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HEADER TRANSPORT PROTEIN 05-SEP-18 6MDQ
TITLE CRYSTAL STRUCTURE OF EQUINE SERUM ALBUMIN IN COMPLEX WITH TESTOSTERONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796
KEYWDS ALBUMIN, EQUINE SERUM ALBUMIN, TESTOSTERONE, CSGID, STRUCTURAL
KEYWDS 2 GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES,
KEYWDS 3 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.CZUB,K.A.MAJOREK,I.G.SHABALIN,K.B.HANDING,B.S.VENKATARAMANY,
AUTHOR 2 M.T.CYMBOROWSKI,K.J.SATCHELL,A.JOACHIMIAK,W.MINOR,CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 03-APR-19 6MDQ 1 JRNL
REVDAT 1 26-SEP-18 6MDQ 0
JRNL AUTH M.P.CZUB,B.S.VENKATARAMANY,K.A.MAJOREK,K.B.HANDING,
JRNL AUTH 2 P.J.POREBSKI,S.R.BEERAM,K.SUH,A.G.WOOLFORK,D.S.HAGE,
JRNL AUTH 3 I.G.SHABALIN,W.MINOR
JRNL TITL TESTOSTERONE MEETS ALBUMIN - THE MOLECULAR MECHANISM OF SEX
JRNL TITL 2 HORMONE TRANSPORT BY SERUM ALBUMINS.
JRNL REF CHEM SCI V. 10 1607 2019
JRNL REFN ISSN 2041-6520
JRNL PMID 30842823
JRNL DOI 10.1039/C8SC04397C
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 36951
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 + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1859
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4475
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.18000
REMARK 3 B22 (A**2) : 2.18000
REMARK 3 B33 (A**2) : -7.07000
REMARK 3 B12 (A**2) : 1.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.178
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.041
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 6MDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000236023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
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) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 1.02700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3V08
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL OF 15 MG/ML PROTEIN WAS MIXED
REMARK 280 WITH 0.2 UL OF THE WELL CONDITION (1.8 M AMMONIUM DIHYDROGEN
REMARK 280 CITRATE, PH 7.0) AND EQUILIBRATED AGAINST WELL SOLUTION IN 96-
REMARK 280 WELL SITTING DROP CRYSTALLIZATION PLATE (SWISSCI). TESTOSTERONE
REMARK 280 POWDER WAS ADDED TO THE CRYSTALLIZATION DROP, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 47.44833
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 94.89667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 71.17250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 118.62083
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 23.72417
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 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 ASP A 1
REMARK 465 THR A 2
REMARK 465 HIS A 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 SER A 58 OG
REMARK 470 ARG A 81 CD NE CZ NH1 NH2
REMARK 470 LYS A 114 CD CE NZ
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 GLU A 118 CD OE1 OE2
REMARK 470 LYS A 132 CE NZ
REMARK 470 LYS A 136 CE NZ
REMARK 470 ASP A 171 CG OD1 OD2
REMARK 470 ASP A 172 CG OD1 OD2
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 ILE A 178 CG1 CG2 CD1
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 GLU A 265 CG CD OE1 OE2
REMARK 470 LYS A 275 CD CE NZ
REMARK 470 LYS A 293 CD CE NZ
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 LYS A 316 CD CE NZ
REMARK 470 LYS A 319 CD CE NZ
REMARK 470 LYS A 322 CG CD CE NZ
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 388 CD CE NZ
REMARK 470 LYS A 389 CE NZ
REMARK 470 LYS A 438 CD CE NZ
REMARK 470 LYS A 474 CD CE NZ
REMARK 470 LYS A 502 CD CE NZ
REMARK 470 GLU A 504 CD OE1 OE2
REMARK 470 GLU A 517 CG CD OE1 OE2
REMARK 470 LYS A 523 CD CE NZ
REMARK 470 LYS A 573 CG CD CE NZ
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 61 -4.81 72.57
REMARK 500 LEU A 174 43.96 -106.63
REMARK 500 LEU A 177 -71.15 -76.85
REMARK 500 PHE A 222 64.46 -119.36
REMARK 500 ALA A 309 -37.79 -130.75
REMARK 500 ALA A 321 85.78 -157.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TES A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TES A 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP95820 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS MUTATION IS CHARACTERISTIC FOR EQUUS FERUS PRZEWALSKII, A RARE
REMARK 999 SUBSPECIES OF WILD HORSE FROM CENTRAL ASIA. SEE NCBI DATABASE,
REMARK 999 ACCESSION CODE: XP_008524663.1
DBREF 6MDQ A 1 583 UNP P35747 ALBU_HORSE 25 607
SEQADV 6MDQ ALA A 560 UNP P35747 ARG 584 SEE REMARK 999
SEQRES 1 A 583 ASP THR HIS LYS SER GLU ILE ALA HIS ARG PHE ASN ASP
SEQRES 2 A 583 LEU GLY GLU LYS HIS PHE LYS GLY LEU VAL LEU VAL ALA
SEQRES 3 A 583 PHE SER GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 A 583 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS LYS
SEQRES 5 A 583 CYS ALA ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 A 583 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 A 583 THR LEU ARG ALA THR TYR GLY GLU LEU ALA ASP CYS CYS
SEQRES 8 A 583 GLU LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU THR
