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1fmk_cleaned.pdb
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3968 lines (3968 loc) · 314 KB
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HEADER PHOSPHOTRANSFERASE 24-JAN-97 1FMK
TITLE CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE SRC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 86-836, CONTAINING SH2, SH3, KINASE 2
COMPND 5 DOMAINS AND C-TERMINAL TAIL;
COMPND 6 SYNONYM: C-SRC, P60-SRC;
COMPND 7 EC: 2.7.1.112;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS SRC, TYROSINE KINASE, PHOSPHORYLATION, SH2, SH3,
KEYWDS 2 PHOSPHOTYROSINE, PROTO-ONCOGENE, PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XU,S.C.HARRISON,M.J.ECK
REVDAT 2 24-FEB-09 1FMK 1 VERSN
REVDAT 1 20-AUG-97 1FMK 0
JRNL AUTH W.XU,S.C.HARRISON,M.J.ECK
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE TYROSINE KINASE
JRNL TITL 2 C-SRC.
JRNL REF NATURE V. 385 595 1997
JRNL REFN ISSN 0028-0836
JRNL PMID 9024657
JRNL DOI 10.1038/385595A0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 165384
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FMK 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 : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48728
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 66.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
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: MULTIPLE ISOMORPHOUS
REMARK 200 HEAVY-ATOM REPLACEMENT (MIR) METHOD. THREE DERIVATIVES USED
REMARK 200 FOR PHASING.
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
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 25.87950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.64750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.69000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.64750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.87950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.69000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A 410
REMARK 465 ILE A 411
REMARK 465 GLU A 412
REMARK 465 ASP A 413
REMARK 465 ASN A 414
REMARK 465 GLU A 415
REMARK 465 TYR A 416
REMARK 465 THR A 417
REMARK 465 ALA A 418
REMARK 465 ARG A 419
REMARK 465 GLN A 420
REMARK 465 GLY A 421
REMARK 465 ALA A 422
REMARK 465 LYS A 423
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 424 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N MET A 82 O HOH A 1256 3545 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 205 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH1 ANGL. DEV. = -3.3 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 THR A 96 -169.62 -121.89
REMARK 500 ASN A 113 40.44 -99.49
REMARK 500 ASP A 141 10.26 84.34
REMARK 500 TRP A 260 -74.11 -140.33
REMARK 500 PHE A 278 -36.23 -135.22
REMARK 500 ARG A 385 -11.38 83.91
REMARK 500 ASP A 386 50.29 -149.15
REMARK 500 ASP A 404 53.60 39.96
REMARK 500 GLU A 486 3.53 91.32
REMARK 500 THR A 521 97.10 73.76
REMARK 500 SER A 522 116.21 -176.94
REMARK 500 GLU A 524 62.56 76.33
REMARK 500 GLU A 531 32.19 -164.38
REMARK 500 ASN A 532 -158.99 -115.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 332 PRO A 333 61.14
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 A 156 0.24 SIDE_CHAIN
REMARK 500 ARG A 169 0.10 SIDE_CHAIN
REMARK 500 ARG A 205 0.13 SIDE_CHAIN
REMARK 500 ARG A 268 0.21 SIDE_CHAIN
REMARK 500 ARG A 291 0.18 SIDE_CHAIN
REMARK 500 ARG A 359 0.14 SIDE_CHAIN
REMARK 500 ARG A 409 0.08 SIDE_CHAIN
REMARK 500 ARG A 506 0.11 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FMK A 83 533 UNP P12931 SRC_HUMAN 85 535
SEQADV 1FMK PTR A 527 UNP P12931 TYR 529 MODIFIED RESIDUE
SEQRES 1 A 452 MET VAL THR THR PHE VAL ALA LEU TYR ASP TYR GLU SER
SEQRES 2 A 452 ARG THR GLU THR ASP LEU SER PHE LYS LYS GLY GLU ARG
SEQRES 3 A 452 LEU GLN ILE VAL ASN ASN THR GLU GLY ASP TRP TRP LEU
SEQRES 4 A 452 ALA HIS SER LEU SER THR GLY GLN THR GLY TYR ILE PRO
SEQRES 5 A 452 SER ASN TYR VAL ALA PRO SER ASP SER ILE GLN ALA GLU
SEQRES 6 A 452 GLU TRP TYR PHE GLY LYS ILE THR ARG ARG GLU SER GLU
SEQRES 7 A 452 ARG LEU LEU LEU ASN ALA GLU ASN PRO ARG GLY THR PHE
SEQRES 8 A 452 LEU VAL ARG GLU SER GLU THR THR LYS GLY ALA TYR CYS
SEQRES 9 A 452 LEU SER VAL SER ASP PHE ASP ASN ALA LYS GLY LEU ASN
SEQRES 10 A 452 VAL LYS HIS TYR LYS ILE ARG LYS LEU ASP SER GLY GLY
SEQRES 11 A 452 PHE TYR ILE THR SER ARG THR GLN PHE ASN SER LEU GLN
SEQRES 12 A 452 GLN LEU VAL ALA TYR TYR SER LYS HIS ALA ASP GLY LEU
SEQRES 13 A 452 CYS HIS ARG LEU THR THR VAL CYS PRO THR SER LYS PRO
SEQRES 14 A 452 GLN THR GLN GLY LEU ALA LYS ASP ALA TRP GLU ILE PRO
SEQRES 15 A 452 ARG GLU SER LEU ARG LEU GLU VAL LYS LEU GLY GLN GLY
SEQRES 16 A 452 CYS PHE GLY GLU VAL TRP MET GLY THR TRP ASN GLY THR
SEQRES 17 A 452 THR ARG VAL ALA ILE LYS THR LEU LYS PRO GLY THR MET
SEQRES 18 A 452 SER PRO GLU ALA PHE LEU GLN GLU ALA GLN VAL MET LYS
SEQRES 19 A 452 LYS LEU ARG HIS GLU LYS LEU VAL GLN LEU TYR ALA VAL
