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1KTZ.pdb
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1KTZ.pdb
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HEADER CYTOKINE/CYTOKINE RECEPTOR 18-JAN-02 1KTZ
TITLE CRYSTAL STRUCTURE OF THE HUMAN TGF-BETA TYPE II RECEPTOR
TITLE 2 EXTRACELLULAR DOMAIN IN COMPLEX WITH TGF-BETA3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TGF-BETA3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TGF-BETA TYPE II RECEPTOR;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 10 SYNONYM: TBR-2;
COMPND 11 EC: 2.7.1.37;
COMPND 12 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYTOKINE-RECEPTOR COMPLEX, CYTOKINE/CYTOKINE RECEPTOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.HART,S.DEEP,A.B.TAYLOR,Z.SHU,C.S.HINCK,A.P.HINCK
REVDAT 3 24-FEB-09 1KTZ 1 VERSN
REVDAT 2 01-APR-03 1KTZ 1 JRNL
REVDAT 1 27-FEB-02 1KTZ 0
JRNL AUTH P.J.HART,S.DEEP,A.B.TAYLOR,Z.SHU,C.S.HINCK,
JRNL AUTH 2 A.P.HINCK
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN TBETAR2
JRNL TITL 2 ECTODOMAIN--TGF-BETA3 COMPLEX.
JRNL REF NAT.STRUCT.BIOL. V. 9 203 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11850637
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3888970.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28916
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2632
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 200
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1493
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 163
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.25000
REMARK 3 B22 (A**2) : -2.25000
REMARK 3 B33 (A**2) : 4.51000
REMARK 3 B12 (A**2) : 0.34000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 26.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.74
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.560 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.480 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.970 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.380 ; 4.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 61.04
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KTZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-02.
REMARK 100 THE RCSB ID CODE IS RCSB015342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29006
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 26.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.53300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOR DIFFUSION USING
REMARK 280 A WELL SOLUTION CONTAINING 20% (V/V) 2-METHYL-2,4-PENTANEDIOL
REMARK 280 AND 0.1 M CITRATE PH 4.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 57.20500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 33.02732
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 69.81000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 57.20500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 33.02732
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 69.81000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 57.20500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 33.02732
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 69.81000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 57.20500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 33.02732
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 69.81000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 57.20500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 33.02732
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 69.81000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 57.20500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 33.02732
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 69.81000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 66.05464
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 139.62000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 66.05464
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 139.62000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 66.05464
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 139.62000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 66.05464
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 139.62000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 66.05464
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 139.62000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 66.05464
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 139.62000
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE CRYSTALLOGRAPHIC SYMMETRY OPERATOR Y, X, -Z AND A
REMARK 300 TRANSLATION OF ONE UNIT CELL LENGTH ALONG THE Z-AXIS.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 209.43000
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 ALA A 1
REMARK 465 LEU A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 ASN A 5
REMARK 465 TYR A 6
REMARK 465 CYS A 7