SEQRES 9 A 583 HIS LYS ASP ASP HIS PRO ASN LEU PRO LYS LEU LYS PRO
SEQRES 10 A 583 GLU PRO ASP ALA GLN CYS ALA ALA PHE GLN GLU ASP PRO
SEQRES 11 A 583 ASP LYS PHE LEU GLY LYS TYR LEU TYR GLU VAL ALA ARG
SEQRES 12 A 583 ARG HIS PRO TYR PHE TYR GLY PRO GLU LEU LEU PHE HIS
SEQRES 13 A 583 ALA GLU GLU TYR LYS ALA ASP PHE THR GLU CYS CYS PRO
SEQRES 14 A 583 ALA ASP ASP LYS LEU ALA CYS LEU ILE PRO LYS LEU ASP
SEQRES 15 A 583 ALA LEU LYS GLU ARG ILE LEU LEU SER SER ALA LYS GLU
SEQRES 16 A 583 ARG LEU LYS CYS SER SER PHE GLN ASN PHE GLY GLU ARG
SEQRES 17 A 583 ALA VAL LYS ALA TRP SER VAL ALA ARG LEU SER GLN LYS
SEQRES 18 A 583 PHE PRO LYS ALA ASP PHE ALA GLU VAL SER LYS ILE VAL
SEQRES 19 A 583 THR ASP LEU THR LYS VAL HIS LYS GLU CYS CYS HIS GLY
SEQRES 20 A 583 ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA
SEQRES 21 A 583 LYS TYR ILE CYS GLU HIS GLN ASP SER ILE SER GLY LYS
SEQRES 22 A 583 LEU LYS ALA CYS CYS ASP LYS PRO LEU LEU GLN LYS SER
SEQRES 23 A 583 HIS CYS ILE ALA GLU VAL LYS GLU ASP ASP LEU PRO SER
SEQRES 24 A 583 ASP LEU PRO ALA LEU ALA ALA ASP PHE ALA GLU ASP LYS
SEQRES 25 A 583 GLU ILE CYS LYS HIS TYR LYS ASP ALA LYS ASP VAL PHE
SEQRES 26 A 583 LEU GLY THR PHE LEU TYR GLU TYR SER ARG ARG HIS PRO
SEQRES 27 A 583 ASP TYR SER VAL SER LEU LEU LEU ARG ILE ALA LYS THR
SEQRES 28 A 583 TYR GLU ALA THR LEU GLU LYS CYS CYS ALA GLU ALA ASP
SEQRES 29 A 583 PRO PRO ALA CYS TYR ARG THR VAL PHE ASP GLN PHE THR
SEQRES 30 A 583 PRO LEU VAL GLU GLU PRO LYS SER LEU VAL LYS LYS ASN
SEQRES 31 A 583 CYS ASP LEU PHE GLU GLU VAL GLY GLU TYR ASP PHE GLN
SEQRES 32 A 583 ASN ALA LEU ILE VAL ARG TYR THR LYS LYS ALA PRO GLN
SEQRES 33 A 583 VAL SER THR PRO THR LEU VAL GLU ILE GLY ARG THR LEU
SEQRES 34 A 583 GLY LYS VAL GLY SER ARG CYS CYS LYS LEU PRO GLU SER
SEQRES 35 A 583 GLU ARG LEU PRO CYS SER GLU ASN HIS LEU ALA LEU ALA
SEQRES 36 A 583 LEU ASN ARG LEU CYS VAL LEU HIS GLU LYS THR PRO VAL
SEQRES 37 A 583 SER GLU LYS ILE THR LYS CYS CYS THR ASP SER LEU ALA
SEQRES 38 A 583 GLU ARG ARG PRO CYS PHE SER ALA LEU GLU LEU ASP GLU
SEQRES 39 A 583 GLY TYR VAL PRO LYS GLU PHE LYS ALA GLU THR PHE THR
SEQRES 40 A 583 PHE HIS ALA ASP ILE CYS THR LEU PRO GLU ASP GLU LYS
SEQRES 41 A 583 GLN ILE LYS LYS GLN SER ALA LEU ALA GLU LEU VAL LYS
SEQRES 42 A 583 HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS THR VAL
SEQRES 43 A 583 LEU GLY ASN PHE SER ALA PHE VAL ALA LYS CYS CYS GLY
SEQRES 44 A 583 ALA GLU ASP LYS GLU ALA CYS PHE ALA GLU GLU GLY PRO
SEQRES 45 A 583 LYS LEU VAL ALA SER SER GLN LEU ALA LEU ALA
HET FLC A 601 13
HET FLC A 602 13
HET FLC A 603 13
HET TES A 604 21
HET TES A 605 21
HETNAM FLC CITRATE ANION
HETNAM TES TESTOSTERONE
FORMUL 2 FLC 3(C6 H5 O7 3-)
FORMUL 5 TES 2(C19 H28 O2)
FORMUL 7 HOH *214(H2 O)
HELIX 1 AA1 SER A 5 GLY A 15 1 11
HELIX 2 AA2 GLY A 15 LEU A 31 1 17
HELIX 3 AA3 PRO A 35 ASP A 56 1 22
HELIX 4 AA4 SER A 65 CYS A 75 1 11
HELIX 5 AA5 THR A 79 TYR A 84 1 6
HELIX 6 AA6 GLU A 86 LYS A 93 1 8
HELIX 7 AA7 PRO A 96 HIS A 105 1 10
HELIX 8 AA8 GLU A 118 ASP A 129 1 12
HELIX 9 AA9 ASP A 129 HIS A 145 1 17
HELIX 10 AB1 TYR A 149 CYS A 168 1 20
HELIX 11 AB2 LYS A 180 GLY A 206 1 27
HELIX 12 AB3 GLY A 206 PHE A 222 1 17
HELIX 13 AB4 ASP A 226 HIS A 246 1 21
HELIX 14 AB5 ASP A 248 HIS A 266 1 19
HELIX 15 AB6 HIS A 266 SER A 271 1 6
HELIX 16 AB7 LYS A 273 ASP A 279 1 7
HELIX 17 AB8 PRO A 281 GLU A 291 1 11
HELIX 18 AB9 LEU A 304 ALA A 309 1 6
HELIX 19 AC1 GLU A 313 ALA A 321 1 9
HELIX 20 AC2 ALA A 321 HIS A 337 1 17
HELIX 21 AC3 SER A 341 CYS A 360 1 20
HELIX 22 AC4 ASP A 364 ARG A 370 1 7
HELIX 23 AC5 THR A 371 GLN A 375 5 5
HELIX 24 AC6 PHE A 376 GLY A 398 1 23
HELIX 25 AC7 GLY A 398 ALA A 414 1 17
HELIX 26 AC8 SER A 418 CYS A 437 1 20
HELIX 27 AC9 PRO A 440 SER A 442 5 3
HELIX 28 AD1 GLU A 443 THR A 466 1 24
HELIX 29 AD2 SER A 469 ASP A 478 1 10
HELIX 30 AD3 GLU A 482 LEU A 490 1 9
HELIX 31 AD4 LYS A 502 THR A 507 5 6
HELIX 32 AD5 HIS A 509 LEU A 515 5 7
HELIX 33 AD6 PRO A 516 LYS A 535 1 20
HELIX 34 AD7 THR A 539 GLY A 559 1 21
HELIX 35 AD8 ASP A 562 LEU A 582 1 21
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.03
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.04
SSBOND 4 CYS A 123 CYS A 168 1555 1555 2.04
SSBOND 5 CYS A 167 CYS A 176 1555 1555 2.03
SSBOND 6 CYS A 199 CYS A 245 1555 1555 2.03
SSBOND 7 CYS A 244 CYS A 252 1555 1555 2.02
SSBOND 8 CYS A 264 CYS A 278 1555 1555 2.03
SSBOND 9 CYS A 277 CYS A 288 1555 1555 2.04
SSBOND 10 CYS A 315 CYS A 360 1555 1555 2.03
SSBOND 11 CYS A 359 CYS A 368 1555 1555 2.04
SSBOND 12 CYS A 391 CYS A 437 1555 1555 2.04
SSBOND 13 CYS A 436 CYS A 447 1555 1555 2.03
SSBOND 14 CYS A 460 CYS A 476 1555 1555 2.03
SSBOND 15 CYS A 475 CYS A 486 1555 1555 2.05
SSBOND 16 CYS A 513 CYS A 558 1555 1555 2.03
SSBOND 17 CYS A 557 CYS A 566 1555 1555 2.04
CISPEP 1 GLU A 95 PRO A 96 0 3.26
SITE 1 AC1 4 HIS A 337 TYR A 340 THR A 377 HOH A 701
SITE 1 AC2 8 ASP A 108 HIS A 109 PRO A 110 ASN A 111
SITE 2 AC2 8 LEU A 112 HIS A 145 LEU A 189 ARG A 458
SITE 1 AC3 8 LYS A 194 TRP A 213 ARG A 217 GLU A 291
