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HEADER CYTOKINE 12-MAR-99 3BMP
TITLE HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (BONE MORPHOGENETIC PROTEIN 2 (BMP-2));
COMPND 3 CHAIN: A;
COMPND 4 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
KEYWDS CYTOKINE, BONE MORPHOGENETIC PROTEIN, CYSTIN-KNOT, TGFB-FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SCHEUFLER,W.SEBALD,M.HUELSMEYER
REVDAT 5 04-APR-18 3BMP 1 REMARK
REVDAT 4 13-JUL-11 3BMP 1 VERSN
REVDAT 3 24-FEB-09 3BMP 1 VERSN
REVDAT 2 01-APR-03 3BMP 1 JRNL
REVDAT 1 12-MAR-00 3BMP 0
SPRSDE 12-MAR-00 3BMP 2BMP
JRNL AUTH C.SCHEUFLER,W.SEBALD,M.HULSMEYER
JRNL TITL CRYSTAL STRUCTURE OF HUMAN BONE MORPHOGENETIC PROTEIN-2 AT
JRNL TITL 2 2.7 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 287 103 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10074410
JRNL DOI 10.1006/JMBI.1999.2590
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.RUPPERT,E.HOFFMANN,W.SEBALD
REMARK 1 TITL HUMAN BONE MORPHOGENETIC PROTEIN 2 CONTAINS A
REMARK 1 TITL 2 HEPARIN-BINDING SITE WHICH MODIFIES ITS BIOLOGICAL ACTIVITY
REMARK 1 REF EUR.J.BIOCHEM. V. 237 295 1996
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 4647
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) : 0.242
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 296
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.016
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 638
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 42
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.064
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 833
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.85000
REMARK 3 B22 (A**2) : 0.85000
REMARK 3 B33 (A**2) : -1.70000
REMARK 3 B12 (A**2) : 4.10000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.55
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.990
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) : 1.410 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.550 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.510 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.470 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 44.60
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 3BMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4647
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.12300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1TFG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION CONDITIONS: PROTEIN
REMARK 280 WAS CRYSTALLIZED FROM 100 MM LITHIUM SULFATE, 12% TERT-BUTANOL,
REMARK 280 50 MM CITRATE, PH 5.4
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 45.72000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 26.39645
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.91667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 45.72000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 26.39645
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.91667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 45.72000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 26.39645
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 35.91667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 45.72000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 26.39645
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 35.91667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 26.39645
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 35.91667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 45.72000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 26.39645
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 35.91667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 52.79291
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 71.83333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 52.79291
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 71.83333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 52.79291
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 71.83333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 52.79291
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 71.83333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 52.79291
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 71.83333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 52.79291
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 71.83333
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 NATIVE HOMODIMERIC FORM OF BMP-2 IS BUILT BY
REMARK 300 CRYSTALLOGRAPHIC SYMMETRY. THE MONOMERS ARE LINKED VIA A
REMARK 300 CYSTINE BRIDGE (CYS78 FROM BOTH SUBUNITS)
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 0.866025 0.000000 -45.72000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 26.39645
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 35.91667
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 GLN A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 HIS A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 LYS A 8
