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1jsu-original.pdb
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1jsu-original.pdb
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HEADER COMPLEX (TRANSFERASE/CYCLIN/INHIBITOR) 03-JUL-96 1JSU
TITLE P27(KIP1)/CYCLIN A/CDK2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CDK2;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYCLIN A;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 173 - 432;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: P27;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: RESIDUES 22 - 106;
COMPND 17 SYNONYM: KIP1, CIP2;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: SF9;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 12 OTHER_DETAILS: CYCLIN A-BOUND FORM PHOSPHORYLATED ON THR
SOURCE 13 160 IN VITRO USING A CDK-ACTIVATING KINASE CONSISTING OF
SOURCE 14 THE CYCLINH-CDK7 COMPLEX;
SOURCE 15 MOL_ID: 2;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 CELL_LINE: SF9;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 23 OTHER_DETAILS: THE FRAGMENT USED IN THE CRYSTALLIZATION
SOURCE 24 WAS PRODUCED BY THE CLEAVAGE OF FULL-LENGTH CYCLIN A BY
SOURCE 25 SUBTILISIN;
SOURCE 26 MOL_ID: 3;
SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 28 ORGANISM_COMMON: HUMAN;
SOURCE 29 ORGANISM_TAXID: 9606;
SOURCE 30 CELL_LINE: SF9;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS COMPLEX (TRANSFERASE/CYCLIN/INHIBITOR), KINASE, CELL CYCLE,
KEYWDS 2 CELL DIVISION, CDK, CYCLIN, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.RUSSO,P.D.JEFFREY,N.P.PAVLETICH
REVDAT 2 24-FEB-09 1JSU 1 VERSN
REVDAT 1 29-JUL-97 1JSU 0
JRNL AUTH A.A.RUSSO,P.D.JEFFREY,A.K.PATTEN,J.MASSAGUE,
JRNL AUTH 2 N.P.PAVLETICH
JRNL TITL CRYSTAL STRUCTURE OF THE P27KIP1
JRNL TITL 2 CYCLIN-DEPENDENT-KINASE INHIBITOR BOUND TO THE
JRNL TITL 3 CYCLIN A-CDK2 COMPLEX.
JRNL REF NATURE V. 382 325 1996
JRNL REFN ISSN 0028-0836
JRNL PMID 8684460
JRNL DOI 10.1038/382325A0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 31351
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4980
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.012 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.450 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 3.600 ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JSU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-96
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 162339
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.15000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU A 2
REMARK 465 ASN A 3
REMARK 465 PHE A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 VAL A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 ILE A 10
REMARK 465 GLY A 11
REMARK 465 GLU A 12
REMARK 465 ASN B 173
REMARK 465 GLU B 174
REMARK 465 HIS C 23
REMARK 465 PRO C 24
REMARK 465 PRO C 94
REMARK 465 PRO C 95
REMARK 465 LYS C 96
REMARK 465 GLY C 97
REMARK 465 ALA C 98
REMARK 465 CYS C 99
REMARK 465 LYS C 100
REMARK 465 VAL C 101
REMARK 465 PRO C 102
REMARK 465 ALA C 103
REMARK 465 GLN C 104
REMARK 465 GLU C 105
REMARK 465 SER C 106
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 THR A 14 114.30 66.95
REMARK 500 ASN A 23 -102.56 -119.76
REMARK 500 LYS A 24 -162.17 -174.92
REMARK 500 LEU A 25 -162.68 64.06
REMARK 500 GLU A 42 -53.39 79.19
REMARK 500 ASN A 74 12.37 -146.76
REMARK 500 ASP A 127 53.29 -155.05
REMARK 500 ASP A 145 89.08 63.39
REMARK 500 VAL A 164 131.57 74.10
REMARK 500 SER A 181 -155.35 -144.32
REMARK 500 CYS B 193 29.29 -76.92
REMARK 500 PHE B 304 11.02 57.96
REMARK 500 LEU B 320 5.63 -64.57
REMARK 500 GLN B 323 73.00 -118.00
REMARK 500 TRP B 372 114.93 -38.64
REMARK 500 MET C 52 84.65 -66.91
REMARK 500 GLU C 53 -64.13 -155.92
REMARK 500 GLU C 54 -105.01 -11.78
REMARK 500 LEU C 70 -161.25 -166.34
REMARK 500 GLU C 71 -106.52 33.98
REMARK 500 LYS C 73 -31.77 134.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 299
DBREF 1JSU A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 1JSU B 173 432 UNP P20248 CCNA2_HUMAN 173 432
DBREF 1JSU C 23 106 UNP P46527 CDN1B_HUMAN 23 106
SEQADV 1JSU TPO A 160 UNP P24941 THR 160 MODIFIED RESIDUE
SEQRES 1 A 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 A 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 A 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 A 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 A 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 A 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 A 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 A 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 A 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 A 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 A 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 A 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 A 298 ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 A 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 A 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 A 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 A 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 A 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 A 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 A 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 A 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 A 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 A 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