REMARK 465 PHE A 8
REMARK 465 ARG A 9
REMARK 465 ASN A 10
REMARK 465 LEU A 11
REMARK 465 GLU A 12
REMARK 465 ASP A 55
REMARK 465 THR A 56
REMARK 465 THR A 57
REMARK 465 HIS A 58
REMARK 465 SER A 59
REMARK 465 THR A 60
REMARK 465 VAL A 61
REMARK 465 LEU A 62
REMARK 465 GLY A 63
REMARK 465 LEU A 64
REMARK 465 TYR A 65
REMARK 465 ASN A 66
REMARK 465 THR A 67
REMARK 465 LEU A 68
REMARK 465 ASN A 69
REMARK 465 PRO A 70
REMARK 465 GLU A 71
REMARK 465 ALA A 72
REMARK 465 VAL B 15
REMARK 465 THR B 16
REMARK 465 ASP B 17
REMARK 465 ASN B 18
REMARK 465 ASN B 19
REMARK 465 GLY B 20
REMARK 465 ALA B 21
REMARK 465 VAL B 22
REMARK 465 LYS B 23
REMARK 465 PHE B 24
REMARK 465 ASN B 131
REMARK 465 THR B 132
REMARK 465 SER B 133
REMARK 465 ASN B 134
REMARK 465 PRO B 135
REMARK 465 ASP B 136
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 ASN A 42 175.06 62.20
REMARK 500 SER A 53 51.44 -119.48
REMARK 500 GLN A 81 -76.05 -114.05
REMARK 500 ASP B 32 -146.68 55.23
REMARK 500 ASN B 68 -168.45 -112.51
REMARK 500 SER B 127 179.59 61.13
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KTZ A 1 112 UNP P10600 TGFB3_HUMAN 301 412
DBREF 1KTZ B 15 136 UNP P37173 TGFR2_HUMAN 38 159
SEQRES 1 A 112 ALA LEU ASP THR ASN TYR CYS PHE ARG ASN LEU GLU GLU
SEQRES 2 A 112 ASN CYS CYS VAL ARG PRO LEU TYR ILE ASP PHE ARG GLN
SEQRES 3 A 112 ASP LEU GLY TRP LYS TRP VAL HIS GLU PRO LYS GLY TYR
SEQRES 4 A 112 TYR ALA ASN PHE CYS SER GLY PRO CYS PRO TYR LEU ARG
SEQRES 5 A 112 SER ALA ASP THR THR HIS SER THR VAL LEU GLY LEU TYR
SEQRES 6 A 112 ASN THR LEU ASN PRO GLU ALA SER ALA SER PRO CYS CYS
SEQRES 7 A 112 VAL PRO GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR
SEQRES 8 A 112 VAL GLY ARG THR PRO LYS VAL GLU GLN LEU SER ASN MET
SEQRES 9 A 112 VAL VAL LYS SER CYS LYS CYS SER
SEQRES 1 B 122 VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU
SEQRES 2 B 122 CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN
SEQRES 3 B 122 GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE
SEQRES 4 B 122 CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG
SEQRES 5 B 122 LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS
SEQRES 6 B 122 ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP
SEQRES 7 B 122 ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS
SEQRES 8 B 122 PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP
SEQRES 9 B 122 GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR ASN
SEQRES 10 B 122 THR SER ASN PRO ASP
FORMUL 3 HOH *163(H2 O)
HELIX 1 1 PHE A 24 GLY A 29 1 6
HELIX 2 2 GLU B 119 ASN B 121 5 3
SHEET 1 A 2 CYS A 16 ARG A 18 0
SHEET 2 A 2 PHE A 43 SER A 45 -1 O PHE A 43 N ARG A 18
SHEET 1 B 2 TYR A 21 ASP A 23 0
SHEET 2 B 2 GLY A 38 TYR A 40 -1 O TYR A 39 N ILE A 22
SHEET 1 C 3 THR A 95 VAL A 106 0
SHEET 2 C 3 LEU A 83 VAL A 92 -1 N GLU A 84 O VAL A 105
SHEET 3 C 3 VAL A 33 GLU A 35 -1 N GLU A 35 O LEU A 89
SHEET 1 D 4 THR A 95 VAL A 106 0
SHEET 2 D 4 LEU A 83 VAL A 92 -1 N GLU A 84 O VAL A 105
SHEET 3 D 4 THR B 51 ILE B 53 1 O ILE B 53 N TYR A 91
SHEET 4 D 4 LEU B 27 LYS B 29 -1 N CYS B 28 O SER B 52
SHEET 1 E 2 CYS A 77 PRO A 80 0
SHEET 2 E 2 CYS A 109 SER A 112 -1 O SER A 112 N CYS A 77
SHEET 1 F 7 ASP B 32 PHE B 35 0
SHEET 2 F 7 ILE B 72 HIS B 79 -1 O LEU B 74 N ARG B 34
SHEET 3 F 7 VAL B 60 LYS B 67 -1 N VAL B 64 O GLU B 75
SHEET 4 F 7 THR B 109 CYS B 115 -1 O PHE B 111 N TRP B 65
SHEET 5 F 7 CYS B 98 LYS B 103 -1 N LYS B 103 O PHE B 110
SHEET 6 F 7 ASN B 123 PHE B 126 1 O ILE B 125 N CYS B 98
SHEET 7 F 7 SER B 43 MET B 45 -1 N CYS B 44 O ILE B 124
SSBOND 1 CYS A 15 CYS A 78 1555 1555 2.04
SSBOND 2 CYS A 44 CYS A 109 1555 1555 2.03
SSBOND 3 CYS A 48 CYS A 111 1555 1555 2.04
SSBOND 4 CYS B 28 CYS B 61 1555 1555 2.05
SSBOND 5 CYS B 31 CYS B 48 1555 1555 2.05
SSBOND 6 CYS B 38 CYS B 44 1555 1555 2.05
SSBOND 7 CYS B 54 CYS B 78 1555 1555 2.08
SSBOND 8 CYS B 98 CYS B 113 1555 1555 2.01
SSBOND 9 CYS B 115 CYS B 120 1555 1555 2.03
CISPEP 1 GLU A 35 PRO A 36 0 -0.86
CRYST1 114.410 114.410 209.430 90.00 90.00 120.00 H 3 2 18
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 0.008740 0.005046 0.000000 0.00000
SCALE2 0.000000 0.010092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004775 0.00000
ATOM 1 N GLU A 13 44.993 92.605 105.474 1.00 76.90 N
ATOM 2 CA GLU A 13 43.867 91.726 105.044 1.00 77.18 C
ATOM 3 C GLU A 13 43.546 90.572 105.996 1.00 77.35 C
ATOM 4 O GLU A 13 44.285 90.276 106.940 1.00 77.84 O
ATOM 5 CB GLU A 13 44.159 91.144 103.656 1.00 76.81 C
ATOM 6 CG GLU A 13 43.529 91.943 102.529 1.00 78.95 C
ATOM 7 CD GLU A 13 42.009 92.035 102.656 1.00 83.06 C
ATOM 8 OE1 GLU A 13 41.379 92.724 101.828 1.00 83.54 O
ATOM 9 OE2 GLU A 13 41.435 91.420 103.581 1.00 83.51 O
ATOM 10 N ASN A 14 42.422 89.922 105.731 1.00 75.22 N
ATOM 11 CA ASN A 14 41.989 88.809 106.544 1.00 73.16 C
ATOM 12 C ASN A 14 41.200 87.823 105.694 1.00 70.71 C
ATOM 13 O ASN A 14 41.087 87.970 104.482 1.00 70.41 O