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 10 115.96 176.60
REMARK 500 SER A 12 -163.49 -64.12
REMARK 500 SER A 13 157.47 -39.98
REMARK 500 LEU A 19 109.21 -165.40
REMARK 500 PHE A 41 177.84 67.24
REMARK 500 PRO A 50 6.67 -62.54
REMARK 500 LEU A 51 88.17 39.68
REMARK 500 ASN A 71 118.53 -167.77
REMARK 500 ASP A 93 -175.53 -66.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 600
DBREF 3BMP A 1 114 UNP P12643 BMP2_HUMAN 283 396
SEQRES 1 A 114 GLN ALA LYS HIS LYS GLN ARG LYS ARG LEU LYS SER SER
SEQRES 2 A 114 CYS LYS ARG HIS PRO LEU TYR VAL ASP PHE SER ASP VAL
SEQRES 3 A 114 GLY TRP ASN ASP TRP ILE VAL ALA PRO PRO GLY TYR HIS
SEQRES 4 A 114 ALA PHE TYR CYS HIS GLY GLU CYS PRO PHE PRO LEU ALA
SEQRES 5 A 114 ASP HIS LEU ASN SER THR ASN HIS ALA ILE VAL GLN THR
SEQRES 6 A 114 LEU VAL ASN SER VAL ASN SER LYS ILE PRO LYS ALA CYS
SEQRES 7 A 114 CYS VAL PRO THR GLU LEU SER ALA ILE SER MET LEU TYR
SEQRES 8 A 114 LEU ASP GLU ASN GLU LYS VAL VAL LEU LYS ASN TYR GLN
SEQRES 9 A 114 ASP MET VAL VAL GLU GLY CYS GLY CYS ARG
HET MPD A 600 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 MPD C6 H14 O2
FORMUL 3 HOH *33(H2 O)
HELIX 1 1 ASN A 59 VAL A 70 1 12
SHEET 1 A 2 LYS A 15 HIS A 17 0
SHEET 2 A 2 TYR A 42 HIS A 44 -1 N HIS A 44 O LYS A 15
SHEET 1 B 2 TYR A 20 ASP A 22 0
SHEET 2 B 2 GLY A 37 HIS A 39 -1 N TYR A 38 O VAL A 21
SHEET 1 C 2 ILE A 87 LEU A 92 0
SHEET 2 C 2 VAL A 98 TYR A 103 -1 N TYR A 103 O ILE A 87
SHEET 1 D 2 CYS A 79 GLU A 83 0
SHEET 2 D 2 GLY A 110 CYS A 113 -1 N GLY A 112 O VAL A 80
SSBOND 1 CYS A 14 CYS A 79 1555 1555 1.96
SSBOND 2 CYS A 43 CYS A 111 1555 1555 2.03
SSBOND 3 CYS A 47 CYS A 113 1555 1555 2.03
SSBOND 4 CYS A 78 CYS A 78 1555 10455 1.98
CISPEP 1 ALA A 34 PRO A 35 0 0.02
SITE 1 AC1 5 TRP A 28 ASN A 59 ILE A 62 TYR A 103
SITE 2 AC1 5 HOH A 332
CRYST1 91.440 91.440 107.750 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 0.010936 0.006314 0.000000 0.00000
SCALE2 0.000000 0.012628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009281 0.00000
ATOM 1 N ARG A 9 -3.401 42.188 9.100 1.00 85.11 N
ATOM 2 CA ARG A 9 -4.461 41.378 9.771 1.00 84.76 C
ATOM 3 C ARG A 9 -5.606 42.255 10.288 1.00 83.82 C
ATOM 4 O ARG A 9 -5.605 42.678 11.446 1.00 83.96 O
ATOM 5 CB ARG A 9 -3.848 40.573 10.926 1.00 85.57 C
ATOM 6 CG ARG A 9 -3.125 41.413 11.979 1.00 86.89 C
ATOM 7 CD ARG A 9 -2.493 40.528 13.049 1.00 88.20 C
ATOM 8 NE ARG A 9 -1.923 41.289 14.162 1.00 88.92 N
ATOM 9 CZ ARG A 9 -2.635 41.993 15.039 1.00 89.17 C
ATOM 10 NH1 ARG A 9 -3.957 42.043 14.942 1.00 89.49 N
ATOM 11 NH2 ARG A 9 -2.024 42.651 16.016 1.00 89.25 N
ATOM 12 N LEU A 10 -6.583 42.522 9.423 1.00 82.48 N
ATOM 13 CA LEU A 10 -7.735 43.347 9.784 1.00 81.21 C
ATOM 14 C LEU A 10 -8.646 43.550 8.571 1.00 80.23 C
ATOM 15 O LEU A 10 -8.241 44.163 7.582 1.00 80.45 O
ATOM 16 CB LEU A 10 -7.263 44.709 10.301 1.00 81.39 C
ATOM 17 CG LEU A 10 -8.312 45.627 10.929 1.00 81.31 C
ATOM 18 CD1 LEU A 10 -8.827 44.996 12.216 1.00 81.15 C
ATOM 19 CD2 LEU A 10 -7.698 46.993 11.209 1.00 81.18 C
ATOM 20 N LYS A 11 -9.873 43.039 8.646 1.00 78.75 N
ATOM 21 CA LYS A 11 -10.817 43.176 7.537 1.00 76.90 C
ATOM 22 C LYS A 11 -12.288 43.058 7.975 1.00 74.81 C
ATOM 23 O LYS A 11 -12.599 42.983 9.167 1.00 75.11 O
ATOM 24 CB LYS A 11 -10.496 42.148 6.446 1.00 77.72 C
ATOM 25 CG LYS A 11 -10.305 40.725 6.965 1.00 78.61 C
ATOM 26 CD LYS A 11 -9.438 39.881 6.030 1.00 78.80 C
ATOM 27 CE LYS A 11 -8.109 40.558 5.696 1.00 78.52 C
ATOM 28 NZ LYS A 11 -7.274 39.770 4.782 1.00 78.85 N
ATOM 29 N SER A 12 -13.163 43.058 6.963 1.00 71.41 N
ATOM 30 CA SER A 12 -14.632 43.028 7.163 1.00 67.85 C
ATOM 31 C SER A 12 -15.085 41.721 7.838 1.00 64.67 C
ATOM 32 O SER A 12 -14.286 40.985 8.421 1.00 64.45 O
ATOM 33 CB SER A 12 -15.364 43.211 5.827 1.00 68.60 C
ATOM 34 OG SER A 12 -15.121 42.112 4.972 1.00 69.38 O
ATOM 35 N SER A 13 -16.378 41.464 7.744 1.00 60.44 N
ATOM 36 CA SER A 13 -17.023 40.304 8.402 1.00 56.05 C
ATOM 37 C SER A 13 -16.173 39.016 8.339 1.00 52.71 C
ATOM 38 O SER A 13 -15.298 38.857 7.474 1.00 52.05 O
ATOM 39 CB SER A 13 -18.377 40.010 7.757 1.00 56.63 C
ATOM 40 OG SER A 13 -18.201 39.516 6.440 1.00 56.46 O
ATOM 41 N CYS A 14 -16.489 38.142 9.293 1.00 48.30 N
ATOM 42 CA CYS A 14 -15.867 36.812 9.446 1.00 43.20 C
ATOM 43 C CYS A 14 -16.057 36.045 8.148 1.00 41.91 C
ATOM 44 O CYS A 14 -17.169 35.961 7.626 1.00 41.24 O
ATOM 45 CB CYS A 14 -16.556 36.083 10.605 1.00 39.73 C
ATOM 46 SG CYS A 14 -15.863 34.395 10.948 1.00 32.56 S
ATOM 47 N LYS A 15 -14.970 35.494 7.622 1.00 40.73 N
ATOM 48 CA LYS A 15 -15.048 34.729 6.386 1.00 39.80 C
ATOM 49 C LYS A 15 -13.836 33.822 6.218 1.00 38.26 C
ATOM 50 O LYS A 15 -12.848 33.939 6.950 1.00 36.56 O
ATOM 51 CB LYS A 15 -15.183 35.676 5.187 1.00 40.62 C
ATOM 52 CG LYS A 15 -13.957 36.539 4.909 1.00 42.68 C
ATOM 53 CD LYS A 15 -14.323 37.877 4.261 1.00 44.77 C
ATOM 54 CE LYS A 15 -15.091 37.703 2.953 1.00 45.98 C
ATOM 55 NZ LYS A 15 -16.442 37.093 3.144 1.00 46.50 N
ATOM 56 N ARG A 16 -13.929 32.906 5.259 1.00 37.60 N