SITE 2 AC3 8 HIS A 451 HOH A 733 HOH A 759 HOH A 835
SITE 1 AC4 3 ARG A 208 ALA A 212 GLU A 353
SITE 1 AC5 6 LYS A 17 GLY A 21 ASP A 131 LEU A 134
SITE 2 AC5 6 GLY A 135 GLU A 158
CRYST1 94.244 94.244 142.345 90.00 90.00 120.00 P 61 6
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 0.010611 0.006126 0.000000 0.00000
SCALE2 0.000000 0.012252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007025 0.00000
ATOM 1 N LYS A 4 45.442 49.274 89.740 1.00 96.03 N
ANISOU 1 N LYS A 4 12529 11357 12599 -1883 2170 -2343 N
ATOM 2 CA LYS A 4 45.568 47.834 89.356 1.00 92.53 C
ANISOU 2 CA LYS A 4 12095 11047 12015 -1886 2011 -2052 C
ATOM 3 C LYS A 4 45.070 47.608 87.928 1.00 87.47 C
ANISOU 3 C LYS A 4 11112 10337 11787 -1697 1918 -1884 C
ATOM 4 O LYS A 4 43.864 47.546 87.680 1.00 94.83 O
ANISOU 4 O LYS A 4 11843 11202 12987 -1641 2136 -1945 O
ATOM 5 CB LYS A 4 44.809 46.942 90.348 1.00102.11 C
ANISOU 5 CB LYS A 4 13510 12352 12934 -2053 2297 -2092 C
ATOM 6 CG LYS A 4 45.053 45.445 90.182 1.00105.30 C
ANISOU 6 CG LYS A 4 14004 12873 13132 -2091 2115 -1801 C
ATOM 7 CD LYS A 4 44.007 44.766 89.307 1.00108.48 C
ANISOU 7 CD LYS A 4 14109 13247 13861 -1992 2228 -1692 C
ATOM 8 CE LYS A 4 44.047 43.251 89.453 1.00103.43 C
ANISOU 8 CE LYS A 4 13622 12704 12974 -2083 2147 -1458 C
ATOM 9 NZ LYS A 4 45.265 42.645 88.847 1.00103.32 N
ANISOU 9 NZ LYS A 4 13642 12733 12881 -2003 1708 -1214 N
ATOM 10 N SER A 5 46.015 47.496 86.999 1.00 75.74 N
ANISOU 10 N SER A 5 9566 8857 10353 -1613 1595 -1688 N
ATOM 11 CA SER A 5 45.713 47.259 85.590 1.00 65.32 C
ANISOU 11 CA SER A 5 8007 7473 9340 -1462 1465 -1512 C
ATOM 12 C SER A 5 45.911 45.782 85.263 1.00 63.61 C
ANISOU 12 C SER A 5 7820 7380 8967 -1475 1333 -1284 C
ATOM 13 O SER A 5 47.024 45.267 85.371 1.00 64.58 O
ANISOU 13 O SER A 5 8071 7590 8875 -1518 1134 -1174 O
ATOM 14 CB SER A 5 46.621 48.120 84.708 1.00 58.73 C
ANISOU 14 CB SER A 5 7118 6544 8652 -1391 1249 -1459 C
ATOM 15 OG SER A 5 46.461 47.808 83.334 1.00 57.67 O
ANISOU 15 OG SER A 5 6839 6354 8717 -1280 1106 -1270 O
ATOM 16 N GLU A 6 44.830 45.109 84.868 1.00 61.22 N
ANISOU 16 N GLU A 6 7381 7063 8817 -1434 1432 -1226 N
ATOM 17 CA AGLU A 6 44.888 43.690 84.512 0.50 63.11 C
ANISOU 17 CA AGLU A 6 7642 7390 8948 -1445 1319 -1022 C
ATOM 18 CA BGLU A 6 44.896 43.689 84.519 0.50 63.06 C
ANISOU 18 CA BGLU A 6 7637 7385 8939 -1446 1319 -1022 C
ATOM 19 C GLU A 6 45.804 43.457 83.309 1.00 56.71 C
ANISOU 19 C GLU A 6 6785 6572 8191 -1353 1036 -848 C
ATOM 20 O GLU A 6 46.624 42.542 83.315 1.00 53.88 O
ANISOU 20 O GLU A 6 6523 6295 7652 -1381 887 -722 O
ATOM 21 CB AGLU A 6 43.484 43.152 84.216 0.50 62.55 C
ANISOU 21 CB AGLU A 6 7391 7273 9101 -1423 1474 -1020 C
ATOM 22 CB BGLU A 6 43.493 43.124 84.256 0.50 62.42 C
ANISOU 22 CB BGLU A 6 7382 7262 9072 -1428 1478 -1020 C
ATOM 23 CG AGLU A 6 43.381 41.635 84.248 0.50 68.83 C
ANISOU 23 CG AGLU A 6 8257 8153 9742 -1488 1436 -853 C
ATOM 24 CG BGLU A 6 43.430 41.603 84.260 0.50 68.52 C
ANISOU 24 CG BGLU A 6 8228 8119 9689 -1490 1429 -847 C
ATOM 25 CD AGLU A 6 43.573 41.070 85.641 0.50 71.35 C
ANISOU 25 CD AGLU A 6 8848 8569 9693 -1668 1581 -875 C
ATOM 26 CD BGLU A 6 42.009 41.068 84.209 0.50 72.14 C
ANISOU 26 CD BGLU A 6 8512 8532 10367 -1516 1628 -879 C
ATOM 27 OE1AGLU A 6 43.309 41.794 86.622 0.50 74.75 O
ANISOU 27 OE1AGLU A 6 9375 9001 10027 -1761 1818 -1064 O
ATOM 28 OE1BGLU A 6 41.059 41.877 84.266 0.50 75.20 O
ANISOU 28 OE1BGLU A 6 8702 8827 11045 -1482 1819 -1056 O
ATOM 29 OE2AGLU A 6 43.984 39.898 85.755 0.50 70.12 O
ANISOU 29 OE2AGLU A 6 8837 8471 9335 -1723 1452 -704 O
ATOM 30 OE2BGLU A 6 41.840 39.834 84.112 0.50 62.82 O
ANISOU 30 OE2BGLU A 6 7369 7391 9109 -1570 1589 -738 O
ATOM 31 N ILE A 7 45.665 44.292 82.281 1.00 50.08 N
ANISOU 31 N ILE A 7 5811 5615 7605 -1250 970 -849 N
ATOM 32 CA ILE A 7 46.480 44.152 81.067 1.00 50.29 C
ANISOU 32 CA ILE A 7 5829 5620 7661 -1194 763 -703 C
ATOM 33 C ILE A 7 47.979 44.378 81.334 1.00 51.16 C
ANISOU 33 C ILE A 7 6038 5787 7614 -1248 668 -708 C
ATOM 34 O ILE A 7 48.829 43.694 80.757 1.00 51.17 O
ANISOU 34 O ILE A 7 6048 5830 7562 -1242 544 -601 O
ATOM 35 CB ILE A 7 45.961 45.051 79.913 1.00 55.61 C
ANISOU 35 CB ILE A 7 6405 6126 8598 -1103 700 -684 C
ATOM 36 CG1 ILE A 7 46.652 44.675 78.598 1.00 60.80 C
ANISOU 36 CG1 ILE A 7 7112 6768 9222 -1083 533 -523 C
ATOM 37 CG2 ILE A 7 46.137 46.536 80.226 1.00 60.83 C
ANISOU 37 CG2 ILE A 7 7070 6675 9367 -1101 752 -820 C
ATOM 38 CD1 ILE A 7 46.035 45.314 77.373 1.00 66.02 C
ANISOU 38 CD1 ILE A 7 7756 7254 10075 -1015 420 -454 C
ATOM 39 N ALA A 8 48.291 45.328 82.213 1.00 56.72 N
ANISOU 39 N ALA A 8 6799 6478 8276 -1302 729 -856 N
ATOM 40 CA ALA A 8 49.671 45.577 82.637 1.00 63.26 C
ANISOU 40 CA ALA A 8 7700 7349 8986 -1368 615 -891 C
ATOM 41 C ALA A 8 50.196 44.411 83.467 1.00 59.58 C
ANISOU 41 C ALA A 8 7341 7010 8287 -1427 512 -837 C
ATOM 42 O ALA A 8 51.343 43.992 83.316 1.00 51.22 O
ANISOU 42 O ALA A 8 6267 5984 7212 -1434 338 -782 O
ATOM 43 CB ALA A 8 49.748 46.859 83.446 1.00 55.09 C
ANISOU 43 CB ALA A 8 6722 6253 7956 -1424 691 -1081 C
