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755e9b9
HEADER TRANSLATION 13-FEB-25 9NB9
TITLE VIRAL PROTEIN DP71L IN COMPLEX WITH PHOSPHORYLATED EIF2ALPHA (NTD) AND
TITLE 2 PROTEIN PHOSPHATASE 1A (D64A), STABILIZED BY G-ACTIN/DNASEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DP71L;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: MYD116 HOMOLOG;
COMPND 5 ENGINEERED: YES;
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AFRICAN SWINE FEVER VIRUS;
SOURCE 3 ORGANISM_TAXID: 10497;
SOURCE 4 GENE: PRET-172;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: PPP1CA, PPP1A;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 16 ORGANISM_COMMON: RABBIT;
SOURCE 17 ORGANISM_TAXID: 9986;
SOURCE 18 MOL_ID: 4;
SOURCE 19 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 20 ORGANISM_COMMON: DOMESTIC CATTLE;
SOURCE 21 ORGANISM_TAXID: 9913;
SOURCE 22 MOL_ID: 5;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 GENE: EIF2S1, EIF2A;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHATASE, COMPLEX, ISR, TRANSLATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR L.C.REINEKE,U.DALWADI,T.CROLL,C.ARTHUR,D.J.LEE,A.FROST,M.COSTA-
AUTHOR 2 MATTIOLI
REVDAT 1 09-JUL-25 9NB9 0
JRNL AUTH L.C.REINEKE,P.J.ZHU,U.DALWADI,S.W.DOOLING,Y.LIU,I.C.WANG,
JRNL AUTH 2 S.YOUNG-BAIRD,J.OKOH,S.K.KUNCHA,H.ZHOU,A.KANNAN,H.PARK,
JRNL AUTH 3 N.A.DEBEAUBIEN,T.CROLL,D.J.LEE,C.ARTHUR,T.E.DEVER,P.WALTER,
JRNL AUTH 4 J.CHEN,A.FROST,M.COSTA-MATTIOLI
JRNL TITL HARNESSING THE EVOLUTION OF PROTEOSTASIS NETWORKS TO REVERSE
JRNL TITL 2 COGNITIVE DYSFUNCTION.
JRNL REF BIORXIV 2025
JRNL REFN ISSN 2692-8205
JRNL PMID 40568171
JRNL DOI 10.1101/2025.02.28.640897
REMARK 2
REMARK 2 RESOLUTION. 3.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF
REMARK 3 CHIMERAX, ISOLDE, ISOLDE, SERVALCAT,
REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC,
REMARK 3 CRYOSPARC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.030
REMARK 3 NUMBER OF PARTICLES : 309745
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 9NB9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-25.
REMARK 100 THE DEPOSITION ID IS D_1000292753.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : PP1A HOLO-PHOSPHATASE COMPLEX
REMARK 245 WITH VIRAL PROTEIN DP71L, G-
REMARK 245 ACTIN, DNASEI, AND SUBSTRATE
REMARK 245 PHOSPHO-EIF2ALPHA (2-187)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.50
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : 3.5 UL VOLUME, -5 BLOT FORCE,
REMARK 245 1.5 BLOT TIME
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 5236
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 130000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, E, 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 B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 ARG B 4
REMARK 465 ARG B 5
REMARK 465 ARG B 6
REMARK 465 LYS B 7
REMARK 465 LYS B 8
REMARK 465 ARG B 9
REMARK 465 THR B 10
REMARK 465 ASN B 11
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASP C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 LYS C 301
REMARK 465 ASN C 302
REMARK 465 LYS C 303
REMARK 465 GLY C 304
REMARK 465 LYS C 305
REMARK 465 TYR C 306
REMARK 465 GLY C 307
REMARK 465 GLN C 308
REMARK 465 PHE C 309
REMARK 465 SER C 310
REMARK 465 GLY C 311
REMARK 465 LEU C 312
REMARK 465 ASN C 313
REMARK 465 PRO C 314
REMARK 465 GLY C 315
REMARK 465 GLY C 316
REMARK 465 ARG C 317
REMARK 465 PRO C 318
REMARK 465 ILE C 319
REMARK 465 THR C 320
REMARK 465 PRO C 321
REMARK 465 PRO C 322
REMARK 465 ARG C 323
REMARK 465 ASN C 324
REMARK 465 SER C 325
REMARK 465 ALA C 326
REMARK 465 LYS C 327
REMARK 465 ALA C 328
REMARK 465 LYS C 329
REMARK 465 LYS C 330
REMARK 465 MET E 1
REMARK 465 ARG E 2
REMARK 465 GLY E 3
REMARK 465 THR E 4
REMARK 465 ARG E 5
REMARK 465 LEU E 6
REMARK 465 MET E 7
REMARK 465 GLY E 8
REMARK 465 LEU E 9
REMARK 465 LEU E 10
REMARK 465 LEU E 11
REMARK 465 ALA E 12
REMARK 465 LEU E 13
REMARK 465 ALA E 14
REMARK 465 GLY E 15
REMARK 465 LEU E 16
REMARK 465 LEU E 17
REMARK 465 GLN E 18
REMARK 465 LEU E 19
REMARK 465 GLY E 20
REMARK 465 LEU E 21
REMARK 465 SER E 22
REMARK 465 LEU E 23
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 41 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET D 229 CG - SD - CE ANGL. DEV. = 9.9 DEGREES
REMARK 500 CYS D 259 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 MET E 188 CG - SD - CE ANGL. DEV. = -11.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU C 90 49.28 -98.48
REMARK 500 ASP C 92 69.17 62.86
REMARK 500 ASP C 95 153.00 75.43
REMARK 500 ARG C 96 -55.43 74.50
REMARK 500 TYR C 144 -109.19 -133.02
REMARK 500 ASN C 157 4.81 -65.00
REMARK 500 GLU C 167 14.42 55.81
REMARK 500 LYS C 168 -32.16 -130.50
REMARK 500 SER C 224 -166.48 62.62
REMARK 500 ALA C 247 -130.80 -131.89
REMARK 500 CYS C 273 8.46 55.78
REMARK 500 THR D 7 131.02 70.87
REMARK 500 ARG D 64 -58.68 -22.09
REMARK 500 PHE D 202 44.85 -141.26
REMARK 500 LYS D 217 -51.23 -132.29
REMARK 500 CYS D 259 -74.26 -52.57
REMARK 500 ALA D 367 -16.28 -148.65
REMARK 500 ASN E 40 95.88 -65.39
REMARK 500 ARG E 63 50.21 -91.34
REMARK 500 ASN E 96 -156.53 -87.39
REMARK 500 GLU E 134 94.09 -34.88
REMARK 500 CYS E 195 -112.08 57.76
REMARK 500 THR E 229 178.53 -52.97
REMARK 500 ALA E 232 47.29 -88.29
REMARK 500 GLU A 16 -0.16 76.07
REMARK 500 TYR A 38 51.88 -114.42
REMARK 500 GLU A 49 -112.39 52.33
REMARK 500 ARG A 63 -144.61 56.83
REMARK 500 THR A 133 -75.25 -105.95
REMARK 500 ASP A 166 67.72 62.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG C 96 0.10 SIDE CHAIN
REMARK 500 ARG D 41 0.09 SIDE CHAIN
REMARK 500 ARG D 149 0.08 SIDE CHAIN
REMARK 500 ARG E 235 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C1000 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 92 OD2
REMARK 620 2 ASN C 124 OD1 98.5
REMARK 620 3 HIS C 248 ND1 140.1 82.2
REMARK 620 4 SEP A 51 O1P 113.4 96.1 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 139 OE1
REMARK 620 2 ATP D 402 O3G 108.9
REMARK 620 3 ATP D 402 O2B 148.8 71.0
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-49124 RELATED DB: EMDB
REMARK 900 RAW CONSENSUS RECONSTRUCTION OF THE DP71L-PP1A-EIF2ALPHA-GACTIN-
REMARK 900 DNASEI COMPLEX
REMARK 900 RELATED ID: EMD-49163 RELATED DB: EMDB
REMARK 900 CONSTITUENT EM MAP: FOCUSED REFINEMENT OF THE DP71L-PP1A-EIF2ALPHA
REMARK 900 SUBCOMPLEX
REMARK 900 RELATED ID: EMD-49162 RELATED DB: EMDB
REMARK 900 CONSTITUENT EM MAP: FOCUSED REFINEMENT OF G-ACTIN IN THE
REMARK 900 HOLOPHOSPHATASE COMPLEX
REMARK 900 RELATED ID: EMD-49164 RELATED DB: EMDB
REMARK 900 CONSTITUENT EM MAP: FOCUSED REFINEMENT OF DNASEI IN THE
REMARK 900 HOLOPHOSPHATASE COMPLEX
REMARK 900 RELATED ID: EMD-49223 RELATED DB: EMDB
REMARK 900 VIRAL PROTEIN DP71L IN COMPLEX WITH PHOSPHORYLATED EIF2ALPHA (NTD)
REMARK 900 AND PROTEIN PHOSPHATASE 1A (D64A), STABILIZED BY G-ACTIN/DNASEI.
