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2rku.pdb
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HEADER TRANSFERASE 17-OCT-07 2RKU
TITLE STRUCTURE OF PLK1 IN COMPLEX WITH BI2536
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 5 13, STPK13;
COMPND 6 EC: 2.7.11.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLK1, PLK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS STRUCTURE OF PLK1, SELECTIVITY RESIDUES, KINASE, POLO-LIKE KINASE,
KEYWDS 2 STRUCTURE BASED DRUG DESIGN, ATP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 3 NUCLEUS, PHOSPHORYLATION, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 4 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-H.DING,M.KOTHE,D.KOHLS,S.LOW
REVDAT 5 20-OCT-21 2RKU 1 REMARK SEQADV
REVDAT 4 25-OCT-17 2RKU 1 REMARK
REVDAT 3 13-JUL-11 2RKU 1 VERSN
REVDAT 2 24-FEB-09 2RKU 1 VERSN
REVDAT 1 05-FEB-08 2RKU 0
JRNL AUTH M.KOTHE,D.KOHLS,S.LOW,R.COLI,G.R.RENNIE,F.FERU,C.KUHN,
JRNL AUTH 2 Y.-H.DING
JRNL TITL SELECTIVITY-DETERMINING RESIDUES IN PLK1.
JRNL REF CHEM.BIOL.DRUG DES. V. 70 540 2007
JRNL REFN ISSN 1747-0277
JRNL PMID 18005335
JRNL DOI 10.1111/J.1747-0285.2007.00594.X
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 29416
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1494
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1943
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2379
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.37000
REMARK 3 B22 (A**2) : 2.37000
REMARK 3 B33 (A**2) : -3.55000
REMARK 3 B12 (A**2) : 1.18000
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): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.232
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2558 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3462 ; 1.438 ; 2.014
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 303 ; 5.491 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;34.619 ;22.455
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 454 ;14.890 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;16.163 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1929 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1119 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1755 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 265 ; 0.199 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.012 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 49 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.222 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1550 ; 0.845 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2446 ; 1.351 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1154 ; 2.185 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1016 ; 3.520 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 37 A 50
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2378 -1.8107 3.8106
REMARK 3 T TENSOR
REMARK 3 T11: 0.3212 T22: 0.1678
REMARK 3 T33: -0.2158 T12: -0.1087
REMARK 3 T13: 0.2629 T23: 0.1141
REMARK 3 L TENSOR
REMARK 3 L11: 13.6610 L22: 13.0700
REMARK 3 L33: 11.8916 L12: -2.0564
REMARK 3 L13: 6.1372 L23: 1.6663
REMARK 3 S TENSOR
REMARK 3 S11: -1.7459 S12: -1.0295 S13: -0.9041
REMARK 3 S21: -0.1702 S22: 0.7168 S23: 0.1412
REMARK 3 S31: 0.0820 S32: -1.6849 S33: 1.0291
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 51 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9653 7.7123 6.7972
REMARK 3 T TENSOR
REMARK 3 T11: -0.1207 T22: -0.2169
REMARK 3 T33: -0.1699 T12: -0.0590
REMARK 3 T13: 0.0537 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 1.1398 L22: 2.5081
REMARK 3 L33: 6.1352 L12: 0.6483
REMARK 3 L13: -1.6425 L23: -0.3816
REMARK 3 S TENSOR
REMARK 3 S11: -0.1077 S12: 0.1684 S13: -0.1163
REMARK 3 S21: -0.0765 S22: -0.1325 S23: 0.1774
REMARK 3 S31: 0.7831 S32: -0.2912 S33: 0.2402
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2718 23.5720 19.3793
REMARK 3 T TENSOR
REMARK 3 T11: -0.2739 T22: -0.1477
REMARK 3 T33: -0.1498 T12: 0.0325
REMARK 3 T13: -0.0217 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 2.4487 L22: 1.7511
REMARK 3 L33: 5.6065 L12: -0.0316
REMARK 3 L13: -0.4016 L23: 0.3936
REMARK 3 S TENSOR