ATOM 44 N HIS A 9 49.343 43.905 84.351 1.00 60.56 N
ANISOU 44 N HIS A 9 7574 7183 8252 -1477 625 -860 N
ATOM 45 CA HIS A 9 49.680 42.774 85.204 1.00 64.74 C
ANISOU 45 CA HIS A 9 8270 7801 8526 -1552 519 -781 C
ATOM 46 C HIS A 9 50.038 41.541 84.369 1.00 57.88 C
ANISOU 46 C HIS A 9 7320 6948 7725 -1480 365 -598 C
ATOM 47 O HIS A 9 51.042 40.881 84.639 1.00 54.17 O
ANISOU 47 O HIS A 9 6904 6503 7176 -1491 146 -531 O
ATOM 48 CB HIS A 9 48.511 42.482 86.148 1.00 71.74 C
ANISOU 48 CB HIS A 9 9303 8716 9239 -1646 746 -833 C
ATOM 49 CG HIS A 9 48.718 41.290 87.028 1.00 83.21 C
ANISOU 49 CG HIS A 9 10993 10232 10390 -1751 648 -720 C
ATOM 50 ND1 HIS A 9 47.934 40.160 86.939 1.00 75.79 N
ANISOU 50 ND1 HIS A 9 10072 9303 9422 -1771 732 -595 N
ATOM 51 CD2 HIS A 9 49.611 41.053 88.018 1.00 82.75 C
ANISOU 51 CD2 HIS A 9 11185 10205 10051 -1850 440 -703 C
ATOM 52 CE1 HIS A 9 48.337 39.277 87.835 1.00 74.37 C
ANISOU 52 CE1 HIS A 9 10162 9151 8944 -1881 596 -493 C
ATOM 53 NE2 HIS A 9 49.353 39.794 88.502 1.00 77.29 N
ANISOU 53 NE2 HIS A 9 10684 9532 9151 -1926 397 -550 N
ATOM 54 N ARG A 10 49.232 41.247 83.349 1.00 54.84 N
ANISOU 54 N ARG A 10 6800 6528 7508 -1402 456 -533 N
ATOM 55 CA ARG A 10 49.502 40.102 82.469 1.00 56.87 C
ANISOU 55 CA ARG A 10 6993 6784 7831 -1338 335 -389 C
ATOM 56 C ARG A 10 50.723 40.339 81.588 1.00 55.87 C
ANISOU 56 C ARG A 10 6762 6632 7833 -1283 211 -385 C
ATOM 57 O ARG A 10 51.480 39.408 81.314 1.00 50.99 O
ANISOU 57 O ARG A 10 6116 6018 7238 -1253 78 -318 O
ATOM 58 CB ARG A 10 48.294 39.771 81.582 1.00 53.45 C
ANISOU 58 CB ARG A 10 6464 6309 7536 -1287 440 -337 C
ATOM 59 CG ARG A 10 47.012 39.420 82.327 1.00 53.12 C
ANISOU 59 CG ARG A 10 6461 6279 7445 -1351 606 -353 C
ATOM 60 CD ARG A 10 47.169 38.255 83.291 1.00 60.01 C
ANISOU 60 CD ARG A 10 7507 7202 8090 -1444 569 -269 C
ATOM 61 NE ARG A 10 46.006 38.145 84.168 1.00 60.46 N
ANISOU 61 NE ARG A 10 7634 7269 8067 -1556 806 -319 N
ATOM 62 CZ ARG A 10 45.961 37.443 85.299 1.00 65.86 C
ANISOU 62 CZ ARG A 10 8552 7987 8486 -1696 851 -273 C
ATOM 63 NH1 ARG A 10 47.018 36.758 85.727 1.00 67.58 N
ANISOU 63 NH1 ARG A 10 8955 8219 8504 -1720 607 -159 N
ATOM 64 NH2 ARG A 10 44.842 37.426 86.014 1.00 73.54 N
ANISOU 64 NH2 ARG A 10 9577 8961 9403 -1822 1144 -346 N
ATOM 65 N PHE A 11 50.906 41.579 81.141 1.00 54.16 N
ANISOU 65 N PHE A 11 6486 6369 7726 -1279 274 -468 N
ATOM 66 CA PHE A 11 52.063 41.927 80.322 1.00 50.02 C
ANISOU 66 CA PHE A 11 5871 5809 7326 -1269 221 -482 C
ATOM 67 C PHE A 11 53.366 41.751 81.097 1.00 52.44 C
ANISOU 67 C PHE A 11 6157 6151 7619 -1306 63 -531 C
ATOM 68 O PHE A 11 54.354 41.256 80.552 1.00 50.31 O
ANISOU 68 O PHE A 11 5774 5867 7474 -1283 -11 -522 O
ATOM 69 CB PHE A 11 51.957 43.364 79.817 1.00 50.65 C
ANISOU 69 CB PHE A 11 5931 5804 7509 -1286 320 -548 C
ATOM 70 CG PHE A 11 53.066 43.757 78.887 1.00 51.25 C
ANISOU 70 CG PHE A 11 5939 5830 7706 -1314 327 -557 C
ATOM 71 CD1 PHE A 11 53.010 43.418 77.545 1.00 56.31 C
ANISOU 71 CD1 PHE A 11 6583 6425 8389 -1295 383 -477 C
ATOM 72 CD2 PHE A 11 54.172 44.458 79.354 1.00 54.98 C
ANISOU 72 CD2 PHE A 11 6354 6291 8244 -1383 291 -660 C
ATOM 73 CE1 PHE A 11 54.031 43.774 76.680 1.00 53.25 C
ANISOU 73 CE1 PHE A 11 6159 5985 8087 -1356 457 -500 C
ATOM 74 CE2 PHE A 11 55.197 44.816 78.495 1.00 54.12 C
ANISOU 74 CE2 PHE A 11 6158 6126 8278 -1436 349 -685 C
ATOM 75 CZ PHE A 11 55.126 44.473 77.154 1.00 54.05 C
ANISOU 75 CZ PHE A 11 6169 6076 8292 -1429 459 -606 C
ATOM 76 N ASN A 12 53.364 42.167 82.361 1.00 53.66 N
ANISOU 76 N ASN A 12 6417 6334 7636 -1370 6 -602 N
ATOM 77 CA ASN A 12 54.542 42.023 83.216 1.00 56.85 C
ANISOU 77 CA ASN A 12 6831 6755 8015 -1414 -221 -647 C
ATOM 78 C ASN A 12 54.847 40.562 83.530 1.00 57.69 C
ANISOU 78 C ASN A 12 6972 6879 8068 -1377 -419 -533 C
ATOM 79 O ASN A 12 56.008 40.154 83.513 1.00 63.31 O
ANISOU 79 O ASN A 12 7562 7560 8932 -1350 -627 -542 O
ATOM 80 CB ASN A 12 54.362 42.797 84.523 1.00 57.38 C
ANISOU 80 CB ASN A 12 7079 6840 7882 -1513 -248 -754 C
ATOM 81 CG ASN A 12 54.397 44.300 84.323 1.00 62.47 C
ANISOU 81 CG ASN A 12 7672 7429 8635 -1550 -116 -894 C
ATOM 82 OD1 ASN A 12 55.043 44.807 83.405 1.00 62.32 O
ANISOU 82 OD1 ASN A 12 7483 7354 8842 -1532 -91 -913 O
ATOM 83 ND2 ASN A 12 53.701 45.024 85.191 1.00 71.14 N
ANISOU 83 ND2 ASN A 12 8931 8526 9574 -1615 -10 -1004 N
ATOM 84 N ASP A 13 53.807 39.784 83.820 1.00 58.86 N
ANISOU 84 N ASP A 13 7268 7055 8042 -1379 -356 -434 N
ATOM 85 CA ASP A 13 53.978 38.375 84.181 1.00 59.93 C
ANISOU 85 CA ASP A 13 7483 7177 8109 -1358 -547 -305 C
ATOM 86 C ASP A 13 54.427 37.519 83.006 1.00 53.22 C
ANISOU 86 C ASP A 13 6435 6278 7506 -1246 -577 -252 C
ATOM 87 O ASP A 13 55.315 36.680 83.146 1.00 59.81 O
ANISOU 87 O ASP A 13 7215 7060 8451 -1197 -812 -215 O
ATOM 88 CB ASP A 13 52.676 37.799 84.745 1.00 66.10 C
ANISOU 88 CB ASP A 13 8477 7987 8652 -1421 -417 -218 C
ATOM 89 CG ASP A 13 52.372 38.296 86.146 1.00 66.74 C
ANISOU 89 CG ASP A 13 8827 8104 8428 -1562 -403 -270 C
ATOM 90 OD1 ASP A 13 53.173 39.076 86.700 1.00 60.69 O