DBREF 9NB9 B 1 71 UNP P0C756 DP71L_ASFP4 1 71
DBREF 9NB9 C 1 330 UNP P62136 PP1A_HUMAN 1 330
DBREF 9NB9 D 1 377 UNP P68135 ACTS_RABIT 1 377
DBREF 9NB9 E 1 282 UNP P00639 DNAS1_BOVIN 1 282
DBREF 9NB9 A 1 186 UNP P05198 IF2A_HUMAN 2 187
SEQADV 9NB9 ALA C 64 UNP P62136 ASP 64 ENGINEERED MUTATION
SEQRES 1 B 71 MET GLY GLY ARG ARG ARG LYS LYS ARG THR ASN ASP VAL
SEQRES 2 B 71 LYS HIS VAL ARG PHE ALA ALA ALA VAL GLU VAL TRP GLU
SEQRES 3 B 71 ALA ASP ASP ILE GLU ARG LYS GLY PRO TRP GLU GLN ALA
SEQRES 4 B 71 ALA VAL ASP ARG PHE ARG PHE GLN ARG ARG ILE ALA SER
SEQRES 5 B 71 VAL GLU GLU LEU LEU SER ALA VAL LEU LEU ARG GLN LYS
SEQRES 6 B 71 LYS LEU LEU GLU GLN GLN
SEQRES 1 C 330 MET SER ASP SER GLU LYS LEU ASN LEU ASP SER ILE ILE
SEQRES 2 C 330 GLY ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS
SEQRES 3 C 330 ASN VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS
SEQRES 4 C 330 LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU
SEQRES 5 C 330 LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ALA ILE
SEQRES 6 C 330 HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR
SEQRES 7 C 330 GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY
SEQRES 8 C 330 ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE
SEQRES 9 C 330 CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN
SEQRES 10 C 330 PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE
SEQRES 11 C 330 ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG
SEQRES 12 C 330 TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE
SEQRES 13 C 330 ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE
SEQRES 14 C 330 PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER
SEQRES 15 C 330 MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL
SEQRES 16 C 330 PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP
SEQRES 17 C 330 PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG
SEQRES 18 C 330 GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS
SEQRES 19 C 330 PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA
SEQRES 20 C 330 HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS
SEQRES 21 C 330 ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS
SEQRES 22 C 330 GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP
SEQRES 23 C 330 GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA
SEQRES 24 C 330 ASP LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY LEU
SEQRES 25 C 330 ASN PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN SER
SEQRES 26 C 330 ALA LYS ALA LYS LYS
SEQRES 1 D 377 MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP
SEQRES 2 D 377 ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP
SEQRES 3 D 377 ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG
SEQRES 4 D 377 PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS
SEQRES 5 D 377 ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY
SEQRES 6 D 377 ILE LEU THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE
SEQRES 7 D 377 THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR
SEQRES 8 D 377 PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO
SEQRES 9 D 377 THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN
SEQRES 10 D 377 ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN
SEQRES 11 D 377 VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER
SEQRES 12 D 377 LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP
SEQRES 13 D 377 SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU
SEQRES 14 D 377 GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU
SEQRES 15 D 377 ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU
SEQRES 16 D 377 THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG
SEQRES 17 D 377 GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL
SEQRES 18 D 377 ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER
SEQRES 19 D 377 SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY
SEQRES 20 D 377 GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO
SEQRES 21 D 377 GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER
SEQRES 22 D 377 ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS
SEQRES 23 D 377 CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN
SEQRES 24 D 377 VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA
SEQRES 25 D 377 ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER
SEQRES 26 D 377 THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS
SEQRES 27 D 377 TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU
SEQRES 28 D 377 SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR
SEQRES 29 D 377 ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 E 282 MET ARG GLY THR ARG LEU MET GLY LEU LEU LEU ALA LEU
SEQRES 2 E 282 ALA GLY LEU LEU GLN LEU GLY LEU SER LEU LYS ILE ALA
SEQRES 3 E 282 ALA PHE ASN ILE ARG THR PHE GLY GLU THR LYS MET SER
SEQRES 4 E 282 ASN ALA THR LEU ALA SER TYR ILE VAL ARG ILE VAL ARG
SEQRES 5 E 282 ARG TYR ASP ILE VAL LEU ILE GLN GLU VAL ARG ASP SER
SEQRES 6 E 282 HIS LEU VAL ALA VAL GLY LYS LEU LEU ASP TYR LEU ASN
SEQRES 7 E 282 GLN ASP ASP PRO ASN THR TYR HIS TYR VAL VAL SER GLU
SEQRES 8 E 282 PRO LEU GLY ARG ASN SER TYR LYS GLU ARG TYR LEU PHE
SEQRES 9 E 282 LEU PHE ARG PRO ASN LYS VAL SER VAL LEU ASP THR TYR
SEQRES 10 E 282 GLN TYR ASP ASP GLY CYS GLU SER CYS GLY ASN ASP SER
SEQRES 11 E 282 PHE SER ARG GLU PRO ALA VAL VAL LYS PHE SER SER HIS
SEQRES 12 E 282 SER THR LYS VAL LYS GLU PHE ALA ILE VAL ALA LEU HIS
SEQRES 13 E 282 SER ALA PRO SER ASP ALA VAL ALA GLU ILE ASN SER LEU
SEQRES 14 E 282 TYR ASP VAL TYR LEU ASP VAL GLN GLN LYS TRP HIS LEU
SEQRES 15 E 282 ASN ASP VAL MET LEU MET GLY ASP PHE ASN ALA ASP CYS
SEQRES 16 E 282 SER TYR VAL THR SER SER GLN TRP SER SER ILE ARG LEU
SEQRES 17 E 282 ARG THR SER SER THR PHE GLN TRP LEU ILE PRO ASP SER
SEQRES 18 E 282 ALA ASP THR THR ALA THR SER THR ASN CYS ALA TYR ASP
SEQRES 19 E 282 ARG ILE VAL VAL ALA GLY SER LEU LEU GLN SER SER VAL
SEQRES 20 E 282 VAL PRO GLY SER ALA ALA PRO PHE ASP PHE GLN ALA ALA
SEQRES 21 E 282 TYR GLY LEU SER ASN GLU MET ALA LEU ALA ILE SER ASP
SEQRES 22 E 282 HIS TYR PRO VAL GLU VAL THR LEU THR
SEQRES 1 A 186 PRO GLY LEU SER CYS ARG PHE TYR GLN HIS LYS PHE PRO