SEQRES 1 B 260 ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR
SEQRES 2 B 260 LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY
SEQRES 3 B 260 TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG
SEQRES 4 B 260 ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU
SEQRES 5 B 260 TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN
SEQRES 6 B 260 TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG
SEQRES 7 B 260 GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU
SEQRES 8 B 260 ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA
SEQRES 9 B 260 GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS
SEQRES 10 B 260 GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU
SEQRES 11 B 260 THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU
SEQRES 12 B 260 THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS
SEQRES 13 B 260 VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU
SEQRES 14 B 260 ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL
SEQRES 15 B 260 ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL
SEQRES 16 B 260 THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR
SEQRES 17 B 260 GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP
SEQRES 18 B 260 LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN
SEQRES 19 B 260 GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS
SEQRES 20 B 260 GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
SEQRES 1 C 84 HIS PRO LYS PRO SER ALA CYS ARG ASN LEU PHE GLY PRO
SEQRES 2 C 84 VAL ASP HIS GLU GLU LEU THR ARG ASP LEU GLU LYS HIS
SEQRES 3 C 84 CYS ARG ASP MET GLU GLU ALA SER GLN ARG LYS TRP ASN
SEQRES 4 C 84 PHE ASP PHE GLN ASN HIS LYS PRO LEU GLU GLY LYS TYR
SEQRES 5 C 84 GLU TRP GLN GLU VAL GLU LYS GLY SER LEU PRO GLU PHE
SEQRES 6 C 84 TYR TYR ARG PRO PRO ARG PRO PRO LYS GLY ALA CYS LYS
SEQRES 7 C 84 VAL PRO ALA GLN GLU SER
MODRES 1JSU TPO A 160 THR PHOSPHOTHREONINE
HET TPO A 160 11
HET SO4 A 299 5
HETNAM TPO PHOSPHOTHREONINE
HETNAM SO4 SULFATE ION
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *197(H2 O)
HELIX 1 1 SER A 46 GLU A 57 1 12
HELIX 2 2 LEU A 87 ALA A 93 1 7
HELIX 3 3 LEU A 101 HIS A 121 1 21
HELIX 4 4 PRO A 130 ASN A 132 5 3
HELIX 5 5 LEU A 166 TYR A 168 5 3
HELIX 6 6 PRO A 171 LEU A 174 1 4
HELIX 7 7 THR A 182 THR A 198 5 17
HELIX 8 8 GLU A 208 LEU A 219 1 12
HELIX 9 9 VAL A 230 SER A 232 5 3
HELIX 10 10 PHE A 248 VAL A 251 1 4
HELIX 11 11 GLU A 257 MET A 266 1 10
HELIX 12 12 ALA A 277 ALA A 282 1 6
HELIX 13 13 PRO A 284 ASP A 288 5 5
HELIX 14 14 HIS B 179 LYS B 192 1 14
HELIX 15 15 TYR B 199 LYS B 202 5 4
HELIX 16 16 ASN B 208 GLU B 224 1 17
HELIX 17 17 ASN B 229 LEU B 243 1 15
HELIX 18 18 ARG B 250 GLU B 268 1 19
HELIX 19 19 VAL B 275 THR B 282 1 8
HELIX 20 20 LYS B 288 VAL B 301 1 14
HELIX 21 21 VAL B 311 HIS B 321 1 11
HELIX 22 22 CYS B 327 ILE B 342 1 16
HELIX 23 23 ALA B 344 LYS B 349 1 6
HELIX 24 24 PRO B 352 THR B 368 1 17
HELIX 25 25 GLU B 374 THR B 380 1 7
HELIX 26 26 LEU B 384 GLN B 403 1 20
HELIX 27 27 SER B 408 LYS B 414 1 7
HELIX 28 28 SER B 416 TYR B 418 5 3
HELIX 29 29 VAL B 421 LEU B 423 5 3
HELIX 30 30 HIS C 38 ARG C 50 1 13
HELIX 31 31 GLU C 54 LYS C 59 1 6
HELIX 32 32 LYS C 81 SER C 83 5 3
HELIX 33 33 GLU C 86 TYR C 89 5 4
SHEET 1 A 5 GLU C 75 GLU C 80 0
SHEET 2 A 5 VAL A 17 ARG A 22 -1 N ARG A 22 O GLU C 75
SHEET 3 A 5 VAL A 29 ARG A 36 -1 N VAL A 30 O ALA A 21
SHEET 4 A 5 LYS A 75 GLU A 81 -1 N PHE A 80 O ALA A 31
SHEET 5 A 5 LEU A 66 HIS A 71 -1 N ILE A 70 O TYR A 77
SHEET 1 B 2 LEU A 133 ILE A 135 0
SHEET 2 B 2 ILE A 141 LEU A 143 -1 N LYS A 142 O LEU A 134
LINK N TPO A 160 C TYR A 159 1555 1555 1.33
LINK C TPO A 160 N HIS A 161 1555 1555 1.32
CISPEP 1 VAL A 154 PRO A 155 0 0.01
CISPEP 2 GLN B 323 PRO B 324 0 -0.16
CISPEP 3 ASP B 345 PRO B 346 0 0.59
CISPEP 4 LYS C 25 PRO C 26 0 -0.35
SITE 1 AC1 5 ARG A 214 ARG A 217 LYS A 278 HOH A 318
SITE 2 AC1 5 HOH A 384
CRYST1 73.800 78.300 137.200 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013550 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012771 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007289 0.00000
ATOM 1 N GLY A 13 3.980 -6.119 88.369 1.00 71.79 N
ATOM 2 CA GLY A 13 3.313 -5.970 87.051 1.00 70.19 C
ATOM 3 C GLY A 13 4.194 -6.679 86.048 1.00 67.78 C
ATOM 4 O GLY A 13 5.302 -7.087 86.404 1.00 68.53 O
ATOM 5 N THR A 14 3.699 -6.865 84.829 1.00 63.28 N
ATOM 6 CA THR A 14 4.459 -7.536 83.778 1.00 57.46 C
ATOM 7 C THR A 14 4.707 -9.019 84.060 1.00 50.10 C
ATOM 8 O THR A 14 5.421 -9.387 85.005 1.00 50.40 O
ATOM 9 CB THR A 14 5.802 -6.835 83.533 1.00 60.47 C
ATOM 10 OG1 THR A 14 5.605 -5.414 83.572 1.00 60.35 O
