392 46.974 1.00 23.25 O
ATOM 303 CB SER A 59 19.196 63.469 45.643 1.00 29.36 C
ATOM 304 OG SER A 59 18.466 64.510 46.253 1.00 28.64 O
ATOM 305 N THR A 60 15.945 62.269 45.609 1.00 26.58 N
ATOM 306 CA THR A 60 14.831 61.866 46.459 1.00 26.01 C
ATOM 307 C THR A 60 14.824 60.349 46.611 1.00 22.75 C
ATOM 308 O THR A 60 14.756 59.839 47.726 1.00 21.25 O
ATOM 309 CB THR A 60 13.454 62.307 45.875 1.00 27.02 C
ATOM 310 OG1 THR A 60 13.416 63.735 45.751 1.00 30.42 O
ATOM 311 CG2 THR A 60 12.307 61.861 46.803 1.00 27.76 C
ATOM 312 N ALA A 61 14.892 59.646 45.481 1.00 19.78 N
ATOM 313 CA ALA A 61 14.894 58.187 45.454 1.00 18.26 C
ATOM 314 C ALA A 61 16.084 57.603 46.213 1.00 16.54 C
ATOM 315 O ALA A 61 15.957 56.579 46.890 1.00 16.59 O
ATOM 316 CB ALA A 61 14.906 57.691 44.004 1.00 19.74 C
ATOM 317 N VAL A 62 17.241 58.246 46.094 1.00 15.94 N
ATOM 318 CA VAL A 62 18.442 57.775 46.782 1.00 16.68 C
ATOM 319 C VAL A 62 18.263 57.872 48.302 1.00 14.96 C
ATOM 320 O VAL A 62 18.515 56.916 49.024 1.00 16.40 O
ATOM 321 CB VAL A 62 19.693 58.596 46.343 1.00 17.97 C
ATOM 322 CG1 VAL A 62 20.916 58.163 47.153 1.00 16.21 C
ATOM 323 CG2 VAL A 62 19.954 58.383 44.839 1.00 18.05 C
ATOM 324 N ARG A 63 17.817 59.028 48.782 1.00 15.40 N
ATOM 325 CA ARG A 63 17.598 59.224 50.209 1.00 16.88 C
ATOM 326 C ARG A 63 16.496 58.313 50.742 1.00 15.71 C
ATOM 327 O ARG A 63 16.566 57.835 51.876 1.00 13.41 O
ATOM 328 CB ARG A 63 17.268 60.693 50.486 1.00 18.86 C
ATOM 329 CG ARG A 63 18.508 61.562 50.392 1.00 22.98 C
ATOM 330 CD ARG A 63 18.244 63.044 50.532 1.00 28.28 C
ATOM 331 NE ARG A 63 19.519 63.761 50.516 1.00 30.94 N
ATOM 332 CZ ARG A 63 20.386 63.759 51.525 1.00 32.55 C
ATOM 333 NH1 ARG A 63 20.114 63.091 52.641 1.00 30.69 N
ATOM 334 NH2 ARG A 63 21.541 64.400 51.409 1.00 33.31 N
ATOM 335 N ALA A 64 15.489 58.064 49.915 1.00 13.37 N
ATOM 336 CA ALA A 64 14.395 57.187 50.315 1.00 15.56 C
ATOM 337 C ALA A 64 14.917 55.755 50.452 1.00 15.76 C
ATOM 338 O ALA A 64 14.576 55.046 51.403 1.00 16.00 O
ATOM 339 CB ALA A 64 13.266 57.243 49.277 1.00 13.83 C
ATOM 340 N LEU A 65 15.739 55.324 49.501 1.00 15.74 N
ATOM 341 CA LEU A 65 16.282 53.969 49.567 1.00 17.35 C
ATOM 342 C LEU A 65 17.133 53.843 50.827 1.00 16.88 C
ATOM 343 O LEU A 65 16.986 52.897 51.605 1.00 18.55 O
ATOM 344 CB LEU A 65 17.143 53.659 48.335 1.00 17.92 C