ATOM 57 CA ARG A 16 -12.843 31.977 4.988 1.00 37.66 C
ATOM 58 C ARG A 16 -11.862 32.555 3.981 1.00 39.44 C
ATOM 59 O ARG A 16 -12.258 33.129 2.962 1.00 39.70 O
ATOM 60 CB ARG A 16 -13.385 30.657 4.454 1.00 34.99 C
ATOM 61 CG ARG A 16 -12.330 29.593 4.345 1.00 31.82 C
ATOM 62 CD ARG A 16 -12.912 28.268 3.902 1.00 30.30 C
ATOM 63 NE ARG A 16 -13.270 28.269 2.489 1.00 28.87 N
ATOM 64 CZ ARG A 16 -13.524 27.174 1.780 1.00 28.27 C
ATOM 65 NH1 ARG A 16 -13.460 25.973 2.345 1.00 28.90 N
ATOM 66 NH2 ARG A 16 -13.852 27.280 0.503 1.00 28.24 N
ATOM 67 N HIS A 17 -10.577 32.393 4.280 1.00 40.61 N
ATOM 68 CA HIS A 17 -9.508 32.886 3.428 1.00 41.41 C
ATOM 69 C HIS A 17 -8.651 31.734 2.924 1.00 41.18 C
ATOM 70 O HIS A 17 -8.504 30.717 3.602 1.00 41.87 O
ATOM 71 CB HIS A 17 -8.656 33.883 4.207 1.00 42.73 C
ATOM 72 CG HIS A 17 -9.426 35.073 4.684 1.00 45.55 C
ATOM 73 ND1 HIS A 17 -10.345 35.003 5.709 1.00 46.33 N
ATOM 74 CD2 HIS A 17 -9.451 36.354 4.244 1.00 46.53 C
ATOM 75 CE1 HIS A 17 -10.903 36.188 5.880 1.00 46.82 C
ATOM 76 NE2 HIS A 17 -10.379 37.025 5.003 1.00 47.35 N
ATOM 77 N PRO A 18 -8.087 31.870 1.715 1.00 40.65 N
ATOM 78 CA PRO A 18 -7.250 30.806 1.157 1.00 39.51 C
ATOM 79 C PRO A 18 -5.927 30.693 1.892 1.00 38.45 C
ATOM 80 O PRO A 18 -5.385 31.692 2.371 1.00 38.47 O
ATOM 81 CB PRO A 18 -7.057 31.238 -0.296 1.00 39.76 C
ATOM 82 CG PRO A 18 -8.274 32.055 -0.581 1.00 40.57 C
ATOM 83 CD PRO A 18 -8.389 32.876 0.684 1.00 40.86 C
ATOM 84 N LEU A 19 -5.419 29.469 1.983 1.00 36.91 N
ATOM 85 CA LEU A 19 -4.149 29.213 2.642 1.00 35.69 C
ATOM 86 C LEU A 19 -3.626 27.825 2.304 1.00 35.56 C
ATOM 87 O LEU A 19 -4.179 26.808 2.731 1.00 35.90 O
ATOM 88 CB LEU A 19 -4.283 29.355 4.158 1.00 34.55 C
ATOM 89 CG LEU A 19 -3.028 28.947 4.937 1.00 34.15 C
ATOM 90 CD1 LEU A 19 -1.827 29.763 4.481 1.00 32.66 C
ATOM 91 CD2 LEU A 19 -3.277 29.130 6.418 1.00 33.40 C
ATOM 92 N TYR A 20 -2.566 27.788 1.511 1.00 34.50 N
ATOM 93 CA TYR A 20 -1.970 26.523 1.141 1.00 33.68 C
ATOM 94 C TYR A 20 -0.841 26.324 2.124 1.00 33.39 C
ATOM 95 O TYR A 20 -0.114 27.267 2.432 1.00 34.62 O
ATOM 96 CB TYR A 20 -1.404 26.574 -0.275 1.00 32.39 C
ATOM 97 CG TYR A 20 -0.687 25.301 -0.644 1.00 32.10 C
ATOM 98 CD1 TYR A 20 -1.389 24.200 -1.125 1.00 30.46 C
ATOM 99 CD2 TYR A 20 0.690 25.170 -0.436 1.00 31.85 C
ATOM 100 CE1 TYR A 20 -0.746 23.001 -1.383 1.00 30.81 C
ATOM 101 CE2 TYR A 20 1.342 23.977 -0.685 1.00 31.58 C
ATOM 102 CZ TYR A 20 0.620 22.891 -1.158 1.00 31.91 C
ATOM 103 OH TYR A 20 1.259 21.688 -1.386 1.00 31.93 O
ATOM 104 N VAL A 21 -0.690 25.112 2.631 1.00 32.29 N
ATOM 105 CA VAL A 21 0.378 24.865 3.574 1.00 32.42 C
ATOM 106 C VAL A 21 1.374 23.853 3.050 1.00 33.94 C
ATOM 107 O VAL A 21 1.039 22.688 2.793 1.00 34.03 O
ATOM 108 CB VAL A 21 -0.149 24.360 4.910 1.00 31.74 C
ATOM 109 CG1 VAL A 21 1.003 24.236 5.892 1.00 30.35 C
ATOM 110 CG2 VAL A 21 -1.213 25.305 5.434 1.00 31.81 C
ATOM 111 N ASP A 22 2.606 24.318 2.897 1.00 34.06 N
ATOM 112 CA ASP A 22 3.686 23.486 2.420 1.00 33.24 C
ATOM 113 C ASP A 22 4.400 22.918 3.635 1.00 32.91 C
ATOM 114 O ASP A 22 4.983 23.656 4.429 1.00 33.45 O
ATOM 115 CB ASP A 22 4.639 24.322 1.579 1.00 33.87 C
ATOM 116 CG ASP A 22 5.786 23.516 1.043 1.00 34.95 C
ATOM 117 OD1 ASP A 22 6.709 23.203 1.828 1.00 34.79 O
ATOM 118 OD2 ASP A 22 5.749 23.186 -0.163 1.00 35.74 O
ATOM 119 N PHE A 23 4.346 21.599 3.776 1.00 32.24 N
ATOM 120 CA PHE A 23 4.958 20.906 4.904 1.00 31.26 C
ATOM 121 C PHE A 23 6.452 21.138 5.083 1.00 32.12 C
ATOM 122 O PHE A 23 6.989 20.930 6.171 1.00 30.43 O
ATOM 123 CB PHE A 23 4.655 19.414 4.787 1.00 30.34 C
ATOM 124 CG PHE A 23 3.192 19.088 4.931 1.00 30.59 C
ATOM 125 CD1 PHE A 23 2.424 19.694 5.935 1.00 30.36 C
ATOM 126 CD2 PHE A 23 2.573 18.194 4.064 1.00 29.00 C
ATOM 127 CE1 PHE A 23 1.064 19.417 6.072 1.00 28.80 C
ATOM 128 CE2 PHE A 23 1.217 17.910 4.189 1.00 29.66 C
ATOM 129 CZ PHE A 23 0.459 18.525 5.198 1.00 29.98 C
ATOM 130 N SER A 24 7.123 21.576 4.021 1.00 34.48 N
ATOM 131 CA SER A 24 8.556 21.841 4.084 1.00 36.46 C
ATOM 132 C SER A 24 8.829 23.183 4.745 1.00 37.90 C
ATOM 133 O SER A 24 9.853 23.352 5.414 1.00 38.49 O
ATOM 134 CB SER A 24 9.168 21.823 2.686 1.00 37.27 C
ATOM 135 OG SER A 24 9.126 20.517 2.138 1.00 39.46 O
ATOM 136 N ASP A 25 7.915 24.133 4.565 1.00 38.43 N
ATOM 137 CA ASP A 25 8.073 25.448 5.170 1.00 39.75 C
ATOM 138 C ASP A 25 7.873 25.387 6.674 1.00 39.61 C
ATOM 139 O ASP A 25 8.504 26.136 7.418 1.00 40.42 O
ATOM 140 CB ASP A 25 7.083 26.449 4.574 1.00 41.43 C
ATOM 141 CG ASP A 25 7.323 26.689 3.106 1.00 44.30 C
ATOM 142 OD1 ASP A 25 8.503 26.881 2.729 1.00 45.72 O
ATOM 143 OD2 ASP A 25 6.340 26.690 2.331 1.00 45.56 O
ATOM 144 N VAL A 26 6.989 24.504 7.123 1.00 39.00 N
ATOM 145 CA VAL A 26 6.733 24.375 8.550 1.00 38.81 C
ATOM 146 C VAL A 26 7.533 23.226 9.140 1.00 38.26 C
ATOM 147 O VAL A 26 7.315 22.825 10.285 1.00 38.72 O
ATOM 148 CB VAL A 26 5.225 24.172 8.844 1.00 39.67 C
ATOM 149 CG1 VAL A 26 4.432 25.284 8.185 1.00 40.00 C
ATOM 150 CG2 VAL A 26 4.755 22.802 8.361 1.00 39.09 C
ATOM 151 N GLY A 27 8.451 22.696 8.338 1.00 37.26 N