ATOM 11 CG2 THR A 14 6.356 -7.234 82.170 1.00 63.03 C
ATOM 12 N TYR A 15 4.107 -9.858 83.219 1.00 42.15 N
ATOM 13 CA TYR A 15 4.220 -11.307 83.326 1.00 36.28 C
ATOM 14 C TYR A 15 5.593 -11.782 82.828 1.00 32.11 C
ATOM 15 O TYR A 15 6.074 -11.336 81.791 1.00 33.37 O
ATOM 16 CB TYR A 15 3.091 -11.968 82.508 1.00 35.94 C
ATOM 17 CG TYR A 15 3.001 -13.478 82.646 1.00 31.90 C
ATOM 18 CD1 TYR A 15 2.543 -14.056 83.821 1.00 29.44 C
ATOM 19 CD2 TYR A 15 3.425 -14.323 81.620 1.00 28.92 C
ATOM 20 CE1 TYR A 15 2.514 -15.425 83.976 1.00 29.24 C
ATOM 21 CE2 TYR A 15 3.398 -15.699 81.770 1.00 26.57 C
ATOM 22 CZ TYR A 15 2.942 -16.239 82.952 1.00 30.01 C
ATOM 23 OH TYR A 15 2.920 -17.598 83.138 1.00 36.23 O
ATOM 24 N GLY A 16 6.233 -12.667 83.581 1.00 28.03 N
ATOM 25 CA GLY A 16 7.519 -13.180 83.163 1.00 26.59 C
ATOM 26 C GLY A 16 8.661 -12.913 84.124 1.00 27.78 C
ATOM 27 O GLY A 16 8.545 -12.106 85.052 1.00 24.57 O
ATOM 28 N VAL A 17 9.793 -13.554 83.836 1.00 27.44 N
ATOM 29 CA VAL A 17 11.012 -13.464 84.629 1.00 27.48 C
ATOM 30 C VAL A 17 12.211 -13.197 83.674 1.00 29.98 C
ATOM 31 O VAL A 17 12.071 -13.350 82.459 1.00 33.66 O
ATOM 32 CB VAL A 17 11.221 -14.812 85.382 1.00 24.45 C
ATOM 33 CG1 VAL A 17 12.517 -14.830 86.047 1.00 28.63 C
ATOM 34 CG2 VAL A 17 10.149 -15.020 86.430 1.00 20.68 C
ATOM 35 N VAL A 18 13.348 -12.745 84.213 1.00 24.69 N
ATOM 36 CA VAL A 18 14.570 -12.493 83.443 1.00 21.51 C
ATOM 37 C VAL A 18 15.712 -13.051 84.293 1.00 24.46 C
ATOM 38 O VAL A 18 15.756 -12.812 85.498 1.00 25.58 O
ATOM 39 CB VAL A 18 14.863 -10.976 83.230 1.00 18.04 C
ATOM 40 CG1 VAL A 18 16.229 -10.798 82.582 1.00 12.19 C
ATOM 41 CG2 VAL A 18 13.778 -10.295 82.376 1.00 18.54 C
ATOM 42 N TYR A 19 16.609 -13.820 83.685 1.00 22.84 N
ATOM 43 CA TYR A 19 17.745 -14.385 84.410 1.00 21.19 C
ATOM 44 C TYR A 19 18.785 -13.295 84.608 1.00 25.19 C
ATOM 45 O TYR A 19 19.265 -12.693 83.645 1.00 27.44 O
ATOM 46 CB TYR A 19 18.376 -15.536 83.634 1.00 20.62 C
ATOM 47 CG TYR A 19 17.985 -16.925 84.090 1.00 24.95 C
ATOM 48 CD1 TYR A 19 18.355 -17.403 85.357 1.00 24.86 C
ATOM 49 CD2 TYR A 19 17.290 -17.788 83.231 1.00 28.33 C
ATOM 50 CE1 TYR A 19 18.044 -18.716 85.755 1.00 27.42 C
ATOM 51 CE2 TYR A 19 16.971 -19.089 83.613 1.00 29.58 C
ATOM 52 CZ TYR A 19 17.350 -19.552 84.874 1.00 32.64 C
ATOM 53 OH TYR A 19 17.032 -20.849 85.235 1.00 36.65 O
ATOM 54 N LYS A 20 19.141 -13.060 85.858 1.00 23.95 N
ATOM 55 CA LYS A 20 20.108 -12.047 86.221 1.00 18.78 C
ATOM 56 C LYS A 20 21.223 -12.807 86.925 1.00 22.00 C
ATOM 57 O LYS A 20 21.020 -13.941 87.345 1.00 25.57 O
ATOM 58 CB LYS A 20 19.418 -11.064 87.164 1.00 19.52 C
ATOM 59 CG LYS A 20 20.207 -9.834 87.498 1.00 22.63 C
ATOM 60 CD LYS A 20 19.462 -8.925 88.461 1.00 22.86 C
ATOM 61 CE LYS A 20 20.407 -7.851 88.959 1.00 26.09 C
ATOM 62 NZ LYS A 20 19.833 -6.962 89.995 1.00 28.29 N
ATOM 63 N ALA A 21 22.411 -12.232 87.021 1.00 23.49 N
ATOM 64 CA ALA A 21 23.503 -12.927 87.687 1.00 24.04 C
ATOM 65 C ALA A 21 24.609 -11.992 88.069 1.00 30.08 C
ATOM 66 O ALA A 21 24.938 -11.070 87.324 1.00 31.41 O
ATOM 67 CB ALA A 21 24.063 -14.015 86.796 1.00 24.12 C
ATOM 68 N ARG A 22 25.212 -12.261 89.218 1.00 38.92 N
ATOM 69 CA ARG A 22 26.323 -11.460 89.708 1.00 46.05 C
ATOM 70 C ARG A 22 27.559 -12.346 89.799 1.00 51.11 C
ATOM 71 O ARG A 22 27.463 -13.541 90.076 1.00 51.80 O
ATOM 72 CB ARG A 22 25.996 -10.851 91.080 1.00 44.89 C
ATOM 73 CG ARG A 22 27.043 -9.882 91.606 1.00 45.70 C
ATOM 74 CD ARG A 22 26.608 -9.298 92.941 1.00 51.55 C
ATOM 75 NE ARG A 22 27.658 -8.505 93.581 1.00 55.64 N
ATOM 76 CZ ARG A 22 28.638 -9.012 94.328 1.00 58.24 C
ATOM 77 NH1 ARG A 22 28.716 -10.323 94.543 1.00 58.86 N
ATOM 78 NH2 ARG A 22 29.552 -8.206 94.858 1.00 58.09 N
ATOM 79 N ASN A 23 28.705 -11.766 89.479 1.00 56.03 N
ATOM 80 CA ASN A 23 29.976 -12.461 89.543 1.00 62.33 C
ATOM 81 C ASN A 23 30.797 -11.658 90.543 1.00 67.87 C
ATOM 82 O ASN A 23 30.530 -11.698 91.746 1.00 68.40 O
ATOM 83 CB ASN A 23 30.644 -12.461 88.163 1.00 66.98 C
ATOM 84 CG ASN A 23 32.092 -12.944 88.201 1.00 72.12 C
ATOM 85 OD1 ASN A 23 32.480 -13.727 89.069 1.00 74.86 O
ATOM 86 ND2 ASN A 23 32.900 -12.462 87.262 1.00 73.62 N
ATOM 87 N LYS A 24 31.717 -10.851 90.014 1.00 72.80 N
ATOM 88 CA LYS A 24 32.611 -9.984 90.775 1.00 73.73 C
ATOM 89 C LYS A 24 33.385 -9.167 89.749 1.00 74.21 C
ATOM 90 O LYS A 24 32.985 -9.101 88.579 1.00 72.33 O
ATOM 91 CB LYS A 24 33.546 -10.789 91.702 1.00 71.85 C
ATOM 92 CG LYS A 24 34.296 -11.967 91.090 1.00 66.07 C
ATOM 93 CD LYS A 24 34.743 -12.920 92.196 1.00 61.12 C
ATOM 94 CE LYS A 24 35.783 -13.931 91.724 1.00 59.51 C
ATOM 95 NZ LYS A 24 35.269 -14.958 90.777 1.00 58.61 N
ATOM 96 N LEU A 25 34.499 -8.577 90.159 1.00 78.17 N
ATOM 97 CA LEU A 25 35.285 -7.748 89.253 1.00 84.38 C
ATOM 98 C LEU A 25 34.451 -6.533 88.841 1.00 87.30 C
ATOM 99 O LEU A 25 33.447 -6.206 89.486 1.00 88.20 O
ATOM 100 CB LEU A 25 35.727 -8.532 88.007 1.00 87.38 C
ATOM 101 CG LEU A 25 37.110 -9.190 87.997 1.00 89.71 C
ATOM 102 CD1 LEU A 25 37.191 -10.316 89.028 1.00 90.00 C