ATOM 345 CG LEU A 65 17.769 52.257 48.343 1.00 21.79 C
ATOM 346 CD1 LEU A 65 16.671 51.192 48.333 1.00 19.73 C
ATOM 347 CD2 LEU A 65 18.681 52.101 47.134 1.00 23.94 C
ATOM 348 N ALA A 66 18.004 54.819 51.047 1.00 16.69 N
ATOM 349 CA ALA A 66 18.885 54.783 52.215 1.00 19.02 C
ATOM 350 C ALA A 66 18.077 54.715 53.510 1.00 18.91 C
ATOM 351 O ALA A 66 18.483 54.065 54.493 1.00 21.20 O
ATOM 352 CB ALA A 66 19.801 56.011 52.225 1.00 15.18 C
ATOM 353 N ALA A 67 16.931 55.393 53.503 1.00 19.07 N
ATOM 354 CA ALA A 67 16.052 55.425 54.671 1.00 19.15 C
ATOM 355 C ALA A 67 15.255 54.162 54.904 1.00 18.92 C
ATOM 356 O ALA A 67 14.779 53.937 56.006 1.00 20.09 O
ATOM 357 CB ALA A 67 15.075 56.609 54.599 1.00 17.71 C
ATOM 358 N LEU A 68 15.056 53.358 53.870 1.00 18.44 N
ATOM 359 CA LEU A 68 14.300 52.122 54.069 1.00 20.02 C
ATOM 360 C LEU A 68 15.229 50.957 54.410 1.00 20.88 C
ATOM 361 O LEU A 68 14.784 49.882 54.839 1.00 23.13 O
ATOM 362 CB LEU A 68 13.431 51.787 52.846 1.00 21.56 C
ATOM 363 CG LEU A 68 13.976 51.255 51.524 1.00 23.29 C
ATOM 364 CD1 LEU A 68 14.436 49.804 51.640 1.00 22.31 C
ATOM 365 CD2 LEU A 68 12.847 51.332 50.517 1.00 23.99 C
ATOM 366 N LEU A 69 16.528 51.174 54.232 1.00 19.38 N
ATOM 367 CA LEU A 69 17.487 50.133 54.558 1.00 18.16 C
ATOM 368 C LEU A 69 17.708 50.121 56.063 1.00 16.15 C
ATOM 369 O LEU A 69 17.594 51.150 56.727 1.00 13.28 O
ATOM 370 CB LEU A 69 18.831 50.362 53.842 1.00 16.57 C
ATOM 371 CG LEU A 69 18.857 50.188 52.316 1.00 18.06 C
ATOM 372 CD1 LEU A 69 20.238 50.554 51.771 1.00 16.49 C
ATOM 373 CD2 LEU A 69 18.493 48.754 51.944 1.00 19.97 C
ATOM 374 N PRO A 70 18.005 48.942 56.625 1.00 16.80 N
ATOM 375 CA PRO A 70 18.244 48.827 58.066 1.00 16.13 C
ATOM 376 C PRO A 70 19.330 49.815 58.479 1.00 16.39 C
ATOM 377 O PRO A 70 20.236 50.093 57.701 1.00 16.90 O
ATOM 378 CB PRO A 70 18.718 47.376 58.217 1.00 17.97 C
ATOM 379 CG PRO A 70 17.993 46.673 57.112 1.00 15.12 C
ATOM 380 CD PRO A 70 18.114 47.629 55.958 1.00 15.10 C
ATOM 381 N GLU A 71 19.243 50.356 59.689 1.00 16.98 N
ATOM 382 CA GLU A 71 20.269 51.280 60.153 1.00 20.30 C
ATOM 383 C GLU A 71 21.535 50.463 60.390 1.00 21.06 C
ATOM 384 O GLU A 71 21.461 49.274 60.704 1.00 20.90 O
ATOM 385 CB GLU A 71 19.853 51.954 61.458 1.00 20.85 C
ATOM 386 CG GLU A 71 18.616 52.822 61.345 1.00 26.90 C