ATOM 152 CA GLY A 27 9.309 21.614 8.785 1.00 36.59 C
ATOM 153 C GLY A 27 8.629 20.319 9.170 1.00 36.58 C
ATOM 154 O GLY A 27 8.954 19.730 10.205 1.00 36.32 O
ATOM 155 N TRP A 28 7.693 19.870 8.336 1.00 36.44 N
ATOM 156 CA TRP A 28 6.971 18.625 8.586 1.00 35.78 C
ATOM 157 C TRP A 28 7.229 17.572 7.516 1.00 35.43 C
ATOM 158 O TRP A 28 6.908 16.399 7.697 1.00 35.20 O
ATOM 159 CB TRP A 28 5.470 18.889 8.684 1.00 34.47 C
ATOM 160 CG TRP A 28 5.028 19.281 10.047 1.00 34.49 C
ATOM 161 CD1 TRP A 28 5.820 19.492 11.135 1.00 34.43 C
ATOM 162 CD2 TRP A 28 3.682 19.518 10.477 1.00 34.62 C
ATOM 163 NE1 TRP A 28 5.053 19.844 12.218 1.00 35.17 N
ATOM 164 CE2 TRP A 28 3.736 19.869 11.842 1.00 34.35 C
ATOM 165 CE3 TRP A 28 2.434 19.470 9.840 1.00 33.89 C
ATOM 166 CZ2 TRP A 28 2.592 20.168 12.583 1.00 33.83 C
ATOM 167 CZ3 TRP A 28 1.297 19.767 10.574 1.00 32.79 C
ATOM 168 CH2 TRP A 28 1.385 20.112 11.933 1.00 34.19 C
ATOM 169 N ASN A 29 7.811 17.991 6.401 1.00 35.66 N
ATOM 170 CA ASN A 29 8.095 17.066 5.314 1.00 35.88 C
ATOM 171 C ASN A 29 9.053 15.980 5.794 1.00 35.27 C
ATOM 172 O ASN A 29 9.252 14.967 5.121 1.00 35.23 O
ATOM 173 CB ASN A 29 8.680 17.817 4.110 1.00 36.39 C
ATOM 174 CG ASN A 29 9.924 18.602 4.463 1.00 38.27 C
ATOM 175 OD1 ASN A 29 9.917 19.425 5.379 1.00 39.74 O
ATOM 176 ND2 ASN A 29 11.003 18.353 3.735 1.00 38.98 N
ATOM 177 N ASP A 30 9.634 16.182 6.971 1.00 34.80 N
ATOM 178 CA ASP A 30 10.548 15.188 7.498 1.00 35.15 C
ATOM 179 C ASP A 30 9.776 13.931 7.883 1.00 33.53 C
ATOM 180 O ASP A 30 10.239 12.823 7.622 1.00 34.69 O
ATOM 181 CB ASP A 30 11.359 15.747 8.695 1.00 37.73 C
ATOM 182 CG ASP A 30 10.478 16.252 9.849 1.00 40.74 C
ATOM 183 OD1 ASP A 30 9.572 17.091 9.604 1.00 40.95 O
ATOM 184 OD2 ASP A 30 10.707 15.817 11.008 1.00 39.73 O
ATOM 185 N TRP A 31 8.595 14.091 8.477 1.00 30.82 N
ATOM 186 CA TRP A 31 7.811 12.923 8.877 1.00 29.66 C
ATOM 187 C TRP A 31 6.604 12.648 7.971 1.00 27.19 C
ATOM 188 O TRP A 31 6.106 11.524 7.921 1.00 26.37 O
ATOM 189 CB TRP A 31 7.350 13.039 10.347 1.00 30.17 C
ATOM 190 CG TRP A 31 6.402 14.169 10.623 1.00 31.18 C
ATOM 191 CD1 TRP A 31 6.700 15.500 10.650 1.00 32.02 C
ATOM 192 CD2 TRP A 31 4.989 14.070 10.859 1.00 31.32 C
ATOM 193 NE1 TRP A 31 5.563 16.239 10.884 1.00 32.83 N
ATOM 194 CE2 TRP A 31 4.498 15.387 11.016 1.00 32.23 C
ATOM 195 CE3 TRP A 31 4.091 12.998 10.950 1.00 31.03 C
ATOM 196 CZ2 TRP A 31 3.144 15.661 11.259 1.00 31.37 C
ATOM 197 CZ3 TRP A 31 2.744 13.271 11.190 1.00 30.14 C
ATOM 198 CH2 TRP A 31 2.287 14.594 11.341 1.00 30.72 C
ATOM 199 N ILE A 32 6.135 13.663 7.254 1.00 24.18 N
ATOM 200 CA ILE A 32 5.000 13.457 6.372 1.00 22.42 C
ATOM 201 C ILE A 32 5.471 13.173 4.962 1.00 22.65 C
ATOM 202 O ILE A 32 6.008 14.047 4.288 1.00 22.93 O
ATOM 203 CB ILE A 32 4.054 14.672 6.324 1.00 20.89 C
ATOM 204 CG1 ILE A 32 3.475 14.947 7.705 1.00 18.86 C
ATOM 205 CG2 ILE A 32 2.918 14.401 5.352 1.00 17.69 C
ATOM 206 CD1 ILE A 32 2.524 16.103 7.700 1.00 18.30 C
ATOM 207 N VAL A 33 5.249 11.941 4.524 1.00 22.49 N
ATOM 208 CA VAL A 33 5.635 11.501 3.201 1.00 21.53 C
ATOM 209 C VAL A 33 4.762 12.173 2.147 1.00 21.71 C
ATOM 210 O VAL A 33 5.261 12.715 1.168 1.00 20.75 O
ATOM 211 CB VAL A 33 5.493 9.965 3.100 1.00 22.43 C
ATOM 212 CG1 VAL A 33 5.978 9.476 1.748 1.00 22.54 C
ATOM 213 CG2 VAL A 33 6.264 9.303 4.230 1.00 21.17 C
ATOM 214 N ALA A 34 3.450 12.136 2.351 1.00 22.91 N
ATOM 215 CA ALA A 34 2.516 12.735 1.399 1.00 23.03 C
ATOM 216 C ALA A 34 1.219 13.131 2.095 1.00 24.01 C
ATOM 217 O ALA A 34 0.810 12.506 3.079 1.00 25.20 O
ATOM 218 CB ALA A 34 2.223 11.759 0.267 1.00 19.82 C
ATOM 219 N PRO A 35 0.547 14.174 1.591 1.00 23.78 N
ATOM 220 CA PRO A 35 0.939 14.973 0.432 1.00 22.81 C
ATOM 221 C PRO A 35 2.100 15.882 0.795 1.00 22.78 C
ATOM 222 O PRO A 35 2.635 15.807 1.903 1.00 21.86 O
ATOM 223 CB PRO A 35 -0.321 15.767 0.139 1.00 23.38 C
ATOM 224 CG PRO A 35 -0.795 16.092 1.521 1.00 24.09 C
ATOM 225 CD PRO A 35 -0.650 14.750 2.234 1.00 24.44 C
ATOM 226 N PRO A 36 2.521 16.742 -0.145 1.00 22.70 N
ATOM 227 CA PRO A 36 3.629 17.653 0.147 1.00 23.28 C
ATOM 228 C PRO A 36 3.085 18.849 0.922 1.00 23.57 C
ATOM 229 O PRO A 36 3.804 19.511 1.671 1.00 25.17 O
ATOM 230 CB PRO A 36 4.148 18.028 -1.243 1.00 21.70 C
ATOM 231 CG PRO A 36 2.921 17.961 -2.088 1.00 22.31 C
ATOM 232 CD PRO A 36 2.206 16.730 -1.586 1.00 21.95 C
ATOM 233 N GLY A 37 1.798 19.111 0.739 1.00 22.42 N
ATOM 234 CA GLY A 37 1.172 20.217 1.429 1.00 24.42 C
ATOM 235 C GLY A 37 -0.315 20.135 1.201 1.00 24.66 C
ATOM 236 O GLY A 37 -0.800 19.105 0.722 1.00 25.59 O
ATOM 237 N TYR A 38 -1.054 21.188 1.541 1.00 23.45 N
ATOM 238 CA TYR A 38 -2.487 21.136 1.309 1.00 23.86 C
ATOM 239 C TYR A 38 -3.207 22.454 1.507 1.00 23.99 C
ATOM 240 O TYR A 38 -2.715 23.360 2.182 1.00 24.17 O
ATOM 241 CB TYR A 38 -3.132 20.046 2.187 1.00 24.61 C
ATOM 242 CG TYR A 38 -3.409 20.450 3.616 1.00 24.05 C
ATOM 243 CD1 TYR A 38 -2.375 20.537 4.549 1.00 23.95 C
ATOM 244 CD2 TYR A 38 -4.706 20.757 4.036 1.00 23.22 C
ATOM 245 CE1 TYR A 38 -2.626 20.924 5.865 1.00 23.89 C