ATOM 103 CD2 LEU A 25 37.396 -9.723 86.595 1.00 90.00 C
ATOM 104 N THR A 26 34.865 -5.876 87.765 1.00 87.02 N
ATOM 105 CA THR A 26 34.170 -4.693 87.286 1.00 86.53 C
ATOM 106 C THR A 26 32.778 -4.992 86.714 1.00 83.15 C
ATOM 107 O THR A 26 31.793 -4.387 87.141 1.00 81.89 O
ATOM 108 CB THR A 26 35.062 -3.902 86.278 1.00 89.46 C
ATOM 109 OG1 THR A 26 34.411 -2.683 85.898 1.00 90.00 O
ATOM 110 CG2 THR A 26 35.381 -4.739 85.034 1.00 90.00 C
ATOM 111 N GLY A 27 32.692 -5.946 85.786 1.00 81.51 N
ATOM 112 CA GLY A 27 31.412 -6.292 85.178 1.00 77.87 C
ATOM 113 C GLY A 27 30.741 -7.486 85.838 1.00 71.35 C
ATOM 114 O GLY A 27 30.566 -8.539 85.203 1.00 71.26 O
ATOM 115 N GLU A 28 30.314 -7.296 87.089 1.00 61.92 N
ATOM 116 CA GLU A 28 29.696 -8.360 87.864 1.00 51.83 C
ATOM 117 C GLU A 28 28.241 -8.718 87.639 1.00 40.96 C
ATOM 118 O GLU A 28 27.916 -9.899 87.671 1.00 45.08 O
ATOM 119 CB GLU A 28 29.959 -8.173 89.343 1.00 54.18 C
ATOM 120 CG GLU A 28 29.391 -6.928 89.929 1.00 58.03 C
ATOM 121 CD GLU A 28 29.533 -6.925 91.423 1.00 63.72 C
ATOM 122 OE1 GLU A 28 30.411 -7.663 91.935 1.00 63.93 O
ATOM 123 OE2 GLU A 28 28.755 -6.203 92.084 1.00 67.26 O
ATOM 124 N VAL A 29 27.344 -7.749 87.489 1.00 30.43 N
ATOM 125 CA VAL A 29 25.951 -8.122 87.235 1.00 24.18 C
ATOM 126 C VAL A 29 25.636 -8.052 85.741 1.00 25.91 C
ATOM 127 O VAL A 29 25.960 -7.071 85.048 1.00 25.78 O
ATOM 128 CB VAL A 29 24.940 -7.288 88.036 1.00 20.61 C
ATOM 129 CG1 VAL A 29 23.555 -7.866 87.878 1.00 18.14 C
ATOM 130 CG2 VAL A 29 25.307 -7.302 89.496 1.00 22.27 C
ATOM 131 N VAL A 30 25.028 -9.114 85.235 1.00 23.15 N
ATOM 132 CA VAL A 30 24.687 -9.188 83.827 1.00 21.69 C
ATOM 133 C VAL A 30 23.263 -9.686 83.726 1.00 23.64 C
ATOM 134 O VAL A 30 22.760 -10.307 84.653 1.00 27.55 O
ATOM 135 CB VAL A 30 25.619 -10.182 83.073 1.00 18.90 C
ATOM 136 CG1 VAL A 30 27.077 -9.864 83.369 1.00 14.01 C
ATOM 137 CG2 VAL A 30 25.296 -11.635 83.455 1.00 17.40 C
ATOM 138 N ALA A 31 22.609 -9.409 82.610 1.00 21.49 N
ATOM 139 CA ALA A 31 21.249 -9.867 82.401 1.00 17.82 C
ATOM 140 C ALA A 31 21.235 -10.753 81.157 1.00 17.25 C
ATOM 141 O ALA A 31 21.995 -10.529 80.227 1.00 19.82 O
ATOM 142 CB ALA A 31 20.335 -8.689 82.226 1.00 17.26 C
ATOM 143 N LEU A 32 20.404 -11.784 81.157 1.00 18.95 N
ATOM 144 CA LEU A 32 20.300 -12.677 80.019 1.00 15.93 C
ATOM 145 C LEU A 32 19.083 -12.295 79.216 1.00 21.14 C
ATOM 146 O LEU A 32 18.015 -12.032 79.777 1.00 25.05 O
ATOM 147 CB LEU A 32 20.122 -14.116 80.476 1.00 17.91 C
ATOM 148 CG LEU A 32 21.086 -15.160 79.936 1.00 21.71 C
ATOM 149 CD1 LEU A 32 20.472 -16.535 80.133 1.00 22.50 C
ATOM 150 CD2 LEU A 32 21.355 -14.903 78.455 1.00 22.16 C
ATOM 151 N LYS A 33 19.236 -12.254 77.900 1.00 22.90 N
ATOM 152 CA LYS A 33 18.117 -11.945 77.030 1.00 23.09 C
ATOM 153 C LYS A 33 18.053 -13.117 76.066 1.00 26.26 C
ATOM 154 O LYS A 33 19.087 -13.615 75.633 1.00 25.65 O
ATOM 155 CB LYS A 33 18.338 -10.621 76.308 1.00 21.24 C
ATOM 156 CG LYS A 33 17.044 -9.982 75.890 1.00 18.83 C
ATOM 157 CD LYS A 33 17.201 -8.548 75.428 1.00 16.05 C
ATOM 158 CE LYS A 33 15.855 -8.072 74.906 1.00 16.01 C
ATOM 159 NZ LYS A 33 15.855 -6.736 74.247 1.00 16.99 N
ATOM 160 N LYS A 34 16.857 -13.609 75.784 1.00 29.03 N
ATOM 161 CA LYS A 34 16.723 -14.757 74.897 1.00 35.08 C
ATOM 162 C LYS A 34 15.672 -14.558 73.809 1.00 36.59 C
ATOM 163 O LYS A 34 14.616 -13.958 74.041 1.00 36.49 O
ATOM 164 CB LYS A 34 16.384 -15.992 75.714 1.00 38.61 C
ATOM 165 CG LYS A 34 16.677 -17.289 75.021 1.00 42.90 C
ATOM 166 CD LYS A 34 15.814 -18.381 75.611 1.00 47.67 C
ATOM 167 CE LYS A 34 14.350 -18.071 75.359 1.00 49.76 C
ATOM 168 NZ LYS A 34 14.105 -17.841 73.904 1.00 49.72 N
ATOM 169 N ILE A 35 15.968 -15.089 72.627 1.00 35.89 N
ATOM 170 CA ILE A 35 15.086 -14.981 71.471 1.00 33.91 C
ATOM 171 C ILE A 35 14.724 -16.362 70.932 1.00 32.83 C
ATOM 172 O ILE A 35 15.593 -17.214 70.749 1.00 29.80 O
ATOM 173 CB ILE A 35 15.790 -14.197 70.331 1.00 35.67 C
ATOM 174 CG1 ILE A 35 16.137 -12.782 70.799 1.00 37.39 C
ATOM 175 CG2 ILE A 35 14.940 -14.186 69.065 1.00 36.06 C
ATOM 176 CD1 ILE A 35 17.005 -12.004 69.821 1.00 38.76 C
ATOM 177 N ARG A 36 13.438 -16.600 70.729 1.00 39.88 N
ATOM 178 CA ARG A 36 12.999 -17.866 70.166 1.00 49.33 C
ATOM 179 C ARG A 36 13.124 -17.660 68.657 1.00 49.61 C
ATOM 180 O ARG A 36 12.777 -16.589 68.146 1.00 48.95 O
ATOM 181 CB ARG A 36 11.542 -18.156 70.537 1.00 59.81 C
ATOM 182 CG ARG A 36 11.331 -19.421 71.383 1.00 68.18 C
ATOM 183 CD ARG A 36 11.565 -19.184 72.872 1.00 74.54 C
ATOM 184 NE ARG A 36 10.494 -18.408 73.507 1.00 80.31 N
ATOM 185 CZ ARG A 36 10.538 -17.096 73.749 1.00 83.18 C
ATOM 186 NH1 ARG A 36 11.604 -16.379 73.408 1.00 83.13 N
ATOM 187 NH2 ARG A 36 9.516 -16.501 74.355 1.00 84.12 N
ATOM 188 N LEU A 37 13.626 -18.668 67.949 1.00 51.29 N
ATOM 189 CA LEU A 37 13.811 -18.560 66.501 1.00 52.90 C
ATOM 190 C LEU A 37 12.906 -19.439 65.606 1.00 59.71 C
ATOM 191 O LEU A 37 12.566 -20.583 65.961 1.00 59.87 O
ATOM 192 CB LEU A 37 15.283 -18.816 66.157 1.00 44.36 C
ATOM 193 CG LEU A 37 16.301 -17.917 66.859 1.00 39.34 C