ATOM 387 CD GLU A 71 18.530 53.828 62.471 1.00 30.24 C
ATOM 388 OE1 GLU A 71 18.664 53.423 63.644 1.00 31.68 O
ATOM 389 OE2 GLU A 71 18.329 55.024 62.183 1.00 34.51 O
ATOM 390 N ILE A 72 22.692 51.099 60.247 1.00 20.81 N
ATOM 391 CA ILE A 72 23.966 50.409 60.433 1.00 20.35 C
ATOM 392 C ILE A 72 24.543 50.617 61.828 1.00 20.96 C
ATOM 393 O ILE A 72 24.312 51.644 62.464 1.00 20.13 O
ATOM 394 CB ILE A 72 25.015 50.893 59.421 1.00 20.37 C
ATOM 395 CG1 ILE A 72 25.239 52.404 59.589 1.00 22.16 C
ATOM 396 CG2 ILE A 72 24.566 50.555 58.016 1.00 22.39 C
ATOM 397 CD1 ILE A 72 26.448 52.952 58.846 1.00 23.88 C
ATOM 398 N GLU A 73 25.298 49.636 62.304 1.00 21.55 N
ATOM 399 CA GLU A 73 25.915 49.756 63.611 1.00 22.41 C
ATOM 400 C GLU A 73 27.299 50.373 63.399 1.00 21.29 C
ATOM 401 O GLU A 73 28.015 50.006 62.473 1.00 21.91 O
ATOM 402 CB GLU A 73 26.026 48.382 64.283 1.00 22.48 C
ATOM 403 CG GLU A 73 27.229 47.541 63.876 1.00 24.42 C
ATOM 404 CD GLU A 73 27.095 46.887 62.511 1.00 25.38 C
ATOM 405 OE1 GLU A 73 26.113 47.158 61.791 1.00 26.51 O
ATOM 406 OE2 GLU A 73 27.988 46.090 62.157 1.00 28.54 O
ATOM 407 N ALA A 74 27.672 51.319 64.246 1.00 21.49 N
ATOM 408 CA ALA A 74 28.973 51.956 64.099 1.00 22.65 C
ATOM 409 C ALA A 74 29.411 52.633 65.379 1.00 22.49 C
ATOM 410 O ALA A 74 28.578 53.018 66.201 1.00 21.88 O
ATOM 411 CB ALA A 74 28.917 52.985 62.979 1.00 21.13 C
ATOM 412 N VAL A 75 30.724 52.787 65.531 1.00 22.81 N
ATOM 413 CA VAL A 75 31.282 53.468 66.690 1.00 23.39 C
ATOM 414 C VAL A 75 30.831 54.924 66.586 1.00 23.72 C
ATOM 415 O VAL A 75 31.102 55.609 65.597 1.00 24.21 O
ATOM 416 CB VAL A 75 32.835 53.389 66.708 1.00 22.44 C
ATOM 417 CG1 VAL A 75 33.385 54.176 67.889 1.00 22.46 C
ATOM 418 CG2 VAL A 75 33.286 51.923 66.799 1.00 22.21 C
ATOM 419 N GLU A 76 30.136 55.383 67.617 1.00 25.29 N
ATOM 420 CA GLU A 76 29.592 56.734 67.665 1.00 27.12 C
ATOM 421 C GLU A 76 30.518 57.866 67.220 1.00 27.02 C
ATOM 422 O GLU A 76 30.127 58.705 66.410 1.00 26.71 O
ATOM 423 CB GLU A 76 29.060 57.013 69.076 1.00 28.56 C
ATOM 424 CG GLU A 76 28.613 58.438 69.301 1.00 32.12 C
ATOM 425 CD GLU A 76 27.745 58.587 70.534 1.00 34.95 C
ATOM 426 OE1 GLU A 76 28.026 57.926 71.558 1.00 37.38 O
ATOM 427 OE2 GLU A 76 26.787 59.379 70.480 1.00 36.40 O
ATOM 428 N GLY A 77 31.738 57.903 67.738 1.00 27.70 N