SEQRES 2 A 186 GLU VAL GLU ASP VAL VAL MET VAL ASN VAL ARG SER ILE
SEQRES 3 A 186 ALA GLU MET GLY ALA TYR VAL SER LEU LEU GLU TYR ASN
SEQRES 4 A 186 ASN ILE GLU GLY MET ILE LEU LEU SER GLU LEU SEP ARG
SEQRES 5 A 186 ARG ARG ILE ARG SER ILE ASN LYS LEU ILE ARG ILE GLY
SEQRES 6 A 186 ARG ASN GLU CYS VAL VAL VAL ILE ARG VAL ASP LYS GLU
SEQRES 7 A 186 LYS GLY TYR ILE ASP LEU SER LYS ARG ARG VAL SER PRO
SEQRES 8 A 186 GLU GLU ALA ILE LYS CYS GLU ASP LYS PHE THR LYS SER
SEQRES 9 A 186 LYS THR VAL TYR SER ILE LEU ARG HIS VAL ALA GLU VAL
SEQRES 10 A 186 LEU GLU TYR THR LYS ASP GLU GLN LEU GLU SER LEU PHE
SEQRES 11 A 186 GLN ARG THR ALA TRP VAL PHE ASP ASP LYS TYR LYS ARG
SEQRES 12 A 186 PRO GLY TYR GLY ALA TYR ASP ALA PHE LYS HIS ALA VAL
SEQRES 13 A 186 SER ASP PRO SER ILE LEU ASP SER LEU ASP LEU ASN GLU
SEQRES 14 A 186 ASP GLU ARG GLU VAL LEU ILE ASN ASN ILE ASN ARG ARG
SEQRES 15 A 186 LEU THR PRO GLN
MODRES 9NB9 SEP A 51 SER MODIFIED RESIDUE
HET SEP A 51 10
HET MN C1000 1
HET CA D 401 1
HET ATP D 402 31
HETNAM SEP PHOSPHOSERINE
HETNAM MN MANGANESE (II) ION
HETNAM CA CALCIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN SEP PHOSPHONOSERINE
FORMUL 5 SEP C3 H8 N O6 P
FORMUL 6 MN MN 2+
FORMUL 7 CA CA 2+
FORMUL 8 ATP C10 H16 N5 O13 P3
HELIX 1 AA1 PRO B 35 GLU B 69 1 35
HELIX 2 AA2 ASN C 8 GLU C 18 1 11
HELIX 3 AA3 THR C 31 GLN C 49 1 19
HELIX 4 AA4 GLN C 68 GLY C 80 1 13
HELIX 5 AA5 GLN C 99 TYR C 114 1 16
HELIX 6 AA6 CYS C 127 GLY C 135 1 9
HELIX 7 AA7 GLY C 135 TYR C 144 1 10
HELIX 8 AA8 ASN C 145 ASN C 157 1 13
HELIX 9 AA9 MET C 183 ARG C 188 1 6
HELIX 10 AB1 GLY C 199 SER C 207 1 9
HELIX 11 AB2 GLY C 228 HIS C 239 1 12
HELIX 12 AB3 ASN C 271 GLU C 275 5 5
HELIX 13 AB4 GLY D 57 SER D 62 1 6
HELIX 14 AB5 LYS D 63 GLY D 65 5 3
HELIX 15 AB6 ASN D 80 GLU D 95 1 16
HELIX 16 AB7 ALA D 99 HIS D 103 5 5
HELIX 17 AB8 PRO D 114 THR D 128 1 15
HELIX 18 AB9 GLN D 139 SER D 147 1 9
HELIX 19 AC1 ALA D 183 THR D 196 1 14
HELIX 20 AC2 GLU D 197 GLY D 199 5 3
HELIX 21 AC3 ALA D 206 CYS D 219 1 14
HELIX 22 AC4 ASP D 224 SER D 235 1 12
HELIX 23 AC5 SER D 236 GLU D 239 5 4
HELIX 24 AC6 ASN D 254 THR D 262 1 9
HELIX 25 AC7 LEU D 263 PHE D 264 5 2
HELIX 26 AC8 GLN D 265 GLY D 270 5 6
HELIX 27 AC9 GLY D 275 CYS D 287 1 13
HELIX 28 AD1 ASP D 288 ASN D 298 1 11
HELIX 29 AD2 GLY D 303 TYR D 308 5 6
HELIX 30 AD3 GLY D 310 ALA D 323 1 14
HELIX 31 AD4 GLU D 336 LYS D 338 5 3
HELIX 32 AD5 TYR D 339 SER D 350 1 12
HELIX 33 AD6 THR D 353 MET D 357 5 5
HELIX 34 AD7 LYS D 361 GLY D 368 1 8
HELIX 35 AD8 PRO D 369 LYS D 375 5 7
HELIX 36 AD9 ASN E 40 ARG E 52 1 13
HELIX 37 AE1 LEU E 67 ASN E 78 1 12
HELIX 38 AE2 ALA E 158 SER E 160 5 3
HELIX 39 AE3 ASP E 161 HIS E 181 1 21
HELIX 40 AE4 SER E 201 SER E 205 5 5
HELIX 41 AE5 ILE E 206 SER E 211 1 6
HELIX 42 AE6 GLY E 240 VAL E 247 1 8
HELIX 43 AE7 ASP E 256 GLY E 262 1 7
HELIX 44 AE8 SER E 264 SER E 272 1 9
HELIX 45 AE9 GLU A 37 ASN A 39 5 3
HELIX 46 AF1 ILE A 58 ILE A 62 5 5
HELIX 47 AF2 SER A 90 LEU A 118 1 29
HELIX 48 AF3 LYS A 122 TYR A 141 1 20
HELIX 49 AF4 GLY A 145 ASP A 158 1 14
HELIX 50 AF5 PRO A 159 ASP A 166 5 8
HELIX 51 AF6 ASN A 168 THR A 184 1 17
SHEET 1 AA1 3 ARG B 17 PHE B 18 0
SHEET 2 AA1 3 MET C 290 LYS C 297 1 O CYS C 291 N ARG B 17
SHEET 3 AA1 3 GLU B 23 GLU B 26 1 N TRP B 25 O ILE C 295
SHEET 1 AA2 6 ARG B 17 PHE B 18 0
SHEET 2 AA2 6 MET C 290 LYS C 297 1 O CYS C 291 N ARG B 17
SHEET 3 AA2 6 GLY C 280 VAL C 285 -1 N GLY C 280 O LEU C 296
SHEET 4 AA2 6 LEU C 59 CYS C 62 -1 N ILE C 61 O MET C 283
SHEET 5 AA2 6 TYR C 87 PHE C 89 1 O LEU C 88 N LYS C 60
SHEET 6 AA2 6 PHE C 118 LEU C 120 1 O PHE C 119 N PHE C 89
SHEET 1 AA3 6 LEU C 52 LEU C 55 0
SHEET 2 AA3 6 ALA C 162 VAL C 165 1 O ALA C 162 N LEU C 53
SHEET 3 AA3 6 ILE C 169 CYS C 172 -1 O CYS C 171 N ALA C 163
SHEET 4 AA3 6 LEU C 243 ARG C 246 1 O CYS C 245 N PHE C 170
SHEET 5 AA3 6 LEU C 263 LEU C 266 1 O LEU C 266 N ARG C 246
SHEET 6 AA3 6 TYR C 255 PHE C 258 -1 N GLU C 256 O THR C 265
SHEET 1 AA4 3 ASP C 208 PRO C 209 0
SHEET 2 AA4 3 PHE C 225 PHE C 227 1 O PHE C 227 N ASP C 208
SHEET 3 AA4 3 TRP C 216 GLU C 218 -1 N GLY C 217 O THR C 226
SHEET 1 AA5 6 ALA D 31 PRO D 34 0
SHEET 2 AA5 6 LEU D 18 PHE D 23 -1 N VAL D 19 O PHE D 33
SHEET 3 AA5 6 LEU D 10 ASN D 14 -1 N ASP D 13 O LYS D 20
SHEET 4 AA5 6 THR D 105 GLU D 109 1 O LEU D 106 N CYS D 12
SHEET 5 AA5 6 ALA D 133 ILE D 138 1 O TYR D 135 N LEU D 107
SHEET 6 AA5 6 ILE D 359 THR D 360 -1 O ILE D 359 N MET D 134
SHEET 1 AA6 3 TYR D 55 VAL D 56 0
SHEET 2 AA6 3 VAL D 37 PRO D 40 -1 N GLY D 38 O TYR D 55
SHEET 3 AA6 3 LEU D 67 LYS D 70 -1 O THR D 68 N ARG D 39
SHEET 1 AA7 7 GLY D 44 MET D 46 0
SHEET 2 AA7 7 HIS E 86 VAL E 89 1 O VAL E 89 N VAL D 45
SHEET 3 AA7 7 ARG E 101 PHE E 106 -1 O PHE E 104 N VAL E 88
SHEET 4 AA7 7 ILE E 56 VAL E 62 -1 N ILE E 59 O LEU E 103
SHEET 5 AA7 7 ILE E 25 PHE E 33 1 N PHE E 28 O LEU E 58
SHEET 6 AA7 7 VAL E 277 VAL E 279 -1 O VAL E 277 N ALA E 27
SHEET 7 AA7 7 ALA E 253 PRO E 254 -1 N ALA E 253 O GLU E 278
SHEET 1 AA8 2 ILE D 73 GLU D 74 0
SHEET 2 AA8 2 ILE D 77 ILE D 78 -1 O ILE D 77 N GLU D 74
SHEET 1 AA9 3 TYR D 171 ALA D 172 0
SHEET 2 AA9 3 THR D 162 TYR D 168 -1 N TYR D 168 O TYR D 171
SHEET 3 AA9 3 MET D 178 LEU D 180 -1 O MET D 178 N ASN D 164
SHEET 1 AB1 5 TYR D 171 ALA D 172 0
SHEET 2 AB1 5 THR D 162 TYR D 168 -1 N TYR D 168 O TYR D 171
SHEET 3 AB1 5 GLY D 152 SER D 157 -1 N ASP D 156 O HIS D 163
SHEET 4 AB1 5 ASN D 299 SER D 302 1 O VAL D 300 N ILE D 153
SHEET 5 AB1 5 ILE D 331 ILE D 332 1 O ILE D 332 N ASN D 299
SHEET 1 AB2 2 LYS D 240 GLU D 243 0
SHEET 2 AB2 2 VAL D 249 ILE D 252 -1 O ILE D 252 N LYS D 240
SHEET 1 AB3 6 SER E 112 GLN E 118 0
SHEET 2 AB3 6 ALA E 136 SER E 141 -1 O LYS E 139 N LEU E 114
SHEET 3 AB3 6 GLU E 149 HIS E 156 -1 O ILE E 152 N VAL E 138
SHEET 4 AB3 6 VAL E 185 ASP E 190 1 O MET E 186 N ALA E 151
SHEET 5 AB3 6 ARG E 235 ALA E 239 -1 O VAL E 237 N LEU E 187
SHEET 6 AB3 6 PHE E 214 TRP E 216 -1 N GLN E 215 O VAL E 238
SHEET 1 AB4 6 VAL A 18 ALA A 27 0
SHEET 2 AB4 6 GLY A 30 LEU A 35 -1 O SER A 34 N ASN A 22
SHEET 3 AB4 6 GLU A 42 LEU A 46 -1 O ILE A 45 N ALA A 31
SHEET 4 AB4 6 TYR A 81 SER A 85 1 O LEU A 84 N MET A 44
SHEET 5 AB4 6 ASN A 67 ASP A 76 -1 N ARG A 74 O ASP A 83