ATOM 194 CD1 LEU A 37 17.688 -18.416 66.569 1.00 38.67 C
ATOM 195 CD2 LEU A 37 16.146 -16.475 66.426 1.00 37.15 C
ATOM 196 N ASP A 38 12.480 -18.870 64.473 1.00 63.10 N
ATOM 197 CA ASP A 38 11.674 -19.593 63.489 1.00 67.20 C
ATOM 198 C ASP A 38 12.710 -20.369 62.656 1.00 66.59 C
ATOM 199 O ASP A 38 13.585 -19.776 62.007 1.00 62.38 O
ATOM 200 CB ASP A 38 10.870 -18.622 62.606 1.00 70.95 C
ATOM 201 CG ASP A 38 9.932 -19.339 61.609 1.00 74.34 C
ATOM 202 OD1 ASP A 38 9.981 -20.586 61.480 1.00 75.44 O
ATOM 203 OD2 ASP A 38 9.148 -18.634 60.928 1.00 74.73 O
ATOM 204 N THR A 39 12.610 -21.694 62.702 1.00 67.70 N
ATOM 205 CA THR A 39 13.545 -22.575 62.017 1.00 68.22 C
ATOM 206 C THR A 39 13.303 -22.862 60.540 1.00 65.89 C
ATOM 207 O THR A 39 14.251 -23.163 59.820 1.00 66.42 O
ATOM 208 CB THR A 39 13.659 -23.915 62.772 1.00 73.08 C
ATOM 209 OG1 THR A 39 13.694 -23.656 64.182 1.00 75.08 O
ATOM 210 CG2 THR A 39 14.936 -24.672 62.364 1.00 74.28 C
ATOM 211 N GLU A 40 12.055 -22.800 60.086 1.00 64.10 N
ATOM 212 CA GLU A 40 11.759 -23.089 58.680 1.00 63.99 C
ATOM 213 C GLU A 40 11.577 -21.854 57.814 1.00 58.44 C
ATOM 214 O GLU A 40 11.644 -21.924 56.593 1.00 54.99 O
ATOM 215 CB GLU A 40 10.526 -24.000 58.571 1.00 71.23 C
ATOM 216 CG GLU A 40 9.890 -24.131 57.164 1.00 77.42 C
ATOM 217 CD GLU A 40 10.783 -24.799 56.110 1.00 81.39 C
ATOM 218 OE1 GLU A 40 11.925 -25.207 56.422 1.00 82.55 O
ATOM 219 OE2 GLU A 40 10.329 -24.917 54.949 1.00 82.85 O
ATOM 220 N THR A 41 11.382 -20.711 58.448 1.00 58.92 N
ATOM 221 CA THR A 41 11.171 -19.486 57.706 1.00 57.60 C
ATOM 222 C THR A 41 11.703 -18.288 58.489 1.00 53.98 C
ATOM 223 O THR A 41 11.608 -18.238 59.710 1.00 57.47 O
ATOM 224 CB THR A 41 9.660 -19.356 57.326 1.00 60.73 C
ATOM 225 OG1 THR A 41 9.446 -19.927 56.024 1.00 61.15 O
ATOM 226 CG2 THR A 41 9.177 -17.913 57.351 1.00 61.46 C
ATOM 227 N GLU A 42 12.370 -17.388 57.780 1.00 48.05 N
ATOM 228 CA GLU A 42 12.941 -16.180 58.359 1.00 40.33 C
ATOM 229 C GLU A 42 14.256 -16.320 59.102 1.00 27.34 C
ATOM 230 O GLU A 42 15.202 -15.634 58.761 1.00 26.53 O
ATOM 231 CB GLU A 42 11.900 -15.426 59.178 1.00 47.63 C
ATOM 232 CG GLU A 42 10.696 -14.993 58.326 1.00 54.50 C
ATOM 233 CD GLU A 42 11.100 -14.290 57.024 1.00 59.10 C
ATOM 234 OE1 GLU A 42 11.356 -13.064 57.072 1.00 62.20 O
ATOM 235 OE2 GLU A 42 11.156 -14.959 55.958 1.00 57.93 O
ATOM 236 N GLY A 43 14.347 -17.221 60.074 1.00 20.51 N
ATOM 237 CA GLY A 43 15.601 -17.394 60.795 1.00 16.51 C
ATOM 238 C GLY A 43 15.893 -16.253 61.754 1.00 20.46 C
ATOM 239 O GLY A 43 14.978 -15.738 62.395 1.00 24.98 O
ATOM 240 N VAL A 44 17.152 -15.841 61.857 1.00 19.80 N
ATOM 241 CA VAL A 44 17.525 -14.753 62.771 1.00 19.30 C
ATOM 242 C VAL A 44 16.891 -13.427 62.334 1.00 22.86 C
ATOM 243 O VAL A 44 17.110 -12.968 61.211 1.00 23.10 O
ATOM 244 CB VAL A 44 19.068 -14.568 62.868 1.00 18.56 C
ATOM 245 CG1 VAL A 44 19.415 -13.500 63.912 1.00 19.20 C
ATOM 246 CG2 VAL A 44 19.760 -15.890 63.189 1.00 14.34 C
ATOM 247 N PRO A 45 16.109 -12.787 63.231 1.00 24.15 N
ATOM 248 CA PRO A 45 15.459 -11.515 62.898 1.00 20.06 C
ATOM 249 C PRO A 45 16.477 -10.484 62.446 1.00 17.54 C
ATOM 250 O PRO A 45 17.580 -10.427 62.984 1.00 21.73 O
ATOM 251 CB PRO A 45 14.807 -11.107 64.226 1.00 18.54 C
ATOM 252 CG PRO A 45 14.545 -12.429 64.909 1.00 15.03 C
ATOM 253 CD PRO A 45 15.821 -13.174 64.628 1.00 19.94 C
ATOM 254 N SER A 46 16.112 -9.659 61.470 1.00 16.37 N
ATOM 255 CA SER A 46 17.034 -8.644 60.997 1.00 15.55 C
ATOM 256 C SER A 46 17.315 -7.600 62.055 1.00 17.44 C
ATOM 257 O SER A 46 18.415 -7.052 62.082 1.00 18.77 O
ATOM 258 CB SER A 46 16.575 -8.026 59.682 1.00 21.97 C
ATOM 259 OG SER A 46 15.248 -7.566 59.749 1.00 30.22 O
ATOM 260 N THR A 47 16.367 -7.392 62.977 1.00 20.40 N
ATOM 261 CA THR A 47 16.550 -6.436 64.080 1.00 22.21 C
ATOM 262 C THR A 47 17.693 -6.938 64.949 1.00 22.42 C
ATOM 263 O THR A 47 18.560 -6.167 65.356 1.00 25.57 O
ATOM 264 CB THR A 47 15.294 -6.307 65.003 1.00 21.38 C
ATOM 265 OG1 THR A 47 14.717 -7.598 65.231 1.00 22.45 O
ATOM 266 CG2 THR A 47 14.284 -5.402 64.405 1.00 19.39 C
ATOM 267 N ALA A 48 17.663 -8.233 65.256 1.00 21.21 N
ATOM 268 CA ALA A 48 18.708 -8.853 66.063 1.00 17.39 C
ATOM 269 C ALA A 48 20.019 -8.792 65.275 1.00 21.64 C
ATOM 270 O ALA A 48 21.068 -8.496 65.841 1.00 25.12 O
ATOM 271 CB ALA A 48 18.345 -10.307 66.410 1.00 11.53 C
ATOM 272 N ILE A 49 19.954 -9.012 63.963 1.00 22.62 N
ATOM 273 CA ILE A 49 21.161 -8.961 63.136 1.00 23.06 C
ATOM 274 C ILE A 49 21.839 -7.582 63.139 1.00 20.08 C
ATOM 275 O ILE A 49 23.072 -7.484 63.214 1.00 17.61 O
ATOM 276 CB ILE A 49 20.879 -9.483 61.714 1.00 19.16 C
ATOM 277 CG1 ILE A 49 21.127 -10.988 61.699 1.00 17.46 C
ATOM 278 CG2 ILE A 49 21.733 -8.754 60.679 1.00 17.04 C
ATOM 279 CD1 ILE A 49 20.486 -11.683 60.566 1.00 20.19 C
ATOM 280 N ARG A 50 21.029 -6.529 63.119 1.00 16.42 N
ATOM 281 CA ARG A 50 21.536 -5.164 63.154 1.00 14.35 C
ATOM 282 C ARG A 50 22.039 -4.795 64.546 1.00 15.05 C
ATOM 283 O ARG A 50 23.148 -4.274 64.687 1.00 15.96 O
ATOM 284 CB ARG A 50 20.457 -4.194 62.702 1.00 10.88 C