ATOM 429 CA GLY A 77 32.635 58.975 67.346 1.00 28.28 C
ATOM 430 C GLY A 77 33.511 58.728 66.127 1.00 27.32 C
ATOM 431 O GLY A 77 34.336 59.576 65.779 1.00 27.63 O
ATOM 432 N CYS A 78 33.339 57.595 65.455 1.00 25.88 N
ATOM 433 CA CYS A 78 34.186 57.311 64.307 1.00 23.25 C
ATOM 434 C CYS A 78 33.842 58.057 63.025 1.00 21.88 C
ATOM 435 O CYS A 78 32.723 57.971 62.525 1.00 19.66 O
ATOM 436 CB CYS A 78 34.220 55.817 64.014 1.00 23.31 C
ATOM 437 SG CYS A 78 35.401 55.466 62.701 1.00 23.00 S
ATOM 438 N PRO A 79 34.824 58.784 62.460 1.00 21.56 N
ATOM 439 CA PRO A 79 34.620 59.547 61.224 1.00 21.87 C
ATOM 440 C PRO A 79 34.330 58.693 59.994 1.00 21.51 C
ATOM 441 O PRO A 79 33.786 59.190 59.010 1.00 21.71 O
ATOM 442 CB PRO A 79 35.916 60.354 61.095 1.00 22.89 C
ATOM 443 CG PRO A 79 36.936 59.451 61.731 1.00 24.02 C
ATOM 444 CD PRO A 79 36.207 58.935 62.953 1.00 22.63 C
ATOM 445 N VAL A 80 34.688 57.414 60.039 1.00 20.12 N
ATOM 446 CA VAL A 80 34.426 56.538 58.902 1.00 20.93 C
ATOM 447 C VAL A 80 33.398 55.458 59.221 1.00 19.81 C
ATOM 448 O VAL A 80 33.281 54.470 58.499 1.00 22.02 O
ATOM 449 CB VAL A 80 35.729 55.861 58.379 1.00 21.15 C
ATOM 450 CG1 VAL A 80 36.732 56.918 57.988 1.00 19.74 C
ATOM 451 CG2 VAL A 80 36.313 54.927 59.434 1.00 18.40 C
ATOM 452 N SER A 81 32.646 55.653 60.302 1.00 21.13 N
ATOM 453 CA SER A 81 31.609 54.705 60.707 1.00 20.66 C
ATOM 454 C SER A 81 32.126 53.280 60.908 1.00 21.86 C
ATOM 455 O SER A 81 31.498 52.322 60.454 1.00 20.56 O
ATOM 456 CB SER A 81 30.477 54.683 59.664 1.00 22.12 C
ATOM 457 OG SER A 81 29.992 55.989 59.387 1.00 19.87 O
ATOM 458 N SER A 82 33.267 53.128 61.580 1.00 22.28 N
ATOM 459 CA SER A 82 33.802 51.789 61.815 1.00 22.10 C
ATOM 460 C SER A 82 32.734 50.942 62.502 1.00 22.76 C
ATOM 461 O SER A 82 32.042 51.412 63.402 1.00 24.57 O
ATOM 462 CB SER A 82 35.057 51.839 62.704 1.00 21.56 C
ATOM 463 OG SER A 82 36.101 52.563 62.079 1.00 20.78 O
ATOM 464 N PRO A 83 32.570 49.687 62.064 1.00 24.50 N
ATOM 465 CA PRO A 83 31.585 48.763 62.635 1.00 25.24 C
ATOM 466 C PRO A 83 31.891 48.476 64.107 1.00 26.48 C
ATOM 467 O PRO A 83 31.000 48.140 64.885 1.00 25.56 O
ATOM 468 CB PRO A 83 31.733 47.518 61.760 1.00 24.35 C
ATOM 469 CG PRO A 83 32.136 48.087 60.440 1.00 24.78 C
ATOM 470 CD PRO A 83 33.159 49.127 60.835 1.00 23.73 C
ATOM 471 N ASN A 84 33.161 48.609 64.478 1.00 27.02 N