REMARK 3 S11: -0.1138 S12: -0.0585 S13: -0.0282
REMARK 3 S21: 0.1607 S22: 0.0579 S23: -0.1354
REMARK 3 S31: 0.0641 S32: 0.2433 S33: 0.0559
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 201 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5824 34.3778 10.9320
REMARK 3 T TENSOR
REMARK 3 T11: -0.1896 T22: -0.2040
REMARK 3 T33: -0.1323 T12: -0.0112
REMARK 3 T13: -0.0289 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.9048 L22: 0.9809
REMARK 3 L33: 6.4368 L12: -0.5113
REMARK 3 L13: -1.6760 L23: 0.4792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0899 S12: 0.1762 S13: 0.3805
REMARK 3 S21: -0.1045 S22: 0.0733 S23: -0.1101
REMARK 3 S31: -0.7222 S32: 0.0713 S33: 0.0165
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 251 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0269 40.7659 18.4090
REMARK 3 T TENSOR
REMARK 3 T11: -0.1276 T22: -0.3127
REMARK 3 T33: -0.1448 T12: 0.0167
REMARK 3 T13: -0.0609 T23: -0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 3.5222 L22: 2.1400
REMARK 3 L33: 6.1711 L12: -0.0667
REMARK 3 L13: 1.7478 L23: -0.0639
REMARK 3 S TENSOR
REMARK 3 S11: -0.3677 S12: -0.2599 S13: 0.6680
REMARK 3 S21: -0.0206 S22: 0.2258 S23: -0.1992
REMARK 3 S31: -0.9117 S32: -0.3115 S33: 0.1419
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 507
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4911 25.8842 37.3979
REMARK 3 T TENSOR
REMARK 3 T11: -0.1500 T22: -0.0682
REMARK 3 T33: -0.2162 T12: 0.0589
REMARK 3 T13: -0.0095 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 4.0836 L22: 1.7111
REMARK 3 L33: 5.3953 L12: 1.3720
REMARK 3 L13: 0.7399 L23: -0.1778
REMARK 3 S TENSOR
REMARK 3 S11: -0.0100 S12: -0.5493 S13: -0.1186
REMARK 3 S21: 0.5604 S22: -0.0010 S23: -0.0022
REMARK 3 S31: 0.2500 S32: -0.3905 S33: 0.0110
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2RKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000044981.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29527
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 102.74000
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 51.37000
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 51.37000
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 102.74000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2
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 -99.88950
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 57.67123
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 732 O HOH A 733 1.97
REMARK 500 O HOH A 513 O HOH A 787 1.99
REMARK 500 OD2 ASP A 176 O HOH A 513 2.03
REMARK 500 O HOH A 687 O HOH A 761 2.10
REMARK 500 O HOH A 675 O HOH A 752 2.12
REMARK 500 O HOH A 508 O HOH A 697 2.18
REMARK 500 O HOH A 510 O HOH A 700 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER A 99 O ILE A 327 2564 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 42 CG GLU A 42 CD 0.117
REMARK 500 GLU A 42 CD GLU A 42 OE1 0.105
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 38 117.61 54.24
REMARK 500 ASP A 122 -161.58 -121.70
REMARK 500 ARG A 136 -125.32 60.55
REMARK 500 LYS A 146 -134.80 55.34
REMARK 500 ARG A 175 -2.57 75.93
REMARK 500 ASP A 176 37.18 -141.48
REMARK 500 ASP A 194 79.11 54.06
REMARK 500 SER A 229 -148.69 -150.19
REMARK 500 LEU A 286 30.33 -94.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 CYS A 212 SG 118.1
REMARK 620 3 TLA A 502 O1 101.9 109.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R78 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 503
DBREF 2RKU A 37 330 UNP P53350 PLK1_HUMAN 37 330
SEQADV 2RKU VAL A 210 UNP P53350 THR 210 ENGINEERED MUTATION
SEQRES 1 A 294 ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER
SEQRES 2 A 294 ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY
SEQRES 3 A 294 GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR
SEQRES 4 A 294 LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU
SEQRES 5 A 294 LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU
SEQRES 6 A 294 ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL
SEQRES 7 A 294 GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE
SEQRES 8 A 294 VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU
SEQRES 9 A 294 LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA
SEQRES 10 A 294 ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR
SEQRES 11 A 294 LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU
SEQRES 12 A 294 GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE
SEQRES 13 A 294 GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY
SEQRES 14 A 294 GLU ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE
SEQRES 15 A 294 ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU
SEQRES 16 A 294 VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU
SEQRES 17 A 294 LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS
SEQRES 18 A 294 GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE
SEQRES 19 A 294 PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN
SEQRES 20 A 294 LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE
SEQRES 21 A 294 ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR
SEQRES 22 A 294 ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO
SEQRES 23 A 294 PRO ARG PHE SER ILE ALA PRO SER
HET ZN A 501 1
HET R78 A 500 38
HET TLA A 502 10
HET TLA A 504 10
HET SRT A 505 10
HET SRT A 507 10
HET TAR A 503 10
HETNAM ZN ZINC ION
HETNAM R78 4-{[(7R)-8-CYCLOPENTYL-7-ETHYL-5-METHYL-6-OXO-5,6,7,8-
HETNAM 2 R78 TETRAHYDROPTERIDIN-2-YL]AMINO}-3-METHOXY-N-(1-
HETNAM 3 R78 METHYLPIPERIDIN-4-YL)BENZAMIDE
HETNAM TLA L(+)-TARTARIC ACID
HETNAM SRT S,R MESO-TARTARIC ACID
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 2 ZN ZN 2+
FORMUL 3 R78 C28 H39 N7 O3
FORMUL 4 TLA 2(C4 H6 O6)
FORMUL 6 SRT 2(C4 H6 O6)
FORMUL 8 TAR C4 H6 O6
FORMUL 9 HOH *285(H2 O)
HELIX 1 1 SER A 87 LEU A 89 5 3
HELIX 2 2 LYS A 91 SER A 107 1 17
HELIX 3 3 SER A 137 LYS A 146 1 10
HELIX 4 4 THR A 149 ASN A 170 1 22
HELIX 5 5 LYS A 178 GLY A 180 5 3
HELIX 6 6 ALA A 219 SER A 224 1 6
HELIX 7 7 PHE A 230 GLY A 247 1 18
HELIX 8 8 CYS A 255 LYS A 265 1 11
HELIX 9 9 ASN A 275 LEU A 286 1 12
HELIX 10 10 ASP A 289 ARG A 293 5 5
HELIX 11 11 THR A 295 ASN A 301 5 7
HELIX 12 12 ASP A 302 SER A 307 1 6
HELIX 13 13 PRO A 315 THR A 320 5 6
SHEET 1 A 6 VAL A 43 ASP A 46 0
SHEET 2 A 6 ARG A 51 GLY A 62 -1 O TYR A 53 N LEU A 44
SHEET 3 A 6 ALA A 65 ASP A 72 -1 O GLU A 69 N GLY A 56
SHEET 4 A 6 VAL A 78 PRO A 85 -1 O GLY A 81 N PHE A 68
SHEET 5 A 6 PHE A 125 GLU A 131 -1 O LEU A 130 N ALA A 80
SHEET 6 A 6 PHE A 116 GLU A 121 -1 N GLY A 118 O VAL A 129
SHEET 1 B 2 VAL A 172 ILE A 173 0
SHEET 2 B 2 THR A 199 LYS A 200 -1 O THR A 199 N ILE A 173
SHEET 1 C 2 LEU A 182 LEU A 184 0
SHEET 2 C 2 VAL A 190 ILE A 192 -1 O LYS A 191 N PHE A 183
LINK NE2 HIS A 93 ZN ZN A 501 1555 1555 2.09
LINK SG CYS A 212 ZN ZN A 501 1555 1555 2.25
LINK ZN ZN A 501 O1 TLA A 502 1555 1555 2.01
SITE 1 AC1 4 HIS A 93 CYS A 212 CYS A 255 TLA A 502
SITE 1 AC2 15 ARG A 57 PHE A 58 LEU A 59 LYS A 61
SITE 2 AC2 15 GLU A 69 VAL A 114 LEU A 130 GLU A 131
SITE 3 AC2 15 LEU A 132 CYS A 133 ARG A 136 PHE A 183
SITE 4 AC2 15 HOH A 527 HOH A 563 HOH A 619
SITE 1 AC3 11 LYS A 91 HIS A 93 LYS A 97 CYS A 212
SITE 2 AC3 11 SER A 254 CYS A 255 LEU A 256 ZN A 501
SITE 3 AC3 11 TLA A 504 HOH A 608 HOH A 677
SITE 1 AC4 8 PHE A 64 LYS A 91 GLN A 94 LYS A 97
SITE 2 AC4 8 TLA A 502 HOH A 552 HOH A 608 HOH A 733
SITE 1 AC5 5 ASN A 266 TYR A 268 SER A 269 ILE A 270
SITE 2 AC5 5 GLN A 283
SITE 1 AC6 7 ARG A 135 GLU A 140 LEU A 141 LEU A 319
SITE 2 AC6 7 HOH A 592 HOH A 648 HOH A 698
SITE 1 AC7 7 LEU A 139 LYS A 178 LEU A 179 GLY A 180
SITE 2 AC7 7 ASN A 216 HOH A 743 HOH A 783
CRYST1 66.593 66.593 154.110 90.00 90.00 120.00 P 32 2 1 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 0.015017 0.008670 0.000000 0.00000
SCALE2 0.000000 0.017340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006489 0.00000
ATOM 1 N ALA A 37 -54.071 2.229 -5.927 1.00 45.42 N
ATOM 2 CA ALA A 37 -54.286 2.976 -4.649 1.00 45.50 C
ATOM 3 C ALA A 37 -53.007 3.130 -3.816 1.00 45.46 C
ATOM 4 O ALA A 37 -52.869 4.101 -3.070 1.00 45.43 O
ATOM 5 CB ALA A 37 -55.387 2.313 -3.829 1.00 45.57 C
ATOM 6 N LYS A 38 -52.083 2.173 -3.966 1.00 45.50 N
ATOM 7 CA LYS A 38 -50.795 2.094 -3.221 1.00 45.24 C
ATOM 8 C LYS A 38 -50.918 2.129 -1.702 1.00 45.11 C