ATOM 246 CE2 TYR A 38 -4.968 21.141 5.350 1.00 22.60 C
ATOM 247 CZ TYR A 38 -3.923 21.226 6.259 1.00 22.73 C
ATOM 248 OH TYR A 38 -4.158 21.636 7.550 1.00 21.96 O
ATOM 249 N HIS A 39 -4.377 22.553 0.888 1.00 24.35 N
ATOM 250 CA HIS A 39 -5.198 23.746 0.991 1.00 25.88 C
ATOM 251 C HIS A 39 -6.012 23.688 2.275 1.00 25.12 C
ATOM 252 O HIS A 39 -7.081 23.081 2.325 1.00 23.53 O
ATOM 253 CB HIS A 39 -6.113 23.873 -0.233 1.00 28.03 C
ATOM 254 CG HIS A 39 -5.384 24.291 -1.471 1.00 31.54 C
ATOM 255 ND1 HIS A 39 -4.830 23.386 -2.350 1.00 32.76 N
ATOM 256 CD2 HIS A 39 -5.015 25.519 -1.912 1.00 32.28 C
ATOM 257 CE1 HIS A 39 -4.147 24.038 -3.275 1.00 33.86 C
ATOM 258 NE2 HIS A 39 -4.242 25.333 -3.030 1.00 33.15 N
ATOM 259 N ALA A 40 -5.483 24.334 3.308 1.00 23.97 N
ATOM 260 CA ALA A 40 -6.114 24.352 4.609 1.00 24.74 C
ATOM 261 C ALA A 40 -7.118 25.489 4.826 1.00 25.93 C
ATOM 262 O ALA A 40 -8.141 25.293 5.492 1.00 26.83 O
ATOM 263 CB ALA A 40 -5.031 24.399 5.691 1.00 22.98 C
ATOM 264 N PHE A 41 -6.837 26.661 4.255 1.00 25.82 N
ATOM 265 CA PHE A 41 -7.676 27.847 4.437 1.00 25.67 C
ATOM 266 C PHE A 41 -7.553 28.263 5.898 1.00 26.69 C
ATOM 267 O PHE A 41 -6.874 27.604 6.690 1.00 24.48 O
ATOM 268 CB PHE A 41 -9.161 27.577 4.167 1.00 25.37 C
ATOM 269 CG PHE A 41 -9.461 27.070 2.791 1.00 26.44 C
ATOM 270 CD1 PHE A 41 -9.275 25.727 2.473 1.00 26.11 C
ATOM 271 CD2 PHE A 41 -9.958 27.932 1.814 1.00 26.53 C
ATOM 272 CE1 PHE A 41 -9.582 25.246 1.199 1.00 26.11 C
ATOM 273 CE2 PHE A 41 -10.267 27.463 0.543 1.00 26.10 C
ATOM 274 CZ PHE A 41 -10.079 26.114 0.235 1.00 26.43 C
ATOM 275 N TYR A 42 -8.218 29.361 6.246 1.00 28.40 N
ATOM 276 CA TYR A 42 -8.230 29.862 7.612 1.00 30.00 C
ATOM 277 C TYR A 42 -9.351 30.867 7.750 1.00 30.89 C
ATOM 278 O TYR A 42 -9.919 31.314 6.759 1.00 31.69 O
ATOM 279 CB TYR A 42 -6.887 30.497 7.992 1.00 32.21 C
ATOM 280 CG TYR A 42 -6.596 31.873 7.422 1.00 35.30 C
ATOM 281 CD1 TYR A 42 -6.195 32.032 6.092 1.00 36.46 C
ATOM 282 CD2 TYR A 42 -6.639 33.008 8.238 1.00 35.70 C
ATOM 283 CE1 TYR A 42 -5.835 33.283 5.590 1.00 37.81 C
ATOM 284 CE2 TYR A 42 -6.279 34.267 7.749 1.00 37.21 C
ATOM 285 CZ TYR A 42 -5.875 34.397 6.424 1.00 38.63 C
ATOM 286 OH TYR A 42 -5.496 35.632 5.938 1.00 38.39 O
ATOM 287 N CYS A 43 -9.684 31.210 8.985 1.00 31.70 N
ATOM 288 CA CYS A 43 -10.761 32.149 9.227 1.00 31.79 C
ATOM 289 C CYS A 43 -10.269 33.464 9.826 1.00 33.42 C
ATOM 290 O CYS A 43 -9.322 33.499 10.616 1.00 33.36 O
ATOM 291 CB CYS A 43 -11.783 31.515 10.159 1.00 30.44 C
ATOM 292 SG CYS A 43 -12.523 29.961 9.566 1.00 27.91 S
ATOM 293 N HIS A 44 -10.925 34.548 9.444 1.00 34.68 N
ATOM 294 CA HIS A 44 -10.566 35.860 9.948 1.00 36.02 C
ATOM 295 C HIS A 44 -11.660 36.848 9.555 1.00 36.97 C
ATOM 296 O HIS A 44 -12.378 36.649 8.570 1.00 36.16 O
ATOM 297 CB HIS A 44 -9.201 36.276 9.385 1.00 37.45 C
ATOM 298 CG HIS A 44 -8.694 37.577 9.925 1.00 38.70 C
ATOM 299 ND1 HIS A 44 -8.954 38.788 9.316 1.00 37.64 N
ATOM 300 CD2 HIS A 44 -7.972 37.857 11.036 1.00 37.75 C
ATOM 301 CE1 HIS A 44 -8.413 39.757 10.030 1.00 38.47 C
ATOM 302 NE2 HIS A 44 -7.812 39.220 11.079 1.00 38.94 N
ATOM 303 N GLY A 45 -11.795 37.910 10.337 1.00 38.26 N
ATOM 304 CA GLY A 45 -12.829 38.886 10.057 1.00 40.27 C
ATOM 305 C GLY A 45 -13.628 39.147 11.314 1.00 41.77 C
ATOM 306 O GLY A 45 -13.990 38.227 12.047 1.00 41.91 O
ATOM 307 N GLU A 46 -13.900 40.418 11.567 1.00 43.43 N
ATOM 308 CA GLU A 46 -14.641 40.827 12.746 1.00 44.64 C
ATOM 309 C GLU A 46 -16.043 40.233 12.828 1.00 44.61 C
ATOM 310 O GLU A 46 -16.686 39.997 11.804 1.00 43.74 O
ATOM 311 CB GLU A 46 -14.734 42.351 12.774 1.00 46.15 C
ATOM 312 CG GLU A 46 -15.658 42.909 13.842 1.00 48.23 C
ATOM 313 CD GLU A 46 -15.809 44.406 13.735 1.00 48.95 C
ATOM 314 OE1 GLU A 46 -16.220 44.883 12.657 1.00 49.11 O
ATOM 315 OE2 GLU A 46 -15.512 45.105 14.727 1.00 50.75 O
ATOM 316 N CYS A 47 -16.494 39.988 14.061 1.00 45.34 N
ATOM 317 CA CYS A 47 -17.835 39.466 14.341 1.00 46.69 C
ATOM 318 C CYS A 47 -18.660 40.662 14.832 1.00 50.48 C
ATOM 319 O CYS A 47 -18.701 40.957 16.032 1.00 51.06 O
ATOM 320 CB CYS A 47 -17.775 38.383 15.420 1.00 42.28 C
ATOM 321 SG CYS A 47 -16.989 36.845 14.845 1.00 37.55 S
ATOM 322 N PRO A 48 -19.320 41.370 13.899 1.00 53.69 N
ATOM 323 CA PRO A 48 -20.152 42.551 14.153 1.00 57.15 C
ATOM 324 C PRO A 48 -21.294 42.376 15.145 1.00 60.08 C
ATOM 325 O PRO A 48 -21.789 41.267 15.353 1.00 60.13 O
ATOM 326 CB PRO A 48 -20.652 42.921 12.759 1.00 56.74 C
ATOM 327 CG PRO A 48 -20.763 41.589 12.093 1.00 55.58 C
ATOM 328 CD PRO A 48 -19.463 40.936 12.498 1.00 54.33 C
ATOM 329 N PHE A 49 -21.704 43.488 15.752 1.00 63.47 N
ATOM 330 CA PHE A 49 -22.788 43.472 16.724 1.00 67.14 C
ATOM 331 C PHE A 49 -24.157 43.244 16.076 1.00 69.38 C
ATOM 332 O PHE A 49 -24.975 42.477 16.591 1.00 69.86 O
ATOM 333 CB PHE A 49 -22.802 44.769 17.543 1.00 67.60 C
ATOM 334 CG PHE A 49 -24.127 45.052 18.192 1.00 69.40 C
ATOM 335 CD1 PHE A 49 -24.732 44.107 19.015 1.00 69.61 C
ATOM 336 CD2 PHE A 49 -24.803 46.240 17.929 1.00 70.50 C