SHEET 6 AB4 6 VAL A 18 ALA A 27 -1 N VAL A 19 O VAL A 70
LINK C LEU A 50 N SEP A 51 1555 1555 1.34
LINK C SEP A 51 N ARG A 52 1555 1555 1.35
LINK OD2 ASP C 92 MN MN C1000 1555 1555 1.92
LINK OD1 ASN C 124 MN MN C1000 1555 1555 1.94
LINK ND1 HIS C 248 MN MN C1000 1555 1555 2.38
LINK MN MN C1000 O1P SEP A 51 1555 1555 2.18
LINK OE1 GLN D 139 CA CA D 401 1555 1555 2.39
LINK CA CA D 401 O3G ATP D 402 1555 1555 2.40
LINK CA CA D 401 O2B ATP D 402 1555 1555 2.28
CISPEP 1 ARG C 23 PRO C 24 0 11.95
CISPEP 2 ALA C 57 PRO C 58 0 -7.82
CISPEP 3 PRO C 82 PRO C 83 0 -2.82
CISPEP 4 ARG C 191 PRO C 192 0 6.48
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
ATOM 1 N ASP B 12 141.825 193.475 110.387 1.00121.05 N
ATOM 2 CA ASP B 12 142.765 193.167 111.505 1.00121.87 C
ATOM 3 C ASP B 12 143.342 191.758 111.304 1.00119.68 C
ATOM 4 O ASP B 12 143.094 190.849 112.101 1.00117.40 O
ATOM 5 CB ASP B 12 142.106 193.423 112.859 1.00121.81 C
ATOM 6 CG ASP B 12 141.726 194.872 113.163 1.00122.98 C
ATOM 7 OD1 ASP B 12 141.695 195.697 112.216 1.00123.22 O
ATOM 8 OD2 ASP B 12 141.475 195.178 114.352 1.00122.69 O
ATOM 9 N VAL B 13 144.155 191.610 110.243 1.00118.79 N
ATOM 10 CA VAL B 13 144.615 190.305 109.770 1.00117.81 C
ATOM 11 C VAL B 13 145.908 189.922 110.511 1.00114.83 C
ATOM 12 O VAL B 13 147.027 190.126 110.029 1.00113.86 O
ATOM 13 CB VAL B 13 144.732 190.232 108.221 1.00117.95 C
ATOM 14 CG1 VAL B 13 145.646 191.302 107.604 1.00117.51 C
ATOM 15 CG2 VAL B 13 145.122 188.832 107.730 1.00117.91 C
ATOM 16 N LYS B 14 145.733 189.328 111.701 1.00113.44 N
ATOM 17 CA LYS B 14 146.848 188.851 112.512 1.00111.18 C
ATOM 18 C LYS B 14 147.404 187.590 111.844 1.00110.17 C
ATOM 19 O LYS B 14 146.648 186.851 111.217 1.00105.12 O
ATOM 20 CB LYS B 14 146.410 188.576 113.959 1.00108.82 C
ATOM 21 CG LYS B 14 145.507 189.634 114.588 1.00108.22 C
ATOM 22 CD LYS B 14 144.853 189.245 115.908 1.00104.85 C
ATOM 23 CE LYS B 14 145.762 189.382 117.092 1.00103.04 C
ATOM 24 NZ LYS B 14 145.018 189.427 118.358 1.00100.25 N
ATOM 25 N HIS B 15 148.720 187.346 111.960 1.00108.73 N
ATOM 26 CA HIS B 15 149.333 186.168 111.352 1.00106.20 C
ATOM 27 C HIS B 15 150.500 185.678 112.217 1.00103.94 C
ATOM 28 O HIS B 15 151.184 186.482 112.853 1.00104.13 O
ATOM 29 CB HIS B 15 149.673 186.435 109.876 1.00106.62 C
ATOM 30 CG HIS B 15 150.427 187.696 109.630 1.00109.27 C
ATOM 31 ND1 HIS B 15 149.832 188.939 109.519 1.00111.80 N
ATOM 32 CD2 HIS B 15 151.747 187.896 109.491 1.00109.73 C
ATOM 33 CE1 HIS B 15 150.771 189.858 109.317 1.00113.31 C
ATOM 34 NE2 HIS B 15 151.943 189.246 109.293 1.00113.14 N
ATOM 35 N VAL B 16 150.714 184.349 112.213 1.00100.07 N
ATOM 36 CA VAL B 16 151.381 183.648 113.306 1.00 99.32 C
ATOM 37 C VAL B 16 152.898 183.806 113.186 1.00 98.45 C
ATOM 38 O VAL B 16 153.458 183.897 112.093 1.00 99.15 O
ATOM 39 CB VAL B 16 150.968 182.163 113.423 1.00 95.88 C
ATOM 40 CG1 VAL B 16 151.752 181.424 114.506 1.00 96.00 C
ATOM 41 CG2 VAL B 16 149.471 182.001 113.674 1.00 92.03 C
ATOM 42 N ARG B 17 153.521 183.883 114.368 1.00 98.51 N
ATOM 43 CA ARG B 17 154.928 184.185 114.555 1.00100.14 C
ATOM 44 C ARG B 17 155.419 183.291 115.685 1.00 97.36 C
ATOM 45 O ARG B 17 154.600 182.824 116.473 1.00 96.15 O
ATOM 46 CB ARG B 17 155.087 185.652 114.977 1.00101.15 C
ATOM 47 CG ARG B 17 154.434 186.707 114.083 1.00102.82 C
ATOM 48 CD ARG B 17 154.106 188.011 114.811 1.00105.17 C
ATOM 49 NE ARG B 17 155.311 188.574 115.442 1.00107.37 N
ATOM 50 CZ ARG B 17 155.364 189.490 116.422 1.00109.23 C
ATOM 51 NH1 ARG B 17 156.553 189.862 116.891 1.00108.83 N
ATOM 52 NH2 ARG B 17 154.253 190.021 116.934 1.00107.43 N
ATOM 53 N PHE B 18 156.732 183.065 115.786 1.00 96.49 N
ATOM 54 CA PHE B 18 157.252 182.277 116.888 1.00 95.37 C
ATOM 55 C PHE B 18 158.397 183.008 117.574 1.00 98.16 C
ATOM 56 O PHE B 18 159.293 183.509 116.902 1.00100.17 O
ATOM 57 CB PHE B 18 157.733 180.912 116.395 1.00 93.95 C
ATOM 58 CG PHE B 18 156.581 179.971 116.088 1.00 93.85 C
ATOM 59 CD1 PHE B 18 156.077 179.874 114.794 1.00 93.81 C
ATOM 60 CD2 PHE B 18 155.982 179.217 117.102 1.00 92.69 C
ATOM 61 CE1 PHE B 18 155.019 179.017 114.511 1.00 92.75 C
ATOM 62 CE2 PHE B 18 154.899 178.387 116.824 1.00 90.38 C
ATOM 63 CZ PHE B 18 154.419 178.289 115.528 1.00 88.88 C
ATOM 64 N ALA B 19 158.367 183.055 118.914 1.00 98.95 N
ATOM 65 CA ALA B 19 159.592 183.240 119.677 1.00 99.54 C
ATOM 66 C ALA B 19 160.427 181.970 119.510 1.00102.45 C
ATOM 67 O ALA B 19 159.933 180.866 119.745 1.00101.75 O
ATOM 68 CB ALA B 19 159.309 183.539 121.134 1.00 98.37 C
ATOM 69 N ALA B 20 161.676 182.140 119.054 1.00101.81 N
ATOM 70 CA ALA B 20 162.518 181.017 118.674 1.00102.95 C
ATOM 71 C ALA B 20 163.063 180.332 119.928 1.00104.34 C
ATOM 72 O ALA B 20 163.012 179.105 120.029 1.00104.01 O
ATOM 73 CB ALA B 20 163.622 181.494 117.752 1.00103.27 C
ATOM 74 N ALA B 21 163.561 181.137 120.883 1.00104.10 N
ATOM 75 CA ALA B 21 164.073 180.636 122.154 1.00105.62 C
ATOM 76 C ALA B 21 162.920 180.329 123.112 1.00105.95 C
ATOM 77 O ALA B 21 161.842 180.924 123.010 1.00105.06 O
ATOM 78 CB ALA B 21 165.034 181.634 122.767 1.00106.29 C
ATOM 79 N VAL B 22 163.171 179.409 124.059 1.00105.79 N
ATOM 80 CA VAL B 22 162.113 178.798 124.855 1.00105.78 C
ATOM 81 C VAL B 22 162.516 178.826 126.334 1.00105.02 C
ATOM 82 O VAL B 22 163.692 178.685 126.673 1.00105.11 O
ATOM 83 CB VAL B 22 161.788 177.363 124.369 1.00105.16 C
ATOM 84 CG1 VAL B 22 161.270 177.334 122.923 1.00103.04 C
ATOM 85 CG2 VAL B 22 162.975 176.407 124.545 1.00104.81 C
ATOM 86 N GLU B 23 161.517 179.011 127.208 1.00105.52 N
ATOM 87 CA GLU B 23 161.740 178.960 128.646 1.00106.40 C
ATOM 88 C GLU B 23 161.820 177.498 129.065 1.00105.45 C
ATOM 89 O GLU B 23 161.164 176.636 128.473 1.00103.05 O
ATOM 90 CB GLU B 23 160.634 179.621 129.475 1.00105.77 C
ATOM 91 CG GLU B 23 160.263 181.027 129.002 1.00106.87 C
ATOM 92 CD GLU B 23 159.277 181.779 129.885 1.00106.23 C
ATOM 93 OE1 GLU B 23 159.513 181.852 131.122 1.00106.32 O
ATOM 94 OE2 GLU B 23 158.287 182.312 129.319 1.00103.58 O
ATOM 95 N VAL B 24 162.604 177.220 130.106 1.00105.74 N
ATOM 96 CA VAL B 24 162.681 175.857 130.597 1.00106.19 C
ATOM 97 C VAL B 24 162.607 175.889 132.123 1.00105.84 C