SEQRES 20 A 452 VAL SER GLU GLU PRO ILE TYR ILE VAL THR GLU TYR MET
SEQRES 21 A 452 SER LYS GLY SER LEU LEU ASP PHE LEU LYS GLY GLU THR
SEQRES 22 A 452 GLY LYS TYR LEU ARG LEU PRO GLN LEU VAL ASP MET ALA
SEQRES 23 A 452 ALA GLN ILE ALA SER GLY MET ALA TYR VAL GLU ARG MET
SEQRES 24 A 452 ASN TYR VAL HIS ARG ASP LEU ARG ALA ALA ASN ILE LEU
SEQRES 25 A 452 VAL GLY GLU ASN LEU VAL CYS LYS VAL ALA ASP PHE GLY
SEQRES 26 A 452 LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR THR ALA ARG
SEQRES 27 A 452 GLN GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU
SEQRES 28 A 452 ALA ALA LEU TYR GLY ARG PHE THR ILE LYS SER ASP VAL
SEQRES 29 A 452 TRP SER PHE GLY ILE LEU LEU THR GLU LEU THR THR LYS
SEQRES 30 A 452 GLY ARG VAL PRO TYR PRO GLY MET VAL ASN ARG GLU VAL
SEQRES 31 A 452 LEU ASP GLN VAL GLU ARG GLY TYR ARG MET PRO CYS PRO
SEQRES 32 A 452 PRO GLU CYS PRO GLU SER LEU HIS ASP LEU MET CYS GLN
SEQRES 33 A 452 CYS TRP ARG LYS GLU PRO GLU GLU ARG PRO THR PHE GLU
SEQRES 34 A 452 TYR LEU GLN ALA PHE LEU GLU ASP TYR PHE THR SER THR
SEQRES 35 A 452 GLU PRO GLN PTR GLN PRO GLY GLU ASN LEU
MODRES 1FMK PTR A 527 TYR O-PHOSPHOTYROSINE
HET PTR A 527 16
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 HOH *490(H2 O)
HELIX 1 1 SER A 134 TYR A 136 5 3
HELIX 2 2 ILE A 143 ALA A 145 5 3
HELIX 3 3 ARG A 155 LEU A 162 1 8
HELIX 4 4 LEU A 223 TYR A 230 1 8
HELIX 5 5 ARG A 264 SER A 266 5 3
HELIX 6 6 PRO A 304 LYS A 316 1 13
HELIX 7 7 LEU A 346 LEU A 350 1 5
HELIX 8 8 GLY A 352 TYR A 357 1 6
HELIX 9 9 LEU A 360 ARG A 379 1 20
HELIX 10 10 ALA A 389 ASN A 391 5 3
HELIX 11 11 GLU A 396 LEU A 398 5 3
HELIX 12 12 ILE A 426 TRP A 428 5 3
HELIX 13 13 PRO A 431 TYR A 436 1 6
HELIX 14 14 ILE A 441 THR A 456 1 16
HELIX 15 15 ASN A 468 GLU A 476 1 9
HELIX 16 16 GLU A 489 CYS A 498 1 10
HELIX 17 17 PRO A 503 GLU A 505 5 3
HELIX 18 18 PHE A 509 GLU A 517 1 9
SHEET 1 A 3 ARG A 107 ILE A 110 0
SHEET 2 A 3 THR A 84 ALA A 88 -1 N PHE A 86 O LEU A 108
SHEET 3 A 3 VAL A 137 PRO A 139 -1 N ALA A 138 O VAL A 87
SHEET 1 B 2 TRP A 118 HIS A 122 0
SHEET 2 B 2 THR A 129 PRO A 133 -1 N ILE A 132 O TRP A 119
SHEET 1 C 3 PHE A 172 GLU A 176 0
SHEET 2 C 3 TYR A 184 ASP A 192 -1 N SER A 187 O LEU A 173
SHEET 3 C 3 GLY A 196 ILE A 204 -1 N ILE A 204 O TYR A 184
SHEET 1 D 5 LEU A 325 VAL A 329 0
SHEET 2 D 5 ILE A 334 THR A 338 -1 N VAL A 337 O TYR A 326
SHEET 3 D 5 THR A 290 LEU A 297 -1 N LEU A 297 O ILE A 334
SHEET 4 D 5 VAL A 281 TRP A 286 -1 N TRP A 286 O THR A 290
SHEET 5 D 5 LEU A 267 LYS A 272 -1 N VAL A 271 O MET A 283
SHEET 1 E 2 ILE A 392 VAL A 394 0
SHEET 2 E 2 CYS A 400 VAL A 402 -1 N LYS A 401 O LEU A 393
LINK N PTR A 527 C GLN A 526 1555 1555 1.34
LINK C PTR A 527 N GLN A 528 1555 1555 1.32
CRYST1 51.759 87.380 101.295 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 0.019320 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009872 0.00000
ATOM 1 N MET A 82 -9.402 -13.576 46.488 1.00 43.03 N
ATOM 2 CA MET A 82 -9.988 -14.896 46.009 1.00 44.85 C
ATOM 3 C MET A 82 -9.622 -15.153 44.545 1.00 42.30 C
ATOM 4 O MET A 82 -8.907 -14.300 43.943 1.00 44.13 O
ATOM 5 CB MET A 82 -11.547 -14.902 45.915 1.00 48.19 C
ATOM 6 CG MET A 82 -12.254 -15.475 47.158 1.00 52.71 C
ATOM 7 SD MET A 82 -14.047 -15.703 46.508 1.00 57.50 S
ATOM 8 CE MET A 82 -14.102 -14.213 45.349 1.00 57.22 C
ATOM 9 N VAL A 83 -10.311 -16.104 43.966 1.00 38.49 N
ATOM 10 CA VAL A 83 -10.604 -16.166 42.541 1.00 34.62 C
ATOM 11 C VAL A 83 -11.354 -14.872 42.145 1.00 32.37 C
ATOM 12 O VAL A 83 -12.385 -14.518 42.736 1.00 35.28 O
ATOM 13 CB VAL A 83 -11.525 -17.417 42.258 1.00 33.08 C
ATOM 14 CG1 VAL A 83 -11.659 -17.626 40.802 1.00 33.66 C
ATOM 15 CG2 VAL A 83 -10.878 -18.634 42.903 1.00 34.53 C
ATOM 16 N THR A 84 -10.822 -14.124 41.189 1.00 27.75 N
ATOM 17 CA THR A 84 -11.525 -12.937 40.709 1.00 25.11 C
ATOM 18 C THR A 84 -12.534 -13.327 39.626 1.00 23.33 C
ATOM 19 O THR A 84 -12.256 -14.204 38.806 1.00 22.96 O
ATOM 20 CB THR A 84 -10.523 -11.883 40.161 1.00 26.50 C
ATOM 21 OG1 THR A 84 -9.510 -11.628 41.148 1.00 25.81 O
ATOM 22 CG2 THR A 84 -11.245 -10.576 39.827 1.00 26.20 C
ATOM 23 N THR A 85 -13.765 -12.834 39.752 1.00 22.19 N
ATOM 24 CA THR A 85 -14.777 -13.001 38.700 1.00 21.75 C
ATOM 25 C THR A 85 -14.663 -11.893 37.652 1.00 21.95 C
ATOM 26 O THR A 85 -14.723 -10.712 37.983 1.00 20.40 O
ATOM 27 CB THR A 85 -16.223 -12.966 39.254 1.00 21.21 C
ATOM 28 OG1 THR A 85 -16.333 -13.857 40.366 1.00 23.57 O
ATOM 29 CG2 THR A 85 -17.204 -13.421 38.194 1.00 20.38 C
ATOM 30 N PHE A 86 -14.429 -12.280 36.403 1.00 21.79 N
ATOM 31 CA PHE A 86 -14.312 -11.329 35.296 1.00 18.83 C
ATOM 32 C PHE A 86 -15.545 -11.368 34.403 1.00 16.69 C
ATOM 33 O PHE A 86 -16.279 -12.341 34.415 1.00 18.95 O
ATOM 34 CB PHE A 86 -13.060 -11.648 34.476 1.00 18.30 C
ATOM 35 CG PHE A 86 -11.777 -11.157 35.102 1.00 18.19 C
ATOM 36 CD1 PHE A 86 -11.114 -11.920 36.056 1.00 19.32 C