ATOM 14 CB ASN A 14 41.129 89.322 107.706 1.00 75.07 C
ATOM 15 CG ASN A 14 40.299 90.547 107.330 1.00 80.30 C
ATOM 16 OD1 ASN A 14 39.598 90.550 106.311 1.00 83.53 O
ATOM 17 ND2 ASN A 14 40.374 91.595 108.157 1.00 77.90 N
ATOM 18 N CYS A 15 40.657 86.816 106.352 1.00 67.99 N
ATOM 19 CA CYS A 15 39.889 85.776 105.700 1.00 64.54 C
ATOM 20 C CYS A 15 38.471 86.207 105.377 1.00 63.10 C
ATOM 21 O CYS A 15 37.748 86.656 106.262 1.00 62.08 O
ATOM 22 CB CYS A 15 39.854 84.548 106.612 1.00 60.31 C
ATOM 23 SG CYS A 15 38.608 83.252 106.274 1.00 56.64 S
ATOM 24 N CYS A 16 38.072 86.080 104.113 1.00 60.91 N
ATOM 25 CA CYS A 16 36.690 86.380 103.742 1.00 59.99 C
ATOM 26 C CYS A 16 36.272 85.934 102.351 1.00 56.43 C
ATOM 27 O CYS A 16 37.064 85.407 101.564 1.00 54.51 O
ATOM 28 CB CYS A 16 36.388 87.878 103.891 1.00 62.85 C
ATOM 29 SG CYS A 16 37.638 88.973 103.285 1.00 78.18 S
ATOM 30 N VAL A 17 34.997 86.148 102.078 1.00 54.29 N
ATOM 31 CA VAL A 17 34.402 85.771 100.819 1.00 52.95 C
ATOM 32 C VAL A 17 34.928 86.640 99.685 1.00 51.25 C
ATOM 33 O VAL A 17 34.928 87.866 99.781 1.00 50.23 O
ATOM 34 CB VAL A 17 32.861 85.906 100.885 1.00 52.79 C
ATOM 35 CG1 VAL A 17 32.228 85.124 99.740 1.00 52.80 C
ATOM 36 CG2 VAL A 17 32.360 85.383 102.218 1.00 52.40 C
ATOM 37 N ARG A 18 35.385 85.995 98.619 1.00 49.19 N
ATOM 38 CA ARG A 18 35.875 86.710 97.446 1.00 46.95 C
ATOM 39 C ARG A 18 34.872 86.411 96.322 1.00 44.61 C
ATOM 40 O ARG A 18 34.468 85.267 96.120 1.00 43.40 O
ATOM 41 CB ARG A 18 37.252 86.202 97.011 1.00 48.50 C
ATOM 42 CG ARG A 18 38.273 86.098 98.112 1.00 54.10 C
ATOM 43 CD ARG A 18 38.689 87.452 98.638 1.00 58.09 C
ATOM 44 NE ARG A 18 39.627 87.290 99.744 1.00 67.80 N
ATOM 45 CZ ARG A 18 40.112 88.285 100.481 1.00 69.94 C
ATOM 46 NH1 ARG A 18 40.960 88.020 101.474 1.00 63.24 N
ATOM 47 NH2 ARG A 18 39.749 89.540 100.225 1.00 70.79 N
ATOM 48 N PRO A 19 34.455 87.442 95.581 1.00 42.46 N
ATOM 49 CA PRO A 19 33.508 87.206 94.499 1.00 40.77 C
ATOM 50 C PRO A 19 34.126 86.361 93.386 1.00 39.83 C
ATOM 51 O PRO A 19 35.306 86.524 93.029 1.00 38.58 O
ATOM 52 CB PRO A 19 33.122 88.617 94.057 1.00 40.11 C
ATOM 53 CG PRO A 19 34.402 89.394 94.319 1.00 43.77 C
ATOM 54 CD PRO A 19 34.823 88.868 95.676 1.00 42.65 C
ATOM 55 N LEU A 20 33.333 85.444 92.846 1.00 37.11 N
ATOM 56 CA LEU A 20 33.795 84.628 91.734 1.00 37.08 C
ATOM 57 C LEU A 20 32.582 84.198 90.924 1.00 38.11 C
ATOM 58 O LEU A 20 31.700 83.487 91.419 1.00 37.44 O
ATOM 59 CB LEU A 20 34.543 83.395 92.226 1.00 34.71 C
ATOM 60 CG LEU A 20 35.158 82.583 91.081 1.00 37.34 C
ATOM 61 CD1 LEU A 20 36.225 83.414 90.387 1.00 38.40 C
ATOM 62 CD2 LEU A 20 35.762 81.297 91.619 1.00 41.32 C
ATOM 63 N TYR A 21 32.535 84.640 89.671 1.00 37.94 N
ATOM 64 CA TYR A 21 31.425 84.294 88.794 1.00 35.82 C
ATOM 65 C TYR A 21 31.776 83.025 88.024 1.00 34.37 C
ATOM 66 O TYR A 21 32.871 82.903 87.465 1.00 32.25 O
ATOM 67 CB TYR A 21 31.153 85.446 87.830 1.00 35.57 C
ATOM 68 CG TYR A 21 30.008 85.170 86.890 1.00 37.32 C
ATOM 69 CD1 TYR A 21 30.228 84.588 85.636 1.00 34.89 C
ATOM 70 CD2 TYR A 21 28.695 85.497 87.251 1.00 41.75 C
ATOM 71 CE1 TYR A 21 29.172 84.340 84.757 1.00 36.86 C
ATOM 72 CE2 TYR A 21 27.618 85.251 86.376 1.00 37.89 C
ATOM 73 CZ TYR A 21 27.868 84.678 85.138 1.00 37.27 C
ATOM 74 OH TYR A 21 26.813 84.468 84.297 1.00 40.81 O
ATOM 75 N ILE A 22 30.837 82.086 88.008 1.00 32.54 N
ATOM 76 CA ILE A 22 31.007 80.798 87.356 1.00 32.74 C
ATOM 77 C ILE A 22 30.014 80.742 86.209 1.00 34.42 C
ATOM 78 O ILE A 22 28.827 81.044 86.405 1.00 33.79 O
ATOM 79 CB ILE A 22 30.696 79.638 88.347 1.00 39.05 C
ATOM 80 CG1 ILE A 22 31.769 79.615 89.443 1.00 37.53 C
ATOM 81 CG2 ILE A 22 30.593 78.298 87.581 1.00 35.53 C
ATOM 82 CD1 ILE A 22 33.103 79.097 88.979 1.00 42.44 C
ATOM 83 N ASP A 23 30.495 80.366 85.026 1.00 33.28 N
ATOM 84 CA ASP A 23 29.645 80.250 83.838 1.00 33.62 C
ATOM 85 C ASP A 23 29.354 78.755 83.665 1.00 33.16 C
ATOM 86 O ASP A 23 30.284 77.969 83.530 1.00 31.65 O
ATOM 87 CB ASP A 23 30.381 80.765 82.598 1.00 34.75 C
ATOM 88 CG ASP A 23 29.546 80.644 81.348 1.00 35.51 C
ATOM 89 OD1 ASP A 23 28.910 81.652 80.975 1.00 38.58 O
ATOM 90 OD2 ASP A 23 29.523 79.540 80.754 1.00 36.43 O
ATOM 91 N PHE A 24 28.088 78.346 83.656 1.00 32.45 N
ATOM 92 CA PHE A 24 27.829 76.896 83.562 1.00 33.15 C
ATOM 93 C PHE A 24 28.471 76.184 82.398 1.00 31.99 C
ATOM 94 O PHE A 24 29.137 75.183 82.571 1.00 32.29 O
ATOM 95 CB PHE A 24 26.306 76.626 83.533 1.00 34.40 C
ATOM 96 CG PHE A 24 25.638 76.862 84.861 1.00 30.78 C
ATOM 97 CD1 PHE A 24 25.960 76.076 85.957 1.00 35.24 C
ATOM 98 CD2 PHE A 24 24.716 77.882 85.016 1.00 31.32 C
ATOM 99 CE1 PHE A 24 25.367 76.306 87.208 1.00 33.54 C
ATOM 100 CE2 PHE A 24 24.126 78.120 86.243 1.00 35.47 C
ATOM 101 CZ PHE A 24 24.454 77.327 87.346 1.00 35.51 C
ATOM 102 N ARG A 25 28.273 76.697 81.197 1.00 34.83 N
ATOM 103 CA ARG A 25 28.832 76.059 80.007 1.00 34.60 C