ATOM 98 O VAL B 24 163.184 176.762 132.771 1.00106.06 O
ATOM 99 CB VAL B 24 163.907 175.093 130.032 1.00106.85 C
ATOM 100 CG1 VAL B 24 165.250 175.714 130.424 1.00107.78 C
ATOM 101 CG2 VAL B 24 163.877 173.600 130.377 1.00106.87 C
ATOM 102 N TRP B 25 161.845 174.928 132.656 1.00105.76 N
ATOM 103 CA TRP B 25 161.628 174.747 134.078 1.00106.77 C
ATOM 104 C TRP B 25 161.908 173.285 134.427 1.00108.06 C
ATOM 105 O TRP B 25 161.539 172.383 133.673 1.00106.68 O
ATOM 106 CB TRP B 25 160.188 175.146 134.429 1.00105.89 C
ATOM 107 CG TRP B 25 159.767 176.528 133.992 1.00105.19 C
ATOM 108 CD1 TRP B 25 160.471 177.690 134.123 1.00105.72 C
ATOM 109 CD2 TRP B 25 158.507 176.902 133.381 1.00105.22 C
ATOM 110 NE1 TRP B 25 159.751 178.749 133.635 1.00105.36 N
ATOM 111 CE2 TRP B 25 158.541 178.300 133.174 1.00105.08 C
ATOM 112 CE3 TRP B 25 157.357 176.200 132.984 1.00105.45 C
ATOM 113 CZ2 TRP B 25 157.474 178.994 132.596 1.00104.45 C
ATOM 114 CZ3 TRP B 25 156.300 176.888 132.418 1.00104.08 C
ATOM 115 CH2 TRP B 25 156.355 178.271 132.237 1.00103.63 C
ATOM 116 N GLU B 26 162.562 173.039 135.567 1.00108.99 N
ATOM 117 CA GLU B 26 162.920 171.677 135.938 1.00110.51 C
ATOM 118 C GLU B 26 161.683 170.938 136.458 1.00110.31 C
ATOM 119 O GLU B 26 161.039 171.394 137.408 1.00109.84 O
ATOM 120 CB GLU B 26 164.058 171.664 136.961 1.00112.50 C
ATOM 121 CG GLU B 26 164.431 170.265 137.454 1.00112.45 C
ATOM 122 CD GLU B 26 165.625 170.210 138.398 1.00115.83 C
ATOM 123 OE1 GLU B 26 165.706 171.061 139.316 1.00115.83 O
ATOM 124 OE2 GLU B 26 166.470 169.297 138.228 1.00116.64 O
ATOM 125 N ALA B 27 161.381 169.780 135.843 1.00109.32 N
ATOM 126 CA ALA B 27 160.306 168.909 136.295 1.00108.88 C
ATOM 127 C ALA B 27 160.773 168.061 137.479 1.00109.53 C
ATOM 128 O ALA B 27 161.956 167.748 137.618 1.00109.51 O
ATOM 129 CB ALA B 27 159.819 168.037 135.165 1.00108.02 C
ATOM 130 N ASP B 28 159.804 167.679 138.318 1.00109.07 N
ATOM 131 CA ASP B 28 160.064 166.992 139.572 1.00109.41 C
ATOM 132 C ASP B 28 160.578 165.570 139.331 1.00109.74 C
ATOM 133 O ASP B 28 160.329 164.966 138.287 1.00108.09 O
ATOM 134 CB ASP B 28 158.803 166.949 140.425 1.00110.38 C
ATOM 135 CG ASP B 28 158.277 168.276 140.956 1.00110.00 C
ATOM 136 OD1 ASP B 28 159.006 169.292 140.850 1.00109.14 O
ATOM 137 OD2 ASP B 28 157.134 168.278 141.476 1.00107.79 O
ATOM 138 N ASP B 29 161.251 165.028 140.357 1.00111.10 N
ATOM 139 CA ASP B 29 161.625 163.619 140.444 1.00111.98 C
ATOM 140 C ASP B 29 160.436 162.725 140.832 1.00110.55 C
ATOM 141 O ASP B 29 160.573 161.498 140.780 1.00109.07 O
ATOM 142 CB ASP B 29 162.756 163.423 141.452 1.00112.90 C
ATOM 143 CG ASP B 29 162.469 163.875 142.886 1.00113.30 C
ATOM 144 OD1 ASP B 29 162.000 165.027 143.055 1.00112.71 O
ATOM 145 OD2 ASP B 29 162.720 163.080 143.831 1.00113.81 O
ATOM 146 N ILE B 30 159.297 163.332 141.237 1.00110.50 N
ATOM 147 CA ILE B 30 158.170 162.626 141.840 1.00109.84 C
ATOM 148 C ILE B 30 157.725 161.543 140.865 1.00106.95 C
ATOM 149 O ILE B 30 157.484 161.833 139.698 1.00104.00 O
ATOM 150 CB ILE B 30 157.017 163.589 142.227 1.00110.13 C
ATOM 151 CG1 ILE B 30 157.420 164.573 143.374 1.00112.76 C
ATOM 152 CG2 ILE B 30 155.712 162.848 142.562 1.00108.50 C
ATOM 153 CD1 ILE B 30 157.627 163.960 144.758 1.00114.25 C
ATOM 154 N GLU B 31 157.636 160.303 141.372 1.00106.41 N
ATOM 155 CA GLU B 31 157.469 159.111 140.552 1.00103.59 C
ATOM 156 C GLU B 31 156.021 159.045 140.054 1.00100.48 C
ATOM 157 O GLU B 31 155.094 159.391 140.788 1.00100.50 O
ATOM 158 CB GLU B 31 157.965 157.934 141.397 1.00102.45 C
ATOM 159 CG GLU B 31 157.975 156.589 140.674 1.00102.93 C
ATOM 160 CD GLU B 31 156.597 155.975 140.476 1.00101.40 C
ATOM 161 OE1 GLU B 31 155.855 155.870 141.480 1.00100.48 O
ATOM 162 OE2 GLU B 31 156.269 155.598 139.326 1.00 99.16 O
ATOM 163 N ARG B 32 155.837 158.581 138.804 1.00 99.71 N
ATOM 164 CA ARG B 32 154.695 158.985 137.993 1.00 97.34 C
ATOM 165 C ARG B 32 153.760 157.843 137.589 1.00 94.53 C
ATOM 166 O ARG B 32 152.628 158.128 137.207 1.00 90.80 O
ATOM 167 CB ARG B 32 155.201 159.695 136.732 1.00 95.96 C
ATOM 168 CG ARG B 32 155.879 161.016 137.058 1.00 97.68 C
ATOM 169 CD ARG B 32 156.271 161.816 135.843 1.00 96.21 C
ATOM 170 NE ARG B 32 156.587 163.206 136.195 1.00 96.95 N
ATOM 171 CZ ARG B 32 157.734 163.689 136.673 1.00 99.66 C
ATOM 172 NH1 ARG B 32 157.793 164.955 137.044 1.00102.10 N
ATOM 173 NH2 ARG B 32 158.811 162.929 136.811 1.00 99.46 N
ATOM 174 N LYS B 33 154.193 156.575 137.657 1.00 94.39 N
ATOM 175 CA LYS B 33 153.406 155.498 137.071 1.00 92.13 C
ATOM 176 C LYS B 33 152.187 155.174 137.941 1.00 87.56 C
ATOM 177 O LYS B 33 152.315 154.911 139.137 1.00 87.41 O
ATOM 178 CB LYS B 33 154.233 154.234 136.807 1.00 92.55 C
ATOM 179 CG LYS B 33 153.489 153.259 135.900 1.00 91.80 C
ATOM 180 CD LYS B 33 154.294 152.184 135.176 1.00 95.16 C
ATOM 181 CE LYS B 33 153.420 151.453 134.180 1.00 95.71 C
ATOM 182 NZ LYS B 33 154.101 150.377 133.452 1.00 98.53 N
ATOM 183 N GLY B 34 151.003 155.178 137.305 1.00 86.44 N
ATOM 184 CA GLY B 34 149.752 154.836 137.961 1.00 81.67 C
ATOM 185 C GLY B 34 149.555 153.323 138.059 1.00 77.23 C
ATOM 186 O GLY B 34 149.765 152.604 137.086 1.00 76.82 O
ATOM 187 N PRO B 35 149.092 152.795 139.213 1.00 74.80 N
ATOM 188 CA PRO B 35 148.809 151.375 139.333 1.00 73.34 C
ATOM 189 C PRO B 35 147.551 150.937 138.590 1.00 69.56 C
ATOM 190 O PRO B 35 147.360 149.754 138.335 1.00 66.18 O
ATOM 191 CB PRO B 35 148.648 151.197 140.835 1.00 73.87 C
ATOM 192 CG PRO B 35 148.062 152.528 141.274 1.00 73.49 C
ATOM 193 CD PRO B 35 148.782 153.536 140.446 1.00 73.25 C
ATOM 194 N TRP B 36 146.700 151.897 138.234 1.00 69.75 N
ATOM 195 CA TRP B 36 145.377 151.599 137.708 1.00 66.78 C
ATOM 196 C TRP B 36 145.463 150.868 136.373 1.00 65.28 C
ATOM 197 O TRP B 36 144.654 149.987 136.100 1.00 62.02 O
ATOM 198 CB TRP B 36 144.583 152.903 137.575 1.00 65.78 C
ATOM 199 CG TRP B 36 144.643 153.694 138.850 1.00 67.93 C
ATOM 200 CD1 TRP B 36 145.355 154.827 139.103 1.00 70.63 C
ATOM 201 CD2 TRP B 36 144.012 153.326 140.091 1.00 66.61 C
ATOM 202 NE1 TRP B 36 145.192 155.202 140.409 1.00 70.93 N
ATOM 203 CE2 TRP B 36 144.378 154.298 141.040 1.00 67.60 C