ATOM 37 CD2 PHE A 86 -11.218 -9.938 34.715 1.00 17.84 C
ATOM 38 CE1 PHE A 86 -9.909 -11.477 36.616 1.00 22.28 C
ATOM 39 CE2 PHE A 86 -10.025 -9.485 35.258 1.00 18.97 C
ATOM 40 CZ PHE A 86 -9.362 -10.253 36.211 1.00 22.40 C
ATOM 41 N VAL A 87 -15.844 -10.253 33.747 1.00 17.55 N
ATOM 42 CA VAL A 87 -16.924 -10.188 32.754 1.00 19.49 C
ATOM 43 C VAL A 87 -16.334 -10.000 31.348 1.00 19.54 C
ATOM 44 O VAL A 87 -15.499 -9.123 31.144 1.00 19.95 O
ATOM 45 CB VAL A 87 -17.884 -8.985 33.020 1.00 21.94 C
ATOM 46 CG1 VAL A 87 -19.049 -9.022 32.051 1.00 25.75 C
ATOM 47 CG2 VAL A 87 -18.409 -9.010 34.440 1.00 24.25 C
ATOM 48 N ALA A 88 -16.752 -10.825 30.391 1.00 21.42 N
ATOM 49 CA ALA A 88 -16.343 -10.663 28.977 1.00 23.13 C
ATOM 50 C ALA A 88 -16.896 -9.377 28.326 1.00 23.10 C
ATOM 51 O ALA A 88 -18.108 -9.153 28.291 1.00 22.83 O
ATOM 52 CB ALA A 88 -16.775 -11.878 28.155 1.00 22.00 C
ATOM 53 N LEU A 89 -16.007 -8.580 27.744 1.00 23.14 N
ATOM 54 CA LEU A 89 -16.397 -7.353 27.075 1.00 22.74 C
ATOM 55 C LEU A 89 -16.751 -7.582 25.599 1.00 24.95 C
ATOM 56 O LEU A 89 -17.473 -6.781 25.000 1.00 28.83 O
ATOM 57 CB LEU A 89 -15.273 -6.330 27.212 1.00 21.42 C
ATOM 58 CG LEU A 89 -14.758 -6.108 28.642 1.00 22.46 C
ATOM 59 CD1 LEU A 89 -13.517 -5.248 28.600 1.00 23.14 C
ATOM 60 CD2 LEU A 89 -15.823 -5.462 29.508 1.00 21.54 C
ATOM 61 N TYR A 90 -16.277 -8.693 25.029 1.00 25.65 N
ATOM 62 CA TYR A 90 -16.610 -9.104 23.654 1.00 24.62 C
ATOM 63 C TYR A 90 -16.825 -10.617 23.532 1.00 25.84 C
ATOM 64 O TYR A 90 -16.472 -11.389 24.424 1.00 24.29 O
ATOM 65 CB TYR A 90 -15.501 -8.707 22.670 1.00 22.49 C
ATOM 66 CG TYR A 90 -14.800 -7.419 23.000 1.00 23.56 C
ATOM 67 CD1 TYR A 90 -15.356 -6.182 22.643 1.00 24.27 C
ATOM 68 CD2 TYR A 90 -13.621 -7.422 23.738 1.00 21.38 C
ATOM 69 CE1 TYR A 90 -14.756 -4.986 23.018 1.00 20.97 C
ATOM 70 CE2 TYR A 90 -13.018 -6.231 24.126 1.00 21.95 C
ATOM 71 CZ TYR A 90 -13.588 -5.022 23.754 1.00 21.78 C
ATOM 72 OH TYR A 90 -12.933 -3.859 24.055 1.00 25.67 O
ATOM 73 N ASP A 91 -17.412 -11.030 22.414 1.00 25.87 N
ATOM 74 CA ASP A 91 -17.411 -12.437 22.021 1.00 26.72 C
ATOM 75 C ASP A 91 -16.009 -12.866 21.659 1.00 27.00 C
ATOM 76 O ASP A 91 -15.254 -12.096 21.075 1.00 28.84 O
ATOM 77 CB ASP A 91 -18.285 -12.661 20.795 1.00 29.20 C
ATOM 78 CG ASP A 91 -19.714 -12.269 21.028 1.00 31.28 C
ATOM 79 OD1 ASP A 91 -20.369 -12.892 21.886 1.00 32.39 O
ATOM 80 OD2 ASP A 91 -20.166 -11.306 20.385 1.00 33.72 O
ATOM 81 N TYR A 92 -15.740 -14.150 21.816 1.00 25.52 N
ATOM 82 CA TYR A 92 -14.449 -14.693 21.434 1.00 24.36 C
ATOM 83 C TYR A 92 -14.653 -16.158 21.061 1.00 27.04 C
ATOM 84 O TYR A 92 -15.291 -16.911 21.798 1.00 26.64 O
ATOM 85 CB TYR A 92 -13.450 -14.549 22.591 1.00 19.85 C
ATOM 86 CG TYR A 92 -12.119 -15.214 22.334 1.00 20.30 C
ATOM 87 CD1 TYR A 92 -11.156 -14.608 21.513 1.00 19.26 C
ATOM 88 CD2 TYR A 92 -11.878 -16.514 22.778 1.00 19.04 C
ATOM 89 CE1 TYR A 92 -9.997 -15.292 21.126 1.00 18.76 C
ATOM 90 CE2 TYR A 92 -10.723 -17.208 22.398 1.00 19.92 C
ATOM 91 CZ TYR A 92 -9.793 -16.593 21.571 1.00 20.72 C
ATOM 92 OH TYR A 92 -8.678 -17.288 21.171 1.00 22.06 O
ATOM 93 N GLU A 93 -14.278 -16.505 19.831 1.00 28.46 N
ATOM 94 CA GLU A 93 -14.359 -17.886 19.352 1.00 29.19 C
ATOM 95 C GLU A 93 -13.035 -18.627 19.551 1.00 27.58 C
ATOM 96 O GLU A 93 -11.957 -18.055 19.363 1.00 24.95 O
ATOM 97 CB GLU A 93 -14.751 -17.928 17.866 1.00 33.89 C
ATOM 98 CG GLU A 93 -15.256 -16.594 17.299 1.00 44.88 C
ATOM 99 CD GLU A 93 -15.838 -16.696 15.891 1.00 50.33 C
ATOM 100 OE1 GLU A 93 -15.859 -17.801 15.309 1.00 53.26 O
ATOM 101 OE2 GLU A 93 -16.261 -15.650 15.351 1.00 53.61 O
ATOM 102 N SER A 94 -13.145 -19.865 20.049 1.00 26.06 N
ATOM 103 CA SER A 94 -12.033 -20.808 20.199 1.00 24.59 C
ATOM 104 C SER A 94 -11.211 -20.999 18.916 1.00 24.24 C
ATOM 105 O SER A 94 -11.773 -21.164 17.832 1.00 24.13 O
ATOM 106 CB SER A 94 -12.579 -22.169 20.644 1.00 24.30 C
ATOM 107 OG SER A 94 -11.534 -23.084 20.904 1.00 24.88 O
ATOM 108 N ARG A 95 -9.889 -21.084 19.080 1.00 23.48 N
ATOM 109 CA ARG A 95 -8.933 -21.152 17.956 1.00 23.18 C
ATOM 110 C ARG A 95 -8.072 -22.411 18.019 1.00 23.58 C
ATOM 111 O ARG A 95 -7.543 -22.866 17.005 1.00 23.81 O
ATOM 112 CB ARG A 95 -7.980 -19.954 17.969 1.00 23.51 C
ATOM 113 CG ARG A 95 -8.551 -18.640 17.470 1.00 20.29 C
ATOM 114 CD ARG A 95 -7.546 -17.519 17.668 1.00 18.02 C
ATOM 115 NE ARG A 95 -8.184 -16.213 17.598 1.00 16.20 N
ATOM 116 CZ ARG A 95 -7.591 -15.067 17.918 1.00 13.70 C
ATOM 117 NH1 ARG A 95 -6.311 -15.037 18.265 1.00 15.81 N
ATOM 118 NH2 ARG A 95 -8.276 -13.943 17.926 1.00 15.31 N
ATOM 119 N THR A 96 -7.770 -22.834 19.240 1.00 23.37 N
ATOM 120 CA THR A 96 -6.933 -24.006 19.467 1.00 23.68 C
ATOM 121 C THR A 96 -7.719 -25.016 20.297 1.00 25.26 C
ATOM 122 O THR A 96 -8.902 -24.803 20.580 1.00 25.37 O
ATOM 123 CB THR A 96 -5.631 -23.649 20.239 1.00 23.84 C
ATOM 124 OG1 THR A 96 -5.958 -23.285 21.584 1.00 22.91 O