ATOM 285 CG ARG A 50 20.172 -4.330 61.220 1.00 15.62 C
ATOM 286 CD ARG A 50 18.912 -3.594 60.800 1.00 21.38 C
ATOM 287 NE ARG A 50 19.000 -3.170 59.404 1.00 28.98 N
ATOM 288 CZ ARG A 50 18.112 -2.396 58.783 1.00 31.25 C
ATOM 289 NH1 ARG A 50 17.039 -1.942 59.426 1.00 32.52 N
ATOM 290 NH2 ARG A 50 18.296 -2.084 57.508 1.00 27.90 N
ATOM 291 N GLU A 51 21.263 -5.114 65.578 1.00 11.92 N
ATOM 292 CA GLU A 51 21.678 -4.795 66.940 1.00 12.40 C
ATOM 293 C GLU A 51 22.944 -5.518 67.335 1.00 10.50 C
ATOM 294 O GLU A 51 23.841 -4.925 67.914 1.00 15.35 O
ATOM 295 CB GLU A 51 20.595 -5.118 67.979 1.00 15.83 C
ATOM 296 CG GLU A 51 21.125 -4.979 69.421 1.00 18.70 C
ATOM 297 CD GLU A 51 20.040 -4.929 70.480 1.00 27.25 C
ATOM 298 OE1 GLU A 51 19.119 -5.776 70.410 1.00 29.47 O
ATOM 299 OE2 GLU A 51 20.115 -4.044 71.380 1.00 28.61 O
ATOM 300 N ILE A 52 23.029 -6.805 67.038 1.00 8.24 N
ATOM 301 CA ILE A 52 24.206 -7.562 67.427 1.00 6.91 C
ATOM 302 C ILE A 52 25.436 -7.134 66.667 1.00 9.92 C
ATOM 303 O ILE A 52 26.460 -6.842 67.275 1.00 16.18 O
ATOM 304 CB ILE A 52 24.010 -9.068 67.260 1.00 8.34 C
ATOM 305 CG1 ILE A 52 22.884 -9.550 68.166 1.00 8.04 C
ATOM 306 CG2 ILE A 52 25.314 -9.796 67.580 1.00 6.40 C
ATOM 307 CD1 ILE A 52 22.601 -11.045 68.039 1.00 11.72 C
ATOM 308 N SER A 53 25.333 -7.046 65.346 1.00 13.76 N
ATOM 309 CA SER A 53 26.494 -6.658 64.545 1.00 18.16 C
ATOM 310 C SER A 53 26.996 -5.253 64.876 1.00 18.05 C
ATOM 311 O SER A 53 28.197 -5.047 65.053 1.00 18.64 O
ATOM 312 CB SER A 53 26.224 -6.812 63.033 1.00 16.59 C
ATOM 313 OG SER A 53 25.179 -5.972 62.569 1.00 15.35 O
ATOM 314 N LEU A 54 26.066 -4.318 65.044 1.00 17.36 N
ATOM 315 CA LEU A 54 26.413 -2.931 65.339 1.00 15.24 C
ATOM 316 C LEU A 54 26.855 -2.697 66.761 1.00 16.39 C
ATOM 317 O LEU A 54 27.859 -2.026 67.004 1.00 18.12 O
ATOM 318 CB LEU A 54 25.244 -2.000 64.994 1.00 12.41 C
ATOM 319 CG LEU A 54 24.828 -2.025 63.512 1.00 9.06 C
ATOM 320 CD1 LEU A 54 23.625 -1.125 63.304 1.00 3.65 C
ATOM 321 CD2 LEU A 54 26.015 -1.617 62.611 1.00 8.75 C
ATOM 322 N LEU A 55 26.112 -3.274 67.698 1.00 18.49 N
ATOM 323 CA LEU A 55 26.393 -3.128 69.124 1.00 20.63 C
ATOM 324 C LEU A 55 27.751 -3.670 69.495 1.00 20.84 C
ATOM 325 O LEU A 55 28.434 -3.103 70.335 1.00 21.51 O
ATOM 326 CB LEU A 55 25.318 -3.825 69.948 1.00 22.26 C
ATOM 327 CG LEU A 55 25.069 -3.251 71.327 1.00 20.66 C
ATOM 328 CD1 LEU A 55 25.260 -1.749 71.297 1.00 22.03 C
ATOM 329 CD2 LEU A 55 23.672 -3.638 71.780 1.00 16.95 C
ATOM 330 N LYS A 56 28.175 -4.747 68.848 1.00 25.52 N
ATOM 331 CA LYS A 56 29.485 -5.290 69.164 1.00 28.06 C
ATOM 332 C LYS A 56 30.618 -4.390 68.662 1.00 29.43 C
ATOM 333 O LYS A 56 31.784 -4.628 68.964 1.00 31.34 O
ATOM 334 CB LYS A 56 29.621 -6.731 68.674 1.00 29.96 C
ATOM 335 CG LYS A 56 29.693 -6.934 67.178 1.00 31.85 C
ATOM 336 CD LYS A 56 29.224 -8.347 66.836 1.00 34.85 C
ATOM 337 CE LYS A 56 29.766 -9.413 67.797 1.00 36.10 C
ATOM 338 NZ LYS A 56 31.225 -9.690 67.605 1.00 38.94 N
ATOM 339 N GLU A 57 30.263 -3.343 67.919 1.00 29.60 N
ATOM 340 CA GLU A 57 31.229 -2.375 67.415 1.00 31.00 C
ATOM 341 C GLU A 57 31.106 -1.065 68.195 1.00 37.72 C
ATOM 342 O GLU A 57 31.732 -0.058 67.845 1.00 43.20 O
ATOM 343 CB GLU A 57 30.981 -2.085 65.941 1.00 31.96 C
ATOM 344 CG GLU A 57 31.517 -3.151 65.017 1.00 37.93 C
ATOM 345 CD GLU A 57 31.569 -2.703 63.568 1.00 44.94 C
ATOM 346 OE1 GLU A 57 31.623 -1.481 63.308 1.00 46.79 O
ATOM 347 OE2 GLU A 57 31.579 -3.581 62.684 1.00 49.01 O
ATOM 348 N LEU A 58 30.311 -1.077 69.263 1.00 34.17 N
ATOM 349 CA LEU A 58 30.096 0.125 70.058 1.00 27.16 C
ATOM 350 C LEU A 58 30.404 -0.049 71.557 1.00 25.13 C
ATOM 351 O LEU A 58 29.520 -0.035 72.414 1.00 25.05 O
ATOM 352 CB LEU A 58 28.664 0.632 69.828 1.00 19.93 C
ATOM 353 CG LEU A 58 28.314 0.967 68.379 1.00 11.20 C
ATOM 354 CD1 LEU A 58 26.855 1.217 68.252 1.00 8.24 C
ATOM 355 CD2 LEU A 58 29.117 2.161 67.908 1.00 10.87 C
ATOM 356 N ASN A 59 31.679 -0.215 71.860 1.00 23.86 N
ATOM 357 CA ASN A 59 32.114 -0.376 73.228 1.00 25.49 C
ATOM 358 C ASN A 59 32.418 1.029 73.766 1.00 21.12 C
ATOM 359 O ASN A 59 33.465 1.623 73.467 1.00 18.99 O
ATOM 360 CB ASN A 59 33.355 -1.269 73.264 1.00 34.44 C
ATOM 361 CG ASN A 59 33.666 -1.796 74.653 1.00 45.52 C
ATOM 362 OD1 ASN A 59 33.149 -1.302 75.659 1.00 51.97 O
ATOM 363 ND2 ASN A 59 34.518 -2.811 74.716 1.00 47.36 N
ATOM 364 N HIS A 60 31.474 1.576 74.523 1.00 17.21 N
ATOM 365 CA HIS A 60 31.613 2.906 75.108 1.00 14.65 C
ATOM 366 C HIS A 60 30.996 2.856 76.501 1.00 13.02 C
ATOM 367 O HIS A 60 30.030 2.135 76.720 1.00 14.70 O
ATOM 368 CB HIS A 60 30.881 3.940 74.237 1.00 14.76 C
ATOM 369 CG HIS A 60 31.142 5.365 74.625 1.00 16.11 C
ATOM 370 ND1 HIS A 60 30.333 6.063 75.497 1.00 18.45 N
ATOM 371 CD2 HIS A 60 32.116 6.228 74.248 1.00 15.01 C
ATOM 372 CE1 HIS A 60 30.801 7.291 75.645 1.00 14.87 C
ATOM 373 NE2 HIS A 60 31.882 7.416 74.898 1.00 12.55 N
ATOM 374 N PRO A 61 31.527 3.642 77.457 1.00 14.18 N
ATOM 375 CA PRO A 61 30.981 3.645 78.822 1.00 12.13 C
ATOM 376 C PRO A 61 29.527 4.116 78.924 1.00 14.95 C