ATOM 9 O LYS A 38 -51.364 3.117 -1.115 1.00 45.30 O
ATOM 10 CB LYS A 38 -49.754 3.120 -3.704 1.00 45.27 C
ATOM 11 CG LYS A 38 -49.191 2.874 -5.116 1.00 46.00 C
ATOM 12 CD LYS A 38 -48.662 1.442 -5.314 1.00 45.97 C
ATOM 13 CE LYS A 38 -48.294 1.181 -6.778 1.00 45.60 C
ATOM 14 NZ LYS A 38 -48.538 -0.250 -7.169 1.00 46.17 N
ATOM 15 N GLU A 39 -50.486 1.042 -1.073 1.00 44.78 N
ATOM 16 CA GLU A 39 -50.681 0.844 0.352 1.00 44.31 C
ATOM 17 C GLU A 39 -49.333 0.738 1.040 1.00 44.07 C
ATOM 18 O GLU A 39 -48.385 0.189 0.469 1.00 43.74 O
ATOM 19 CB GLU A 39 -51.506 -0.425 0.581 1.00 44.45 C
ATOM 20 CG GLU A 39 -52.357 -0.416 1.844 1.00 44.99 C
ATOM 21 CD GLU A 39 -53.699 -1.121 1.658 1.00 45.69 C
ATOM 22 OE1 GLU A 39 -54.383 -1.384 2.673 1.00 45.56 O
ATOM 23 OE2 GLU A 39 -54.075 -1.410 0.499 1.00 45.87 O
ATOM 24 N ILE A 40 -49.251 1.271 2.259 1.00 43.56 N
ATOM 25 CA ILE A 40 -48.021 1.235 3.047 1.00 43.47 C
ATOM 26 C ILE A 40 -47.769 -0.169 3.613 1.00 43.63 C
ATOM 27 O ILE A 40 -48.677 -0.765 4.190 1.00 43.62 O
ATOM 28 CB ILE A 40 -48.052 2.276 4.219 1.00 43.41 C
ATOM 29 CG1 ILE A 40 -48.285 3.696 3.687 1.00 42.89 C
ATOM 30 CG2 ILE A 40 -46.774 2.190 5.066 1.00 42.82 C
ATOM 31 CD1 ILE A 40 -48.477 4.751 4.763 1.00 43.39 C
ATOM 32 N PRO A 41 -46.537 -0.699 3.448 1.00 43.85 N
ATOM 33 CA PRO A 41 -46.133 -1.975 4.044 1.00 44.48 C
ATOM 34 C PRO A 41 -46.383 -2.051 5.552 1.00 45.34 C
ATOM 35 O PRO A 41 -46.294 -1.035 6.247 1.00 45.59 O
ATOM 36 CB PRO A 41 -44.627 -2.030 3.765 1.00 44.07 C
ATOM 37 CG PRO A 41 -44.421 -1.189 2.606 1.00 44.06 C
ATOM 38 CD PRO A 41 -45.452 -0.111 2.637 1.00 43.85 C
ATOM 39 N GLU A 42 -46.720 -3.242 6.043 1.00 46.15 N
ATOM 40 CA GLU A 42 -46.893 -3.466 7.472 1.00 47.04 C
ATOM 41 C GLU A 42 -45.548 -3.709 8.153 1.00 47.34 C
ATOM 42 O GLU A 42 -45.375 -3.405 9.338 1.00 47.79 O
ATOM 43 CB GLU A 42 -47.853 -4.631 7.734 1.00 46.80 C
ATOM 44 CG GLU A 42 -49.357 -4.334 7.267 1.00 47.51 C
ATOM 45 CD GLU A 42 -50.253 -5.545 7.894 1.00 47.57 C
ATOM 46 OE1 GLU A 42 -49.756 -6.806 7.953 1.00 49.63 O
ATOM 47 OE2 GLU A 42 -51.453 -5.226 8.240 1.00 48.22 O
ATOM 48 N VAL A 43 -44.618 -4.289 7.406 1.00 48.02 N
ATOM 49 CA VAL A 43 -43.219 -4.400 7.820 1.00 48.82 C
ATOM 50 C VAL A 43 -42.346 -3.583 6.859 1.00 48.66 C
ATOM 51 O VAL A 43 -42.410 -3.758 5.630 1.00 48.92 O
ATOM 52 CB VAL A 43 -42.742 -5.878 7.876 1.00 49.02 C
ATOM 53 CG1 VAL A 43 -41.252 -5.976 8.238 1.00 50.22 C
ATOM 54 CG2 VAL A 43 -43.592 -6.686 8.852 1.00 49.32 C
ATOM 55 N LEU A 44 -41.541 -2.677 7.415 1.00 48.75 N
ATOM 56 CA LEU A 44 -40.682 -1.798 6.593 1.00 48.66 C
ATOM 57 C LEU A 44 -39.264 -2.325 6.649 1.00 49.07 C
ATOM 58 O LEU A 44 -38.669 -2.414 7.725 1.00 49.30 O
ATOM 59 CB LEU A 44 -40.700 -0.352 7.112 1.00 48.44 C
ATOM 60 CG LEU A 44 -41.996 0.300 7.609 1.00 47.48 C
ATOM 61 CD1 LEU A 44 -41.667 1.556 8.369 1.00 46.91 C
ATOM 62 CD2 LEU A 44 -42.932 0.609 6.463 1.00 46.29 C
ATOM 63 N VAL A 45 -38.719 -2.674 5.494 1.00 49.90 N
ATOM 64 CA VAL A 45 -37.401 -3.301 5.444 1.00 50.61 C
ATOM 65 C VAL A 45 -36.375 -2.360 4.843 1.00 50.22 C
ATOM 66 O VAL A 45 -36.581 -1.814 3.770 1.00 50.55 O
ATOM 67 CB VAL A 45 -37.426 -4.671 4.677 1.00 50.93 C
ATOM 68 CG1 VAL A 45 -36.082 -5.386 4.791 1.00 51.89 C
ATOM 69 CG2 VAL A 45 -38.540 -5.566 5.211 1.00 49.21 C
ATOM 70 N ASP A 46 -35.273 -2.166 5.554 1.00 50.63 N
ATOM 71 CA ASP A 46 -34.140 -1.392 5.031 1.00 51.25 C
ATOM 72 C ASP A 46 -33.089 -2.371 4.484 1.00 51.45 C
ATOM 73 O ASP A 46 -32.352 -2.981 5.258 1.00 51.22 O
ATOM 74 CB ASP A 46 -33.560 -0.520 6.153 1.00 51.26 C
ATOM 75 CG ASP A 46 -32.361 0.315 5.716 1.00 52.05 C
ATOM 76 OD1 ASP A 46 -31.849 0.166 4.587 1.00 51.22 O
ATOM 77 OD2 ASP A 46 -31.922 1.150 6.534 1.00 54.26 O
ATOM 78 N PRO A 47 -32.986 -2.494 3.145 1.00 51.87 N
ATOM 79 CA PRO A 47 -32.168 -3.567 2.570 1.00 51.98 C
ATOM 80 C PRO A 47 -30.665 -3.375 2.842 1.00 52.12 C
ATOM 81 O PRO A 47 -29.909 -4.343 2.880 1.00 52.17 O
ATOM 82 CB PRO A 47 -32.470 -3.454 1.074 1.00 52.13 C
ATOM 83 CG PRO A 47 -32.775 -1.982 0.858 1.00 52.52 C
ATOM 84 CD PRO A 47 -33.566 -1.622 2.101 1.00 52.19 C
ATOM 85 N ARG A 48 -30.255 -2.127 3.043 1.00 51.36 N