ATOM 125 CG2 THR A 96 -4.882 -22.501 19.587 1.00 22.58 C
ATOM 126 N GLU A 97 -7.038 -26.054 20.779 1.00 26.48 N
ATOM 127 CA GLU A 97 -7.660 -27.063 21.636 1.00 29.59 C
ATOM 128 C GLU A 97 -7.728 -26.637 23.120 1.00 27.28 C
ATOM 129 O GLU A 97 -8.494 -27.210 23.888 1.00 26.83 O
ATOM 130 CB GLU A 97 -6.897 -28.394 21.528 1.00 34.19 C
ATOM 131 CG GLU A 97 -6.868 -29.040 20.130 1.00 43.85 C
ATOM 132 CD GLU A 97 -5.991 -30.312 20.050 1.00 51.15 C
ATOM 133 OE1 GLU A 97 -5.474 -30.778 21.092 1.00 57.26 O
ATOM 134 OE2 GLU A 97 -5.818 -30.859 18.937 1.00 55.81 O
ATOM 135 N THR A 98 -6.945 -25.629 23.514 1.00 25.62 N
ATOM 136 CA THR A 98 -6.774 -25.285 24.941 1.00 23.22 C
ATOM 137 C THR A 98 -7.157 -23.848 25.342 1.00 21.22 C
ATOM 138 O THR A 98 -6.907 -23.418 26.469 1.00 21.19 O
ATOM 139 CB THR A 98 -5.325 -25.536 25.401 1.00 24.23 C
ATOM 140 OG1 THR A 98 -4.434 -24.751 24.605 1.00 25.97 O
ATOM 141 CG2 THR A 98 -4.953 -27.014 25.252 1.00 24.37 C
ATOM 142 N ASP A 99 -7.776 -23.114 24.425 1.00 19.33 N
ATOM 143 CA ASP A 99 -8.387 -21.836 24.766 1.00 18.65 C
ATOM 144 C ASP A 99 -9.897 -21.975 24.979 1.00 18.89 C
ATOM 145 O ASP A 99 -10.461 -23.035 24.752 1.00 20.62 O
ATOM 146 CB ASP A 99 -8.071 -20.775 23.696 1.00 18.91 C
ATOM 147 CG ASP A 99 -8.591 -21.138 22.299 1.00 22.09 C
ATOM 148 OD1 ASP A 99 -9.133 -22.249 22.094 1.00 23.10 O
ATOM 149 OD2 ASP A 99 -8.453 -20.286 21.393 1.00 23.78 O
ATOM 150 N LEU A 100 -10.551 -20.906 25.415 1.00 19.87 N
ATOM 151 CA LEU A 100 -11.951 -20.978 25.847 1.00 20.21 C
ATOM 152 C LEU A 100 -12.836 -19.946 25.145 1.00 19.81 C
ATOM 153 O LEU A 100 -12.542 -18.744 25.166 1.00 19.20 O
ATOM 154 CB LEU A 100 -12.045 -20.790 27.372 1.00 19.20 C
ATOM 155 CG LEU A 100 -13.426 -20.558 28.005 1.00 19.62 C
ATOM 156 CD1 LEU A 100 -14.242 -21.833 27.899 1.00 19.66 C
ATOM 157 CD2 LEU A 100 -13.285 -20.139 29.464 1.00 18.79 C
ATOM 158 N SER A 101 -13.832 -20.458 24.414 1.00 21.61 N
ATOM 159 CA SER A 101 -14.955 -19.681 23.866 1.00 23.54 C
ATOM 160 C SER A 101 -15.789 -18.971 24.943 1.00 24.41 C
ATOM 161 O SER A 101 -16.150 -19.572 25.965 1.00 25.74 O
ATOM 162 CB SER A 101 -15.909 -20.596 23.073 1.00 24.65 C
ATOM 163 OG SER A 101 -15.267 -21.270 22.002 1.00 28.99 O
ATOM 164 N PHE A 102 -16.210 -17.747 24.636 1.00 21.99 N
ATOM 165 CA PHE A 102 -17.161 -17.034 25.470 1.00 21.58 C
ATOM 166 C PHE A 102 -17.931 -15.963 24.704 1.00 23.51 C
ATOM 167 O PHE A 102 -17.520 -15.519 23.621 1.00 23.13 O
ATOM 168 CB PHE A 102 -16.464 -16.414 26.699 1.00 21.76 C
ATOM 169 CG PHE A 102 -15.268 -15.551 26.375 1.00 19.96 C
ATOM 170 CD1 PHE A 102 -15.419 -14.198 26.121 1.00 20.39 C
ATOM 171 CD2 PHE A 102 -13.982 -16.083 26.389 1.00 21.06 C
ATOM 172 CE1 PHE A 102 -14.307 -13.391 25.885 1.00 19.33 C
ATOM 173 CE2 PHE A 102 -12.873 -15.280 26.154 1.00 19.14 C
ATOM 174 CZ PHE A 102 -13.034 -13.937 25.903 1.00 18.88 C
ATOM 175 N LYS A 103 -19.071 -15.579 25.264 1.00 24.37 N
ATOM 176 CA LYS A 103 -19.873 -14.512 24.696 1.00 28.18 C
ATOM 177 C LYS A 103 -19.872 -13.264 25.591 1.00 28.40 C
ATOM 178 O LYS A 103 -19.567 -13.350 26.778 1.00 30.02 O
ATOM 179 CB LYS A 103 -21.293 -15.014 24.438 1.00 31.30 C
ATOM 180 CG LYS A 103 -21.737 -16.137 25.347 1.00 38.49 C
ATOM 181 CD LYS A 103 -22.803 -15.648 26.318 1.00 43.78 C
ATOM 182 CE LYS A 103 -23.101 -16.673 27.397 1.00 45.16 C
ATOM 183 NZ LYS A 103 -24.566 -16.822 27.551 1.00 48.28 N
ATOM 184 N LYS A 104 -20.022 -12.090 24.984 1.00 28.84 N
ATOM 185 CA LYS A 104 -20.071 -10.826 25.728 1.00 31.04 C
ATOM 186 C LYS A 104 -20.957 -10.956 26.981 1.00 30.98 C
ATOM 187 O LYS A 104 -22.002 -11.609 26.943 1.00 32.05 O
ATOM 188 CB LYS A 104 -20.596 -9.697 24.813 1.00 32.58 C
ATOM 189 CG LYS A 104 -20.448 -8.258 25.369 1.00 35.41 C
ATOM 190 CD LYS A 104 -21.298 -7.228 24.602 1.00 37.97 C
ATOM 191 CE LYS A 104 -20.581 -5.882 24.445 1.00 41.26 C
ATOM 192 NZ LYS A 104 -21.359 -4.920 23.601 1.00 43.16 N
ATOM 193 N GLY A 105 -20.435 -10.523 28.123 1.00 31.46 N
ATOM 194 CA GLY A 105 -21.213 -10.553 29.358 1.00 31.82 C
ATOM 195 C GLY A 105 -21.086 -11.829 30.182 1.00 31.23 C
ATOM 196 O GLY A 105 -21.516 -11.884 31.342 1.00 31.00 O
ATOM 197 N GLU A 106 -20.474 -12.853 29.597 1.00 29.06 N
ATOM 198 CA GLU A 106 -20.188 -14.082 30.330 1.00 28.88 C
ATOM 199 C GLU A 106 -19.184 -13.843 31.457 1.00 28.08 C
ATOM 200 O GLU A 106 -18.240 -13.063 31.309 1.00 27.88 O
ATOM 201 CB GLU A 106 -19.651 -15.146 29.381 1.00 28.55 C
ATOM 202 CG GLU A 106 -19.628 -16.541 29.967 1.00 28.76 C
ATOM 203 CD GLU A 106 -19.434 -17.617 28.908 1.00 33.64 C
ATOM 204 OE1 GLU A 106 -19.829 -17.390 27.742 1.00 33.47 O
ATOM 205 OE2 GLU A 106 -18.906 -18.703 29.236 1.00 33.53 O
ATOM 206 N ARG A 107 -19.469 -14.410 32.621 1.00 27.84 N
ATOM 207 CA ARG A 107 -18.605 -14.231 33.784 1.00 27.27 C
ATOM 208 C ARG A 107 -17.641 -15.412 33.882 1.00 26.00 C
ATOM 209 O ARG A 107 -18.045 -16.572 33.726 1.00 26.61 O
ATOM 210 CB ARG A 107 -19.445 -14.109 35.068 1.00 28.72 C