ATOM 104 C ARG A 25 30.361 76.133 79.965 1.00 36.61 C
ATOM 105 O ARG A 25 31.035 75.107 79.799 1.00 37.32 O
ATOM 106 CB ARG A 25 28.226 76.730 78.764 1.00 37.73 C
ATOM 107 CG ARG A 25 28.663 76.149 77.422 1.00 43.96 C
ATOM 108 CD ARG A 25 27.941 76.867 76.260 1.00 43.84 C
ATOM 109 NE ARG A 25 26.502 76.611 76.239 1.00 47.90 N
ATOM 110 CZ ARG A 25 25.939 75.555 75.630 1.00 44.10 C
ATOM 111 NH1 ARG A 25 24.625 75.390 75.660 1.00 41.24 N
ATOM 112 NH2 ARG A 25 26.686 74.660 74.984 1.00 35.09 N
ATOM 113 N GLN A 26 30.918 77.339 80.127 1.00 33.78 N
ATOM 114 CA GLN A 26 32.357 77.497 80.035 1.00 34.79 C
ATOM 115 C GLN A 26 33.146 76.872 81.163 1.00 36.04 C
ATOM 116 O GLN A 26 34.175 76.254 80.912 1.00 35.48 O
ATOM 117 CB GLN A 26 32.741 78.985 79.982 1.00 36.35 C
ATOM 118 CG GLN A 26 32.151 79.739 78.834 1.00 40.75 C
ATOM 119 CD GLN A 26 32.493 79.041 77.527 1.00 51.86 C
ATOM 120 OE1 GLN A 26 31.617 78.798 76.678 1.00 48.00 O
ATOM 121 NE2 GLN A 26 33.776 78.710 77.360 1.00 49.38 N
ATOM 122 N ASP A 27 32.674 77.029 82.399 1.00 34.57 N
ATOM 123 CA ASP A 27 33.451 76.529 83.538 1.00 36.53 C
ATOM 124 C ASP A 27 33.065 75.184 84.121 1.00 38.71 C
ATOM 125 O ASP A 27 33.935 74.471 84.584 1.00 38.25 O
ATOM 126 CB ASP A 27 33.434 77.562 84.670 1.00 30.46 C
ATOM 127 CG ASP A 27 33.928 78.907 84.215 1.00 33.61 C
ATOM 128 OD1 ASP A 27 35.000 78.967 83.559 1.00 37.83 O
ATOM 129 OD2 ASP A 27 33.253 79.904 84.504 1.00 33.29 O
ATOM 130 N LEU A 28 31.779 74.834 84.107 1.00 40.53 N
ATOM 131 CA LEU A 28 31.365 73.544 84.644 1.00 41.17 C
ATOM 132 C LEU A 28 31.126 72.516 83.559 1.00 41.09 C
ATOM 133 O LEU A 28 31.042 71.350 83.847 1.00 42.84 O
ATOM 134 CB LEU A 28 30.089 73.696 85.471 1.00 41.45 C
ATOM 135 CG LEU A 28 30.267 74.585 86.697 1.00 39.51 C
ATOM 136 CD1 LEU A 28 29.001 74.552 87.540 1.00 37.58 C
ATOM 137 CD2 LEU A 28 31.451 74.081 87.523 1.00 40.51 C
ATOM 138 N GLY A 29 31.022 72.941 82.307 1.00 41.77 N
ATOM 139 CA GLY A 29 30.774 71.986 81.248 1.00 39.21 C
ATOM 140 C GLY A 29 29.297 71.582 81.226 1.00 39.72 C
ATOM 141 O GLY A 29 28.946 70.597 80.608 1.00 39.68 O
ATOM 142 N TRP A 30 28.427 72.327 81.893 1.00 39.03 N
ATOM 143 CA TRP A 30 27.018 71.988 81.904 1.00 39.11 C
ATOM 144 C TRP A 30 26.308 72.744 80.797 1.00 40.07 C
ATOM 145 O TRP A 30 26.169 73.966 80.853 1.00 42.27 O
ATOM 146 CB TRP A 30 26.373 72.362 83.236 1.00 38.57 C
ATOM 147 CG TRP A 30 26.929 71.641 84.419 1.00 39.15 C
ATOM 148 CD1 TRP A 30 27.902 70.671 84.426 1.00 36.65 C
ATOM 149 CD2 TRP A 30 26.558 71.848 85.782 1.00 38.51 C
ATOM 150 NE1 TRP A 30 28.157 70.267 85.718 1.00 38.25 N
ATOM 151 CE2 TRP A 30 27.345 70.974 86.569 1.00 40.42 C
ATOM 152 CE3 TRP A 30 25.636 72.689 86.415 1.00 38.45 C
ATOM 153 CZ2 TRP A 30 27.237 70.920 87.964 1.00 41.51 C
ATOM 154 CZ3 TRP A 30 25.525 72.640 87.798 1.00 40.26 C
ATOM 155 CH2 TRP A 30 26.325 71.758 88.560 1.00 41.50 C
ATOM 156 N LYS A 31 25.847 72.019 79.792 1.00 39.04 N
ATOM 157 CA LYS A 31 25.170 72.672 78.689 1.00 40.00 C
ATOM 158 C LYS A 31 23.649 72.681 78.836 1.00 38.49 C
ATOM 159 O LYS A 31 22.948 73.296 78.026 1.00 39.23 O
ATOM 160 CB LYS A 31 25.551 71.957 77.398 1.00 38.31 C
ATOM 161 CG LYS A 31 27.043 71.734 77.269 1.00 41.56 C
ATOM 162 CD LYS A 31 27.355 71.142 75.926 1.00 41.97 C
ATOM 163 CE LYS A 31 28.852 70.962 75.729 1.00 46.56 C
ATOM 164 NZ LYS A 31 29.123 70.095 74.535 1.00 51.76 N
ATOM 165 N TRP A 32 23.155 72.005 79.869 1.00 38.81 N
ATOM 166 CA TRP A 32 21.708 71.837 80.096 1.00 38.62 C
ATOM 167 C TRP A 32 20.996 72.846 80.990 1.00 40.60 C
ATOM 168 O TRP A 32 19.766 72.789 81.129 1.00 40.75 O
ATOM 169 CB TRP A 32 21.469 70.432 80.651 1.00 32.78 C
ATOM 170 CG TRP A 32 22.325 70.158 81.811 1.00 38.34 C
ATOM 171 CD1 TRP A 32 23.599 69.651 81.795 1.00 34.52 C
ATOM 172 CD2 TRP A 32 22.009 70.423 83.200 1.00 37.52 C
ATOM 173 NE1 TRP A 32 24.097 69.588 83.082 1.00 35.22 N
ATOM 174 CE2 TRP A 32 23.143 70.056 83.960 1.00 38.55 C
ATOM 175 CE3 TRP A 32 20.874 70.930 83.864 1.00 38.18 C
ATOM 176 CZ2 TRP A 32 23.180 70.181 85.359 1.00 40.01 C
ATOM 177 CZ3 TRP A 32 20.902 71.057 85.250 1.00 38.72 C
ATOM 178 CH2 TRP A 32 22.055 70.683 85.988 1.00 40.75 C
ATOM 179 N VAL A 33 21.740 73.769 81.606 1.00 40.45 N
ATOM 180 CA VAL A 33 21.091 74.774 82.424 1.00 38.64 C
ATOM 181 C VAL A 33 20.541 75.846 81.489 1.00 39.80 C
ATOM 182 O VAL A 33 21.296 76.458 80.735 1.00 39.96 O
ATOM 183 CB VAL A 33 22.077 75.429 83.420 1.00 38.42 C
ATOM 184 CG1 VAL A 33 21.334 76.467 84.257 1.00 33.81 C
ATOM 185 CG2 VAL A 33 22.667 74.375 84.338 1.00 38.42 C
ATOM 186 N HIS A 34 19.224 76.083 81.521 1.00 37.31 N
ATOM 187 CA HIS A 34 18.639 77.099 80.650 1.00 37.27 C
ATOM 188 C HIS A 34 18.829 78.515 81.217 1.00 37.83 C
ATOM 189 O HIS A 34 19.142 79.452 80.484 1.00 38.33 O
ATOM 190 CB HIS A 34 17.137 76.819 80.459 1.00 37.53 C
ATOM 191 CG HIS A 34 16.482 77.700 79.445 1.00 32.20 C
ATOM 192 ND1 HIS A 34 16.766 77.621 78.096 1.00 35.69 N