ATOM 204 CE3 TRP B 36 143.172 152.281 140.482 1.00 66.07 C
ATOM 205 CZ2 TRP B 36 143.926 154.249 142.355 1.00 70.46 C
ATOM 206 CZ3 TRP B 36 142.734 152.228 141.784 1.00 65.48 C
ATOM 207 CH2 TRP B 36 143.110 153.198 142.707 1.00 70.27 C
ATOM 208 N GLU B 37 146.456 151.243 135.557 1.00 68.11 N
ATOM 209 CA GLU B 37 146.684 150.663 134.241 1.00 66.78 C
ATOM 210 C GLU B 37 146.829 149.149 134.368 1.00 64.07 C
ATOM 211 O GLU B 37 146.360 148.427 133.496 1.00 62.78 O
ATOM 212 CB GLU B 37 147.921 151.363 133.664 1.00 71.27 C
ATOM 213 CG GLU B 37 148.181 151.164 132.167 1.00 72.80 C
ATOM 214 CD GLU B 37 149.342 151.998 131.598 1.00 76.95 C
ATOM 215 OE1 GLU B 37 150.434 152.037 132.229 1.00 81.17 O
ATOM 216 OE2 GLU B 37 149.165 152.604 130.507 1.00 74.82 O
ATOM 217 N GLN B 38 147.476 148.704 135.461 1.00 64.50 N
ATOM 218 CA GLN B 38 147.689 147.299 135.791 1.00 63.64 C
ATOM 219 C GLN B 38 146.452 146.675 136.429 1.00 58.74 C
ATOM 220 O GLN B 38 146.102 145.556 136.098 1.00 56.74 O
ATOM 221 CB GLN B 38 148.864 147.196 136.762 1.00 65.27 C
ATOM 222 CG GLN B 38 149.116 145.815 137.363 1.00 64.66 C
ATOM 223 CD GLN B 38 150.205 145.855 138.415 1.00 69.06 C
ATOM 224 OE1 GLN B 38 151.373 145.542 138.150 1.00 73.03 O
ATOM 225 NE2 GLN B 38 149.848 146.299 139.614 1.00 69.39 N
ATOM 226 N ALA B 39 145.807 147.387 137.351 1.00 60.23 N
ATOM 227 CA ALA B 39 144.663 146.852 138.066 1.00 57.90 C
ATOM 228 C ALA B 39 143.532 146.507 137.108 1.00 54.12 C
ATOM 229 O ALA B 39 142.735 145.628 137.401 1.00 54.06 O
ATOM 230 CB ALA B 39 144.196 147.840 139.096 1.00 59.46 C
ATOM 231 N ALA B 40 143.470 147.190 135.970 1.00 53.83 N
ATOM 232 CA ALA B 40 142.526 146.844 134.928 1.00 53.93 C
ATOM 233 C ALA B 40 142.787 145.443 134.392 1.00 53.68 C
ATOM 234 O ALA B 40 141.854 144.674 134.186 1.00 53.85 O
ATOM 235 CB ALA B 40 142.643 147.841 133.824 1.00 56.78 C
ATOM 236 N VAL B 41 144.060 145.111 134.178 1.00 54.93 N
ATOM 237 CA VAL B 41 144.446 143.801 133.679 1.00 53.23 C
ATOM 238 C VAL B 41 143.952 142.739 134.660 1.00 52.66 C
ATOM 239 O VAL B 41 143.310 141.775 134.255 1.00 51.93 O
ATOM 240 CB VAL B 41 145.971 143.735 133.477 1.00 52.41 C
ATOM 241 CG1 VAL B 41 146.438 142.384 132.976 1.00 55.08 C
ATOM 242 CG2 VAL B 41 146.477 144.808 132.527 1.00 55.33 C
ATOM 243 N ASP B 42 144.227 142.942 135.953 1.00 53.50 N
ATOM 244 CA ASP B 42 143.809 142.015 136.987 1.00 52.13 C
ATOM 245 C ASP B 42 142.307 141.841 136.945 1.00 49.61 C
ATOM 246 O ASP B 42 141.833 140.719 137.038 1.00 48.55 O
ATOM 247 CB ASP B 42 144.244 142.457 138.371 1.00 53.13 C
ATOM 248 CG ASP B 42 145.751 142.579 138.560 1.00 59.80 C
ATOM 249 OD1 ASP B 42 146.488 142.304 137.587 1.00 61.74 O
ATOM 250 OD2 ASP B 42 146.190 142.938 139.680 1.00 63.78 O
ATOM 251 N ARG B 43 141.575 142.941 136.804 1.00 49.57 N
ATOM 252 CA ARG B 43 140.132 142.865 136.734 1.00 49.87 C
ATOM 253 C ARG B 43 139.719 142.019 135.545 1.00 48.64 C
ATOM 254 O ARG B 43 138.728 141.302 135.618 1.00 47.95 O
ATOM 255 CB ARG B 43 139.475 144.238 136.625 1.00 52.17 C
ATOM 256 CG ARG B 43 137.988 144.216 136.283 1.00 52.82 C
ATOM 257 CD ARG B 43 137.361 145.585 136.467 1.00 54.01 C
ATOM 258 NE ARG B 43 138.144 146.624 135.794 1.00 53.90 N
ATOM 259 CZ ARG B 43 138.144 146.870 134.496 1.00 54.67 C
ATOM 260 NH1 ARG B 43 139.018 147.723 133.995 1.00 55.17 N
ATOM 261 NH2 ARG B 43 137.300 146.258 133.690 1.00 62.52 N
ATOM 262 N PHE B 44 140.480 142.081 134.465 1.00 49.89 N
ATOM 263 CA PHE B 44 140.098 141.324 133.294 1.00 52.95 C
ATOM 264 C PHE B 44 140.497 139.855 133.421 1.00 50.65 C
ATOM 265 O PHE B 44 139.709 138.979 133.060 1.00 49.23 O
ATOM 266 CB PHE B 44 140.726 142.000 132.086 1.00 57.90 C
ATOM 267 CG PHE B 44 140.454 141.218 130.816 1.00 61.39 C
ATOM 268 CD1 PHE B 44 139.150 141.105 130.324 1.00 64.20 C
ATOM 269 CD2 PHE B 44 141.499 140.609 130.122 1.00 62.78 C
ATOM 270 CE1 PHE B 44 138.895 140.381 129.160 1.00 70.24 C
ATOM 271 CE2 PHE B 44 141.243 139.884 128.963 1.00 71.26 C
ATOM 272 CZ PHE B 44 139.942 139.773 128.480 1.00 73.82 C
ATOM 273 N ARG B 45 141.710 139.588 133.920 1.00 50.30 N
ATOM 274 CA ARG B 45 142.141 138.228 134.196 1.00 47.65 C
ATOM 275 C ARG B 45 141.104 137.528 135.062 1.00 43.99 C
ATOM 276 O ARG B 45 140.679 136.411 134.768 1.00 44.36 O
ATOM 277 CB ARG B 45 143.472 138.208 134.944 1.00 49.46 C
ATOM 278 CG ARG B 45 144.674 138.604 134.107 1.00 52.45 C
ATOM 279 CD ARG B 45 145.818 139.010 135.037 1.00 58.10 C
ATOM 280 NE ARG B 45 147.161 139.168 134.473 1.00 58.45 N
ATOM 281 CZ ARG B 45 147.881 138.194 133.952 1.00 62.08 C
ATOM 282 NH1 ARG B 45 149.067 138.472 133.455 1.00 71.28 N
ATOM 283 NH2 ARG B 45 147.445 136.943 133.923 1.00 60.26 N
ATOM 284 N PHE B 46 140.721 138.200 136.141 1.00 43.09 N
ATOM 285 CA PHE B 46 139.797 137.624 137.081 1.00 37.93 C
ATOM 286 C PHE B 46 138.453 137.420 136.406 1.00 39.71 C
ATOM 287 O PHE B 46 137.789 136.432 136.673 1.00 39.89 O
ATOM 288 CB PHE B 46 139.642 138.488 138.330 1.00 36.10 C
ATOM 289 CG PHE B 46 138.852 137.788 139.432 1.00 34.01 C
ATOM 290 CD1 PHE B 46 139.507 136.973 140.344 1.00 31.89 C
ATOM 291 CD2 PHE B 46 137.469 137.908 139.544 1.00 31.17 C
ATOM 292 CE1 PHE B 46 138.807 136.322 141.337 1.00 28.04 C
ATOM 293 CE2 PHE B 46 136.783 137.247 140.540 1.00 25.59 C
ATOM 294 CZ PHE B 46 137.450 136.453 141.419 1.00 20.88 C
ATOM 295 N GLN B 47 138.036 138.333 135.544 1.00 41.33 N
ATOM 296 CA GLN B 47 136.724 138.181 134.954 1.00 42.36 C
ATOM 297 C GLN B 47 136.697 136.958 134.043 1.00 43.48 C
ATOM 298 O GLN B 47 135.683 136.267 133.953 1.00 42.16 O
ATOM 299 CB GLN B 47 136.344 139.430 134.176 1.00 45.64 C
ATOM 300 CG GLN B 47 134.898 139.424 133.693 1.00 47.02 C
ATOM 301 CD GLN B 47 133.892 139.343 134.824 1.00 48.10 C
ATOM 302 OE1 GLN B 47 134.057 139.996 135.865 1.00 45.18 O
ATOM 303 NE2 GLN B 47 132.839 138.549 134.637 1.00 48.03 N
ATOM 304 N ARG B 48 137.833 136.680 133.389 1.00 45.92 N
ATOM 305 CA ARG B 48 137.998 135.492 132.559 1.00 49.21 C
ATOM 306 C ARG B 48 137.964 134.231 133.422 1.00 43.55 C
ATOM 307 O ARG B 48 137.348 133.241 133.030 1.00 42.99 O
ATOM 308 CB ARG B 48 139.317 135.568 131.781 1.00 53.36 C
ATOM 309 CG ARG B 48 139.436 134.591 130.615 1.00 59.62 C
ATOM 310 CD ARG B 48 140.754 134.720 129.844 1.00 70.43 C