ANISOU 90 OD1 ASP A 13 8097 7340 7623 -1604 -540 -370 O
ATOM 91 OD2 ASP A 13 51.324 37.905 86.700 1.00 72.66 O
ANISOU 91 OD2 ASP A 13 9760 8874 8974 -1650 -238 -225 O
ATOM 92 N LEU A 14 53.798 37.725 81.854 1.00 55.33 N
ANISOU 92 N LEU A 14 6609 6547 7867 -1207 -352 -258 N
ATOM 93 CA LEU A 14 54.035 36.874 80.691 1.00 59.23 C
ANISOU 93 CA LEU A 14 6978 6993 8534 -1124 -331 -224 C
ATOM 94 C LEU A 14 55.268 37.263 79.889 1.00 55.12 C
ANISOU 94 C LEU A 14 6255 6435 8252 -1095 -315 -329 C
ATOM 95 O LEU A 14 55.963 36.396 79.356 1.00 53.98 O
ANISOU 95 O LEU A 14 5990 6236 8284 -1030 -368 -343 O
ATOM 96 CB LEU A 14 52.804 36.877 79.782 1.00 59.11 C
ANISOU 96 CB LEU A 14 6995 6980 8486 -1115 -134 -182 C
ATOM 97 CG LEU A 14 51.581 36.207 80.409 1.00 59.61 C
ANISOU 97 CG LEU A 14 7194 7059 8396 -1147 -118 -88 C
ATOM 98 CD1 LEU A 14 50.345 36.444 79.557 1.00 55.86 C
ANISOU 98 CD1 LEU A 14 6699 6571 7953 -1141 43 -77 C
ATOM 99 CD2 LEU A 14 51.827 34.715 80.597 1.00 60.75 C
ANISOU 99 CD2 LEU A 14 7380 7156 8545 -1117 -272 9 C
ATOM 100 N GLY A 15 55.533 38.562 79.804 1.00 56.81 N
ANISOU 100 N GLY A 15 6429 6663 8495 -1151 -219 -419 N
ATOM 101 CA GLY A 15 56.588 39.076 78.941 1.00 50.92 C
ANISOU 101 CA GLY A 15 5503 5874 7971 -1166 -124 -524 C
ATOM 102 C GLY A 15 55.975 39.425 77.602 1.00 60.57 C
ANISOU 102 C GLY A 15 6779 7072 9162 -1183 119 -504 C
ATOM 103 O GLY A 15 54.943 38.867 77.218 1.00 55.66 O
ANISOU 103 O GLY A 15 6271 6456 8421 -1147 152 -413 O
ATOM 104 N GLU A 16 56.613 40.346 76.889 1.00 49.99 N
ANISOU 104 N GLU A 16 5375 5691 7929 -1253 272 -583 N
ATOM 105 CA GLU A 16 56.065 40.873 75.642 1.00 56.05 C
ANISOU 105 CA GLU A 16 6267 6411 8620 -1300 471 -544 C
ATOM 106 C GLU A 16 55.850 39.794 74.584 1.00 57.46 C
ANISOU 106 C GLU A 16 6498 6570 8765 -1265 547 -509 C
ATOM 107 O GLU A 16 54.829 39.791 73.896 1.00 49.83 O
ANISOU 107 O GLU A 16 5703 5579 7650 -1265 576 -422 O
ATOM 108 CB GLU A 16 56.978 41.968 75.087 1.00 62.89 C
ANISOU 108 CB GLU A 16 7079 7214 9602 -1417 636 -631 C
ATOM 109 CG GLU A 16 56.519 42.549 73.756 1.00 66.55 C
ANISOU 109 CG GLU A 16 7739 7598 9949 -1496 822 -570 C
ATOM 110 CD GLU A 16 57.351 43.738 73.307 1.00 69.26 C
ANISOU 110 CD GLU A 16 8076 7858 10382 -1646 999 -633 C
ATOM 111 OE1 GLU A 16 58.364 44.056 73.966 1.00 75.27 O
ANISOU 111 OE1 GLU A 16 8628 8629 11342 -1685 992 -751 O
ATOM 112 OE2 GLU A 16 56.993 44.359 72.285 1.00 71.70 O
ANISOU 112 OE2 GLU A 16 8604 8075 10566 -1736 1126 -560 O
ATOM 113 N LYS A 17 56.810 38.885 74.453 1.00 62.51 N
ANISOU 113 N LYS A 17 6983 7200 9569 -1233 560 -593 N
ATOM 114 CA LYS A 17 56.747 37.870 73.407 1.00 56.15 C
ANISOU 114 CA LYS A 17 6226 6357 8751 -1210 666 -605 C
ATOM 115 C LYS A 17 55.565 36.924 73.583 1.00 58.99 C
ANISOU 115 C LYS A 17 6712 6736 8968 -1128 517 -486 C
ATOM 116 O LYS A 17 54.774 36.741 72.658 1.00 58.77 O
ANISOU 116 O LYS A 17 6856 6679 8794 -1149 578 -435 O
ATOM 117 CB LYS A 17 58.066 37.106 73.334 1.00 59.25 C
ANISOU 117 CB LYS A 17 6376 6709 9426 -1176 716 -756 C
ATOM 118 CG LYS A 17 59.169 37.955 72.729 1.00 75.54 C
ANISOU 118 CG LYS A 17 8319 8733 11652 -1297 971 -901 C
ATOM 119 CD LYS A 17 60.416 37.152 72.407 1.00 87.40 C
ANISOU 119 CD LYS A 17 9545 10169 13493 -1268 1093 -1093 C
ATOM 120 CE LYS A 17 61.352 37.935 71.499 1.00 94.71 C
ANISOU 120 CE LYS A 17 10395 11046 14546 -1434 1464 -1250 C
ATOM 121 NZ LYS A 17 60.793 38.149 70.131 1.00101.45 N
ANISOU 121 NZ LYS A 17 11584 11876 15088 -1564 1760 -1216 N
ATOM 122 N HIS A 18 55.430 36.338 74.765 1.00 50.60 N
ANISOU 122 N HIS A 18 5584 5706 7937 -1055 311 -439 N
ATOM 123 CA HIS A 18 54.306 35.447 75.024 1.00 51.14 C
ANISOU 123 CA HIS A 18 5765 5781 7885 -1006 197 -326 C
ATOM 124 C HIS A 18 52.982 36.199 75.080 1.00 49.38 C
ANISOU 124 C HIS A 18 5678 5590 7496 -1044 210 -238 C
ATOM 125 O HIS A 18 51.955 35.679 74.644 1.00 46.54 O
ANISOU 125 O HIS A 18 5409 5209 7064 -1034 192 -171 O
ATOM 126 CB HIS A 18 54.536 34.626 76.292 1.00 52.39 C
ANISOU 126 CB HIS A 18 5869 5944 8092 -950 -16 -281 C
ATOM 127 CG HIS A 18 55.575 33.563 76.124 1.00 58.46 C
ANISOU 127 CG HIS A 18 6499 6632 9082 -875 -87 -350 C
ATOM 128 ND1 HIS A 18 56.045 32.802 77.172 1.00 58.84 N
ANISOU 128 ND1 HIS A 18 6496 6637 9225 -815 -336 -309 N
ATOM 129 CD2 HIS A 18 56.247 33.146 75.025 1.00 56.83 C
ANISOU 129 CD2 HIS A 18 6197 6359 9038 -852 61 -471 C
ATOM 130 CE1 HIS A 18 56.953 31.953 76.723 1.00 63.03 C
ANISOU 130 CE1 HIS A 18 6867 7063 10020 -733 -364 -402 C
ATOM 131 NE2 HIS A 18 57.094 32.142 75.423 1.00 61.31 N
ANISOU 131 NE2 HIS A 18 6609 6836 9851 -757 -94 -519 N
ATOM 132 N PHE A 19 53.010 37.426 75.592 1.00 48.77 N
ANISOU 132 N PHE A 19 5593 5541 7397 -1086 233 -257 N
ATOM 133 CA PHE A 19 51.820 38.270 75.613 1.00 47.90 C
ANISOU 133 CA PHE A 19 5571 5427 7203 -1107 255 -208 C
ATOM 134 C PHE A 19 51.273 38.438 74.200 1.00 52.65 C
ANISOU 134 C PHE A 19 6279 5956 7769 -1123 308 -171 C
ATOM 135 O PHE A 19 50.099 38.178 73.946 1.00 45.11 O
ANISOU 135 O PHE A 19 5381 4974 6786 -1102 246 -106 O