ATOM 193 CD2 HIS A 34 15.562 78.689 79.583 1.00 31.12 C
ATOM 194 CE1 HIS A 34 16.049 78.526 77.447 1.00 38.62 C
ATOM 195 NE2 HIS A 34 15.311 79.187 78.327 1.00 35.55 N
ATOM 196 N GLU A 35 18.619 78.674 82.524 1.00 39.22 N
ATOM 197 CA GLU A 35 18.808 79.962 83.207 1.00 40.25 C
ATOM 198 C GLU A 35 19.147 79.659 84.668 1.00 40.21 C
ATOM 199 O GLU A 35 18.644 78.685 85.221 1.00 39.54 O
ATOM 200 CB GLU A 35 17.537 80.829 83.174 1.00 44.45 C
ATOM 201 CG GLU A 35 17.177 81.447 81.827 1.00 51.93 C
ATOM 202 CD GLU A 35 18.303 82.288 81.217 1.00 59.35 C
ATOM 203 OE1 GLU A 35 19.177 82.773 81.962 1.00 59.73 O
ATOM 204 OE2 GLU A 35 18.312 82.470 79.979 1.00 64.55 O
ATOM 205 N PRO A 36 20.046 80.459 85.296 1.00 38.98 N
ATOM 206 CA PRO A 36 20.748 81.596 84.689 1.00 38.19 C
ATOM 207 C PRO A 36 21.950 80.984 83.912 1.00 37.86 C
ATOM 208 O PRO A 36 22.222 79.793 84.039 1.00 37.81 O
ATOM 209 CB PRO A 36 21.165 82.451 85.902 1.00 38.23 C
ATOM 210 CG PRO A 36 21.526 81.415 86.924 1.00 36.55 C
ATOM 211 CD PRO A 36 20.457 80.285 86.710 1.00 41.00 C
ATOM 212 N LYS A 37 22.663 81.784 83.124 1.00 37.91 N
ATOM 213 CA LYS A 37 23.799 81.267 82.361 1.00 37.66 C
ATOM 214 C LYS A 37 24.995 81.010 83.266 1.00 36.14 C
ATOM 215 O LYS A 37 25.907 80.244 82.936 1.00 36.32 O
ATOM 216 CB LYS A 37 24.145 82.269 81.242 1.00 40.84 C
ATOM 217 CG LYS A 37 23.036 82.318 80.159 1.00 47.40 C
ATOM 218 CD LYS A 37 22.690 80.879 79.698 1.00 51.21 C
ATOM 219 CE LYS A 37 21.518 80.781 78.708 1.00 55.02 C
ATOM 220 NZ LYS A 37 21.331 79.330 78.266 1.00 54.89 N
ATOM 221 N GLY A 38 24.986 81.656 84.422 1.00 36.10 N
ATOM 222 CA GLY A 38 26.066 81.445 85.368 1.00 37.33 C
ATOM 223 C GLY A 38 25.709 82.153 86.660 1.00 38.17 C
ATOM 224 O GLY A 38 24.630 82.738 86.752 1.00 37.28 O
ATOM 225 N TYR A 39 26.590 82.125 87.652 1.00 36.77 N
ATOM 226 CA TYR A 39 26.258 82.796 88.900 1.00 38.70 C
ATOM 227 C TYR A 39 27.511 83.038 89.770 1.00 37.95 C
ATOM 228 O TYR A 39 28.591 82.486 89.523 1.00 36.32 O
ATOM 229 CB TYR A 39 25.262 81.929 89.690 1.00 37.39 C
ATOM 230 CG TYR A 39 25.958 80.712 90.241 1.00 35.78 C
ATOM 231 CD1 TYR A 39 26.438 79.715 89.398 1.00 36.72 C
ATOM 232 CD2 TYR A 39 26.190 80.584 91.608 1.00 39.51 C
ATOM 233 CE1 TYR A 39 27.144 78.616 89.899 1.00 36.46 C
ATOM 234 CE2 TYR A 39 26.889 79.490 92.124 1.00 37.25 C
ATOM 235 CZ TYR A 39 27.362 78.520 91.269 1.00 38.75 C
ATOM 236 OH TYR A 39 28.065 77.454 91.786 1.00 42.92 O
ATOM 237 N TYR A 40 27.337 83.861 90.792 1.00 37.75 N
ATOM 238 CA TYR A 40 28.408 84.133 91.728 1.00 38.33 C
ATOM 239 C TYR A 40 28.509 83.012 92.749 1.00 37.78 C
ATOM 240 O TYR A 40 27.701 82.950 93.674 1.00 39.78 O
ATOM 241 CB TYR A 40 28.132 85.472 92.409 1.00 39.56 C
ATOM 242 CG TYR A 40 28.621 86.582 91.523 1.00 39.63 C
ATOM 243 CD1 TYR A 40 29.980 86.895 91.477 1.00 38.89 C
ATOM 244 CD2 TYR A 40 27.738 87.283 90.685 1.00 39.73 C
ATOM 245 CE1 TYR A 40 30.469 87.883 90.612 1.00 41.16 C
ATOM 246 CE2 TYR A 40 28.207 88.275 89.812 1.00 38.11 C
ATOM 247 CZ TYR A 40 29.575 88.564 89.782 1.00 41.76 C
ATOM 248 OH TYR A 40 30.052 89.519 88.911 1.00 47.96 O
ATOM 249 N ALA A 41 29.490 82.125 92.572 1.00 37.23 N
ATOM 250 CA ALA A 41 29.732 81.018 93.494 1.00 36.88 C
ATOM 251 C ALA A 41 30.634 81.495 94.652 1.00 38.96 C
ATOM 252 O ALA A 41 30.466 81.064 95.806 1.00 37.34 O
ATOM 253 CB ALA A 41 30.422 79.835 92.761 1.00 33.21 C
ATOM 254 N ASN A 42 31.583 82.381 94.318 1.00 37.33 N
ATOM 255 CA ASN A 42 32.555 82.947 95.255 1.00 38.32 C
ATOM 256 C ASN A 42 33.466 81.898 95.871 1.00 40.60 C
ATOM 257 O ASN A 42 33.301 80.699 95.630 1.00 40.50 O
ATOM 258 CB ASN A 42 31.833 83.680 96.370 1.00 39.31 C
ATOM 259 CG ASN A 42 30.750 84.576 95.845 1.00 43.48 C
ATOM 260 OD1 ASN A 42 30.919 85.225 94.806 1.00 44.10 O
ATOM 261 ND2 ASN A 42 29.621 84.627 96.554 1.00 42.01 N
ATOM 262 N PHE A 43 34.444 82.351 96.657 1.00 40.46 N
ATOM 263 CA PHE A 43 35.343 81.435 97.353 1.00 40.91 C
ATOM 264 C PHE A 43 35.947 82.147 98.552 1.00 41.47 C
ATOM 265 O PHE A 43 35.815 83.367 98.681 1.00 41.36 O
ATOM 266 CB PHE A 43 36.480 80.911 96.436 1.00 41.37 C
ATOM 267 CG PHE A 43 37.448 81.976 95.937 1.00 46.66 C
ATOM 268 CD1 PHE A 43 37.095 82.833 94.901 1.00 48.42 C
ATOM 269 CD2 PHE A 43 38.731 82.076 96.476 1.00 45.50 C
ATOM 270 CE1 PHE A 43 38.003 83.787 94.397 1.00 47.94 C
ATOM 271 CE2 PHE A 43 39.645 83.014 95.992 1.00 48.49 C
ATOM 272 CZ PHE A 43 39.284 83.871 94.944 1.00 51.66 C
ATOM 273 N CYS A 44 36.593 81.374 99.425 1.00 42.66 N
ATOM 274 CA CYS A 44 37.225 81.888 100.650 1.00 44.37 C
ATOM 275 C CYS A 44 38.718 82.071 100.487 1.00 45.02 C
ATOM 276 O CYS A 44 39.401 81.196 99.954 1.00 43.60 O
ATOM 277 CB CYS A 44 36.996 80.923 101.817 1.00 45.55 C
ATOM 278 SG CYS A 44 35.249 80.821 102.221 1.00 47.94 S
ATOM 279 N SER A 45 39.224 83.201 100.960 1.00 45.86 N
ATOM 280 CA SER A 45 40.652 83.462 100.844 1.00 49.23 C
ATOM 281 C SER A 45 41.099 84.483 101.876 1.00 50.22 C