ATOM 311 NE ARG B 48 141.874 134.436 130.751 1.00 73.55 N
ATOM 312 CZ ARG B 48 142.934 133.648 130.565 1.00 78.75 C
ATOM 313 NH1 ARG B 48 143.710 133.386 131.612 1.00 82.07 N
ATOM 314 NH2 ARG B 48 143.214 133.119 129.378 1.00 80.73 N
ATOM 315 N ARG B 49 138.627 134.289 134.592 1.00 43.07 N
ATOM 316 CA ARG B 49 138.622 133.219 135.587 1.00 40.68 C
ATOM 317 C ARG B 49 137.209 132.870 136.028 1.00 37.45 C
ATOM 318 O ARG B 49 136.891 131.697 136.126 1.00 39.91 O
ATOM 319 CB ARG B 49 139.427 133.624 136.822 1.00 39.34 C
ATOM 320 CG ARG B 49 139.441 132.625 137.967 1.00 38.07 C
ATOM 321 CD ARG B 49 140.457 133.021 139.032 1.00 36.06 C
ATOM 322 NE ARG B 49 140.435 132.047 140.126 1.00 35.12 N
ATOM 323 CZ ARG B 49 141.290 131.988 141.137 1.00 35.90 C
ATOM 324 NH1 ARG B 49 141.107 131.059 142.061 1.00 29.58 N
ATOM 325 NH2 ARG B 49 142.309 132.841 141.242 1.00 37.64 N
ATOM 326 N ILE B 50 136.389 133.882 136.301 1.00 37.53 N
ATOM 327 CA ILE B 50 134.992 133.670 136.616 1.00 35.65 C
ATOM 328 C ILE B 50 134.317 132.956 135.458 1.00 38.75 C
ATOM 329 O ILE B 50 133.600 131.978 135.661 1.00 40.71 O
ATOM 330 CB ILE B 50 134.264 134.991 136.895 1.00 36.24 C
ATOM 331 CG1 ILE B 50 134.785 135.676 138.168 1.00 34.97 C
ATOM 332 CG2 ILE B 50 132.749 134.774 136.941 1.00 34.70 C
ATOM 333 CD1 ILE B 50 134.388 137.139 138.305 1.00 33.68 C
ATOM 334 N ALA B 51 134.518 133.463 134.247 1.00 38.59 N
ATOM 335 CA ALA B 51 133.771 132.954 133.113 1.00 41.63 C
ATOM 336 C ALA B 51 134.174 131.512 132.797 1.00 42.06 C
ATOM 337 O ALA B 51 133.340 130.732 132.324 1.00 42.19 O
ATOM 338 CB ALA B 51 133.985 133.864 131.933 1.00 45.36 C
ATOM 339 N SER B 52 135.453 131.178 133.052 1.00 41.63 N
ATOM 340 CA SER B 52 135.979 129.818 132.952 1.00 43.44 C
ATOM 341 C SER B 52 135.177 128.831 133.814 1.00 42.61 C
ATOM 342 O SER B 52 134.743 127.768 133.359 1.00 42.19 O
ATOM 343 CB SER B 52 137.454 129.807 133.332 1.00 43.19 C
ATOM 344 OG SER B 52 137.965 128.488 133.473 1.00 44.32 O
ATOM 345 N VAL B 53 134.983 129.222 135.071 1.00 41.08 N
ATOM 346 CA VAL B 53 134.335 128.407 136.070 1.00 39.65 C
ATOM 347 C VAL B 53 132.838 128.339 135.823 1.00 39.72 C
ATOM 348 O VAL B 53 132.217 127.339 136.143 1.00 41.27 O
ATOM 349 CB VAL B 53 134.678 129.052 137.426 1.00 39.47 C
ATOM 350 CG1 VAL B 53 133.676 128.718 138.519 1.00 37.23 C
ATOM 351 CG2 VAL B 53 136.107 128.715 137.856 1.00 40.48 C
ATOM 352 N GLU B 54 132.260 129.398 135.281 1.00 39.49 N
ATOM 353 CA GLU B 54 130.827 129.547 135.374 1.00 42.67 C
ATOM 354 C GLU B 54 130.113 128.359 134.728 1.00 44.79 C
ATOM 355 O GLU B 54 129.091 127.927 135.250 1.00 44.27 O
ATOM 356 CB GLU B 54 130.374 130.886 134.791 1.00 45.41 C
ATOM 357 CG GLU B 54 128.919 131.247 135.113 1.00 45.69 C
ATOM 358 CD GLU B 54 127.810 130.788 134.160 1.00 49.33 C
ATOM 359 OE1 GLU B 54 128.072 130.455 132.962 1.00 48.42 O
ATOM 360 OE2 GLU B 54 126.645 130.787 134.645 1.00 47.55 O
ATOM 361 N GLU B 55 130.615 127.823 133.608 1.00 45.70 N
ATOM 362 CA GLU B 55 129.937 126.705 132.950 1.00 49.69 C
ATOM 363 C GLU B 55 129.639 125.565 133.930 1.00 46.59 C
ATOM 364 O GLU B 55 128.526 125.017 133.956 1.00 45.02 O
ATOM 365 CB GLU B 55 130.790 126.162 131.797 1.00 54.68 C
ATOM 366 CG GLU B 55 130.284 126.567 130.405 1.00 58.61 C
ATOM 367 CD GLU B 55 129.059 125.794 129.876 1.00 62.15 C
ATOM 368 OE1 GLU B 55 128.590 124.811 130.525 1.00 54.44 O
ATOM 369 OE2 GLU B 55 128.566 126.186 128.776 1.00 63.40 O
ATOM 370 N LEU B 56 130.686 125.243 134.709 1.00 44.38 N
ATOM 371 CA LEU B 56 130.747 124.128 135.643 1.00 41.38 C
ATOM 372 C LEU B 56 129.895 124.389 136.881 1.00 40.78 C
ATOM 373 O LEU B 56 129.076 123.565 137.286 1.00 42.27 O
ATOM 374 CB LEU B 56 132.225 124.004 136.003 1.00 39.53 C
ATOM 375 CG LEU B 56 132.545 123.289 137.317 1.00 36.98 C
ATOM 376 CD1 LEU B 56 132.251 121.783 137.124 1.00 38.04 C
ATOM 377 CD2 LEU B 56 133.977 123.608 137.817 1.00 30.82 C
ATOM 378 N LEU B 57 130.145 125.553 137.476 1.00 40.59 N
ATOM 379 CA LEU B 57 129.630 125.903 138.778 1.00 35.08 C
ATOM 380 C LEU B 57 128.157 126.253 138.693 1.00 38.70 C
ATOM 381 O LEU B 57 127.406 126.034 139.627 1.00 41.00 O
ATOM 382 CB LEU B 57 130.504 127.079 139.179 1.00 32.67 C
ATOM 383 CG LEU B 57 130.431 127.495 140.638 1.00 28.73 C
ATOM 384 CD1 LEU B 57 129.932 126.404 141.589 1.00 21.29 C
ATOM 385 CD2 LEU B 57 131.836 127.928 141.036 1.00 20.42 C
ATOM 386 N SER B 58 127.754 126.768 137.542 1.00 40.86 N
ATOM 387 CA SER B 58 126.386 127.179 137.324 1.00 42.64 C
ATOM 388 C SER B 58 125.450 125.972 137.363 1.00 46.17 C
ATOM 389 O SER B 58 124.326 126.078 137.864 1.00 49.77 O
ATOM 390 CB SER B 58 126.292 127.923 136.030 1.00 45.45 C
ATOM 391 OG SER B 58 125.051 128.601 135.914 1.00 45.95 O
ATOM 392 N ALA B 59 125.931 124.825 136.855 1.00 45.17 N
ATOM 393 CA ALA B 59 125.156 123.586 136.845 1.00 49.88 C
ATOM 394 C ALA B 59 124.745 123.178 138.262 1.00 50.56 C
ATOM 395 O ALA B 59 123.603 122.779 138.517 1.00 53.56 O
ATOM 396 CB ALA B 59 125.966 122.487 136.182 1.00 50.61 C
ATOM 397 N VAL B 60 125.729 123.278 139.163 1.00 47.91 N
ATOM 398 CA VAL B 60 125.596 122.971 140.578 1.00 49.21 C
ATOM 399 C VAL B 60 124.491 123.817 141.201 1.00 50.31 C
ATOM 400 O VAL B 60 123.587 123.291 141.843 1.00 56.04 O
ATOM 401 CB VAL B 60 126.987 123.219 141.203 1.00 46.38 C
ATOM 402 CG1 VAL B 60 126.946 123.530 142.692 1.00 44.43 C
ATOM 403 CG2 VAL B 60 127.917 122.050 140.912 1.00 44.42 C
ATOM 404 N LEU B 61 124.575 125.129 140.994 1.00 47.93 N
ATOM 405 CA LEU B 61 123.679 126.047 141.661 1.00 46.93 C
ATOM 406 C LEU B 61 122.273 125.782 141.159 1.00 55.14 C
ATOM 407 O LEU B 61 121.348 125.782 141.962 1.00 60.03 O
ATOM 408 CB LEU B 61 124.091 127.495 141.433 1.00 46.27 C
ATOM 409 CG LEU B 61 125.528 127.829 141.836 1.00 40.07 C
ATOM 410 CD1 LEU B 61 125.939 129.188 141.348 1.00 34.00 C
ATOM 411 CD2 LEU B 61 125.714 127.720 143.321 1.00 39.76 C
ATOM 412 N LEU B 62 122.122 125.529 139.856 1.00 54.85 N
ATOM 413 CA LEU B 62 120.806 125.239 139.306 1.00 58.30 C
ATOM 414 C LEU B 62 120.232 123.966 139.928 1.00 62.95 C
ATOM 415 O LEU B 62 119.034 123.918 140.219 1.00 66.95 O
ATOM 416 CB LEU B 62 120.875 125.144 137.784 1.00 58.86 C