ATOM 377 O PRO A 61 28.842 3.845 79.908 1.00 12.04 O
ATOM 378 CB PRO A 61 31.948 4.563 79.576 1.00 11.75 C
ATOM 379 CG PRO A 61 32.509 5.450 78.511 1.00 14.07 C
ATOM 380 CD PRO A 61 32.727 4.496 77.378 1.00 15.00 C
ATOM 381 N ASN A 62 29.043 4.776 77.879 1.00 13.51 N
ATOM 382 CA ASN A 62 27.676 5.264 77.869 1.00 8.14 C
ATOM 383 C ASN A 62 26.800 4.537 76.870 1.00 11.21 C
ATOM 384 O ASN A 62 25.851 5.118 76.338 1.00 11.27 O
ATOM 385 CB ASN A 62 27.651 6.745 77.587 1.00 9.58 C
ATOM 386 CG ASN A 62 28.238 7.535 78.700 1.00 11.98 C
ATOM 387 OD1 ASN A 62 29.235 8.234 78.517 1.00 12.30 O
ATOM 388 ND2 ASN A 62 27.652 7.407 79.885 1.00 12.04 N
ATOM 389 N ILE A 63 27.172 3.293 76.560 1.00 9.10 N
ATOM 390 CA ILE A 63 26.412 2.446 75.657 1.00 7.80 C
ATOM 391 C ILE A 63 26.383 1.101 76.366 1.00 13.95 C
ATOM 392 O ILE A 63 27.438 0.567 76.698 1.00 15.49 O
ATOM 393 CB ILE A 63 27.079 2.310 74.278 1.00 7.00 C
ATOM 394 CG1 ILE A 63 27.096 3.661 73.568 1.00 6.65 C
ATOM 395 CG2 ILE A 63 26.325 1.289 73.420 1.00 9.14 C
ATOM 396 CD1 ILE A 63 27.746 3.623 72.204 1.00 8.47 C
ATOM 397 N VAL A 64 25.180 0.614 76.692 1.00 16.37 N
ATOM 398 CA VAL A 64 25.014 -0.669 77.387 1.00 18.01 C
ATOM 399 C VAL A 64 25.719 -1.786 76.616 1.00 20.23 C
ATOM 400 O VAL A 64 25.386 -2.067 75.470 1.00 20.72 O
ATOM 401 CB VAL A 64 23.513 -1.033 77.572 1.00 18.30 C
ATOM 402 CG1 VAL A 64 23.371 -2.388 78.246 1.00 15.32 C
ATOM 403 CG2 VAL A 64 22.815 0.032 78.401 1.00 20.39 C
ATOM 404 N LYS A 65 26.687 -2.413 77.268 1.00 18.56 N
ATOM 405 CA LYS A 65 27.490 -3.468 76.693 1.00 17.17 C
ATOM 406 C LYS A 65 26.830 -4.786 76.377 1.00 16.78 C
ATOM 407 O LYS A 65 26.153 -5.365 77.218 1.00 15.38 O
ATOM 408 CB LYS A 65 28.667 -3.770 77.620 1.00 24.55 C
ATOM 409 CG LYS A 65 29.793 -2.765 77.596 1.00 32.66 C
ATOM 410 CD LYS A 65 30.813 -3.146 76.541 1.00 42.64 C
ATOM 411 CE LYS A 65 31.422 -4.516 76.831 1.00 49.26 C
ATOM 412 NZ LYS A 65 32.137 -5.082 75.650 1.00 52.93 N
ATOM 413 N LEU A 66 27.051 -5.265 75.155 1.00 21.04 N
ATOM 414 CA LEU A 66 26.575 -6.583 74.749 1.00 21.87 C
ATOM 415 C LEU A 66 27.827 -7.392 75.100 1.00 25.91 C
ATOM 416 O LEU A 66 28.908 -7.105 74.604 1.00 26.86 O
ATOM 417 CB LEU A 66 26.296 -6.648 73.244 1.00 18.63 C
ATOM 418 CG LEU A 66 25.995 -8.046 72.673 1.00 18.28 C
ATOM 419 CD1 LEU A 66 24.843 -8.731 73.403 1.00 17.02 C
ATOM 420 CD2 LEU A 66 25.691 -7.931 71.203 1.00 16.63 C
ATOM 421 N LEU A 67 27.714 -8.298 76.060 1.00 26.97 N
ATOM 422 CA LEU A 67 28.868 -9.077 76.489 1.00 22.86 C
ATOM 423 C LEU A 67 29.055 -10.408 75.764 1.00 24.12 C
ATOM 424 O LEU A 67 30.180 -10.898 75.659 1.00 27.28 O
ATOM 425 CB LEU A 67 28.809 -9.309 78.001 1.00 20.67 C
ATOM 426 CG LEU A 67 28.525 -8.077 78.870 1.00 24.45 C
ATOM 427 CD1 LEU A 67 28.087 -8.526 80.237 1.00 27.28 C
ATOM 428 CD2 LEU A 67 29.728 -7.158 78.967 1.00 22.70 C
ATOM 429 N ASP A 68 27.975 -11.002 75.267 1.00 20.03 N
ATOM 430 CA ASP A 68 28.111 -12.278 74.590 1.00 20.66 C
ATOM 431 C ASP A 68 26.833 -12.595 73.846 1.00 23.34 C
ATOM 432 O ASP A 68 25.804 -11.980 74.097 1.00 26.92 O
ATOM 433 CB ASP A 68 28.424 -13.385 75.621 1.00 26.88 C
ATOM 434 CG ASP A 68 29.025 -14.657 74.986 1.00 34.57 C
ATOM 435 OD1 ASP A 68 29.193 -14.723 73.748 1.00 38.89 O
ATOM 436 OD2 ASP A 68 29.341 -15.608 75.727 1.00 34.76 O
ATOM 437 N VAL A 69 26.929 -13.518 72.892 1.00 23.12 N
ATOM 438 CA VAL A 69 25.808 -13.976 72.079 1.00 23.37 C
ATOM 439 C VAL A 69 25.943 -15.500 71.989 1.00 26.28 C
ATOM 440 O VAL A 69 27.049 -16.020 71.829 1.00 26.71 O
ATOM 441 CB VAL A 69 25.883 -13.406 70.629 1.00 22.14 C
ATOM 442 CG1 VAL A 69 24.665 -13.856 69.811 1.00 21.56 C
ATOM 443 CG2 VAL A 69 25.994 -11.887 70.647 1.00 19.85 C
ATOM 444 N ILE A 70 24.839 -16.217 72.151 1.00 30.37 N
ATOM 445 CA ILE A 70 24.851 -17.677 72.064 1.00 29.96 C
ATOM 446 C ILE A 70 23.727 -18.099 71.115 1.00 29.35 C
ATOM 447 O ILE A 70 22.551 -17.887 71.398 1.00 29.33 O
ATOM 448 CB ILE A 70 24.674 -18.353 73.460 1.00 29.94 C
ATOM 449 CG1 ILE A 70 25.833 -17.974 74.403 1.00 27.21 C
ATOM 450 CG2 ILE A 70 24.597 -19.876 73.311 1.00 29.85 C
ATOM 451 CD1 ILE A 70 25.717 -16.577 75.068 1.00 25.72 C
ATOM 452 N HIS A 71 24.104 -18.627 69.956 1.00 31.34 N
ATOM 453 CA HIS A 71 23.146 -19.058 68.941 1.00 33.05 C
ATOM 454 C HIS A 71 23.008 -20.584 68.959 1.00 31.53 C
ATOM 455 O HIS A 71 23.821 -21.307 68.378 1.00 31.45 O
ATOM 456 CB HIS A 71 23.609 -18.551 67.556 1.00 35.17 C
ATOM 457 CG HIS A 71 22.568 -18.628 66.471 1.00 36.07 C
ATOM 458 ND1 HIS A 71 21.332 -19.215 66.642 1.00 36.61 N
ATOM 459 CD2 HIS A 71 22.594 -18.184 65.190 1.00 37.56 C
ATOM 460 CE1 HIS A 71 20.643 -19.129 65.518 1.00 37.67 C
ATOM 461 NE2 HIS A 71 21.387 -18.508 64.621 1.00 37.80 N
ATOM 462 N THR A 72 21.958 -21.060 69.615 1.00 32.95 N
ATOM 463 CA THR A 72 21.695 -22.488 69.718 1.00 37.11 C
ATOM 464 C THR A 72 20.826 -22.964 68.564 1.00 42.52 C
ATOM 465 O THR A 72 20.506 -22.207 67.641 1.00 41.50 O
ATOM 466 CB THR A 72 20.957 -22.862 71.039 1.00 35.03 C
ATOM 467 OG1 THR A 72 19.608 -22.372 70.995 1.00 33.59 O
ATOM 468 CG2 THR A 72 21.684 -22.291 72.256 1.00 33.84 C