ATOM 472 CA ASN A 84 33.587 48.377 65.854 1.00 27.96 C
ATOM 473 C ASN A 84 34.920 49.078 66.144 1.00 28.71 C
ATOM 474 O ASN A 84 35.609 49.537 65.229 1.00 26.77 O
ATOM 475 CB ASN A 84 33.716 46.874 66.122 1.00 29.30 C
ATOM 476 CG ASN A 84 34.727 46.211 65.218 1.00 28.91 C
ATOM 477 OD1 ASN A 84 34.392 45.309 64.446 1.00 29.72 O
ATOM 478 ND2 ASN A 84 35.974 46.655 65.302 1.00 28.27 N
ATOM 479 N VAL A 85 35.276 49.155 67.423 1.00 29.47 N
ATOM 480 CA VAL A 85 36.506 49.815 67.848 1.00 31.32 C
ATOM 481 C VAL A 85 37.771 49.303 67.157 1.00 31.80 C
ATOM 482 O VAL A 85 38.648 50.087 66.804 1.00 31.07 O
ATOM 483 CB VAL A 85 36.675 49.699 69.381 1.00 34.43 C
ATOM 484 CG1 VAL A 85 38.018 50.262 69.806 1.00 37.24 C
ATOM 485 CG2 VAL A 85 35.545 50.460 70.084 1.00 33.37 C
ATOM 486 N GLU A 86 37.853 47.993 66.946 1.00 33.26 N
ATOM 487 CA GLU A 86 39.020 47.391 66.312 1.00 34.57 C
ATOM 488 C GLU A 86 39.286 47.860 64.880 1.00 34.93 C
ATOM 489 O GLU A 86 40.432 47.846 64.424 1.00 32.96 O
ATOM 490 CB GLU A 86 38.905 45.861 66.354 1.00 38.23 C
ATOM 491 CG GLU A 86 39.063 45.269 67.758 1.00 41.91 C
ATOM 492 CD GLU A 86 37.899 45.601 68.684 1.00 45.76 C
ATOM 493 OE1 GLU A 86 36.787 45.864 68.172 1.00 46.62 O
ATOM 494 OE2 GLU A 86 38.092 45.587 69.923 1.00 45.65 O
ATOM 495 N MET A 87 38.242 48.289 64.174 1.00 33.36 N
ATOM 496 CA MET A 87 38.410 48.751 62.800 1.00 31.99 C
ATOM 497 C MET A 87 38.654 50.255 62.678 1.00 30.38 C
ATOM 498 O MET A 87 38.809 50.781 61.578 1.00 28.80 O
ATOM 499 CB MET A 87 37.197 48.358 61.965 1.00 33.52 C
ATOM 500 CG MET A 87 37.065 46.867 61.757 1.00 37.41 C
ATOM 501 SD MET A 87 35.565 46.456 60.869 1.00 40.11 S
ATOM 502 CE MET A 87 36.093 46.763 59.169 1.00 39.14 C
ATOM 503 N ILE A 88 38.685 50.952 63.804 1.00 29.62 N
ATOM 504 CA ILE A 88 38.927 52.386 63.772 1.00 30.13 C
ATOM 505 C ILE A 88 40.339 52.656 63.258 1.00 31.76 C
ATOM 506 O ILE A 88 41.315 52.132 63.794 1.00 33.79 O
ATOM 507 CB ILE A 88 38.781 53.007 65.170 1.00 29.27 C
ATOM 508 CG1 ILE A 88 37.326 52.905 65.636 1.00 26.40 C
ATOM 509 CG2 ILE A 88 39.228 54.465 65.144 1.00 27.39 C
ATOM 510 CD1 ILE A 88 37.126 53.339 67.053 1.00 23.72 C
ATOM 511 N PRO A 89 40.466 53.471 62.200 1.00 31.28 N
ATOM 512 CA PRO A 89 41.781 53.792 61.639 1.00 31.38 C
ATOM 513 C PRO A 89 42.709 54.413 62.685 1.00 31.66 C