ATOM 86 CA ARG A 48 -28.867 -1.774 3.299 1.00 50.92 C
ATOM 87 C ARG A 48 -28.460 -2.161 4.722 1.00 50.96 C
ATOM 88 O ARG A 48 -27.459 -2.857 4.928 1.00 50.67 O
ATOM 89 CB ARG A 48 -28.683 -0.276 3.082 1.00 50.63 C
ATOM 90 CG ARG A 48 -27.317 0.120 2.601 1.00 50.62 C
ATOM 91 CD ARG A 48 -27.304 1.570 2.158 1.00 52.35 C
ATOM 92 NE ARG A 48 -27.992 1.785 0.883 1.00 52.13 N
ATOM 93 CZ ARG A 48 -27.379 2.029 -0.268 1.00 52.15 C
ATOM 94 NH1 ARG A 48 -26.052 2.097 -0.327 1.00 52.73 N
ATOM 95 NH2 ARG A 48 -28.094 2.214 -1.368 1.00 53.32 N
ATOM 96 N SER A 49 -29.250 -1.721 5.699 1.00 50.74 N
ATOM 97 CA SER A 49 -28.917 -1.935 7.103 1.00 50.82 C
ATOM 98 C SER A 49 -29.386 -3.295 7.611 1.00 50.99 C
ATOM 99 O SER A 49 -28.934 -3.748 8.658 1.00 51.33 O
ATOM 100 CB SER A 49 -29.494 -0.806 7.966 1.00 50.61 C
ATOM 101 OG SER A 49 -30.899 -0.930 8.087 1.00 49.39 O
ATOM 102 N ARG A 50 -30.285 -3.936 6.863 1.00 51.30 N
ATOM 103 CA ARG A 50 -30.894 -5.228 7.231 1.00 51.96 C
ATOM 104 C ARG A 50 -31.831 -5.127 8.441 1.00 52.14 C
ATOM 105 O ARG A 50 -32.141 -6.124 9.097 1.00 52.28 O
ATOM 106 CB ARG A 50 -29.832 -6.320 7.437 1.00 51.96 C
ATOM 107 CG ARG A 50 -29.239 -6.871 6.130 1.00 52.76 C
ATOM 108 CD ARG A 50 -28.145 -7.918 6.365 1.00 52.62 C
ATOM 109 NE ARG A 50 -28.559 -8.995 7.265 1.00 54.06 N
ATOM 110 CZ ARG A 50 -27.902 -10.146 7.417 1.00 54.94 C
ATOM 111 NH1 ARG A 50 -26.792 -10.383 6.720 1.00 54.95 N
ATOM 112 NH2 ARG A 50 -28.356 -11.069 8.263 1.00 54.80 N
ATOM 113 N ARG A 51 -32.281 -3.912 8.725 1.00 52.28 N
ATOM 114 CA ARG A 51 -33.182 -3.659 9.841 1.00 52.79 C
ATOM 115 C ARG A 51 -34.622 -3.681 9.359 1.00 52.33 C
ATOM 116 O ARG A 51 -34.933 -3.181 8.278 1.00 52.81 O
ATOM 117 CB ARG A 51 -32.860 -2.317 10.490 1.00 53.24 C
ATOM 118 CG ARG A 51 -31.517 -2.282 11.194 1.00 56.49 C
ATOM 119 CD ARG A 51 -31.343 -0.990 11.993 1.00 63.16 C
ATOM 120 NE ARG A 51 -29.968 -0.843 12.476 1.00 67.62 N
ATOM 121 CZ ARG A 51 -29.117 0.108 12.080 1.00 69.60 C
ATOM 122 NH1 ARG A 51 -29.486 1.039 11.199 1.00 69.50 N
ATOM 123 NH2 ARG A 51 -27.888 0.134 12.586 1.00 70.97 N
ATOM 124 N ARG A 52 -35.497 -4.280 10.157 1.00 51.47 N
ATOM 125 CA ARG A 52 -36.910 -4.374 9.821 1.00 51.01 C
ATOM 126 C ARG A 52 -37.702 -3.674 10.916 1.00 50.28 C
ATOM 127 O ARG A 52 -37.360 -3.772 12.092 1.00 49.77 O
ATOM 128 CB ARG A 52 -37.358 -5.844 9.707 1.00 51.12 C
ATOM 129 CG ARG A 52 -36.557 -6.693 8.711 1.00 51.38 C
ATOM 130 CD ARG A 52 -37.254 -8.030 8.422 1.00 52.65 C
ATOM 131 NE ARG A 52 -37.865 -8.575 9.631 1.00 56.84 N
ATOM 132 CZ ARG A 52 -39.017 -9.244 9.672 1.00 58.90 C
ATOM 133 NH1 ARG A 52 -39.705 -9.467 8.552 1.00 60.79 N
ATOM 134 NH2 ARG A 52 -39.480 -9.691 10.837 1.00 58.63 N
ATOM 135 N TYR A 53 -38.754 -2.974 10.515 1.00 49.50 N
ATOM 136 CA TYR A 53 -39.547 -2.174 11.430 1.00 49.44 C
ATOM 137 C TYR A 53 -41.006 -2.565 11.245 1.00 49.58 C
ATOM 138 O TYR A 53 -41.524 -2.560 10.135 1.00 50.32 O
ATOM 139 CB TYR A 53 -39.348 -0.678 11.165 1.00 49.13 C
ATOM 140 CG TYR A 53 -37.922 -0.160 11.308 1.00 48.06 C
ATOM 141 CD1 TYR A 53 -37.445 0.316 12.532 1.00 47.04 C
ATOM 142 CD2 TYR A 53 -37.075 -0.091 10.204 1.00 48.56 C
ATOM 143 CE1 TYR A 53 -36.151 0.810 12.655 1.00 46.65 C
ATOM 144 CE2 TYR A 53 -35.781 0.399 10.314 1.00 46.45 C
ATOM 145 CZ TYR A 53 -35.324 0.844 11.544 1.00 47.82 C
ATOM 146 OH TYR A 53 -34.039 1.327 11.655 1.00 47.94 O
ATOM 147 N VAL A 54 -41.652 -2.959 12.332 1.00 49.13 N
ATOM 148 CA VAL A 54 -43.061 -3.304 12.285 1.00 49.14 C
ATOM 149 C VAL A 54 -43.827 -2.008 12.459 1.00 48.94 C
ATOM 150 O VAL A 54 -43.555 -1.247 13.400 1.00 48.41 O
ATOM 151 CB VAL A 54 -43.442 -4.316 13.380 1.00 48.72 C
ATOM 152 CG1 VAL A 54 -44.943 -4.518 13.423 1.00 49.63 C
ATOM 153 CG2 VAL A 54 -42.737 -5.659 13.139 1.00 48.76 C
ATOM 154 N ARG A 55 -44.758 -1.746 11.542 1.00 48.88 N
ATOM 155 CA ARG A 55 -45.564 -0.523 11.594 1.00 49.87 C
ATOM 156 C ARG A 55 -46.640 -0.622 12.674 1.00 49.76 C
ATOM 157 O ARG A 55 -47.449 -1.570 12.679 1.00 50.93 O
ATOM 158 CB ARG A 55 -46.194 -0.253 10.220 1.00 50.19 C
ATOM 159 CG ARG A 55 -47.092 0.984 10.183 1.00 49.82 C
ATOM 160 CD ARG A 55 -47.313 1.466 8.762 1.00 49.97 C