ATOM 337 CE1 PHE A 49 -25.991 44.336 19.558 1.00 69.81 C
ATOM 338 CE2 PHE A 49 -26.064 46.480 18.469 1.00 70.42 C
ATOM 339 CZ PHE A 49 -26.659 45.524 19.283 1.00 70.39 C
ATOM 340 N PRO A 50 -24.436 43.916 14.948 1.00 71.00 N
ATOM 341 CA PRO A 50 -25.744 43.694 14.326 1.00 72.12 C
ATOM 342 C PRO A 50 -25.952 42.243 13.866 1.00 73.29 C
ATOM 343 O PRO A 50 -26.950 41.933 13.213 1.00 73.81 O
ATOM 344 CB PRO A 50 -25.747 44.700 13.179 1.00 72.19 C
ATOM 345 CG PRO A 50 -24.956 45.842 13.762 1.00 71.52 C
ATOM 346 CD PRO A 50 -23.787 45.113 14.382 1.00 71.16 C
ATOM 347 N LEU A 51 -24.999 41.374 14.212 1.00 74.01 N
ATOM 348 CA LEU A 51 -25.037 39.939 13.900 1.00 74.68 C
ATOM 349 C LEU A 51 -25.573 39.571 12.510 1.00 75.09 C
ATOM 350 O LEU A 51 -26.766 39.286 12.338 1.00 75.26 O
ATOM 351 CB LEU A 51 -25.905 39.214 14.932 1.00 74.70 C
ATOM 352 CG LEU A 51 -25.431 39.371 16.375 1.00 75.33 C
ATOM 353 CD1 LEU A 51 -26.436 38.814 17.390 1.00 75.52 C
ATOM 354 CD2 LEU A 51 -24.116 38.643 16.654 1.00 75.34 C
ATOM 355 N ALA A 52 -24.650 39.545 11.555 1.00 75.30 N
ATOM 356 CA ALA A 52 -24.940 39.000 10.202 1.00 75.11 C
ATOM 357 C ALA A 52 -25.641 37.636 10.260 1.00 75.12 C
ATOM 358 O ALA A 52 -25.236 36.737 11.009 1.00 75.20 O
ATOM 359 CB ALA A 52 -23.647 38.877 9.393 1.00 75.35 C
ATOM 360 N ASP A 53 -26.691 37.502 9.470 1.00 75.21 N
ATOM 361 CA ASP A 53 -27.481 36.260 9.436 1.00 74.88 C
ATOM 362 C ASP A 53 -26.645 35.109 8.901 1.00 73.62 C
ATOM 363 O ASP A 53 -26.344 34.157 9.627 1.00 72.83 O
ATOM 364 CB ASP A 53 -28.713 36.426 8.552 1.00 76.42 C
ATOM 365 CG ASP A 53 -29.765 35.351 8.823 1.00 78.03 C
ATOM 366 OD1 ASP A 53 -29.409 34.116 8.927 1.00 78.66 O
ATOM 367 OD2 ASP A 53 -31.004 35.680 8.949 1.00 78.56 O
ATOM 368 N HIS A 54 -26.278 35.211 7.624 1.00 72.28 N
ATOM 369 CA HIS A 54 -25.470 34.198 6.943 1.00 70.51 C
ATOM 370 C HIS A 54 -24.399 33.651 7.880 1.00 68.44 C
ATOM 371 O HIS A 54 -24.156 32.444 7.930 1.00 68.38 O
ATOM 372 CB HIS A 54 -24.814 34.809 5.698 1.00 71.30 C
ATOM 373 CG HIS A 54 -23.839 35.904 6.000 1.00 72.08 C
ATOM 374 ND1 HIS A 54 -22.572 35.661 6.488 1.00 72.46 N
ATOM 375 CD2 HIS A 54 -23.956 37.251 5.914 1.00 72.28 C
ATOM 376 CE1 HIS A 54 -21.951 36.810 6.689 1.00 72.55 C
ATOM 377 NE2 HIS A 54 -22.769 37.790 6.348 1.00 72.42 N
ATOM 378 N LEU A 55 -23.771 34.555 8.626 1.00 65.74 N
ATOM 379 CA LEU A 55 -22.729 34.199 9.579 1.00 62.50 C
ATOM 380 C LEU A 55 -23.391 33.563 10.801 1.00 59.78 C
ATOM 381 O LEU A 55 -24.391 34.075 11.315 1.00 59.84 O
ATOM 382 CB LEU A 55 -21.963 35.457 9.990 1.00 63.10 C
ATOM 383 CG LEU A 55 -20.692 35.291 10.818 1.00 63.13 C
ATOM 384 CD1 LEU A 55 -19.656 34.533 10.002 1.00 63.06 C
ATOM 385 CD2 LEU A 55 -20.167 36.665 11.220 1.00 63.27 C
ATOM 386 N ASN A 56 -22.837 32.449 11.265 1.00 55.72 N
ATOM 387 CA ASN A 56 -23.406 31.765 12.414 1.00 51.92 C
ATOM 388 C ASN A 56 -22.682 32.057 13.721 1.00 49.67 C
ATOM 389 O ASN A 56 -21.448 32.130 13.766 1.00 49.89 O
ATOM 390 CB ASN A 56 -23.431 30.257 12.177 1.00 51.23 C
ATOM 391 CG ASN A 56 -23.858 29.487 13.411 1.00 51.36 C
ATOM 392 OD1 ASN A 56 -23.120 29.415 14.399 1.00 49.80 O
ATOM 393 ND2 ASN A 56 -25.059 28.915 13.367 1.00 50.78 N
ATOM 394 N SER A 57 -23.468 32.213 14.785 1.00 45.58 N
ATOM 395 CA SER A 57 -22.938 32.494 16.113 1.00 40.84 C
ATOM 396 C SER A 57 -23.646 31.624 17.153 1.00 37.52 C
ATOM 397 O SER A 57 -24.848 31.381 17.046 1.00 35.76 O
ATOM 398 CB SER A 57 -23.159 33.968 16.465 1.00 40.83 C
ATOM 399 OG SER A 57 -22.864 34.819 15.373 1.00 39.61 O
ATOM 400 N THR A 58 -22.899 31.135 18.138 1.00 33.78 N
ATOM 401 CA THR A 58 -23.501 30.343 19.200 1.00 30.93 C
ATOM 402 C THR A 58 -24.245 31.356 20.061 1.00 28.69 C
ATOM 403 O THR A 58 -24.054 32.565 19.898 1.00 26.98 O
ATOM 404 CB THR A 58 -22.447 29.647 20.083 1.00 31.19 C
ATOM 405 OG1 THR A 58 -21.376 30.555 20.351 1.00 31.39 O
ATOM 406 CG2 THR A 58 -21.905 28.404 19.404 1.00 31.90 C
ATOM 407 N ASN A 59 -25.096 30.872 20.960 1.00 25.59 N
ATOM 408 CA ASN A 59 -25.836 31.765 21.835 1.00 22.84 C
ATOM 409 C ASN A 59 -24.858 32.611 22.622 1.00 21.76 C
ATOM 410 O ASN A 59 -25.057 33.816 22.798 1.00 19.75 O
ATOM 411 CB ASN A 59 -26.723 30.974 22.791 1.00 21.12 C
ATOM 412 CG ASN A 59 -27.969 30.463 22.117 1.00 20.45 C
ATOM 413 OD1 ASN A 59 -28.507 31.118 21.228 1.00 20.92 O
ATOM 414 ND2 ASN A 59 -28.444 29.304 22.537 1.00 17.92 N
ATOM 415 N HIS A 60 -23.786 31.976 23.082 1.00 21.26 N
ATOM 416 CA HIS A 60 -22.783 32.692 23.846 1.00 21.46 C
ATOM 417 C HIS A 60 -22.201 33.821 23.006 1.00 21.75 C
ATOM 418 O HIS A 60 -22.129 34.959 23.463 1.00 22.64 O
ATOM 419 CB HIS A 60 -21.659 31.766 24.287 1.00 20.40 C
ATOM 420 CG HIS A 60 -20.697 32.418 25.225 1.00 21.66 C
ATOM 421 ND1 HIS A 60 -20.866 32.404 26.593 1.00 23.00 N
ATOM 422 CD2 HIS A 60 -19.594 33.166 24.991 1.00 21.94 C
ATOM 423 CE1 HIS A 60 -19.909 33.114 27.161 1.00 22.13 C
ATOM 424 NE2 HIS A 60 -19.124 33.587 26.209 1.00 22.87 N
ATOM 425 N ALA A 61 -21.786 33.503 21.779 1.00 20.64 N
ATOM 426 CA ALA A 61 -21.216 34.508 20.887 1.00 19.30 C