ATOM 211 CG ARG A 107 -20.319 -12.846 35.157 1.00 30.72 C
ATOM 212 CD ARG A 107 -20.808 -12.576 36.588 1.00 37.89 C
ATOM 213 NE ARG A 107 -22.168 -13.070 36.833 1.00 44.89 N
ATOM 214 CZ ARG A 107 -23.165 -12.315 37.289 1.00 50.38 C
ATOM 215 NH1 ARG A 107 -22.950 -11.012 37.502 1.00 50.55 N
ATOM 216 NH2 ARG A 107 -24.395 -12.826 37.417 1.00 52.51 N
ATOM 217 N LEU A 108 -16.367 -15.114 34.124 1.00 22.90 N
ATOM 218 CA LEU A 108 -15.322 -16.129 34.138 1.00 19.54 C
ATOM 219 C LEU A 108 -14.478 -15.987 35.392 1.00 20.11 C
ATOM 220 O LEU A 108 -14.206 -14.878 35.841 1.00 19.49 O
ATOM 221 CB LEU A 108 -14.430 -15.978 32.906 1.00 19.92 C
ATOM 222 CG LEU A 108 -15.126 -15.906 31.548 1.00 17.00 C
ATOM 223 CD1 LEU A 108 -14.167 -15.343 30.535 1.00 19.95 C
ATOM 224 CD2 LEU A 108 -15.619 -17.264 31.140 1.00 16.34 C
ATOM 225 N GLN A 109 -14.193 -17.116 36.029 1.00 20.46 N
ATOM 226 CA GLN A 109 -13.335 -17.161 37.218 1.00 19.10 C
ATOM 227 C GLN A 109 -11.901 -17.262 36.774 1.00 18.56 C
ATOM 228 O GLN A 109 -11.587 -18.053 35.892 1.00 17.42 O
ATOM 229 CB GLN A 109 -13.639 -18.395 38.055 1.00 19.19 C
ATOM 230 CG GLN A 109 -15.014 -18.458 38.602 1.00 26.87 C
ATOM 231 CD GLN A 109 -15.188 -17.523 39.754 1.00 33.24 C
ATOM 232 OE1 GLN A 109 -15.114 -17.925 40.915 1.00 36.45 O
ATOM 233 NE2 GLN A 109 -15.307 -16.239 39.449 1.00 37.16 N
ATOM 234 N ILE A 110 -11.039 -16.442 37.359 1.00 20.08 N
ATOM 235 CA ILE A 110 -9.622 -16.442 37.020 1.00 20.09 C
ATOM 236 C ILE A 110 -8.829 -16.288 38.305 1.00 22.43 C
ATOM 237 O ILE A 110 -9.091 -15.367 39.090 1.00 23.48 O
ATOM 238 CB ILE A 110 -9.260 -15.276 36.063 1.00 19.23 C
ATOM 239 CG1 ILE A 110 -10.170 -15.307 34.831 1.00 18.08 C
ATOM 240 CG2 ILE A 110 -7.771 -15.360 35.681 1.00 20.33 C
ATOM 241 CD1 ILE A 110 -9.773 -14.399 33.726 1.00 18.65 C
ATOM 242 N VAL A 111 -7.979 -17.275 38.590 1.00 26.02 N
ATOM 243 CA VAL A 111 -7.197 -17.309 39.837 1.00 30.32 C
ATOM 244 C VAL A 111 -5.956 -16.396 39.790 1.00 34.43 C
ATOM 245 O VAL A 111 -5.804 -15.496 40.618 1.00 35.02 O
ATOM 246 CB VAL A 111 -6.762 -18.766 40.212 1.00 27.66 C
ATOM 247 CG1 VAL A 111 -5.753 -18.744 41.376 1.00 25.75 C
ATOM 248 CG2 VAL A 111 -7.987 -19.600 40.592 1.00 26.13 C
ATOM 249 N ASN A 112 -5.130 -16.534 38.760 1.00 39.18 N
ATOM 250 CA ASN A 112 -3.990 -15.636 38.657 1.00 44.16 C
ATOM 251 C ASN A 112 -4.083 -14.631 37.497 1.00 45.25 C
ATOM 252 O ASN A 112 -3.988 -14.986 36.318 1.00 44.87 O
ATOM 253 CB ASN A 112 -2.680 -16.437 38.672 1.00 48.76 C
ATOM 254 CG ASN A 112 -2.216 -16.771 40.107 1.00 54.12 C
ATOM 255 OD1 ASN A 112 -2.339 -15.938 41.018 1.00 53.84 O
ATOM 256 ND2 ASN A 112 -1.655 -17.961 40.311 1.00 54.91 N
ATOM 257 N ASN A 113 -4.468 -13.411 37.866 1.00 46.29 N
ATOM 258 CA ASN A 113 -4.658 -12.316 36.923 1.00 48.54 C
ATOM 259 C ASN A 113 -3.448 -11.378 36.901 1.00 49.94 C
ATOM 260 O ASN A 113 -3.577 -10.163 36.733 1.00 50.47 O
ATOM 261 CB ASN A 113 -5.959 -11.555 37.239 1.00 48.14 C
ATOM 262 CG ASN A 113 -5.894 -10.756 38.533 1.00 49.10 C
ATOM 263 OD1 ASN A 113 -6.440 -9.653 38.609 1.00 50.69 O
ATOM 264 ND2 ASN A 113 -5.356 -11.349 39.592 1.00 48.95 N
ATOM 265 N THR A 114 -2.267 -11.990 36.960 1.00 50.80 N
ATOM 266 CA THR A 114 -0.981 -11.293 36.808 1.00 51.95 C
ATOM 267 C THR A 114 -0.792 -10.743 35.378 1.00 51.12 C
ATOM 268 O THR A 114 -1.271 -11.360 34.421 1.00 51.83 O
ATOM 269 CB THR A 114 0.203 -12.257 37.194 1.00 51.75 C
ATOM 270 OG1 THR A 114 1.191 -11.518 37.912 1.00 55.19 O
ATOM 271 CG2 THR A 114 0.870 -12.896 35.976 1.00 50.87 C
ATOM 272 N GLU A 115 -0.139 -9.582 35.236 1.00 50.25 N
ATOM 273 CA GLU A 115 0.103 -8.986 33.903 1.00 48.51 C
ATOM 274 C GLU A 115 0.588 -10.029 32.881 1.00 44.28 C
ATOM 275 O GLU A 115 1.587 -10.717 33.110 1.00 44.77 O
ATOM 276 CB GLU A 115 1.129 -7.830 33.971 1.00 52.59 C
ATOM 277 CG GLU A 115 0.760 -6.640 34.890 1.00 60.31 C
ATOM 278 CD GLU A 115 -0.587 -5.943 34.578 1.00 65.33 C
ATOM 279 OE1 GLU A 115 -1.238 -6.253 33.549 1.00 67.94 O
ATOM 280 OE2 GLU A 115 -0.997 -5.070 35.387 1.00 66.39 O
ATOM 281 N GLY A 116 -0.169 -10.175 31.797 1.00 38.94 N
ATOM 282 CA GLY A 116 0.124 -11.176 30.776 1.00 33.43 C
ATOM 283 C GLY A 116 -0.945 -11.145 29.692 1.00 29.79 C
ATOM 284 O GLY A 116 -1.924 -10.415 29.839 1.00 29.15 O
ATOM 285 N ASP A 117 -0.751 -11.865 28.588 1.00 25.80 N
ATOM 286 CA ASP A 117 -1.663 -11.737 27.451 1.00 22.11 C
ATOM 287 C ASP A 117 -2.770 -12.781 27.358 1.00 21.05 C
ATOM 288 O ASP A 117 -3.814 -12.547 26.740 1.00 20.94 O
ATOM 289 CB ASP A 117 -0.876 -11.691 26.148 1.00 24.80 C
ATOM 290 CG ASP A 117 -0.104 -10.403 25.996 1.00 25.41 C
ATOM 291 OD1 ASP A 117 -0.662 -9.333 26.313 1.00 25.64 O
ATOM 292 OD2 ASP A 117 1.083 -10.470 25.631 1.00 31.00 O
ATOM 293 N TRP A 118 -2.533 -13.931 27.976 1.00 19.03 N
ATOM 294 CA TRP A 118 -3.495 -15.028 28.006 1.00 18.31 C
ATOM 295 C TRP A 118 -3.599 -15.552 29.439 1.00 18.11 C
ATOM 296 O TRP A 118 -2.586 -15.748 30.119 1.00 17.73 O