ATOM 282 O SER A 45 40.355 85.394 102.218 1.00 48.54 O
ATOM 283 CB SER A 45 40.980 83.995 99.444 1.00 46.95 C
ATOM 284 OG SER A 45 42.355 83.819 99.164 1.00 47.85 O
ATOM 285 N GLY A 46 42.322 84.340 102.370 1.00 53.47 N
ATOM 286 CA GLY A 46 42.783 85.297 103.362 1.00 56.01 C
ATOM 287 C GLY A 46 43.496 84.674 104.544 1.00 57.21 C
ATOM 288 O GLY A 46 43.248 83.517 104.904 1.00 56.57 O
ATOM 289 N PRO A 47 44.400 85.434 105.176 1.00 58.52 N
ATOM 290 CA PRO A 47 45.153 84.934 106.329 1.00 57.62 C
ATOM 291 C PRO A 47 44.320 84.650 107.566 1.00 56.87 C
ATOM 292 O PRO A 47 43.325 85.320 107.846 1.00 54.67 O
ATOM 293 CB PRO A 47 46.211 86.012 106.561 1.00 56.90 C
ATOM 294 CG PRO A 47 45.500 87.283 106.125 1.00 60.98 C
ATOM 295 CD PRO A 47 44.764 86.830 104.859 1.00 59.79 C
ATOM 296 N CYS A 48 44.755 83.636 108.295 1.00 57.73 N
ATOM 297 CA CYS A 48 44.140 83.230 109.539 1.00 58.78 C
ATOM 298 C CYS A 48 45.232 83.216 110.615 1.00 60.34 C
ATOM 299 O CYS A 48 46.418 83.339 110.315 1.00 60.70 O
ATOM 300 CB CYS A 48 43.552 81.840 109.398 1.00 57.30 C
ATOM 301 SG CYS A 48 41.998 81.798 108.465 1.00 59.27 S
ATOM 302 N PRO A 49 44.847 83.081 111.884 1.00 61.38 N
ATOM 303 CA PRO A 49 45.839 83.050 112.968 1.00 61.97 C
ATOM 304 C PRO A 49 46.712 81.781 112.998 1.00 62.50 C
ATOM 305 O PRO A 49 46.264 80.708 112.615 1.00 62.41 O
ATOM 306 CB PRO A 49 44.990 83.216 114.228 1.00 60.44 C
ATOM 307 CG PRO A 49 43.721 83.883 113.736 1.00 61.50 C
ATOM 308 CD PRO A 49 43.480 83.169 112.427 1.00 62.45 C
ATOM 309 N TYR A 50 47.951 81.942 113.458 1.00 63.80 N
ATOM 310 CA TYR A 50 48.972 80.889 113.606 1.00 64.78 C
ATOM 311 C TYR A 50 48.370 79.714 114.381 1.00 64.93 C
ATOM 312 O TYR A 50 48.348 78.564 113.928 1.00 64.38 O
ATOM 313 CB TYR A 50 50.119 81.437 114.434 1.00 67.75 C
ATOM 314 CG TYR A 50 51.464 80.799 114.246 1.00 69.43 C
ATOM 315 CD1 TYR A 50 52.213 80.378 115.346 1.00 69.86 C
ATOM 316 CD2 TYR A 50 52.021 80.656 112.971 1.00 68.56 C
ATOM 317 CE1 TYR A 50 53.499 79.829 115.180 1.00 70.95 C
ATOM 318 CE2 TYR A 50 53.306 80.107 112.796 1.00 68.83 C
ATOM 319 CZ TYR A 50 54.037 79.701 113.901 1.00 71.83 C
ATOM 320 OH TYR A 50 55.318 79.204 113.731 1.00 75.62 O
ATOM 321 N LEU A 51 47.883 80.070 115.573 1.00 64.74 N
ATOM 322 CA LEU A 51 47.275 79.140 116.523 1.00 63.85 C
ATOM 323 C LEU A 51 45.750 79.079 116.446 1.00 65.00 C
ATOM 324 O LEU A 51 45.066 79.903 115.807 1.00 65.10 O
ATOM 325 CB LEU A 51 47.704 79.509 117.958 1.00 61.28 C
ATOM 326 CG LEU A 51 49.235 79.530 118.089 1.00 58.25 C
ATOM 327 CD1 LEU A 51 49.616 79.891 119.531 1.00 56.91 C
ATOM 328 CD2 LEU A 51 49.806 78.145 117.687 1.00 53.95 C
ATOM 329 N ARG A 52 45.233 78.077 117.142 1.00 67.35 N
ATOM 330 CA ARG A 52 43.824 77.776 117.210 1.00 69.86 C
ATOM 331 C ARG A 52 43.196 78.156 118.550 1.00 72.27 C
ATOM 332 O ARG A 52 43.847 78.043 119.608 1.00 72.07 O
ATOM 333 CB ARG A 52 43.663 76.298 116.947 1.00 70.44 C
ATOM 334 CG ARG A 52 42.886 75.999 115.700 1.00 71.24 C
ATOM 335 CD ARG A 52 43.585 74.864 115.001 1.00 71.63 C
ATOM 336 NE ARG A 52 42.585 74.008 114.392 1.00 75.01 N
ATOM 337 CZ ARG A 52 42.761 73.320 113.268 1.00 77.03 C
ATOM 338 NH1 ARG A 52 43.905 73.375 112.585 1.00 73.71 N
ATOM 339 NH2 ARG A 52 41.762 72.547 112.829 1.00 80.05 N
ATOM 340 N SER A 53 41.926 78.599 118.546 1.00 74.95 N
ATOM 341 CA SER A 53 41.235 78.965 119.791 1.00 78.02 C
ATOM 342 C SER A 53 39.992 78.149 120.075 1.00 80.25 C
ATOM 343 O SER A 53 38.913 78.728 120.308 1.00 80.40 O
ATOM 344 CB SER A 53 40.805 80.444 119.819 1.00 77.22 C
ATOM 345 OG SER A 53 41.177 81.182 118.626 1.00 75.14 O
ATOM 346 N ALA A 54 40.135 76.816 120.025 1.00 82.12 N
ATOM 347 CA ALA A 54 39.117 75.792 120.278 1.00 83.73 C
ATOM 348 C ALA A 54 38.898 75.039 118.959 1.00 85.08 C
ATOM 349 O ALA A 54 39.929 74.912 118.225 1.00 85.59 O
ATOM 350 CB ALA A 54 37.772 76.411 120.746 1.00 82.88 C
ATOM 351 N SER A 73 49.672 68.552 112.537 1.00 57.02 N
ATOM 352 CA SER A 73 48.553 69.163 111.776 1.00 55.75 C
ATOM 353 C SER A 73 48.979 70.484 111.126 1.00 53.83 C
ATOM 354 O SER A 73 50.084 70.593 110.586 1.00 50.10 O
ATOM 355 CB SER A 73 47.364 69.409 112.709 1.00 60.64 C
ATOM 356 OG SER A 73 46.166 69.608 111.947 1.00 70.13 O
ATOM 357 N ALA A 74 48.110 71.493 111.175 1.00 52.84 N
ATOM 358 CA ALA A 74 48.456 72.776 110.563 1.00 54.44 C
ATOM 359 C ALA A 74 47.636 73.990 111.020 1.00 54.09 C
ATOM 360 O ALA A 74 46.526 73.862 111.547 1.00 52.69 O
ATOM 361 CB ALA A 74 48.348 72.644 109.051 1.00 55.42 C
ATOM 362 N SER A 75 48.196 75.174 110.805 1.00 54.19 N
ATOM 363 CA SER A 75 47.521 76.398 111.193 1.00 55.54 C
ATOM 364 C SER A 75 46.127 76.494 110.579 1.00 57.65 C
ATOM 365 O SER A 75 45.807 75.809 109.593 1.00 57.50 O
ATOM 366 CB SER A 75 48.325 77.612 110.752 1.00 55.33 C
ATOM 367 OG SER A 75 49.588 77.670 111.391 1.00 59.48 O
ATOM 368 N PRO A 76 45.259 77.332 111.174 1.00 58.57 N
ATOM 369 CA PRO A 76 43.925 77.457 110.593 1.00 58.60 C