ATOM 427 C ALA A 61 -22.142 35.724 20.792 1.00 18.93 C
ATOM 428 O ALA A 61 -21.694 36.869 20.837 1.00 18.44 O
ATOM 429 CB ALA A 61 -20.985 33.911 19.512 1.00 18.02 C
ATOM 430 N ILE A 62 -23.438 35.462 20.672 1.00 18.61 N
ATOM 431 CA ILE A 62 -24.432 36.518 20.569 1.00 19.26 C
ATOM 432 C ILE A 62 -24.459 37.353 21.844 1.00 21.44 C
ATOM 433 O ILE A 62 -24.423 38.586 21.802 1.00 22.37 O
ATOM 434 CB ILE A 62 -25.824 35.922 20.308 1.00 17.33 C
ATOM 435 CG1 ILE A 62 -25.836 35.268 18.915 1.00 14.24 C
ATOM 436 CG2 ILE A 62 -26.901 37.003 20.474 1.00 16.08 C
ATOM 437 CD1 ILE A 62 -26.967 34.297 18.667 1.00 8.50 C
ATOM 438 N VAL A 63 -24.514 36.672 22.978 1.00 22.55 N
ATOM 439 CA VAL A 63 -24.532 37.342 24.267 1.00 22.65 C
ATOM 440 C VAL A 63 -23.295 38.221 24.411 1.00 23.23 C
ATOM 441 O VAL A 63 -23.393 39.371 24.816 1.00 23.51 O
ATOM 442 CB VAL A 63 -24.556 36.306 25.425 1.00 22.44 C
ATOM 443 CG1 VAL A 63 -24.427 37.007 26.773 1.00 21.90 C
ATOM 444 CG2 VAL A 63 -25.842 35.498 25.370 1.00 21.70 C
ATOM 445 N GLN A 64 -22.135 37.675 24.068 1.00 25.16 N
ATOM 446 CA GLN A 64 -20.875 38.402 24.189 1.00 27.00 C
ATOM 447 C GLN A 64 -20.780 39.566 23.203 1.00 27.80 C
ATOM 448 O GLN A 64 -20.219 40.617 23.511 1.00 26.57 O
ATOM 449 CB GLN A 64 -19.699 37.449 23.979 1.00 27.57 C
ATOM 450 CG GLN A 64 -18.365 38.039 24.415 1.00 29.06 C
ATOM 451 CD GLN A 64 -17.211 37.066 24.274 1.00 29.50 C
ATOM 452 OE1 GLN A 64 -17.272 35.930 24.749 1.00 29.01 O
ATOM 453 NE2 GLN A 64 -16.144 37.514 23.627 1.00 30.77 N
ATOM 454 N THR A 65 -21.323 39.367 22.011 1.00 28.64 N
ATOM 455 CA THR A 65 -21.317 40.409 21.005 1.00 30.36 C
ATOM 456 C THR A 65 -22.086 41.610 21.557 1.00 31.86 C
ATOM 457 O THR A 65 -21.621 42.749 21.488 1.00 32.75 O
ATOM 458 CB THR A 65 -21.982 39.902 19.713 1.00 29.88 C
ATOM 459 OG1 THR A 65 -21.162 38.873 19.144 1.00 31.77 O
ATOM 460 CG2 THR A 65 -22.157 41.017 18.708 1.00 27.66 C
ATOM 461 N LEU A 66 -23.257 41.332 22.125 1.00 32.48 N
ATOM 462 CA LEU A 66 -24.121 42.353 22.695 1.00 32.25 C
ATOM 463 C LEU A 66 -23.440 43.074 23.859 1.00 32.68 C
ATOM 464 O LEU A 66 -23.410 44.307 23.907 1.00 32.48 O
ATOM 465 CB LEU A 66 -25.427 41.706 23.152 1.00 32.18 C
ATOM 466 CG LEU A 66 -26.577 42.588 23.636 1.00 32.68 C
ATOM 467 CD1 LEU A 66 -26.991 43.567 22.559 1.00 31.65 C
ATOM 468 CD2 LEU A 66 -27.747 41.695 24.007 1.00 33.94 C
ATOM 469 N VAL A 67 -22.896 42.309 24.799 1.00 33.09 N
ATOM 470 CA VAL A 67 -22.205 42.898 25.948 1.00 34.01 C
ATOM 471 C VAL A 67 -21.139 43.865 25.442 1.00 35.19 C
ATOM 472 O VAL A 67 -21.040 45.007 25.891 1.00 34.21 O
ATOM 473 CB VAL A 67 -21.520 41.807 26.805 1.00 32.95 C
ATOM 474 CG1 VAL A 67 -20.583 42.437 27.827 1.00 32.03 C
ATOM 475 CG2 VAL A 67 -22.577 40.967 27.502 1.00 33.13 C
ATOM 476 N ASN A 68 -20.355 43.384 24.485 1.00 36.80 N
ATOM 477 CA ASN A 68 -19.280 44.155 23.889 1.00 38.19 C
ATOM 478 C ASN A 68 -19.732 45.528 23.386 1.00 39.91 C
ATOM 479 O ASN A 68 -18.996 46.515 23.515 1.00 39.69 O
ATOM 480 CB ASN A 68 -18.654 43.340 22.750 1.00 36.58 C
ATOM 481 CG ASN A 68 -17.619 44.120 21.972 1.00 34.83 C
ATOM 482 OD1 ASN A 68 -17.909 44.658 20.905 1.00 33.33 O
ATOM 483 ND2 ASN A 68 -16.407 44.193 22.508 1.00 32.07 N
ATOM 484 N SER A 69 -20.939 45.595 22.830 1.00 41.06 N
ATOM 485 CA SER A 69 -21.459 46.854 22.306 1.00 43.33 C
ATOM 486 C SER A 69 -21.909 47.815 23.408 1.00 44.57 C
ATOM 487 O SER A 69 -22.204 48.982 23.148 1.00 45.21 O
ATOM 488 CB SER A 69 -22.622 46.589 21.338 1.00 43.01 C
ATOM 489 OG SER A 69 -23.687 45.907 21.971 1.00 43.55 O
ATOM 490 N VAL A 70 -21.942 47.321 24.639 1.00 45.51 N
ATOM 491 CA VAL A 70 -22.367 48.122 25.775 1.00 46.45 C
ATOM 492 C VAL A 70 -21.213 48.212 26.765 1.00 46.66 C
ATOM 493 O VAL A 70 -21.300 48.873 27.794 1.00 47.18 O
ATOM 494 CB VAL A 70 -23.611 47.478 26.448 1.00 46.97 C
ATOM 495 CG1 VAL A 70 -24.040 48.280 27.668 1.00 47.14 C
ATOM 496 CG2 VAL A 70 -24.758 47.398 25.438 1.00 46.57 C
ATOM 497 N ASN A 71 -20.124 47.539 26.434 1.00 47.00 N
ATOM 498 CA ASN A 71 -18.931 47.533 27.269 1.00 47.56 C
ATOM 499 C ASN A 71 -17.808 46.928 26.445 1.00 47.66 C
ATOM 500 O ASN A 71 -17.889 45.768 26.038 1.00 47.64 O
ATOM 501 CB ASN A 71 -19.159 46.701 28.522 1.00 48.08 C
ATOM 502 CG ASN A 71 -17.872 46.342 29.208 1.00 49.82 C
ATOM 503 OD1 ASN A 71 -17.072 47.210 29.544 1.00 51.49 O
ATOM 504 ND2 ASN A 71 -17.655 45.056 29.414 1.00 51.86 N
ATOM 505 N SER A 72 -16.758 47.707 26.204 1.00 46.93 N
ATOM 506 CA SER A 72 -15.652 47.230 25.385 1.00 45.81 C
ATOM 507 C SER A 72 -14.515 46.518 26.101 1.00 44.72 C
ATOM 508 O SER A 72 -13.591 46.034 25.454 1.00 45.31 O
ATOM 509 CB SER A 72 -15.098 48.381 24.550 1.00 45.95 C
ATOM 510 OG SER A 72 -16.082 48.837 23.635 1.00 47.12 O
ATOM 511 N LYS A 73 -14.570 46.437 27.424 1.00 43.32 N
ATOM 512 CA LYS A 73 -13.512 45.748 28.151 1.00 42.01 C
ATOM 513 C LYS A 73 -13.655 44.259 27.884 1.00 39.91 C
ATOM 514 O LYS A 73 -12.769 43.463 28.197 1.00 39.52 O
ATOM 515 CB LYS A 73 -13.605 46.029 29.652 1.00 43.27 C
ATOM 516 CG LYS A 73 -13.640 47.509 29.991 1.00 44.74 C