ATOM 161 NE ARG A 55 -47.940 0.473 7.881 1.00 52.93 N
ATOM 162 CZ ARG A 55 -49.249 0.235 7.788 1.00 52.04 C
ATOM 163 NH1 ARG A 55 -50.116 0.890 8.546 1.00 53.86 N
ATOM 164 NH2 ARG A 55 -49.689 -0.673 6.933 1.00 49.05 N
ATOM 165 N GLY A 56 -46.646 0.340 13.593 1.00 49.91 N
ATOM 166 CA GLY A 56 -47.601 0.337 14.693 1.00 49.93 C
ATOM 167 C GLY A 56 -48.626 1.450 14.598 1.00 49.60 C
ATOM 168 O GLY A 56 -49.119 1.774 13.512 1.00 49.73 O
ATOM 169 N ARG A 57 -48.911 2.046 15.750 1.00 48.65 N
ATOM 170 CA ARG A 57 -49.964 3.038 15.922 1.00 48.42 C
ATOM 171 C ARG A 57 -49.799 4.296 15.053 1.00 47.49 C
ATOM 172 O ARG A 57 -48.702 4.850 14.940 1.00 46.32 O
ATOM 173 CB ARG A 57 -50.075 3.359 17.418 1.00 49.27 C
ATOM 174 CG ARG A 57 -50.314 4.799 17.804 1.00 53.02 C
ATOM 175 CD ARG A 57 -50.832 4.831 19.243 1.00 60.20 C
ATOM 176 NE ARG A 57 -51.227 6.171 19.679 1.00 64.47 N
ATOM 177 CZ ARG A 57 -50.560 6.899 20.570 1.00 67.61 C
ATOM 178 NH1 ARG A 57 -49.448 6.437 21.142 1.00 67.57 N
ATOM 179 NH2 ARG A 57 -51.018 8.098 20.902 1.00 70.47 N
ATOM 180 N PHE A 58 -50.894 4.699 14.413 1.00 46.46 N
ATOM 181 CA PHE A 58 -50.918 5.890 13.572 1.00 46.14 C
ATOM 182 C PHE A 58 -50.783 7.133 14.451 1.00 45.60 C
ATOM 183 O PHE A 58 -51.496 7.272 15.441 1.00 45.38 O
ATOM 184 CB PHE A 58 -52.211 5.934 12.742 1.00 46.36 C
ATOM 185 CG PHE A 58 -52.376 7.190 11.912 1.00 46.97 C
ATOM 186 CD1 PHE A 58 -51.467 7.512 10.909 1.00 46.57 C
ATOM 187 CD2 PHE A 58 -53.467 8.037 12.119 1.00 47.84 C
ATOM 188 CE1 PHE A 58 -51.633 8.682 10.134 1.00 47.92 C
ATOM 189 CE2 PHE A 58 -53.641 9.199 11.354 1.00 47.05 C
ATOM 190 CZ PHE A 58 -52.724 9.516 10.354 1.00 47.01 C
ATOM 191 N LEU A 59 -49.873 8.031 14.089 1.00 44.06 N
ATOM 192 CA LEU A 59 -49.608 9.226 14.907 1.00 44.39 C
ATOM 193 C LEU A 59 -50.262 10.483 14.326 1.00 44.52 C
ATOM 194 O LEU A 59 -50.505 11.451 15.048 1.00 43.30 O
ATOM 195 CB LEU A 59 -48.085 9.462 15.076 1.00 43.68 C
ATOM 196 CG LEU A 59 -47.173 8.395 15.705 1.00 44.77 C
ATOM 197 CD1 LEU A 59 -45.720 8.845 15.774 1.00 44.72 C
ATOM 198 CD2 LEU A 59 -47.663 7.991 17.094 1.00 47.21 C
ATOM 199 N GLY A 60 -50.527 10.476 13.020 1.00 45.46 N
ATOM 200 CA GLY A 60 -51.111 11.640 12.362 1.00 47.20 C
ATOM 201 C GLY A 60 -50.408 11.952 11.058 1.00 49.22 C
ATOM 202 O GLY A 60 -49.439 11.299 10.704 1.00 48.49 O
ATOM 203 N LYS A 61 -50.904 12.949 10.334 1.00 51.12 N
ATOM 204 CA LYS A 61 -50.199 13.418 9.150 1.00 54.35 C
ATOM 205 C LYS A 61 -49.237 14.533 9.555 1.00 55.62 C
ATOM 206 O LYS A 61 -49.519 15.302 10.483 1.00 56.25 O
ATOM 207 CB LYS A 61 -51.166 13.906 8.062 1.00 54.14 C
ATOM 208 CG LYS A 61 -52.138 12.824 7.569 1.00 55.26 C
ATOM 209 CD LYS A 61 -53.103 13.305 6.473 1.00 55.95 C
ATOM 210 CE LYS A 61 -53.304 12.204 5.396 1.00 58.35 C
ATOM 211 NZ LYS A 61 -54.226 12.539 4.238 1.00 57.72 N
ATOM 212 N GLY A 62 -48.088 14.576 8.884 1.00 56.69 N
ATOM 213 CA GLY A 62 -47.215 15.751 8.886 1.00 58.67 C
ATOM 214 C GLY A 62 -46.894 16.137 7.444 1.00 59.57 C
ATOM 215 O GLY A 62 -45.948 15.613 6.862 1.00 60.50 O
ATOM 216 N GLY A 63 -47.697 17.024 6.856 1.00 60.10 N
ATOM 217 CA GLY A 63 -47.522 17.421 5.452 1.00 60.36 C
ATOM 218 C GLY A 63 -47.878 16.327 4.460 1.00 60.42 C
ATOM 219 O GLY A 63 -48.969 15.774 4.502 1.00 61.50 O
ATOM 220 N PHE A 64 -46.946 16.005 3.568 1.00 60.41 N
ATOM 221 CA PHE A 64 -47.114 14.887 2.634 1.00 59.71 C
ATOM 222 C PHE A 64 -47.010 13.530 3.318 1.00 58.13 C
ATOM 223 O PHE A 64 -47.096 12.506 2.655 1.00 58.31 O
ATOM 224 CB PHE A 64 -46.019 14.900 1.555 1.00 60.39 C
ATOM 225 CG PHE A 64 -46.148 15.998 0.548 1.00 62.24 C
ATOM 226 CD1 PHE A 64 -47.283 16.805 0.495 1.00 63.93 C
ATOM 227 CD2 PHE A 64 -45.129 16.203 -0.382 1.00 63.42 C
ATOM 228 CE1 PHE A 64 -47.391 17.819 -0.459 1.00 65.23 C
ATOM 229 CE2 PHE A 64 -45.227 17.209 -1.340 1.00 64.67 C
ATOM 230 CZ PHE A 64 -46.367 18.015 -1.385 1.00 63.83 C
ATOM 231 N ALA A 65 -46.791 13.517 4.627 1.00 55.65 N
ATOM 232 CA ALA A 65 -46.388 12.296 5.287 1.00 53.50 C
ATOM 233 C ALA A 65 -47.514 11.750 6.146 1.00 51.81 C
ATOM 234 O ALA A 65 -48.279 12.516 6.731 1.00 51.28 O
ATOM 235 CB ALA A 65 -45.115 12.527 6.115 1.00 53.47 C