ATOM 514 O PRO A 89 42.270 55.177 63.546 1.00 31.52 O
ATOM 515 CB PRO A 89 41.443 54.769 60.517 1.00 31.42 C
ATOM 516 CG PRO A 89 40.094 54.294 60.061 1.00 30.57 C
ATOM 517 CD PRO A 89 39.391 54.054 61.377 1.00 30.89 C
ATOM 518 N ASP A 90 43.993 54.085 62.595 1.00 32.60 N
ATOM 519 CA ASP A 90 44.993 54.592 63.527 1.00 33.82 C
ATOM 520 C ASP A 90 45.118 56.107 63.513 1.00 32.03 C
ATOM 521 O ASP A 90 45.406 56.722 64.541 1.00 32.41 O
ATOM 522 CB ASP A 90 46.353 53.968 63.213 1.00 38.77 C
ATOM 523 CG ASP A 90 46.399 52.498 63.546 1.00 43.28 C
ATOM 524 OD1 ASP A 90 45.676 52.078 64.479 1.00 47.53 O
ATOM 525 OD2 ASP A 90 47.163 51.764 62.883 1.00 45.68 O
ATOM 526 N TRP A 91 44.909 56.711 62.352 1.00 28.68 N
ATOM 527 CA TRP A 91 45.010 58.160 62.246 1.00 28.77 C
ATOM 528 C TRP A 91 43.819 58.842 62.906 1.00 29.94 C
ATOM 529 O TRP A 91 43.866 60.033 63.212 1.00 29.79 O
ATOM 530 CB TRP A 91 45.072 58.586 60.780 1.00 26.52 C
ATOM 531 CG TRP A 91 43.926 58.070 59.945 1.00 26.86 C
ATOM 532 CD1 TRP A 91 43.937 56.979 59.125 1.00 26.81 C
ATOM 533 CD2 TRP A 91 42.607 58.628 59.845 1.00 24.26 C
ATOM 534 NE1 TRP A 91 42.717 56.834 58.510 1.00 25.51 N
ATOM 535 CE2 TRP A 91 41.887 57.842 58.924 1.00 24.99 C
ATOM 536 CE3 TRP A 91 41.979 59.741 60.421 1.00 23.90 C
ATOM 537 CZ2 TRP A 91 40.546 58.105 58.594 1.00 23.20 C
ATOM 538 CZ3 TRP A 91 40.649 60.005 60.090 1.00 23.74 C
ATOM 539 CH2 TRP A 91 39.954 59.199 59.174 1.00 22.00 C
ATOM 540 N ALA A 92 42.747 58.083 63.112 1.00 30.15 N
ATOM 541 CA ALA A 92 41.543 58.631 63.705 1.00 30.57 C
ATOM 542 C ALA A 92 41.610 58.691 65.222 1.00 31.55 C
ATOM 543 O ALA A 92 42.177 57.820 65.883 1.00 31.42 O
ATOM 544 CB ALA A 92 40.325 57.819 63.263 1.00 30.08 C
ATOM 545 N THR A 93 41.027 59.744 65.767 1.00 33.13 N
ATOM 546 CA THR A 93 40.984 59.927 67.202 1.00 34.37 C
ATOM 547 C THR A 93 39.514 59.912 67.611 1.00 34.76 C
ATOM 548 O THR A 93 38.785 60.886 67.403 1.00 35.94 O
ATOM 549 CB THR A 93 41.676 61.251 67.604 1.00 35.69 C
ATOM 550 OG1 THR A 93 43.088 61.017 67.752 1.00 38.51 O
ATOM 551 CG2 THR A 93 41.100 61.787 68.907 1.00 35.48 C
ATOM 552 N VAL A 94 39.084 58.781 68.166 1.00 32.94 N
ATOM 553 CA VAL A 94 37.701 58.597 68.591 1.00 32.52 C
ATOM 554 C VAL A 94 37.586 58.464 70.100 1.00 34.61 C
ATOM 555 O VAL A 94 38.208 57.591 70.708 1.00 35.15 O