ATOM 517 CD LYS A 73 -12.615 48.297 29.183 1.00 46.28 C
ATOM 518 CE LYS A 73 -12.625 49.768 29.575 1.00 47.69 C
ATOM 519 NZ LYS A 73 -13.994 50.369 29.497 1.00 49.04 N
ATOM 520 N ILE A 74 -14.792 43.890 27.309 1.00 37.46 N
ATOM 521 CA ILE A 74 -15.051 42.499 26.967 1.00 35.49 C
ATOM 522 C ILE A 74 -14.911 42.370 25.444 1.00 33.98 C
ATOM 523 O ILE A 74 -15.531 43.125 24.683 1.00 32.54 O
ATOM 524 CB ILE A 74 -16.466 42.065 27.401 1.00 34.95 C
ATOM 525 CG1 ILE A 74 -16.630 42.238 28.915 1.00 33.72 C
ATOM 526 CG2 ILE A 74 -16.710 40.629 26.985 1.00 34.66 C
ATOM 527 CD1 ILE A 74 -15.631 41.478 29.750 1.00 32.24 C
ATOM 528 N PRO A 75 -14.085 41.411 24.989 1.00 32.41 N
ATOM 529 CA PRO A 75 -13.789 41.109 23.588 1.00 32.10 C
ATOM 530 C PRO A 75 -14.998 40.695 22.768 1.00 32.71 C
ATOM 531 O PRO A 75 -15.969 40.164 23.305 1.00 33.32 O
ATOM 532 CB PRO A 75 -12.785 39.968 23.688 1.00 31.68 C
ATOM 533 CG PRO A 75 -12.156 40.166 25.007 1.00 32.25 C
ATOM 534 CD PRO A 75 -13.330 40.506 25.867 1.00 32.67 C
ATOM 535 N LYS A 76 -14.937 40.937 21.463 1.00 32.28 N
ATOM 536 CA LYS A 76 -16.023 40.529 20.590 1.00 32.93 C
ATOM 537 C LYS A 76 -15.886 39.015 20.391 1.00 32.69 C
ATOM 538 O LYS A 76 -14.903 38.415 20.831 1.00 31.34 O
ATOM 539 CB LYS A 76 -15.926 41.244 19.245 1.00 33.15 C
ATOM 540 CG LYS A 76 -15.802 42.751 19.355 1.00 35.03 C
ATOM 541 CD LYS A 76 -16.292 43.433 18.083 1.00 35.83 C
ATOM 542 CE LYS A 76 -16.162 44.943 18.177 1.00 36.72 C
ATOM 543 NZ LYS A 76 -16.825 45.628 17.019 1.00 38.30 N
ATOM 544 N ALA A 77 -16.877 38.393 19.759 1.00 33.04 N
ATOM 545 CA ALA A 77 -16.811 36.955 19.507 1.00 32.01 C
ATOM 546 C ALA A 77 -15.772 36.771 18.416 1.00 31.23 C
ATOM 547 O ALA A 77 -15.727 37.534 17.455 1.00 31.07 O
ATOM 548 CB ALA A 77 -18.168 36.419 19.043 1.00 32.18 C
ATOM 549 N CYS A 78 -14.935 35.756 18.562 1.00 30.79 N
ATOM 550 CA CYS A 78 -13.887 35.518 17.584 1.00 29.31 C
ATOM 551 C CYS A 78 -14.347 34.765 16.338 1.00 29.01 C
ATOM 552 O CYS A 78 -15.327 34.018 16.368 1.00 29.44 O
ATOM 553 CB CYS A 78 -12.743 34.768 18.241 1.00 27.84 C
ATOM 554 SG CYS A 78 -11.198 34.959 17.353 1.00 25.21 S
ATOM 555 N CYS A 79 -13.623 34.973 15.243 1.00 28.32 N
ATOM 556 CA CYS A 79 -13.931 34.328 13.969 1.00 26.93 C
ATOM 557 C CYS A 79 -13.091 33.071 13.798 1.00 26.54 C
ATOM 558 O CYS A 79 -11.961 33.123 13.302 1.00 25.62 O
ATOM 559 CB CYS A 79 -13.653 35.290 12.824 1.00 26.32 C
ATOM 560 SG CYS A 79 -13.930 34.633 11.154 1.00 28.45 S
ATOM 561 N VAL A 80 -13.654 31.941 14.209 1.00 24.85 N
ATOM 562 CA VAL A 80 -12.949 30.684 14.110 1.00 23.92 C
ATOM 563 C VAL A 80 -13.653 29.733 13.157 1.00 24.43 C
ATOM 564 O VAL A 80 -14.759 30.016 12.687 1.00 24.12 O
ATOM 565 CB VAL A 80 -12.814 30.038 15.492 1.00 23.41 C
ATOM 566 CG1 VAL A 80 -11.807 30.825 16.337 1.00 22.40 C
ATOM 567 CG2 VAL A 80 -14.161 30.006 16.170 1.00 22.15 C
ATOM 568 N PRO A 81 -13.003 28.601 12.828 1.00 24.09 N
ATOM 569 CA PRO A 81 -13.593 27.615 11.918 1.00 23.99 C
ATOM 570 C PRO A 81 -14.726 26.886 12.631 1.00 23.13 C
ATOM 571 O PRO A 81 -14.581 26.476 13.780 1.00 22.12 O
ATOM 572 CB PRO A 81 -12.423 26.676 11.601 1.00 24.02 C
ATOM 573 CG PRO A 81 -11.204 27.487 11.925 1.00 24.43 C
ATOM 574 CD PRO A 81 -11.620 28.226 13.163 1.00 24.48 C
ATOM 575 N THR A 82 -15.847 26.721 11.942 1.00 22.98 N
ATOM 576 CA THR A 82 -16.999 26.060 12.527 1.00 22.34 C
ATOM 577 C THR A 82 -17.334 24.767 11.804 1.00 21.95 C
ATOM 578 O THR A 82 -18.097 23.943 12.303 1.00 22.37 O
ATOM 579 CB THR A 82 -18.211 27.010 12.523 1.00 22.43 C
ATOM 580 OG1 THR A 82 -18.491 27.445 11.185 1.00 20.26 O
ATOM 581 CG2 THR A 82 -17.902 28.230 13.375 1.00 22.78 C
ATOM 582 N GLU A 83 -16.750 24.586 10.627 1.00 20.56 N
ATOM 583 CA GLU A 83 -16.980 23.377 9.848 1.00 19.97 C
ATOM 584 C GLU A 83 -15.643 22.935 9.246 1.00 20.05 C
ATOM 585 O GLU A 83 -15.029 23.666 8.464 1.00 19.14 O
ATOM 586 CB AGLU A 83 -17.981 23.624 8.715 0.50 18.67 C
ATOM 587 CB BGLU A 83 -18.010 23.677 8.760 0.50 20.01 C
ATOM 588 CG AGLU A 83 -19.421 23.807 9.163 0.50 16.59 C
ATOM 589 CG BGLU A 83 -19.061 22.608 8.549 0.50 19.59 C
ATOM 590 CD AGLU A 83 -19.686 25.166 9.770 0.50 15.18 C
ATOM 591 CD BGLU A 83 -18.783 21.740 7.345 0.50 19.87 C
ATOM 592 OE1AGLU A 83 -19.478 26.175 9.073 0.50 13.77 O
ATOM 593 OE1BGLU A 83 -17.778 20.994 7.360 0.50 19.81 O
ATOM 594 OE2AGLU A 83 -20.111 25.227 10.939 0.50 14.83 O
ATOM 595 OE2BGLU A 83 -19.575 21.811 6.379 0.50 17.92 O
ATOM 596 N LEU A 84 -15.183 21.749 9.622 1.00 18.67 N
ATOM 597 CA LEU A 84 -13.923 21.254 9.104 1.00 18.25 C
ATOM 598 C LEU A 84 -14.062 19.912 8.386 1.00 18.84 C
ATOM 599 O LEU A 84 -15.136 19.299 8.359 1.00 18.63 O
ATOM 600 CB LEU A 84 -12.893 21.144 10.230 1.00 18.02 C
ATOM 601 CG LEU A 84 -12.660 22.422 11.054 1.00 18.71 C
ATOM 602 CD1 LEU A 84 -13.475 22.350 12.337 1.00 17.64 C
ATOM 603 CD2 LEU A 84 -11.181 22.586 11.399 1.00 17.38 C
ATOM 604 N SER A 85 -12.971 19.476 7.771 1.00 18.13 N
ATOM 605 CA SER A 85 -12.964 18.218 7.046 1.00 17.79 C
ATOM 606 C SER A 85 -11.568 17.628 7.164 1.00 18.15 C