ATOM 236 N LYS A 66 -47.629 10.426 6.172 1.00 49.61 N
ATOM 237 CA LYS A 66 -48.383 9.743 7.200 1.00 48.83 C
ATOM 238 C LYS A 66 -47.368 9.209 8.195 1.00 48.21 C
ATOM 239 O LYS A 66 -46.375 8.594 7.789 1.00 46.42 O
ATOM 240 CB LYS A 66 -49.232 8.602 6.608 1.00 49.03 C
ATOM 241 CG LYS A 66 -50.370 9.090 5.730 1.00 50.88 C
ATOM 242 CD LYS A 66 -51.366 7.968 5.433 1.00 55.28 C
ATOM 243 CE LYS A 66 -52.564 8.476 4.637 1.00 56.76 C
ATOM 244 NZ LYS A 66 -53.747 7.586 4.864 1.00 58.82 N
ATOM 245 N CYS A 67 -47.609 9.443 9.493 1.00 47.16 N
ATOM 246 CA CYS A 67 -46.632 9.049 10.512 1.00 46.46 C
ATOM 247 C CYS A 67 -47.132 7.949 11.451 1.00 46.18 C
ATOM 248 O CYS A 67 -48.290 7.927 11.794 1.00 44.43 O
ATOM 249 CB CYS A 67 -46.219 10.264 11.316 1.00 46.65 C
ATOM 250 SG CYS A 67 -45.649 11.629 10.267 1.00 46.88 S
ATOM 251 N PHE A 68 -46.222 7.079 11.892 1.00 45.61 N
ATOM 252 CA PHE A 68 -46.579 5.903 12.690 1.00 46.42 C
ATOM 253 C PHE A 68 -45.511 5.622 13.734 1.00 46.42 C
ATOM 254 O PHE A 68 -44.322 5.927 13.526 1.00 45.88 O
ATOM 255 CB PHE A 68 -46.702 4.650 11.811 1.00 45.22 C
ATOM 256 CG PHE A 68 -47.752 4.742 10.734 1.00 46.23 C
ATOM 257 CD1 PHE A 68 -47.448 5.263 9.486 1.00 47.92 C
ATOM 258 CD2 PHE A 68 -49.027 4.232 10.942 1.00 47.86 C
ATOM 259 CE1 PHE A 68 -48.430 5.334 8.472 1.00 47.15 C
ATOM 260 CE2 PHE A 68 -50.008 4.311 9.950 1.00 48.04 C
ATOM 261 CZ PHE A 68 -49.701 4.869 8.710 1.00 45.99 C
ATOM 262 N GLU A 69 -45.930 5.049 14.856 1.00 46.14 N
ATOM 263 CA GLU A 69 -44.989 4.376 15.740 1.00 46.83 C
ATOM 264 C GLU A 69 -44.431 3.213 14.923 1.00 46.50 C
ATOM 265 O GLU A 69 -45.198 2.507 14.260 1.00 46.52 O
ATOM 266 CB GLU A 69 -45.710 3.844 17.004 1.00 46.97 C
ATOM 267 CG GLU A 69 -46.207 4.976 17.895 1.00 47.48 C
ATOM 268 CD GLU A 69 -46.472 4.572 19.359 1.00 48.19 C
ATOM 269 OE1 GLU A 69 -46.473 5.481 20.210 1.00 52.07 O
ATOM 270 OE2 GLU A 69 -46.664 3.373 19.661 1.00 49.65 O
ATOM 271 N ILE A 70 -43.107 3.033 14.912 1.00 45.69 N
ATOM 272 CA ILE A 70 -42.524 1.840 14.258 1.00 45.30 C
ATOM 273 C ILE A 70 -41.520 1.195 15.189 1.00 46.13 C
ATOM 274 O ILE A 70 -40.780 1.898 15.880 1.00 47.46 O
ATOM 275 CB ILE A 70 -41.853 2.140 12.867 1.00 44.90 C
ATOM 276 CG1 ILE A 70 -40.650 3.095 13.017 1.00 44.83 C
ATOM 277 CG2 ILE A 70 -42.913 2.567 11.818 1.00 43.40 C
ATOM 278 CD1 ILE A 70 -39.867 3.376 11.726 1.00 43.45 C
ATOM 279 N SER A 71 -41.489 -0.131 15.239 1.00 45.88 N
ATOM 280 CA SER A 71 -40.589 -0.786 16.177 1.00 45.67 C
ATOM 281 C SER A 71 -39.645 -1.728 15.456 1.00 45.24 C
ATOM 282 O SER A 71 -40.072 -2.499 14.608 1.00 46.13 O
ATOM 283 CB SER A 71 -41.370 -1.518 17.290 1.00 45.90 C
ATOM 284 OG SER A 71 -42.030 -2.650 16.779 1.00 46.89 O
ATOM 285 N ASP A 72 -38.363 -1.648 15.800 1.00 44.71 N
ATOM 286 CA ASP A 72 -37.328 -2.515 15.242 1.00 44.52 C
ATOM 287 C ASP A 72 -37.626 -3.953 15.702 1.00 44.86 C
ATOM 288 O ASP A 72 -37.785 -4.196 16.900 1.00 44.21 O
ATOM 289 CB ASP A 72 -35.962 -2.026 15.744 1.00 44.40 C
ATOM 290 CG ASP A 72 -34.797 -2.820 15.196 1.00 44.20 C
ATOM 291 OD1 ASP A 72 -33.784 -2.186 14.828 1.00 44.09 O
ATOM 292 OD2 ASP A 72 -34.866 -4.064 15.154 1.00 40.46 O
ATOM 293 N ALA A 73 -37.711 -4.893 14.759 1.00 45.06 N
ATOM 294 CA ALA A 73 -38.121 -6.268 15.082 1.00 45.96 C
ATOM 295 C ALA A 73 -37.079 -7.029 15.900 1.00 46.55 C
ATOM 296 O ALA A 73 -37.398 -8.043 16.546 1.00 46.52 O
ATOM 297 CB ALA A 73 -38.452 -7.028 13.815 1.00 46.29 C
ATOM 298 N ASP A 74 -35.835 -6.551 15.855 1.00 47.00 N
ATOM 299 CA ASP A 74 -34.728 -7.178 16.580 1.00 47.62 C
ATOM 300 C ASP A 74 -34.548 -6.580 17.984 1.00 47.23 C
ATOM 301 O ASP A 74 -34.537 -7.313 18.971 1.00 47.09 O
ATOM 302 CB ASP A 74 -33.429 -7.095 15.765 1.00 48.00 C
ATOM 303 CG ASP A 74 -33.454 -7.989 14.521 1.00 51.14 C
ATOM 304 OD1 ASP A 74 -33.734 -9.201 14.663 1.00 53.44 O
ATOM 305 OD2 ASP A 74 -33.184 -7.488 13.396 1.00 53.83 O
ATOM 306 N THR A 75 -34.429 -5.254 18.071 1.00 46.59 N
ATOM 307 CA THR A 75 -34.176 -4.582 19.348 1.00 46.18 C
ATOM 308 C THR A 75 -35.460 -4.163 20.070 1.00 45.84 C
ATOM 309 O THR A 75 -35.421 -3.822 21.255 1.00 45.70 O
ATOM 310 CB THR A 75 -33.350 -3.316 19.151 1.00 46.29 C