ATOM 370 C PRO A 76 44.007 78.062 109.168 1.00 57.91 C
ATOM 371 O PRO A 76 44.919 78.816 108.818 1.00 56.00 O
ATOM 372 CB PRO A 76 43.168 78.314 111.611 1.00 57.91 C
ATOM 373 CG PRO A 76 44.255 79.084 112.303 1.00 62.57 C
ATOM 374 CD PRO A 76 45.350 78.058 112.453 1.00 58.24 C
ATOM 375 N CYS A 77 43.001 77.690 108.398 1.00 58.25 N
ATOM 376 CA CYS A 77 42.768 77.949 107.002 1.00 60.31 C
ATOM 377 C CYS A 77 41.488 78.720 106.805 1.00 58.89 C
ATOM 378 O CYS A 77 40.609 78.702 107.685 1.00 59.19 O
ATOM 379 CB CYS A 77 42.873 76.723 106.116 1.00 63.30 C
ATOM 380 SG CYS A 77 44.571 76.226 105.720 1.00 78.41 S
ATOM 381 N CYS A 78 41.368 79.424 105.677 1.00 57.09 N
ATOM 382 CA CYS A 78 40.156 80.191 105.392 1.00 54.39 C
ATOM 383 C CYS A 78 39.271 79.345 104.480 1.00 53.18 C
ATOM 384 O CYS A 78 39.594 79.155 103.308 1.00 54.53 O
ATOM 385 CB CYS A 78 40.529 81.490 104.705 1.00 51.85 C
ATOM 386 SG CYS A 78 39.135 82.612 104.411 1.00 53.81 S
ATOM 387 N VAL A 79 38.164 78.841 105.012 1.00 49.99 N
ATOM 388 CA VAL A 79 37.291 77.969 104.254 1.00 49.42 C
ATOM 389 C VAL A 79 35.876 78.416 104.415 1.00 49.24 C
ATOM 390 O VAL A 79 35.571 79.214 105.287 1.00 47.91 O
ATOM 391 CB VAL A 79 37.401 76.506 104.732 1.00 50.98 C
ATOM 392 CG1 VAL A 79 38.838 76.043 104.598 1.00 50.26 C
ATOM 393 CG2 VAL A 79 36.943 76.385 106.197 1.00 53.76 C
ATOM 394 N PRO A 80 34.980 77.913 103.559 1.00 50.80 N
ATOM 395 CA PRO A 80 33.575 78.313 103.654 1.00 52.12 C
ATOM 396 C PRO A 80 32.901 77.922 104.955 1.00 53.31 C
ATOM 397 O PRO A 80 33.209 76.895 105.558 1.00 52.90 O
ATOM 398 CB PRO A 80 32.938 77.679 102.415 1.00 49.52 C
ATOM 399 CG PRO A 80 33.851 76.567 102.074 1.00 51.94 C
ATOM 400 CD PRO A 80 35.215 77.052 102.386 1.00 50.13 C
ATOM 401 N GLN A 81 31.973 78.770 105.379 1.00 53.96 N
ATOM 402 CA GLN A 81 31.223 78.540 106.585 1.00 57.50 C
ATOM 403 C GLN A 81 29.786 78.325 106.103 1.00 56.94 C
ATOM 404 O GLN A 81 29.321 77.190 106.060 1.00 56.67 O
ATOM 405 CB GLN A 81 31.399 79.744 107.521 1.00 60.21 C
ATOM 406 CG GLN A 81 30.283 79.951 108.525 1.00 69.21 C
ATOM 407 CD GLN A 81 30.803 80.495 109.853 1.00 75.65 C
ATOM 408 OE1 GLN A 81 31.444 79.765 110.616 1.00 78.04 O
ATOM 409 NE2 GLN A 81 30.539 81.775 110.131 1.00 73.95 N
ATOM 410 N ASP A 82 29.096 79.379 105.734 1.00 58.03 N
ATOM 411 CA ASP A 82 27.749 79.177 105.226 1.00 60.62 C
ATOM 412 C ASP A 82 27.672 79.039 103.695 1.00 60.61 C
ATOM 413 O ASP A 82 28.094 79.931 102.956 1.00 58.84 O
ATOM 414 CB ASP A 82 26.830 80.320 105.660 1.00 64.15 C
ATOM 415 CG ASP A 82 26.563 80.322 107.169 1.00 76.70 C
ATOM 416 OD1 ASP A 82 26.028 79.302 107.677 1.00 80.14 O
ATOM 417 OD2 ASP A 82 26.880 81.338 107.844 1.00 78.50 O
ATOM 418 N LEU A 83 27.120 77.913 103.238 1.00 60.32 N
ATOM 419 CA LEU A 83 26.917 77.633 101.819 1.00 60.04 C
ATOM 420 C LEU A 83 25.421 77.751 101.518 1.00 61.29 C
ATOM 421 O LEU A 83 24.606 77.165 102.225 1.00 63.52 O
ATOM 422 CB LEU A 83 27.373 76.217 101.476 1.00 54.47 C
ATOM 423 CG LEU A 83 28.857 75.871 101.510 1.00 57.94 C
ATOM 424 CD1 LEU A 83 29.034 74.453 100.957 1.00 54.79 C
ATOM 425 CD2 LEU A 83 29.656 76.863 100.663 1.00 55.11 C
ATOM 426 N GLU A 84 25.050 78.497 100.483 1.00 60.40 N
ATOM 427 CA GLU A 84 23.644 78.641 100.122 1.00 58.30 C
ATOM 428 C GLU A 84 23.327 77.889 98.821 1.00 58.03 C
ATOM 429 O GLU A 84 24.222 77.483 98.063 1.00 56.41 O
ATOM 430 CB GLU A 84 23.284 80.123 99.952 1.00 59.43 C
ATOM 431 CG GLU A 84 23.356 80.954 101.230 1.00 66.51 C
ATOM 432 CD GLU A 84 22.669 80.271 102.417 1.00 74.97 C
ATOM 433 OE1 GLU A 84 21.501 79.850 102.266 1.00 75.95 O
ATOM 434 OE2 GLU A 84 23.293 80.156 103.503 1.00 78.42 O
ATOM 435 N PRO A 85 22.035 77.678 98.547 1.00 56.72 N
ATOM 436 CA PRO A 85 21.666 76.971 97.322 1.00 53.85 C
ATOM 437 C PRO A 85 21.433 77.944 96.176 1.00 50.12 C
ATOM 438 O PRO A 85 21.322 79.151 96.378 1.00 47.78 O
ATOM 439 CB PRO A 85 20.416 76.217 97.734 1.00 55.61 C
ATOM 440 CG PRO A 85 19.706 77.275 98.537 1.00 54.00 C
ATOM 441 CD PRO A 85 20.844 77.881 99.396 1.00 58.24 C
ATOM 442 N LEU A 86 21.359 77.387 94.975 1.00 48.41 N
ATOM 443 CA LEU A 86 21.115 78.156 93.768 1.00 46.62 C
ATOM 444 C LEU A 86 19.878 77.610 93.046 1.00 45.83 C
ATOM 445 O LEU A 86 19.703 76.401 92.883 1.00 45.53 O
ATOM 446 CB LEU A 86 22.326 78.067 92.827 1.00 44.72 C
ATOM 447 CG LEU A 86 22.135 78.833 91.517 1.00 44.25 C
ATOM 448 CD1 LEU A 86 22.299 80.314 91.805 1.00 44.08 C
ATOM 449 CD2 LEU A 86 23.135 78.369 90.464 1.00 40.63 C
ATOM 450 N THR A 87 19.024 78.514 92.608 1.00 44.89 N
ATOM 451 CA THR A 87 17.836 78.128 91.884 1.00 47.73 C
ATOM 452 C THR A 87 18.105 78.197 90.373 1.00 47.40 C
ATOM 453 O THR A 87 18.515 79.249 89.859 1.00 46.79 O
ATOM 454 CB THR A 87 16.662 79.073 92.220 1.00 50.90 C
ATOM 455 OG1 THR A 87 16.352 78.969 93.622 1.00 56.21 O
ATOM 456 CG2 THR A 87 15.429 78.702 91.377 1.00 50.46 C
ATOM 457 N ILE A 88 17.874 77.090 89.672 1.00 46.08 N