ATOM 136 CB PHE A 19 52.148 39.635 76.219 1.00 52.07 C
ANISOU 136 CB PHE A 19 6073 5962 7749 -1150 289 -267 C
ATOM 137 CG PHE A 19 50.986 40.587 76.247 1.00 46.23 C
ANISOU 137 CG PHE A 19 5393 5182 6991 -1154 315 -246 C
ATOM 138 CD1 PHE A 19 50.640 41.317 75.116 1.00 45.95 C
ANISOU 138 CD1 PHE A 19 5435 5051 6974 -1170 347 -212 C
ATOM 139 CD2 PHE A 19 50.247 40.766 77.407 1.00 48.59 C
ANISOU 139 CD2 PHE A 19 5682 5518 7263 -1149 307 -267 C
ATOM 140 CE1 PHE A 19 49.573 42.197 75.140 1.00 46.77 C
ANISOU 140 CE1 PHE A 19 5563 5078 7130 -1149 324 -197 C
ATOM 141 CE2 PHE A 19 49.178 41.647 77.438 1.00 47.93 C
ANISOU 141 CE2 PHE A 19 5601 5372 7237 -1137 350 -284 C
ATOM 142 CZ PHE A 19 48.842 42.365 76.303 1.00 51.46 C
ANISOU 142 CZ PHE A 19 6082 5705 7763 -1123 336 -248 C
ATOM 143 N LYS A 20 52.136 38.871 73.285 1.00 44.87 N
ANISOU 143 N LYS A 20 5333 4928 6787 -1178 416 -217 N
ATOM 144 CA LYS A 20 51.744 39.071 71.888 1.00 52.37 C
ANISOU 144 CA LYS A 20 6468 5794 7637 -1228 459 -175 C
ATOM 145 C LYS A 20 51.281 37.783 71.210 1.00 59.40 C
ANISOU 145 C LYS A 20 7435 6669 8467 -1201 409 -152 C
ATOM 146 O LYS A 20 50.289 37.788 70.479 1.00 49.96 O
ANISOU 146 O LYS A 20 6389 5409 7184 -1211 314 -80 O
ATOM 147 CB LYS A 20 52.893 39.686 71.089 1.00 56.63 C
ANISOU 147 CB LYS A 20 7066 6288 8162 -1333 647 -241 C
ATOM 148 CG LYS A 20 52.973 41.195 71.216 1.00 64.72 C
ANISOU 148 CG LYS A 20 8130 7260 9200 -1398 679 -223 C
ATOM 149 CD LYS A 20 54.234 41.742 70.570 1.00 68.96 C
ANISOU 149 CD LYS A 20 8694 7753 9753 -1532 905 -300 C
ATOM 150 CE LYS A 20 54.047 43.178 70.115 1.00 88.20 C
ANISOU 150 CE LYS A 20 11313 10071 12128 -1635 934 -230 C
ATOM 151 NZ LYS A 20 53.437 43.256 68.763 1.00 95.98 N
ANISOU 151 NZ LYS A 20 12633 10942 12893 -1712 923 -118 N
ATOM 152 N GLY A 21 52.004 36.692 71.447 1.00 52.15 N
ANISOU 152 N GLY A 21 6411 5786 7619 -1164 445 -220 N
ATOM 153 CA GLY A 21 51.656 35.400 70.865 1.00 54.51 C
ANISOU 153 CA GLY A 21 6774 6050 7886 -1137 404 -222 C
ATOM 154 C GLY A 21 50.266 34.951 71.275 1.00 48.72 C
ANISOU 154 C GLY A 21 6054 5318 7141 -1095 227 -120 C
ATOM 155 O GLY A 21 49.459 34.565 70.432 1.00 47.79 O
ANISOU 155 O GLY A 21 6068 5140 6950 -1114 152 -87 O
ATOM 156 N LEU A 22 49.986 35.021 72.573 1.00 46.26 N
ANISOU 156 N LEU A 22 5613 5065 6899 -1057 166 -82 N
ATOM 157 CA LEU A 22 48.682 34.627 73.100 1.00 46.84 C
ANISOU 157 CA LEU A 22 5667 5139 6993 -1043 62 -6 C
ATOM 158 C LEU A 22 47.560 35.538 72.612 1.00 50.81 C
ANISOU 158 C LEU A 22 6212 5593 7500 -1060 9 32 C
ATOM 159 O LEU A 22 46.463 35.063 72.312 1.00 51.98 O
ANISOU 159 O LEU A 22 6364 5693 7695 -1059 -94 72 O
ATOM 160 CB LEU A 22 48.703 34.605 74.627 1.00 43.93 C
ANISOU 160 CB LEU A 22 5202 4840 6651 -1035 62 11 C
ATOM 161 CG LEU A 22 49.581 33.510 75.228 1.00 46.96 C
ANISOU 161 CG LEU A 22 5558 5229 7055 -1009 16 11 C
ATOM 162 CD1 LEU A 22 49.847 33.799 76.693 1.00 46.46 C
ANISOU 162 CD1 LEU A 22 5472 5227 6953 -1026 -11 29 C
ATOM 163 CD2 LEU A 22 48.952 32.134 75.049 1.00 49.82 C
ANISOU 163 CD2 LEU A 22 5958 5532 7441 -1003 -54 66 C
ATOM 164 N VAL A 23 47.832 36.838 72.534 1.00 51.45 N
ANISOU 164 N VAL A 23 6312 5666 7571 -1074 54 18 N
ATOM 165 CA VAL A 23 46.842 37.787 72.029 1.00 54.67 C
ANISOU 165 CA VAL A 23 6763 5984 8024 -1074 -39 59 C
ATOM 166 C VAL A 23 46.546 37.512 70.555 1.00 54.79 C
ANISOU 166 C VAL A 23 6973 5900 7946 -1106 -159 104 C
ATOM 167 O VAL A 23 45.389 37.577 70.130 1.00 50.80 O
ANISOU 167 O VAL A 23 6481 5304 7515 -1091 -340 154 O
ATOM 168 CB VAL A 23 47.283 39.256 72.218 1.00 52.35 C
ANISOU 168 CB VAL A 23 6479 5666 7744 -1087 24 38 C
ATOM 169 CG1 VAL A 23 46.313 40.203 71.525 1.00 52.65 C
ANISOU 169 CG1 VAL A 23 6589 5560 7855 -1075 -122 95 C
ATOM 170 CG2 VAL A 23 47.349 39.600 73.697 1.00 51.42 C
ANISOU 170 CG2 VAL A 23 6204 5631 7704 -1066 112 -23 C
ATOM 171 N LEU A 24 47.585 37.203 69.782 1.00 49.24 N
ANISOU 171 N LEU A 24 6420 5200 7090 -1161 -59 71 N
ATOM 172 CA LEU A 24 47.400 36.845 68.378 1.00 51.26 C
ANISOU 172 CA LEU A 24 6929 5363 7185 -1223 -141 93 C
ATOM 173 C LEU A 24 46.547 35.587 68.244 1.00 49.35 C
ANISOU 173 C LEU A 24 6661 5104 6985 -1196 -287 98 C
ATOM 174 O LEU A 24 45.629 35.531 67.421 1.00 47.63 O
ANISOU 174 O LEU A 24 6582 4785 6729 -1220 -499 148 O
ATOM 175 CB LEU A 24 48.743 36.626 67.681 1.00 52.97 C
ANISOU 175 CB LEU A 24 7289 5593 7244 -1304 81 9 C
ATOM 176 CG LEU A 24 48.649 36.125 66.234 1.00 53.87 C
ANISOU 176 CG LEU A 24 7722 5616 7130 -1398 52 -3 C
ATOM 177 CD1 LEU A 24 47.820 37.064 65.370 1.00 53.37 C
ANISOU 177 CD1 LEU A 24 7930 5423 6924 -1463 -162 120 C
ATOM 178 CD2 LEU A 24 50.037 35.939 65.643 1.00 58.04 C
ANISOU 178 CD2 LEU A 24 8357 6157 7539 -1491 364 -131 C
ATOM 179 N VAL A 25 46.858 34.577 69.048 1.00 52.07 N
ANISOU 179 N VAL A 25 6841 5527 7417 -1153 -203 51 N
ATOM 180 CA VAL A 25 46.094 33.335 69.024 1.00 49.53 C
ANISOU 180 CA VAL A 25 6485 5174 7159 -1140 -322 56 C
ATOM 181 C VAL A 25 44.634 33.612 69.364 1.00 46.16 C
ANISOU 181 C VAL A 25 5937 4707 6895 -1123 -500 122 C