ATOM 297 CB TRP A 118 -3.061 -16.168 27.053 1.00 16.73 C
ATOM 298 CG TRP A 118 -3.107 -15.796 25.573 1.00 15.86 C
ATOM 299 CD1 TRP A 118 -2.144 -15.128 24.867 1.00 17.09 C
ATOM 300 CD2 TRP A 118 -4.214 -15.959 24.680 1.00 16.27 C
ATOM 301 NE1 TRP A 118 -2.598 -14.841 23.599 1.00 16.19 N
ATOM 302 CE2 TRP A 118 -3.864 -15.337 23.452 1.00 14.91 C
ATOM 303 CE3 TRP A 118 -5.472 -16.562 24.789 1.00 15.25 C
ATOM 304 CZ2 TRP A 118 -4.726 -15.293 22.356 1.00 14.61 C
ATOM 305 CZ3 TRP A 118 -6.333 -16.517 23.693 1.00 18.53 C
ATOM 306 CH2 TRP A 118 -5.953 -15.881 22.491 1.00 15.21 C
ATOM 307 N TRP A 119 -4.831 -15.692 29.916 1.00 17.99 N
ATOM 308 CA TRP A 119 -5.093 -16.104 31.295 1.00 16.17 C
ATOM 309 C TRP A 119 -5.887 -17.411 31.257 1.00 16.87 C
ATOM 310 O TRP A 119 -6.667 -17.638 30.337 1.00 17.74 O
ATOM 311 CB TRP A 119 -5.920 -15.033 32.026 1.00 16.21 C
ATOM 312 CG TRP A 119 -5.180 -13.750 32.384 1.00 17.35 C
ATOM 313 CD1 TRP A 119 -3.832 -13.600 32.562 1.00 17.30 C
ATOM 314 CD2 TRP A 119 -5.769 -12.480 32.718 1.00 18.29 C
ATOM 315 NE1 TRP A 119 -3.550 -12.328 33.001 1.00 18.84 N
ATOM 316 CE2 TRP A 119 -4.717 -11.620 33.116 1.00 19.03 C
ATOM 317 CE3 TRP A 119 -7.084 -11.985 32.725 1.00 18.97 C
ATOM 318 CZ2 TRP A 119 -4.938 -10.304 33.525 1.00 19.42 C
ATOM 319 CZ3 TRP A 119 -7.303 -10.670 33.125 1.00 17.94 C
ATOM 320 CH2 TRP A 119 -6.236 -9.848 33.523 1.00 19.33 C
ATOM 321 N LEU A 120 -5.720 -18.245 32.272 1.00 13.85 N
ATOM 322 CA LEU A 120 -6.499 -19.460 32.391 1.00 13.82 C
ATOM 323 C LEU A 120 -7.827 -19.170 33.091 1.00 12.06 C
ATOM 324 O LEU A 120 -7.849 -18.639 34.197 1.00 14.66 O
ATOM 325 CB LEU A 120 -5.682 -20.496 33.160 1.00 12.32 C
ATOM 326 CG LEU A 120 -6.301 -21.870 33.358 1.00 14.61 C
ATOM 327 CD1 LEU A 120 -6.432 -22.576 32.026 1.00 16.41 C
ATOM 328 CD2 LEU A 120 -5.422 -22.665 34.306 1.00 15.14 C
ATOM 329 N ALA A 121 -8.933 -19.467 32.422 1.00 12.54 N
ATOM 330 CA ALA A 121 -10.257 -19.141 32.941 1.00 14.26 C
ATOM 331 C ALA A 121 -11.183 -20.362 33.111 1.00 16.34 C
ATOM 332 O ALA A 121 -11.013 -21.402 32.451 1.00 15.85 O
ATOM 333 CB ALA A 121 -10.930 -18.108 32.044 1.00 14.68 C
ATOM 334 N HIS A 122 -12.193 -20.194 33.962 1.00 16.16 N
ATOM 335 CA HIS A 122 -13.257 -21.175 34.143 1.00 14.51 C
ATOM 336 C HIS A 122 -14.601 -20.462 34.039 1.00 16.09 C
ATOM 337 O HIS A 122 -14.889 -19.572 34.832 1.00 17.37 O
ATOM 338 CB HIS A 122 -13.127 -21.839 35.519 1.00 13.66 C
ATOM 339 CG HIS A 122 -14.240 -22.784 35.853 1.00 14.38 C
ATOM 340 ND1 HIS A 122 -14.818 -22.829 37.102 1.00 18.69 N
ATOM 341 CD2 HIS A 122 -14.830 -23.763 35.121 1.00 16.54 C
ATOM 342 CE1 HIS A 122 -15.719 -23.800 37.123 1.00 18.50 C
ATOM 343 NE2 HIS A 122 -15.751 -24.373 35.960 1.00 17.97 N
ATOM 344 N SER A 123 -15.444 -20.871 33.093 1.00 17.21 N
ATOM 345 CA SER A 123 -16.784 -20.295 32.991 1.00 19.50 C
ATOM 346 C SER A 123 -17.774 -20.957 33.948 1.00 21.98 C
ATOM 347 O SER A 123 -18.022 -22.145 33.860 1.00 20.46 O
ATOM 348 CB SER A 123 -17.321 -20.422 31.572 1.00 20.08 C
ATOM 349 OG SER A 123 -18.704 -20.108 31.541 1.00 21.94 O
ATOM 350 N LEU A 124 -18.451 -20.153 34.751 1.00 26.22 N
ATOM 351 CA LEU A 124 -19.513 -20.665 35.613 1.00 30.90 C
ATOM 352 C LEU A 124 -20.869 -20.809 34.880 1.00 32.45 C
ATOM 353 O LEU A 124 -21.865 -21.223 35.467 1.00 34.11 O
ATOM 354 CB LEU A 124 -19.666 -19.752 36.847 1.00 33.83 C
ATOM 355 CG LEU A 124 -18.483 -19.596 37.819 1.00 33.75 C
ATOM 356 CD1 LEU A 124 -18.776 -18.486 38.832 1.00 35.04 C
ATOM 357 CD2 LEU A 124 -18.201 -20.918 38.524 1.00 33.11 C
ATOM 358 N SER A 125 -20.905 -20.458 33.598 1.00 32.87 N
ATOM 359 CA SER A 125 -22.127 -20.623 32.796 1.00 31.82 C
ATOM 360 C SER A 125 -22.098 -21.969 32.075 1.00 30.00 C
ATOM 361 O SER A 125 -23.101 -22.673 31.988 1.00 30.11 O
ATOM 362 CB SER A 125 -22.261 -19.516 31.738 1.00 32.78 C
ATOM 363 OG SER A 125 -21.539 -18.348 32.082 1.00 39.72 O
ATOM 364 N THR A 126 -20.950 -22.275 31.474 1.00 26.42 N
ATOM 365 CA THR A 126 -20.821 -23.444 30.613 1.00 22.02 C
ATOM 366 C THR A 126 -20.019 -24.543 31.293 1.00 20.77 C
ATOM 367 O THR A 126 -19.957 -25.669 30.804 1.00 21.11 O
ATOM 368 CB THR A 126 -20.101 -23.083 29.324 1.00 21.64 C
ATOM 369 OG1 THR A 126 -18.743 -22.742 29.638 1.00 21.43 O
ATOM 370 CG2 THR A 126 -20.783 -21.888 28.648 1.00 20.37 C
ATOM 371 N GLY A 127 -19.274 -24.166 32.326 1.00 17.91 N
ATOM 372 CA GLY A 127 -18.447 -25.122 33.030 1.00 19.01 C
ATOM 373 C GLY A 127 -17.140 -25.386 32.307 1.00 19.94 C
ATOM 374 O GLY A 127 -16.251 -26.056 32.847 1.00 20.25 O
ATOM 375 N GLN A 128 -16.974 -24.772 31.138 1.00 18.34 N
ATOM 376 CA GLN A 128 -15.782 -25.011 30.322 1.00 20.63 C
ATOM 377 C GLN A 128 -14.582 -24.194 30.836 1.00 19.94 C
ATOM 378 O GLN A 128 -14.750 -23.144 31.455 1.00 18.44 O
ATOM 379 CB GLN A 128 -16.062 -24.662 28.854 1.00 22.20 C
ATOM 380 CG GLN A 128 -17.242 -25.413 28.223 1.00 26.60 C
ATOM 381 CD GLN A 128 -16.854 -26.773 27.726 1.00 31.41 C