ATOM 417 CG LEU B 62 121.071 126.484 137.067 1.00 60.73 C
ATOM 418 CD1 LEU B 62 121.433 126.269 135.596 1.00 61.90 C
ATOM 419 CD2 LEU B 62 119.834 127.389 137.205 1.00 60.85 C
ATOM 420 N ARG B 63 121.084 122.951 140.142 1.00 61.25 N
ATOM 421 CA ARG B 63 120.649 121.715 140.774 1.00 62.82 C
ATOM 422 C ARG B 63 120.198 122.005 142.208 1.00 65.49 C
ATOM 423 O ARG B 63 119.130 121.544 142.597 1.00 71.16 O
ATOM 424 CB ARG B 63 121.763 120.670 140.699 1.00 63.70 C
ATOM 425 CG ARG B 63 121.281 119.252 140.970 1.00 66.03 C
ATOM 426 CD ARG B 63 122.426 118.237 140.937 1.00 67.62 C
ATOM 427 NE ARG B 63 123.181 118.310 139.675 1.00 70.33 N
ATOM 428 CZ ARG B 63 124.482 118.621 139.481 1.00 70.57 C
ATOM 429 NH1 ARG B 63 124.891 118.945 138.256 1.00 72.54 N
ATOM 430 NH2 ARG B 63 125.353 118.689 140.484 1.00 62.25 N
ATOM 431 N GLN B 64 120.982 122.798 142.967 1.00 63.68 N
ATOM 432 CA GLN B 64 120.625 123.210 144.328 1.00 63.88 C
ATOM 433 C GLN B 64 119.292 123.956 144.321 1.00 68.11 C
ATOM 434 O GLN B 64 118.409 123.639 145.113 1.00 73.19 O
ATOM 435 CB GLN B 64 121.745 124.004 145.017 1.00 62.22 C
ATOM 436 CG GLN B 64 122.960 123.124 145.333 1.00 61.91 C
ATOM 437 CD GLN B 64 124.114 123.752 146.102 1.00 60.33 C
ATOM 438 OE1 GLN B 64 124.241 124.982 146.206 1.00 56.73 O
ATOM 439 NE2 GLN B 64 124.994 122.886 146.614 1.00 51.89 N
ATOM 440 N LYS B 65 119.142 124.889 143.376 1.00 65.95 N
ATOM 441 CA LYS B 65 117.913 125.645 143.193 1.00 69.37 C
ATOM 442 C LYS B 65 116.723 124.701 143.027 1.00 73.63 C
ATOM 443 O LYS B 65 115.747 124.819 143.764 1.00 78.05 O
ATOM 444 CB LYS B 65 118.018 126.571 141.975 1.00 68.19 C
ATOM 445 CG LYS B 65 116.987 127.707 141.904 1.00 71.09 C
ATOM 446 CD LYS B 65 117.350 128.850 140.947 1.00 68.92 C
ATOM 447 CE LYS B 65 116.494 130.093 141.060 1.00 68.47 C
ATOM 448 NZ LYS B 65 115.091 129.849 140.682 1.00 75.71 N
ATOM 449 N LYS B 66 116.812 123.769 142.068 1.00 72.99 N
ATOM 450 CA LYS B 66 115.692 122.900 141.727 1.00 77.60 C
ATOM 451 C LYS B 66 115.328 121.950 142.873 1.00 79.41 C
ATOM 452 O LYS B 66 114.149 121.636 143.047 1.00 80.91 O
ATOM 453 CB LYS B 66 115.998 122.119 140.442 1.00 79.13 C
ATOM 454 CG LYS B 66 115.902 122.960 139.174 1.00 81.83 C
ATOM 455 CD LYS B 66 115.874 122.159 137.872 1.00 86.41 C
ATOM 456 CE LYS B 66 115.602 123.024 136.656 1.00 88.80 C
ATOM 457 NZ LYS B 66 115.387 122.266 135.415 1.00 89.25 N
ATOM 458 N LEU B 67 116.334 121.478 143.628 1.00 77.42 N
ATOM 459 CA LEU B 67 116.106 120.594 144.763 1.00 78.43 C
ATOM 460 C LEU B 67 115.465 121.360 145.920 1.00 81.16 C
ATOM 461 O LEU B 67 114.547 120.852 146.565 1.00 84.35 O
ATOM 462 CB LEU B 67 117.423 119.936 145.184 1.00 78.48 C
ATOM 463 CG LEU B 67 117.973 118.861 144.233 1.00 78.97 C
ATOM 464 CD1 LEU B 67 119.402 118.470 144.602 1.00 76.19 C
ATOM 465 CD2 LEU B 67 117.102 117.599 144.160 1.00 80.26 C
ATOM 466 N LEU B 68 115.957 122.580 146.183 1.00 80.34 N
ATOM 467 CA LEU B 68 115.519 123.359 147.338 1.00 81.17 C
ATOM 468 C LEU B 68 114.159 124.031 147.073 1.00 85.18 C
ATOM 469 O LEU B 68 113.423 124.270 148.030 1.00 86.72 O
ATOM 470 CB LEU B 68 116.618 124.351 147.750 1.00 79.50 C
ATOM 471 CG LEU B 68 117.901 123.748 148.359 1.00 76.18 C
ATOM 472 CD1 LEU B 68 119.078 124.744 148.318 1.00 72.18 C
ATOM 473 CD2 LEU B 68 117.683 123.227 149.792 1.00 72.23 C
ATOM 474 N GLU B 69 113.784 124.272 145.798 1.00 84.57 N
ATOM 475 CA GLU B 69 112.454 124.772 145.433 1.00 87.06 C
ATOM 476 C GLU B 69 111.316 123.763 145.699 1.00 89.48 C
ATOM 477 O GLU B 69 110.138 124.120 145.582 1.00 88.76 O
ATOM 478 CB GLU B 69 112.399 125.170 143.953 1.00 86.48 C
ATOM 479 CG GLU B 69 112.977 126.551 143.649 1.00 86.78 C
ATOM 480 CD GLU B 69 112.910 126.950 142.174 1.00 85.48 C
ATOM 481 OE1 GLU B 69 112.308 126.203 141.364 1.00 87.65 O
ATOM 482 OE2 GLU B 69 113.466 128.018 141.827 1.00 79.92 O
ATOM 483 N GLN B 70 111.651 122.509 146.053 1.00 88.24 N
ATOM 484 CA GLN B 70 110.665 121.506 146.444 1.00 90.25 C
ATOM 485 C GLN B 70 110.129 121.753 147.863 1.00 89.96 C
ATOM 486 O GLN B 70 109.003 121.336 148.159 1.00 88.98 O
ATOM 487 CB GLN B 70 111.260 120.093 146.412 1.00 91.74 C
ATOM 488 CG GLN B 70 111.783 119.628 145.052 1.00 91.25 C
ATOM 489 CD GLN B 70 112.318 118.203 145.055 1.00 93.86 C
ATOM 490 OE1 GLN B 70 112.307 117.497 146.073 1.00 95.15 O
ATOM 491 NE2 GLN B 70 112.785 117.749 143.897 1.00 95.45 N
ATOM 492 N GLN B 71 110.933 122.420 148.724 1.00 88.81 N
ATOM 493 CA GLN B 71 110.697 122.539 150.167 1.00 89.24 C
ATOM 494 C GLN B 71 109.687 123.667 150.499 1.00 86.95 C
ATOM 495 O GLN B 71 109.841 124.787 149.923 1.00 84.95 O
ATOM 496 CB GLN B 71 111.991 122.835 150.941 1.00 87.94 C
ATOM 497 CG GLN B 71 113.089 121.773 150.820 1.00 89.12 C
ATOM 498 CD GLN B 71 114.270 121.977 151.759 1.00 88.09 C
ATOM 499 OE1 GLN B 71 114.464 123.046 152.359 1.00 72.04 O
ATOM 500 NE2 GLN B 71 115.086 120.937 151.903 1.00 88.15 N
ATOM 501 OXT GLN B 71 108.798 123.407 151.366 1.00 85.21 O
TER 502 GLN B 71
TER 2873 ASP C 300
TER 5821 PHE D 377
TER 7863 THR E 282
TER 9395 GLN A 186
CONECT 1195 9396
CONECT 1462 9396
CONECT 2463 9396
CONECT 3961 9397
CONECT 8256 8262
CONECT 8262 8256 8263
CONECT 8263 8262 8264 8266
CONECT 8264 8263 8265
CONECT 8265 8264 8268
CONECT 8266 8263 8267 8272
CONECT 8267 8266
CONECT 8268 8265 8269 8270 8271
CONECT 8269 8268 9396
CONECT 8270 8268
CONECT 8271 8268
CONECT 8272 8266
CONECT 9396 1195 1462 2463 8269
CONECT 9397 3961 9401 9404
CONECT 9398 9399 9400 9401 9405
CONECT 9399 9398
CONECT 9400 9398
CONECT 9401 9397 9398
CONECT 9402 9403 9404 9405 9409
CONECT 9403 9402
CONECT 9404 9397 9402
CONECT 9405 9398 9402
CONECT 9406 9407 9408 9409 9410
CONECT 9407 9406
CONECT 9408 9406
CONECT 9409 9402 9406
CONECT 9410 9406 9411
CONECT 9411 9410 9412
CONECT 9412 9411 9413 9414
CONECT 9413 9412 9418
CONECT 9414 9412 9415 9416
CONECT 9415 9414
CONECT 9416 9414 9417 9418
CONECT 9417 9416
CONECT 9418 9413 9416 9419
CONECT 9419 9418 9420 9428
CONECT 9420 9419 9421
CONECT 9421 9420 9422
CONECT 9422 9421 9423 9428
CONECT 9423 9422 9424 9425
CONECT 9424 9423
CONECT 9425 9423 9426
CONECT 9426 9425 9427
CONECT 9427 9426 9428
CONECT 9428 9419 9422 9427
MASTER 304 0 4 51 58 0 0 6 9423 5 49 98
END