ATOM 182 O VAL A 25 43.735 33.178 68.646 1.00 57.13 O
ANISOU 182 O VAL A 25 7388 6005 8313 -1147 -694 141 O
ATOM 183 CB VAL A 25 46.681 32.282 69.986 1.00 46.71 C
ANISOU 183 CB VAL A 25 5983 4879 6886 -1100 -220 22 C
ATOM 184 CG1 VAL A 25 45.694 31.148 70.226 1.00 50.74 C
ANISOU 184 CG1 VAL A 25 6434 5343 7500 -1103 -341 55 C
ATOM 185 CG2 VAL A 25 47.986 31.736 69.425 1.00 49.63 C
ANISOU 185 CG2 VAL A 25 6436 5239 7182 -1103 -82 -79 C
ATOM 186 N ALA A 26 44.404 34.351 70.445 1.00 49.12 N
ANISOU 186 N ALA A 26 6129 5136 7396 -1088 -431 136 N
ATOM 187 CA ALA A 26 43.041 34.641 70.895 1.00 52.37 C
ANISOU 187 CA ALA A 26 6364 5504 8030 -1071 -532 157 C
ATOM 188 C ALA A 26 42.211 35.315 69.804 1.00 57.80 C
ANISOU 188 C ALA A 26 7132 6052 8778 -1066 -782 193 C
ATOM 189 O ALA A 26 41.063 34.938 69.563 1.00 57.36 O
ANISOU 189 O ALA A 26 6977 5910 8908 -1067 -969 200 O
ATOM 190 CB ALA A 26 43.065 35.507 72.146 1.00 54.00 C
ANISOU 190 CB ALA A 26 6409 5781 8329 -1045 -372 130 C
ATOM 191 N PHE A 27 42.806 36.303 69.144 1.00 50.87 N
ANISOU 191 N PHE A 27 6441 5133 7754 -1072 -805 220 N
ATOM 192 CA PHE A 27 42.137 37.053 68.080 1.00 51.78 C
ANISOU 192 CA PHE A 27 6708 5084 7883 -1077 -1086 285 C
ATOM 193 C PHE A 27 41.880 36.195 66.844 1.00 57.00 C
ANISOU 193 C PHE A 27 7610 5662 8386 -1142 -1304 310 C
ATOM 194 O PHE A 27 40.828 36.311 66.210 1.00 50.48 O
ANISOU 194 O PHE A 27 6810 4690 7679 -1137 -1634 356 O
ATOM 195 CB PHE A 27 42.965 38.294 67.720 1.00 64.75 C
ANISOU 195 CB PHE A 27 8547 6691 9365 -1101 -1023 324 C
ATOM 196 CG PHE A 27 42.863 39.410 68.732 1.00 69.32 C
ANISOU 196 CG PHE A 27 8911 7275 10151 -1033 -925 300 C
ATOM 197 CD1 PHE A 27 42.310 39.194 69.996 1.00 78.75 C
ANISOU 197 CD1 PHE A 27 9784 8548 11589 -973 -808 224 C
ATOM 198 CD2 PHE A 27 43.339 40.677 68.428 1.00 71.70 C
ANISOU 198 CD2 PHE A 27 9363 7491 10389 -1050 -924 343 C
ATOM 199 CE1 PHE A 27 42.220 40.219 70.916 1.00 82.61 C
ANISOU 199 CE1 PHE A 27 10108 9034 12244 -924 -692 169 C
ATOM 200 CE2 PHE A 27 43.254 41.708 69.353 1.00 64.16 C
ANISOU 200 CE2 PHE A 27 8221 6522 9634 -990 -834 298 C
ATOM 201 CZ PHE A 27 42.693 41.478 70.597 1.00 75.25 C
ANISOU 201 CZ PHE A 27 9308 8012 11272 -923 -715 199 C
ATOM 202 N SER A 28 42.836 35.333 66.512 1.00 50.69 N
ANISOU 202 N SER A 28 6979 4939 7342 -1201 -1134 263 N
ATOM 203 CA SER A 28 42.684 34.397 65.399 1.00 51.96 C
ANISOU 203 CA SER A 28 7391 5027 7326 -1276 -1287 246 C
ATOM 204 C SER A 28 41.516 33.427 65.619 1.00 54.66 C
ANISOU 204 C SER A 28 7534 5326 7909 -1255 -1487 231 C
ATOM 205 O SER A 28 40.786 33.099 64.684 1.00 58.11 O
ANISOU 205 O SER A 28 8128 5637 8315 -1303 -1790 246 O
ATOM 206 CB SER A 28 43.973 33.596 65.211 1.00 55.14 C
ANISOU 206 CB SER A 28 7929 5515 7506 -1324 -998 151 C
ATOM 207 OG SER A 28 45.047 34.439 64.834 1.00 56.20 O
ANISOU 207 OG SER A 28 8254 5669 7431 -1377 -799 145 O
ATOM 208 N GLN A 29 41.356 32.972 66.857 1.00 51.32 N
ANISOU 208 N GLN A 29 6788 4997 7715 -1203 -1320 202 N
ATOM 209 CA GLN A 29 40.293 32.034 67.217 1.00 52.23 C
ANISOU 209 CA GLN A 29 6687 5073 8086 -1210 -1435 185 C
ATOM 210 C GLN A 29 38.907 32.675 67.209 1.00 63.28 C
ANISOU 210 C GLN A 29 7878 6358 9807 -1182 -1698 211 C
ATOM 211 O GLN A 29 37.927 32.041 66.806 1.00 59.94 O
ANISOU 211 O GLN A 29 7379 5829 9564 -1217 -1943 196 O
ATOM 212 CB GLN A 29 40.575 31.435 68.595 1.00 49.81 C
ANISOU 212 CB GLN A 29 6151 4886 7888 -1194 -1150 163 C
ATOM 213 CG GLN A 29 41.807 30.545 68.615 1.00 51.32 C
ANISOU 213 CG GLN A 29 6492 5142 7867 -1206 -968 129 C
ATOM 214 CD GLN A 29 42.102 29.959 69.980 1.00 59.09 C
ANISOU 214 CD GLN A 29 7303 6211 8938 -1194 -761 139 C
ATOM 215 OE1 GLN A 29 41.881 30.601 71.009 1.00 48.00 O
ANISOU 215 OE1 GLN A 29 5733 4873 7631 -1179 -647 163 O
ATOM 216 NE2 GLN A 29 42.613 28.731 69.996 1.00 49.07 N
ANISOU 216 NE2 GLN A 29 6101 4920 7625 -1208 -719 118 N
ATOM 217 N TYR A 30 38.827 33.923 67.666 1.00 60.63 N
ANISOU 217 N TYR A 30 7424 6026 9586 -1117 -1654 232 N
ATOM 218 CA TYR A 30 37.560 34.660 67.682 1.00 67.90 C
ANISOU 218 CA TYR A 30 8105 6809 10885 -1063 -1897 234 C
ATOM 219 C TYR A 30 37.116 35.043 66.266 1.00 67.34 C
ANISOU 219 C TYR A 30 8281 6547 10757 -1073 -2354 302 C
ATOM 220 O TYR A 30 35.962 34.822 65.890 1.00 69.93 O
ANISOU 220 O TYR A 30 8459 6730 11383 -1068 -2689 293 O
ATOM 221 CB TYR A 30 37.672 35.911 68.561 1.00 67.87 C
ANISOU 221 CB TYR A 30 7928 6836 11022 -985 -1710 216 C
ATOM 222 CG TYR A 30 37.420 35.669 70.037 1.00 66.58 C
ANISOU 222 CG TYR A 30 7438 6790 11071 -983 -1368 129 C
ATOM 223 CD1 TYR A 30 38.180 34.752 70.759 1.00 76.17 C
ANISOU 223 CD1 TYR A 30 8704 8165 12072 -1043 -1079 119 C
ATOM 224 CD2 TYR A 30 36.429 36.375 70.716 1.00 87.78 C
ANISOU 224 CD2 TYR A 30 9783 9402 14168 -929 -1333 48 C
ATOM 225 CE1 TYR A 30 37.953 34.537 72.110 1.00 75.72 C
ANISOU 225 CE1 TYR A 30 8429 8199 12140 -1073 -781 60 C
ATOM 226 CE2 TYR A 30 36.196 36.167 72.066 1.00 80.07 C
ANISOU 226 CE2 TYR A 30 8563 8529 13331 -964 -972 -46 C
ATOM 227 CZ TYR A 30 36.958 35.248 72.757 1.00 80.71 C