ATOM 556 CB VAL A 94 37.071 57.335 67.953 1.00 31.92 C
ATOM 557 CG1 VAL A 94 35.620 57.192 68.413 1.00 29.91 C
ATOM 558 CG2 VAL A 94 37.155 57.414 66.432 1.00 28.61 C
ATOM 559 N LEU A 95 36.781 59.335 70.697 1.00 35.47 N
ATOM 560 CA LEU A 95 36.564 59.326 72.134 1.00 37.80 C
ATOM 561 C LEU A 95 35.323 58.499 72.462 1.00 39.22 C
ATOM 562 O LEU A 95 35.345 57.671 73.371 1.00 40.71 O
ATOM 563 CB LEU A 95 36.409 60.762 72.647 1.00 38.14 C
ATOM 564 CG LEU A 95 37.589 61.698 72.330 1.00 39.78 C
ATOM 565 CD1 LEU A 95 37.329 63.072 72.925 1.00 39.95 C
ATOM 566 CD2 LEU A 95 38.881 61.118 72.885 1.00 38.78 C
ATOM 567 N SER A 96 34.246 58.715 71.712 1.00 40.57 N
ATOM 568 CA SER A 96 33.009 57.970 71.924 1.00 41.20 C
ATOM 569 C SER A 96 33.136 56.614 71.236 1.00 42.02 C
ATOM 570 O SER A 96 32.849 56.485 70.043 1.00 41.67 O
ATOM 571 CB SER A 96 31.813 58.731 71.334 1.00 42.03 C
ATOM 572 OG SER A 96 31.726 60.048 71.853 1.00 42.81 O
ATOM 573 N THR A 97 33.561 55.604 71.991 1.00 41.92 N
ATOM 574 CA THR A 97 33.731 54.261 71.444 1.00 43.02 C
ATOM 575 C THR A 97 32.469 53.401 71.507 1.00 42.62 C
ATOM 576 O THR A 97 32.497 52.247 71.083 1.00 44.02 O
ATOM 577 CB THR A 97 34.848 53.499 72.168 1.00 43.38 C
ATOM 578 OG1 THR A 97 34.526 53.405 73.560 1.00 44.87 O
ATOM 579 CG2 THR A 97 36.178 54.203 71.979 1.00 43.38 C
ATOM 580 N ASN A 98 31.372 53.947 72.032 1.00 41.58 N
ATOM 581 CA ASN A 98 30.115 53.198 72.114 1.00 40.66 C
ATOM 582 C ASN A 98 29.556 52.929 70.722 1.00 37.83 C
ATOM 583 O ASN A 98 29.539 53.814 69.875 1.00 37.94 O
ATOM 584 CB ASN A 98 29.080 53.982 72.924 1.00 43.35 C
ATOM 585 CG ASN A 98 29.076 53.606 74.396 1.00 47.38 C
ATOM 586 OD1 ASN A 98 28.798 54.442 75.261 1.00 49.36 O
ATOM 587 ND2 ASN A 98 29.359 52.339 74.686 1.00 48.68 N
ATOM 588 N VAL A 99 29.109 51.703 70.489 1.00 35.17 N
ATOM 589 CA VAL A 99 28.530 51.352 69.203 1.00 32.32 C
ATOM 590 C VAL A 99 27.054 51.717 69.223 1.00 31.10 C
ATOM 591 O VAL A 99 26.351 51.422 70.187 1.00 29.66 O
ATOM 592 CB VAL A 99 28.656 49.848 68.916 1.00 32.08 C
ATOM 593 CG1 VAL A 99 27.956 49.506 67.602 1.00 30.62 C
ATOM 594 CG2 VAL A 99 30.127 49.457 68.853 1.00 32.54 C
ATOM 595 N ILE A 100 26.588 52.372 68.163 1.00 29.36 N
ATOM 596 CA ILE A 100 25.186 52.767 68.066 1.00 28.33 C
ATOM 597 C ILE A 100 24.633 52.392 66.709 1.00 27.22 C