ATOM 382 OE1 GLN A 128 -17.065 -27.771 28.407 1.00 34.36 O
ATOM 383 NE2 GLN A 128 -16.213 -26.831 26.556 1.00 36.39 N
ATOM 384 N THR A 129 -13.380 -24.660 30.508 1.00 18.17 N
ATOM 385 CA THR A 129 -12.138 -24.045 30.975 1.00 17.66 C
ATOM 386 C THR A 129 -11.178 -23.781 29.808 1.00 15.51 C
ATOM 387 O THR A 129 -11.245 -24.436 28.769 1.00 16.50 O
ATOM 388 CB THR A 129 -11.390 -24.966 32.004 1.00 17.75 C
ATOM 389 OG1 THR A 129 -11.112 -26.240 31.403 1.00 19.72 O
ATOM 390 CG2 THR A 129 -12.217 -25.175 33.277 1.00 17.06 C
ATOM 391 N GLY A 130 -10.266 -22.841 29.997 1.00 14.93 N
ATOM 392 CA GLY A 130 -9.197 -22.671 29.036 1.00 14.11 C
ATOM 393 C GLY A 130 -8.594 -21.292 29.067 1.00 15.00 C
ATOM 394 O GLY A 130 -9.053 -20.433 29.816 1.00 15.71 O
ATOM 395 N TYR A 131 -7.582 -21.068 28.241 1.00 14.37 N
ATOM 396 CA TYR A 131 -6.999 -19.738 28.095 1.00 15.38 C
ATOM 397 C TYR A 131 -7.883 -18.737 27.350 1.00 16.06 C
ATOM 398 O TYR A 131 -8.522 -19.060 26.353 1.00 17.00 O
ATOM 399 CB TYR A 131 -5.658 -19.832 27.401 1.00 16.47 C
ATOM 400 CG TYR A 131 -4.705 -20.713 28.133 1.00 18.72 C
ATOM 401 CD1 TYR A 131 -4.247 -20.373 29.404 1.00 20.09 C
ATOM 402 CD2 TYR A 131 -4.234 -21.882 27.546 1.00 20.09 C
ATOM 403 CE1 TYR A 131 -3.325 -21.188 30.068 1.00 22.16 C
ATOM 404 CE2 TYR A 131 -3.319 -22.689 28.195 1.00 21.21 C
ATOM 405 CZ TYR A 131 -2.871 -22.337 29.444 1.00 20.16 C
ATOM 406 OH TYR A 131 -1.910 -23.110 30.016 1.00 24.14 O
ATOM 407 N ILE A 132 -7.931 -17.518 27.866 1.00 16.86 N
ATOM 408 CA ILE A 132 -8.706 -16.446 27.252 1.00 16.93 C
ATOM 409 C ILE A 132 -7.820 -15.208 27.087 1.00 16.86 C
ATOM 410 O ILE A 132 -6.806 -15.066 27.776 1.00 15.43 O
ATOM 411 CB ILE A 132 -9.975 -16.116 28.090 1.00 15.70 C
ATOM 412 CG1 ILE A 132 -9.603 -15.697 29.517 1.00 18.39 C
ATOM 413 CG2 ILE A 132 -10.869 -17.342 28.144 1.00 17.68 C
ATOM 414 CD1 ILE A 132 -9.521 -14.212 29.714 1.00 19.36 C
ATOM 415 N PRO A 133 -8.067 -14.415 26.036 1.00 17.40 N
ATOM 416 CA PRO A 133 -7.282 -13.199 25.851 1.00 16.33 C
ATOM 417 C PRO A 133 -7.638 -12.187 26.918 1.00 17.78 C
ATOM 418 O PRO A 133 -8.808 -11.859 27.099 1.00 18.87 O
ATOM 419 CB PRO A 133 -7.678 -12.731 24.461 1.00 16.25 C
ATOM 420 CG PRO A 133 -9.057 -13.240 24.277 1.00 18.33 C
ATOM 421 CD PRO A 133 -9.188 -14.505 25.080 1.00 17.18 C
ATOM 422 N SER A 134 -6.633 -11.682 27.618 1.00 17.72 N
ATOM 423 CA SER A 134 -6.878 -10.905 28.824 1.00 20.44 C
ATOM 424 C SER A 134 -7.482 -9.529 28.562 1.00 21.73 C
ATOM 425 O SER A 134 -8.097 -8.945 29.448 1.00 24.66 O
ATOM 426 CB SER A 134 -5.593 -10.773 29.639 1.00 17.99 C
ATOM 427 OG SER A 134 -4.640 -9.996 28.957 1.00 17.84 O
ATOM 428 N ASN A 135 -7.330 -9.007 27.349 1.00 22.51 N
ATOM 429 CA ASN A 135 -7.922 -7.718 26.996 1.00 23.11 C
ATOM 430 C ASN A 135 -9.386 -7.840 26.567 1.00 22.67 C
ATOM 431 O ASN A 135 -10.022 -6.846 26.204 1.00 24.32 O
ATOM 432 CB ASN A 135 -7.097 -7.026 25.897 1.00 26.09 C
ATOM 433 CG ASN A 135 -6.923 -7.875 24.639 1.00 27.26 C
ATOM 434 OD1 ASN A 135 -7.192 -9.085 24.616 1.00 27.16 O
ATOM 435 ND2 ASN A 135 -6.335 -7.279 23.627 1.00 28.35 N
ATOM 436 N TYR A 136 -9.936 -9.045 26.638 1.00 20.62 N
ATOM 437 CA TYR A 136 -11.358 -9.267 26.356 1.00 19.77 C
ATOM 438 C TYR A 136 -12.242 -9.299 27.606 1.00 18.22 C
ATOM 439 O TYR A 136 -13.452 -9.469 27.495 1.00 20.03 O
ATOM 440 CB TYR A 136 -11.560 -10.564 25.575 1.00 18.88 C
ATOM 441 CG TYR A 136 -11.374 -10.425 24.085 1.00 18.10 C
ATOM 442 CD1 TYR A 136 -10.237 -9.813 23.560 1.00 19.61 C
ATOM 443 CD2 TYR A 136 -12.305 -10.958 23.198 1.00 19.59 C
ATOM 444 CE1 TYR A 136 -10.022 -9.746 22.180 1.00 20.82 C
ATOM 445 CE2 TYR A 136 -12.105 -10.895 21.821 1.00 20.30 C
ATOM 446 CZ TYR A 136 -10.957 -10.293 21.318 1.00 21.00 C
ATOM 447 OH TYR A 136 -10.723 -10.261 19.961 1.00 21.65 O
ATOM 448 N VAL A 137 -11.647 -9.122 28.785 1.00 19.64 N
ATOM 449 CA VAL A 137 -12.385 -9.167 30.055 1.00 18.58 C
ATOM 450 C VAL A 137 -12.084 -7.967 30.964 1.00 17.75 C
ATOM 451 O VAL A 137 -11.075 -7.289 30.795 1.00 18.14 O
ATOM 452 CB VAL A 137 -12.098 -10.493 30.862 1.00 17.81 C
ATOM 453 CG1 VAL A 137 -12.648 -11.694 30.128 1.00 17.43 C
ATOM 454 CG2 VAL A 137 -10.601 -10.660 31.127 1.00 16.95 C
ATOM 455 N ALA A 138 -12.981 -7.685 31.901 1.00 17.24 N
ATOM 456 CA ALA A 138 -12.698 -6.733 32.979 1.00 18.41 C
ATOM 457 C ALA A 138 -13.256 -7.265 34.304 1.00 18.53 C
ATOM 458 O ALA A 138 -14.236 -8.016 34.288 1.00 17.34 O
ATOM 459 CB ALA A 138 -13.312 -5.386 32.665 1.00 17.12 C
ATOM 460 N PRO A 139 -12.664 -6.896 35.454 1.00 20.51 N
ATOM 461 CA PRO A 139 -13.171 -7.345 36.758 1.00 22.91 C
ATOM 462 C PRO A 139 -14.655 -7.027 36.870 1.00 25.59 C
ATOM 463 O PRO A 139 -15.072 -5.929 36.479 1.00 26.60 O
ATOM 464 CB PRO A 139 -12.365 -6.556 37.788 1.00 21.34 C
ATOM 465 CG PRO A 139 -11.073 -6.182 37.076 1.00 21.75 C
ATOM 466 CD PRO A 139 -11.336 -6.226 35.573 1.00 20.76 C