ATOM 458 CA ILE A 88 18.090 77.049 88.227 1.00 46.48 C
ATOM 459 C ILE A 88 16.842 76.569 87.502 1.00 48.28 C
ATOM 460 O ILE A 88 15.918 76.001 88.105 1.00 49.55 O
ATOM 461 CB ILE A 88 19.222 76.086 87.835 1.00 45.74 C
ATOM 462 CG1 ILE A 88 18.816 74.662 88.213 1.00 41.75 C
ATOM 463 CG2 ILE A 88 20.513 76.430 88.592 1.00 45.25 C
ATOM 464 CD1 ILE A 88 19.754 73.596 87.681 1.00 44.18 C
ATOM 465 N LEU A 89 16.826 76.801 86.199 1.00 46.18 N
ATOM 466 CA LEU A 89 15.736 76.394 85.342 1.00 44.55 C
ATOM 467 C LEU A 89 16.346 75.592 84.217 1.00 43.59 C
ATOM 468 O LEU A 89 17.312 76.031 83.585 1.00 43.28 O
ATOM 469 CB LEU A 89 15.034 77.602 84.747 1.00 44.92 C
ATOM 470 CG LEU A 89 14.144 77.310 83.531 1.00 51.42 C
ATOM 471 CD1 LEU A 89 12.890 76.613 83.985 1.00 53.67 C
ATOM 472 CD2 LEU A 89 13.762 78.624 82.837 1.00 54.27 C
ATOM 473 N TYR A 90 15.791 74.421 83.961 1.00 42.46 N
ATOM 474 CA TYR A 90 16.269 73.586 82.882 1.00 41.56 C
ATOM 475 C TYR A 90 15.116 72.766 82.312 1.00 42.73 C
ATOM 476 O TYR A 90 14.029 72.702 82.904 1.00 42.85 O
ATOM 477 CB TYR A 90 17.373 72.660 83.382 1.00 38.89 C
ATOM 478 CG TYR A 90 16.926 71.655 84.394 1.00 47.03 C
ATOM 479 CD1 TYR A 90 16.659 72.031 85.712 1.00 48.72 C
ATOM 480 CD2 TYR A 90 16.765 70.308 84.035 1.00 46.61 C
ATOM 481 CE1 TYR A 90 16.237 71.080 86.657 1.00 52.21 C
ATOM 482 CE2 TYR A 90 16.348 69.356 84.961 1.00 52.33 C
ATOM 483 CZ TYR A 90 16.087 69.747 86.270 1.00 54.27 C
ATOM 484 OH TYR A 90 15.690 68.785 87.171 1.00 57.50 O
ATOM 485 N TYR A 91 15.362 72.140 81.163 1.00 41.46 N
ATOM 486 CA TYR A 91 14.362 71.355 80.471 1.00 38.43 C
ATOM 487 C TYR A 91 14.603 69.866 80.436 1.00 38.35 C
ATOM 488 O TYR A 91 15.736 69.440 80.267 1.00 36.97 O
ATOM 489 CB TYR A 91 14.237 71.812 79.012 1.00 33.01 C
ATOM 490 CG TYR A 91 13.497 73.100 78.812 1.00 33.97 C
ATOM 491 CD1 TYR A 91 14.095 74.330 79.080 1.00 34.47 C
ATOM 492 CD2 TYR A 91 12.182 73.093 78.344 1.00 33.43 C
ATOM 493 CE1 TYR A 91 13.396 75.531 78.884 1.00 36.00 C
ATOM 494 CE2 TYR A 91 11.473 74.284 78.143 1.00 33.31 C
ATOM 495 CZ TYR A 91 12.074 75.494 78.409 1.00 37.47 C
ATOM 496 OH TYR A 91 11.359 76.660 78.190 1.00 38.83 O
ATOM 497 N VAL A 92 13.532 69.080 80.593 1.00 36.94 N
ATOM 498 CA VAL A 92 13.596 67.612 80.438 1.00 37.36 C
ATOM 499 C VAL A 92 12.503 67.444 79.355 1.00 37.54 C
ATOM 500 O VAL A 92 11.328 67.776 79.585 1.00 39.23 O
ATOM 501 CB VAL A 92 13.223 66.875 81.753 1.00 39.24 C
ATOM 502 CG1 VAL A 92 13.239 65.376 81.519 1.00 38.68 C
ATOM 503 CG2 VAL A 92 14.244 67.212 82.848 1.00 39.77 C
ATOM 504 N GLY A 93 12.886 66.953 78.173 1.00 35.78 N
ATOM 505 CA GLY A 93 11.947 66.913 77.066 1.00 33.16 C
ATOM 506 C GLY A 93 11.596 68.394 76.818 1.00 36.15 C
ATOM 507 O GLY A 93 12.453 69.296 77.009 1.00 33.05 O
ATOM 508 N ARG A 94 10.355 68.680 76.405 1.00 34.52 N
ATOM 509 CA ARG A 94 9.939 70.068 76.186 1.00 36.53 C
ATOM 510 C ARG A 94 9.385 70.709 77.471 1.00 35.14 C
ATOM 511 O ARG A 94 8.787 71.791 77.427 1.00 38.71 O
ATOM 512 CB ARG A 94 8.860 70.147 75.102 1.00 38.41 C
ATOM 513 CG ARG A 94 7.624 69.246 75.389 1.00 39.00 C
ATOM 514 CD ARG A 94 6.525 69.479 74.327 1.00 37.43 C
ATOM 515 NE ARG A 94 6.913 69.056 72.977 1.00 36.23 N
ATOM 516 CZ ARG A 94 6.905 67.802 72.516 1.00 38.59 C
ATOM 517 NH1 ARG A 94 6.522 66.797 73.294 1.00 39.26 N
ATOM 518 NH2 ARG A 94 7.275 67.542 71.260 1.00 32.99 N
ATOM 519 N THR A 95 9.591 70.059 78.605 1.00 36.48 N
ATOM 520 CA THR A 95 9.063 70.559 79.884 1.00 39.81 C
ATOM 521 C THR A 95 10.040 71.322 80.779 1.00 40.45 C
ATOM 522 O THR A 95 11.038 70.768 81.239 1.00 40.53 O
ATOM 523 CB THR A 95 8.499 69.386 80.742 1.00 40.34 C
ATOM 524 OG1 THR A 95 7.597 68.614 79.948 1.00 45.57 O
ATOM 525 CG2 THR A 95 7.793 69.920 81.986 1.00 41.00 C
ATOM 526 N PRO A 96 9.756 72.598 81.040 1.00 41.71 N
ATOM 527 CA PRO A 96 10.649 73.378 81.901 1.00 43.35 C
ATOM 528 C PRO A 96 10.525 72.924 83.349 1.00 45.98 C
ATOM 529 O PRO A 96 9.438 72.566 83.791 1.00 48.31 O
ATOM 530 CB PRO A 96 10.195 74.808 81.681 1.00 42.72 C
ATOM 531 CG PRO A 96 8.678 74.636 81.448 1.00 45.16 C
ATOM 532 CD PRO A 96 8.634 73.414 80.537 1.00 41.44 C
ATOM 533 N LYS A 97 11.634 72.932 84.073 1.00 46.14 N
ATOM 534 CA LYS A 97 11.663 72.551 85.469 1.00 47.85 C
ATOM 535 C LYS A 97 12.528 73.533 86.234 1.00 50.47 C
ATOM 536 O LYS A 97 13.673 73.825 85.846 1.00 48.80 O
ATOM 537 CB LYS A 97 12.221 71.142 85.625 1.00 48.63 C
ATOM 538 CG LYS A 97 11.270 70.095 85.077 1.00 56.35 C
ATOM 539 CD LYS A 97 11.689 68.683 85.409 1.00 59.75 C
ATOM 540 CE LYS A 97 10.668 67.683 84.827 1.00 64.63 C
ATOM 541 NZ LYS A 97 9.261 67.941 85.306 1.00 63.77 N
ATOM 542 N VAL A 98 11.966 74.053 87.322 1.00 51.33 N
ATOM 543 CA VAL A 98 12.656 75.001 88.178 1.00 52.43 C
ATOM 544 C VAL A 98 13.009 74.257 89.439 1.00 54.92 C
ATOM 545 O VAL A 98 12.133 73.704 90.101 1.00 57.04 O
ATOM 546 CB VAL A 98 11.766 76.185 88.551 1.00 51.36 C