ATOM 311 OG1 THR A 75 -34.175 -2.344 18.515 1.00 46.03 O
ATOM 312 CG2 THR A 75 -32.124 -3.593 18.279 1.00 46.69 C
ATOM 313 N LYS A 76 -36.585 -4.185 19.357 1.00 45.33 N
ATOM 314 CA LYS A 76 -37.903 -3.813 19.916 1.00 45.42 C
ATOM 315 C LYS A 76 -38.029 -2.321 20.227 1.00 45.60 C
ATOM 316 O LYS A 76 -39.048 -1.866 20.748 1.00 44.75 O
ATOM 317 CB LYS A 76 -38.260 -4.634 21.164 1.00 45.25 C
ATOM 318 CG LYS A 76 -37.985 -6.130 21.072 1.00 45.70 C
ATOM 319 CD LYS A 76 -38.663 -6.788 19.890 1.00 45.79 C
ATOM 320 CE LYS A 76 -38.378 -8.259 19.904 1.00 45.63 C
ATOM 321 NZ LYS A 76 -38.947 -8.915 18.716 1.00 47.95 N
ATOM 322 N GLU A 77 -36.990 -1.566 19.899 1.00 46.20 N
ATOM 323 CA GLU A 77 -37.018 -0.116 20.059 1.00 46.95 C
ATOM 324 C GLU A 77 -38.098 0.548 19.213 1.00 46.28 C
ATOM 325 O GLU A 77 -38.336 0.157 18.072 1.00 45.18 O
ATOM 326 CB GLU A 77 -35.669 0.450 19.675 1.00 47.88 C
ATOM 327 CG GLU A 77 -34.857 0.933 20.843 1.00 51.77 C
ATOM 328 CD GLU A 77 -33.944 2.064 20.427 1.00 57.98 C
ATOM 329 OE1 GLU A 77 -32.930 1.769 19.742 1.00 58.39 O
ATOM 330 OE2 GLU A 77 -34.263 3.240 20.765 1.00 60.06 O
ATOM 331 N VAL A 78 -38.729 1.578 19.773 1.00 46.41 N
ATOM 332 CA VAL A 78 -39.800 2.289 19.082 1.00 45.64 C
ATOM 333 C VAL A 78 -39.335 3.667 18.612 1.00 46.14 C
ATOM 334 O VAL A 78 -38.672 4.431 19.349 1.00 45.75 O
ATOM 335 CB VAL A 78 -41.098 2.366 19.951 1.00 46.18 C
ATOM 336 CG1 VAL A 78 -42.251 2.947 19.155 1.00 45.67 C
ATOM 337 CG2 VAL A 78 -41.496 0.963 20.440 1.00 44.99 C
ATOM 338 N PHE A 79 -39.694 3.967 17.369 1.00 45.39 N
ATOM 339 CA PHE A 79 -39.344 5.209 16.733 1.00 45.70 C
ATOM 340 C PHE A 79 -40.633 5.815 16.174 1.00 44.59 C
ATOM 341 O PHE A 79 -41.706 5.206 16.221 1.00 44.78 O
ATOM 342 CB PHE A 79 -38.334 4.950 15.597 1.00 45.21 C
ATOM 343 CG PHE A 79 -37.058 4.285 16.052 1.00 45.72 C
ATOM 344 CD1 PHE A 79 -36.943 2.910 16.037 1.00 47.12 C
ATOM 345 CD2 PHE A 79 -35.980 5.046 16.494 1.00 46.70 C
ATOM 346 CE1 PHE A 79 -35.760 2.271 16.457 1.00 48.74 C
ATOM 347 CE2 PHE A 79 -34.785 4.423 16.917 1.00 49.08 C
ATOM 348 CZ PHE A 79 -34.684 3.036 16.894 1.00 48.08 C
ATOM 349 N ALA A 80 -40.515 7.007 15.641 1.00 43.65 N
ATOM 350 CA ALA A 80 -41.625 7.645 14.948 1.00 43.93 C
ATOM 351 C ALA A 80 -41.233 7.530 13.494 1.00 44.47 C
ATOM 352 O ALA A 80 -40.194 8.056 13.101 1.00 45.15 O
ATOM 353 CB ALA A 80 -41.721 9.113 15.354 1.00 44.73 C
ATOM 354 N GLY A 81 -42.027 6.821 12.706 1.00 44.45 N
ATOM 355 CA GLY A 81 -41.746 6.687 11.272 1.00 46.95 C
ATOM 356 C GLY A 81 -42.496 7.759 10.506 1.00 47.82 C
ATOM 357 O GLY A 81 -43.688 7.944 10.712 1.00 47.58 O
ATOM 358 N LYS A 82 -41.795 8.474 9.634 1.00 47.15 N
ATOM 359 CA LYS A 82 -42.436 9.403 8.736 1.00 48.13 C
ATOM 360 C LYS A 82 -42.403 8.779 7.334 1.00 47.90 C
ATOM 361 O LYS A 82 -41.326 8.448 6.806 1.00 48.07 O
ATOM 362 CB LYS A 82 -41.677 10.712 8.779 1.00 48.75 C
ATOM 363 CG LYS A 82 -42.384 11.901 8.184 1.00 52.15 C
ATOM 364 CD LYS A 82 -41.582 13.123 8.558 1.00 54.85 C
ATOM 365 CE LYS A 82 -42.037 14.351 7.839 1.00 58.12 C
ATOM 366 NZ LYS A 82 -41.105 15.475 8.217 1.00 59.22 N
ATOM 367 N ILE A 83 -43.587 8.575 6.753 1.00 47.63 N
ATOM 368 CA ILE A 83 -43.720 7.812 5.509 1.00 47.45 C
ATOM 369 C ILE A 83 -44.295 8.681 4.385 1.00 47.40 C
ATOM 370 O ILE A 83 -45.425 9.152 4.481 1.00 46.82 O
ATOM 371 CB ILE A 83 -44.600 6.526 5.730 1.00 47.52 C
ATOM 372 CG1 ILE A 83 -43.994 5.673 6.860 1.00 47.98 C
ATOM 373 CG2 ILE A 83 -44.771 5.749 4.401 1.00 45.70 C
ATOM 374 CD1 ILE A 83 -44.765 4.365 7.194 1.00 47.39 C
ATOM 375 N VAL A 84 -43.502 8.905 3.332 1.00 47.31 N
ATOM 376 CA VAL A 84 -43.891 9.839 2.272 1.00 46.79 C
ATOM 377 C VAL A 84 -44.081 9.094 0.970 1.00 46.57 C
ATOM 378 O VAL A 84 -43.159 8.436 0.497 1.00 46.46 O
ATOM 379 CB VAL A 84 -42.862 10.991 2.088 1.00 47.43 C
ATOM 380 CG1 VAL A 84 -43.344 11.972 1.020 1.00 47.72 C
ATOM 381 CG2 VAL A 84 -42.624 11.730 3.405 1.00 47.70 C
ATOM 382 N PRO A 85 -45.286 9.179 0.389 1.00 46.30 N
ATOM 383 CA PRO A 85 -45.458 8.452 -0.848 1.00 46.34 C
ATOM 384 C PRO A 85 -44.788 9.195 -1.987 1.00 45.93 C
ATOM 385 O PRO A 85 -44.948 10.421 -2.131 1.00 45.15 O
ATOM 386 CB PRO A 85 -46.977 8.391 -1.046 1.00 45.73 C