ATOM 467 N SER A 140 -15.461 -7.988 37.297 1.00 27.63 N
ATOM 468 CA SER A 140 -16.891 -7.716 37.485 1.00 30.62 C
ATOM 469 C SER A 140 -17.026 -6.564 38.493 1.00 31.49 C
ATOM 470 O SER A 140 -16.235 -6.465 39.442 1.00 34.14 O
ATOM 471 CB SER A 140 -17.630 -8.971 37.985 1.00 30.81 C
ATOM 472 OG SER A 140 -17.116 -9.433 39.227 1.00 38.12 O
ATOM 473 N ASP A 141 -17.882 -5.601 38.165 1.00 32.39 N
ATOM 474 CA ASP A 141 -18.227 -4.470 39.047 1.00 34.75 C
ATOM 475 C ASP A 141 -17.222 -3.296 38.958 1.00 34.05 C
ATOM 476 O ASP A 141 -17.282 -2.341 39.750 1.00 33.11 O
ATOM 477 CB ASP A 141 -18.386 -4.912 40.517 1.00 38.17 C
ATOM 478 CG ASP A 141 -19.346 -6.069 40.674 1.00 42.63 C
ATOM 479 OD1 ASP A 141 -20.195 -6.259 39.771 1.00 46.60 O
ATOM 480 OD2 ASP A 141 -19.216 -6.814 41.676 1.00 46.07 O
ATOM 481 N SER A 142 -16.322 -3.343 37.982 1.00 31.86 N
ATOM 482 CA SER A 142 -15.321 -2.297 37.777 1.00 29.55 C
ATOM 483 C SER A 142 -15.821 -1.351 36.698 1.00 28.53 C
ATOM 484 O SER A 142 -16.749 -1.685 35.962 1.00 27.22 O
ATOM 485 CB SER A 142 -13.976 -2.905 37.355 1.00 28.61 C
ATOM 486 OG SER A 142 -14.032 -3.489 36.049 1.00 26.99 O
ATOM 487 N ILE A 143 -15.255 -0.148 36.650 1.00 29.72 N
ATOM 488 CA ILE A 143 -15.597 0.820 35.614 1.00 29.75 C
ATOM 489 C ILE A 143 -15.212 0.309 34.202 1.00 27.47 C
ATOM 490 O ILE A 143 -16.004 0.441 33.265 1.00 27.32 O
ATOM 491 CB ILE A 143 -14.967 2.225 35.943 1.00 31.13 C
ATOM 492 CG1 ILE A 143 -15.526 3.301 35.008 1.00 33.50 C
ATOM 493 CG2 ILE A 143 -13.454 2.192 35.848 1.00 30.51 C
ATOM 494 CD1 ILE A 143 -16.923 3.765 35.341 1.00 35.59 C
ATOM 495 N GLN A 144 -14.184 -0.543 34.151 1.00 26.54 N
ATOM 496 CA GLN A 144 -13.732 -1.200 32.906 1.00 26.10 C
ATOM 497 C GLN A 144 -14.709 -2.245 32.346 1.00 25.61 C
ATOM 498 O GLN A 144 -14.630 -2.589 31.168 1.00 25.82 O
ATOM 499 CB GLN A 144 -12.367 -1.889 33.094 1.00 28.38 C
ATOM 500 CG GLN A 144 -11.219 -1.039 33.638 1.00 33.39 C
ATOM 501 CD GLN A 144 -11.419 -0.645 35.079 1.00 37.39 C
ATOM 502 OE1 GLN A 144 -10.976 0.413 35.493 1.00 39.32 O
ATOM 503 NE2 GLN A 144 -12.251 -1.395 35.790 1.00 41.03 N
ATOM 504 N ALA A 145 -15.578 -2.798 33.193 1.00 22.54 N
ATOM 505 CA ALA A 145 -16.615 -3.722 32.725 1.00 22.66 C
ATOM 506 C ALA A 145 -17.762 -3.014 31.996 1.00 23.58 C
ATOM 507 O ALA A 145 -18.647 -3.650 31.433 1.00 23.98 O
ATOM 508 CB ALA A 145 -17.172 -4.524 33.892 1.00 22.11 C
ATOM 509 N GLU A 146 -17.819 -1.697 32.108 1.00 24.46 N
ATOM 510 CA GLU A 146 -18.916 -0.963 31.512 1.00 25.56 C
ATOM 511 C GLU A 146 -18.679 -0.753 30.016 1.00 27.38 C
ATOM 512 O GLU A 146 -17.608 -0.300 29.615 1.00 27.21 O
ATOM 513 CB GLU A 146 -19.099 0.385 32.221 1.00 25.84 C
ATOM 514 CG GLU A 146 -19.527 0.291 33.689 1.00 28.43 C
ATOM 515 CD GLU A 146 -20.951 -0.221 33.891 1.00 30.97 C
ATOM 516 OE1 GLU A 146 -21.843 0.084 33.073 1.00 34.19 O
ATOM 517 OE2 GLU A 146 -21.194 -0.899 34.912 1.00 36.05 O
ATOM 518 N GLU A 147 -19.746 -0.932 29.231 1.00 28.78 N
ATOM 519 CA GLU A 147 -19.733 -0.834 27.763 1.00 28.58 C
ATOM 520 C GLU A 147 -19.287 0.550 27.222 1.00 27.31 C
ATOM 521 O GLU A 147 -18.841 0.667 26.082 1.00 27.75 O
ATOM 522 CB GLU A 147 -21.142 -1.151 27.243 1.00 32.10 C
ATOM 523 CG GLU A 147 -21.240 -2.191 26.142 1.00 38.78 C
ATOM 524 CD GLU A 147 -22.645 -2.267 25.553 1.00 43.43 C
ATOM 525 OE1 GLU A 147 -23.608 -1.839 26.232 1.00 44.61 O
ATOM 526 OE2 GLU A 147 -22.779 -2.698 24.387 1.00 48.93 O
ATOM 527 N TRP A 148 -19.471 1.600 28.020 1.00 25.36 N
ATOM 528 CA TRP A 148 -19.254 2.981 27.571 1.00 21.46 C
ATOM 529 C TRP A 148 -17.963 3.613 28.098 1.00 20.95 C
ATOM 530 O TRP A 148 -17.677 4.783 27.822 1.00 19.26 O
ATOM 531 CB TRP A 148 -20.461 3.867 27.944 1.00 20.53 C
ATOM 532 CG TRP A 148 -21.061 3.563 29.293 1.00 19.12 C
ATOM 533 CD1 TRP A 148 -22.209 2.851 29.551 1.00 17.77 C
ATOM 534 CD2 TRP A 148 -20.492 3.881 30.573 1.00 20.51 C
ATOM 535 NE1 TRP A 148 -22.367 2.690 30.912 1.00 18.62 N
ATOM 536 CE2 TRP A 148 -21.324 3.306 31.560 1.00 20.43 C
ATOM 537 CE3 TRP A 148 -19.347 4.595 30.977 1.00 18.32 C
ATOM 538 CZ2 TRP A 148 -21.044 3.417 32.932 1.00 20.06 C
ATOM 539 CZ3 TRP A 148 -19.069 4.708 32.338 1.00 20.54 C
ATOM 540 CH2 TRP A 148 -19.915 4.121 33.300 1.00 19.81 C
ATOM 541 N TYR A 149 -17.219 2.857 28.905 1.00 19.88 N
ATOM 542 CA TYR A 149 -15.918 3.295 29.410 1.00 20.23 C
ATOM 543 C TYR A 149 -14.796 2.847 28.468 1.00 20.38 C
ATOM 544 O TYR A 149 -14.522 1.658 28.362 1.00 21.88 O
ATOM 545 CB TYR A 149 -15.665 2.714 30.816 1.00 20.90 C
ATOM 546 CG TYR A 149 -14.423 3.258 31.482 1.00 20.14 C
ATOM 547 CD1 TYR A 149 -14.380 4.581 31.906 1.00 21.91 C
ATOM 548 CD2 TYR A 149 -13.251 2.494 31.573 1.00 19.48 C
ATOM 549 CE1 TYR A 149 -13.201 5.148 32.392 1.00 25.43 C
ATOM 550 CE2 TYR A 149 -12.075 3.048 32.054 1.00 19.76 C
ATOM 551 CZ TYR A 149 -12.049 4.379 32.452 1.00 24.89 C
ATOM 552 OH TYR A 149 -10.851 4.974 32.799 1.00 28.05 O
ATOM 553 N PHE A 150 -14.099 3.805 27.862 1.00 21.10 N