ANISOU 227 CZ TYR A 30 8764 8775 13129 -1048 -705 -27 C
ATOM 228 OH TYR A 30 36.723 35.045 74.096 1.00 70.43 O
ANISOU 228 OH TYR A 30 7297 7560 11903 -1112 -362 -101 O
ATOM 229 N LEU A 31 38.039 35.615 65.494 1.00 72.11 N
ANISOU 229 N LEU A 31 9277 7142 10980 -1103 -2372 371 N
ATOM 230 CA LEU A 31 37.778 36.018 64.108 1.00 75.71 C
ANISOU 230 CA LEU A 31 10095 7410 11260 -1149 -2794 462 C
ATOM 231 C LEU A 31 38.621 35.183 63.145 1.00 77.59 C
ANISOU 231 C LEU A 31 10778 7688 11013 -1278 -2744 454 C
ATOM 232 O LEU A 31 39.748 35.554 62.803 1.00 74.07 O
ANISOU 232 O LEU A 31 10639 7300 10203 -1338 -2520 474 O
ATOM 233 CB LEU A 31 38.091 37.504 63.921 1.00 79.26 C
ANISOU 233 CB LEU A 31 10696 7769 11649 -1112 -2850 556 C
ATOM 234 CG LEU A 31 37.375 38.493 64.842 1.00 82.93 C
ANISOU 234 CG LEU A 31 10749 8168 12591 -975 -2867 536 C
ATOM 235 CD1 LEU A 31 37.887 39.902 64.597 1.00 83.97 C
ANISOU 235 CD1 LEU A 31 11097 8198 12608 -956 -2896 631 C
ATOM 236 CD2 LEU A 31 35.872 38.432 64.643 1.00 82.74 C
ANISOU 236 CD2 LEU A 31 10449 7948 13040 -907 -3304 523 C
ATOM 237 N GLN A 32 38.055 34.065 62.698 1.00 79.38 N
ANISOU 237 N GLN A 32 11028 7870 11263 -1331 -2939 405 N
ATOM 238 CA GLN A 32 38.797 33.052 61.942 1.00 70.15 C
ANISOU 238 CA GLN A 32 10219 6742 9695 -1448 -2832 341 C
ATOM 239 C GLN A 32 38.993 33.372 60.453 1.00 76.61 C
ANISOU 239 C GLN A 32 11617 7418 10071 -1575 -3100 397 C
ATOM 240 O GLN A 32 39.791 32.709 59.786 1.00 74.39 O
ANISOU 240 O GLN A 32 11688 7174 9404 -1688 -2921 319 O
ATOM 241 CB GLN A 32 38.110 31.686 62.094 1.00 68.55 C
ANISOU 241 CB GLN A 32 9822 6527 9698 -1468 -2925 251 C
ATOM 242 CG GLN A 32 38.042 31.189 63.533 1.00 64.78 C
ANISOU 242 CG GLN A 32 8871 6184 9559 -1392 -2607 203 C
ATOM 243 CD GLN A 32 37.117 29.998 63.713 1.00 65.55 C
ANISOU 243 CD GLN A 32 8746 6224 9937 -1429 -2744 141 C
ATOM 244 OE1 GLN A 32 36.020 30.130 64.257 1.00 64.84 O
ANISOU 244 OE1 GLN A 32 8285 6077 10273 -1396 -2880 145 O
ATOM 245 NE2 GLN A 32 37.554 28.829 63.257 1.00 59.65 N
ANISOU 245 NE2 GLN A 32 8209 5473 8983 -1505 -2690 66 N
ATOM 246 N GLN A 33 38.281 34.375 59.935 1.00 75.36 N
ANISOU 246 N GLN A 33 11579 7084 9970 -1565 -3521 525 N
ATOM 247 CA GLN A 33 38.317 34.694 58.500 1.00 85.18 C
ANISOU 247 CA GLN A 33 13441 8157 10768 -1710 -3860 611 C
ATOM 248 C GLN A 33 39.238 35.869 58.140 1.00 85.57 C
ANISOU 248 C GLN A 33 13860 8188 10465 -1776 -3681 719 C
ATOM 249 O GLN A 33 39.594 36.035 56.972 1.00 92.72 O
ANISOU 249 O GLN A 33 15369 8987 10872 -1949 -3797 776 O
ATOM 250 CB GLN A 33 36.903 34.984 57.975 1.00 96.97 C
ANISOU 250 CB GLN A 33 14917 9404 12524 -1680 -4557 706 C
ATOM 251 CG GLN A 33 35.834 33.977 58.384 1.00 97.14 C
ANISOU 251 CG GLN A 33 14494 9410 13007 -1620 -4768 602 C
ATOM 252 CD GLN A 33 35.814 32.737 57.510 1.00 99.57 C
ANISOU 252 CD GLN A 33 15137 9686 13007 -1770 -4907 506 C
ATOM 253 OE1 GLN A 33 36.857 32.244 57.081 1.00110.47 O
ANISOU 253 OE1 GLN A 33 16902 11166 13903 -1885 -4563 434 O
ATOM 254 NE2 GLN A 33 34.618 32.223 57.246 1.00 93.94 N
ANISOU 254 NE2 GLN A 33 14259 8820 12613 -1770 -5407 480 N
ATOM 255 N CYS A 34 39.612 36.683 59.128 1.00 86.51 N
ANISOU 255 N CYS A 34 13649 8399 10824 -1663 -3395 743 N
ATOM 256 CA CYS A 34 40.441 37.869 58.883 1.00 89.35 C
ANISOU 256 CA CYS A 34 14305 8724 10921 -1728 -3227 847 C
ATOM 257 C CYS A 34 41.855 37.495 58.435 1.00 83.26 C
ANISOU 257 C CYS A 34 13888 8082 9663 -1895 -2731 758 C
ATOM 258 O CYS A 34 42.389 36.478 58.871 1.00 80.65 O
ANISOU 258 O CYS A 34 13359 7927 9359 -1879 -2384 596 O
ATOM 259 CB CYS A 34 40.524 38.742 60.139 1.00 91.46 C
ANISOU 259 CB CYS A 34 14098 9063 11590 -1569 -3017 854 C
ATOM 260 SG CYS A 34 39.017 39.663 60.512 1.00103.47 S
ANISOU 260 SG CYS A 34 15272 10363 13681 -1390 -3549 954 S
ATOM 261 N PRO A 35 42.466 38.323 57.566 1.00 84.40 N
ANISOU 261 N PRO A 35 14556 8120 9390 -2062 -2689 861 N
ATOM 262 CA PRO A 35 43.831 38.056 57.110 1.00 83.19 C
ANISOU 262 CA PRO A 35 14721 8074 8813 -2243 -2161 751 C
ATOM 263 C PRO A 35 44.874 38.303 58.201 1.00 78.46 C
ANISOU 263 C PRO A 35 13704 7668 8438 -2163 -1627 653 C
ATOM 264 O PRO A 35 44.610 39.030 59.162 1.00 73.52 O
ANISOU 264 O PRO A 35 12692 7062 8181 -2012 -1678 715 O
ATOM 265 CB PRO A 35 44.015 39.038 55.949 1.00 86.15 C
ANISOU 265 CB PRO A 35 15769 8246 8718 -2459 -2304 921 C
ATOM 266 CG PRO A 35 43.085 40.158 56.250 1.00 89.52 C
ANISOU 266 CG PRO A 35 16065 8496 9452 -2329 -2782 1130 C
ATOM 267 CD PRO A 35 41.908 39.544 56.953 1.00 86.94 C
ANISOU 267 CD PRO A 35 15208 8191 9634 -2102 -3131 1083 C
ATOM 268 N PHE A 36 46.048 37.699 58.032 1.00 74.38 N
ANISOU 268 N PHE A 36 13268 7277 7716 -2270 -1132 483 N
ATOM 269 CA PHE A 36 47.125 37.763 59.024 1.00 77.43 C
ANISOU 269 CA PHE A 36 13248 7839 8332 -2200 -655 362 C
ATOM 270 C PHE A 36 47.541 39.193 59.384 1.00 72.02 C
ANISOU 270 C PHE A 36 12534 7118 7714 -2220 -558 476 C
ATOM 271 O PHE A 36 47.781 39.494 60.554 1.00 73.01 O
ANISOU 271 O PHE A 36 12202 7351 8187 -2078 -433 445 O
ATOM 272 CB PHE A 36 48.341 36.976 58.526 1.00 78.74 C