ATOM 469 N GLU A 73 20.393 -24.211 68.680 1.00 45.32 N
ATOM 470 CA GLU A 73 19.562 -24.856 67.689 1.00 48.28 C
ATOM 471 C GLU A 73 18.340 -24.030 67.301 1.00 47.22 C
ATOM 472 O GLU A 73 17.996 -23.934 66.122 1.00 47.31 O
ATOM 473 CB GLU A 73 19.141 -26.255 68.194 1.00 54.71 C
ATOM 474 CG GLU A 73 18.089 -26.323 69.353 1.00 56.45 C
ATOM 475 CD GLU A 73 18.620 -25.976 70.756 1.00 57.34 C
ATOM 476 OE1 GLU A 73 19.815 -26.211 71.053 1.00 57.51 O
ATOM 477 OE2 GLU A 73 17.812 -25.494 71.580 1.00 56.91 O
ATOM 478 N ASN A 74 17.710 -23.398 68.284 1.00 46.70 N
ATOM 479 CA ASN A 74 16.511 -22.618 68.015 1.00 47.04 C
ATOM 480 C ASN A 74 16.353 -21.395 68.903 1.00 43.07 C
ATOM 481 O ASN A 74 15.288 -20.764 68.916 1.00 41.23 O
ATOM 482 CB ASN A 74 15.281 -23.514 68.148 1.00 53.27 C
ATOM 483 CG ASN A 74 15.342 -24.397 69.376 1.00 57.93 C
ATOM 484 OD1 ASN A 74 15.933 -24.032 70.393 1.00 58.81 O
ATOM 485 ND2 ASN A 74 14.777 -25.590 69.271 1.00 60.15 N
ATOM 486 N LYS A 75 17.417 -21.043 69.619 1.00 39.89 N
ATOM 487 CA LYS A 75 17.389 -19.884 70.497 1.00 36.14 C
ATOM 488 C LYS A 75 18.618 -19.029 70.266 1.00 29.22 C
ATOM 489 O LYS A 75 19.630 -19.516 69.765 1.00 28.20 O
ATOM 490 CB LYS A 75 17.361 -20.318 71.965 1.00 38.27 C
ATOM 491 CG LYS A 75 16.047 -20.944 72.444 1.00 37.22 C
ATOM 492 CD LYS A 75 16.236 -21.566 73.819 1.00 34.68 C
ATOM 493 CE LYS A 75 17.347 -22.603 73.788 1.00 31.99 C
ATOM 494 NZ LYS A 75 17.727 -23.081 75.142 1.00 33.36 N
ATOM 495 N LEU A 76 18.498 -17.745 70.580 1.00 25.72 N
ATOM 496 CA LEU A 76 19.607 -16.799 70.468 1.00 24.94 C
ATOM 497 C LEU A 76 19.658 -16.016 71.792 1.00 21.12 C
ATOM 498 O LEU A 76 18.705 -15.324 72.161 1.00 19.48 O
ATOM 499 CB LEU A 76 19.404 -15.857 69.266 1.00 25.95 C
ATOM 500 CG LEU A 76 20.509 -14.839 68.935 1.00 22.13 C
ATOM 501 CD1 LEU A 76 21.855 -15.525 68.719 1.00 19.27 C
ATOM 502 CD2 LEU A 76 20.099 -14.036 67.715 1.00 20.04 C
ATOM 503 N TYR A 77 20.739 -16.206 72.536 1.00 20.88 N
ATOM 504 CA TYR A 77 20.934 -15.557 73.826 1.00 21.95 C
ATOM 505 C TYR A 77 21.845 -14.343 73.729 1.00 25.73 C
ATOM 506 O TYR A 77 22.882 -14.393 73.060 1.00 27.75 O
ATOM 507 CB TYR A 77 21.568 -16.533 74.821 1.00 21.16 C
ATOM 508 CG TYR A 77 20.656 -17.620 75.339 1.00 27.75 C
ATOM 509 CD1 TYR A 77 20.517 -18.832 74.667 1.00 31.21 C
ATOM 510 CD2 TYR A 77 19.969 -17.455 76.536 1.00 32.15 C
ATOM 511 CE1 TYR A 77 19.718 -19.850 75.185 1.00 32.72 C
ATOM 512 CE2 TYR A 77 19.174 -18.458 77.058 1.00 31.26 C
ATOM 513 CZ TYR A 77 19.054 -19.648 76.384 1.00 32.07 C
ATOM 514 OH TYR A 77 18.284 -20.633 76.939 1.00 34.14 O
ATOM 515 N LEU A 78 21.474 -13.264 74.415 1.00 24.66 N
ATOM 516 CA LEU A 78 22.284 -12.055 74.443 1.00 22.27 C
ATOM 517 C LEU A 78 22.580 -11.765 75.898 1.00 20.75 C
ATOM 518 O LEU A 78 21.667 -11.634 76.706 1.00 21.54 O
ATOM 519 CB LEU A 78 21.555 -10.851 73.830 1.00 23.43 C
ATOM 520 CG LEU A 78 20.933 -10.919 72.430 1.00 23.76 C
ATOM 521 CD1 LEU A 78 20.822 -9.510 71.861 1.00 19.52 C
ATOM 522 CD2 LEU A 78 21.781 -11.759 71.524 1.00 25.83 C
ATOM 523 N VAL A 79 23.862 -11.744 76.234 1.00 21.02 N
ATOM 524 CA VAL A 79 24.324 -11.448 77.583 1.00 22.33 C
ATOM 525 C VAL A 79 24.701 -9.964 77.625 1.00 21.59 C
ATOM 526 O VAL A 79 25.692 -9.541 77.020 1.00 21.00 O
ATOM 527 CB VAL A 79 25.560 -12.306 77.956 1.00 23.07 C
ATOM 528 CG1 VAL A 79 26.007 -12.007 79.395 1.00 24.48 C
ATOM 529 CG2 VAL A 79 25.238 -13.781 77.775 1.00 17.41 C
ATOM 530 N PHE A 80 23.891 -9.190 78.337 1.00 20.93 N
ATOM 531 CA PHE A 80 24.069 -7.753 78.462 1.00 17.17 C
ATOM 532 C PHE A 80 24.598 -7.295 79.789 1.00 21.96 C
ATOM 533 O PHE A 80 24.481 -7.984 80.794 1.00 24.78 O
ATOM 534 CB PHE A 80 22.726 -7.053 78.280 1.00 11.09 C
ATOM 535 CG PHE A 80 22.372 -6.788 76.864 1.00 14.38 C
ATOM 536 CD1 PHE A 80 23.049 -5.810 76.143 1.00 12.70 C
ATOM 537 CD2 PHE A 80 21.352 -7.502 76.248 1.00 18.08 C
ATOM 538 CE1 PHE A 80 22.719 -5.545 74.834 1.00 12.92 C
ATOM 539 CE2 PHE A 80 21.007 -7.245 74.925 1.00 17.72 C
ATOM 540 CZ PHE A 80 21.694 -6.262 74.216 1.00 17.80 C
ATOM 541 N GLU A 81 25.134 -6.084 79.785 1.00 22.05 N
ATOM 542 CA GLU A 81 25.611 -5.434 80.987 1.00 19.60 C
ATOM 543 C GLU A 81 24.305 -5.074 81.714 1.00 23.19 C
ATOM 544 O GLU A 81 23.349 -4.600 81.078 1.00 22.67 O
ATOM 545 CB GLU A 81 26.340 -4.153 80.596 1.00 16.06 C
ATOM 546 CG GLU A 81 26.665 -3.241 81.746 1.00 15.58 C
ATOM 547 CD GLU A 81 27.068 -1.849 81.302 1.00 21.57 C
ATOM 548 OE1 GLU A 81 26.920 -1.515 80.102 1.00 19.53 O
ATOM 549 OE2 GLU A 81 27.529 -1.080 82.173 1.00 24.94 O
ATOM 550 N PHE A 82 24.227 -5.322 83.018 1.00 23.33 N
ATOM 551 CA PHE A 82 23.005 -4.993 83.727 1.00 21.87 C
ATOM 552 C PHE A 82 22.989 -3.610 84.368 1.00 18.48 C
ATOM 553 O PHE A 82 23.953 -3.200 85.006 1.00 14.67 O
ATOM 554 CB PHE A 82 22.659 -6.049 84.778 1.00 26.67 C
ATOM 555 CG PHE A 82 21.477 -5.674 85.628 1.00 30.18 C
ATOM 556 CD1 PHE A 82 20.183 -5.940 85.193 1.00 30.74 C
ATOM 557 CD2 PHE A 82 21.655 -4.966 86.824 1.00 30.09 C
ATOM 558 CE1 PHE A 82 19.078 -5.494 85.934 1.00 32.72 C