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3uzd-original_and_AFmimE_aligned.pdb
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HEADER PROTEIN BINDING/HYDROLASE 07-DEC-11 3UZD
TITLE CRYSTAL STRUCTURE OF 14-3-3 GAMMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1, KCIP-1, 14-3-3 PROTEIN
COMPND 5 GAMMA, N-TERMINALLY PROCESSED;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE DEACETYLASE 4;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: HD4;
COMPND 11 EC: 3.5.1.98;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: YWHAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 OTHER_DETAILS: POLYPEPTIDE(L)
KEYWDS STRUCTURAL GENOMICS, SGC, STRUCTURAL GENOMICS CONSORTIUM, MAINLY
KEYWDS 2 ALPHA, PHOSPHOSERINE, PHOSPHOTHREONINE, PROTEIN BINDING-HYDROLASE
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.XU,C.BIAN,F.MACKENZIE,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,J.MIN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 13-JUN-12 3UZD 1
REVDAT 1 21-MAR-12 3UZD 0
JRNL AUTH C.XU,J.JIN,C.BIAN,R.LAM,R.TIAN,R.WEIST,L.YOU,J.NIE,
JRNL AUTH 2 A.BOCHKAREV,W.TEMPEL,C.S.TAN,G.A.WASNEY,M.VEDADI,G.D.GISH,
JRNL AUTH 3 C.H.ARROWSMITH,T.PAWSON,X.J.YANG,J.MIN
JRNL TITL SEQUENCE-SPECIFIC RECOGNITION OF A PXLPXI/L MOTIF BY AN
JRNL TITL 2 ANKYRIN REPEAT TUMBLER LOCK.
JRNL REF SCI.SIGNAL. V. 5 RA39 2012
JRNL REFN ESSN 1937-9145
JRNL PMID 22649097
JRNL DOI 10.1126/SCISIGNAL.2002979
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 24650
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1252
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1862
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 0.82000
REMARK 3 B12 (A**2) : 0.00000
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): 0.135
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.113
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1917 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2592 ; 1.526 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 236 ; 5.888 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;36.789 ;24.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 332 ;17.067 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;21.426 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 295 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1442 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1205 ; 1.331 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1909 ; 2.102 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 712 ; 3.797 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 683 ; 5.715 ; 4.500
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 : 10
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 2 A 35
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6633 28.8793 13.8176
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.0898
REMARK 3 T33: 0.0980 T12: 0.0161
REMARK 3 T13: 0.0273 T23: 0.0647
REMARK 3 L TENSOR
REMARK 3 L11: 2.0838 L22: 3.7423
REMARK 3 L33: 8.7648 L12: 1.2532
REMARK 3 L13: 1.4477 L23: 4.3038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.1277 S13: 0.1277
REMARK 3 S21: 0.0295 S22: -0.0634 S23: 0.2658
REMARK 3 S31: -0.0430 S32: -0.4637 S33: 0.0537
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 36 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0448 23.7154 17.6449
REMARK 3 T TENSOR
REMARK 3 T11: 0.0479 T22: 0.0461
REMARK 3 T33: 0.0886 T12: -0.0126
REMARK 3 T13: -0.0060 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 3.4921 L22: 1.7653
REMARK 3 L33: 7.5197 L12: -0.6385
REMARK 3 L13: -4.1613 L23: 1.2354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.0031 S13: -0.1747
REMARK 3 S21: 0.2427 S22: -0.0040 S23: 0.1204
REMARK 3 S31: 0.2528 S32: -0.0652 S33: 0.0319
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 56 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0619 20.7127 -0.6156
REMARK 3 T TENSOR
REMARK 3 T11: 0.0942 T22: 0.3086
REMARK 3 T33: 0.1086 T12: 0.0498
REMARK 3 T13: -0.0152 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.2027 L22: 4.7495
REMARK 3 L33: 14.3837 L12: -0.0684
REMARK 3 L13: -2.8860 L23: 1.3922
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: 0.1354 S13: -0.1053
REMARK 3 S21: -0.3414 S22: -0.0303 S23: -0.3154
REMARK 3 S31: 0.2161 S32: 1.0660 S33: -0.0008
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 71 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4145 26.8232 -12.1361
REMARK 3 T TENSOR
REMARK 3 T11: 0.4306 T22: 0.9784
REMARK 3 T33: 0.3867 T12: -0.0162
REMARK 3 T13: 0.1562 T23: 0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 5.0441 L22: 56.3737
REMARK 3 L33: 19.4953 L12: -16.8626
REMARK 3 L13: -9.9158 L23: 33.1477
REMARK 3 S TENSOR
REMARK 3 S11: 0.4141 S12: -0.1635 S13: 0.5302
REMARK 3 S21: -1.2767 S22: 0.5818 S23: -1.7794
REMARK 3 S31: -0.7103 S32: 0.2998 S33: -0.9958
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 82 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6493 30.9656 10.3171
REMARK 3 T TENSOR
REMARK 3 T11: 0.0685 T22: 0.0734
REMARK 3 T33: 0.1381 T12: -0.0281
REMARK 3 T13: 0.0088 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 2.1083 L22: 0.9793
REMARK 3 L33: 9.4477 L12: -1.0311
REMARK 3 L13: -2.9711 L23: 1.9920
REMARK 3 S TENSOR
REMARK 3 S11: 0.0557 S12: 0.1111 S13: 0.1651
REMARK 3 S21: -0.0662 S22: 0.0519 S23: -0.1362
REMARK 3 S31: -0.2862 S32: 0.3977 S33: -0.1076
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 110 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5884 26.7765 33.4488
REMARK 3 T TENSOR
REMARK 3 T11: 0.3020 T22: 0.1741
REMARK 3 T33: 0.2081 T12: -0.0347
REMARK 3 T13: 0.0728 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 3.0814 L22: 2.6686
REMARK 3 L33: 9.6788 L12: -1.7564
REMARK 3 L13: -2.6197 L23: -1.9714
REMARK 3 S TENSOR
REMARK 3 S11: -0.2713 S12: -0.5047 S13: -0.0535
REMARK 3 S21: 0.5628 S22: 0.4174 S23: 0.1968
REMARK 3 S31: -0.4380 S32: 0.0243 S33: -0.1461
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 121 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0621 24.9143 17.3737
REMARK 3 T TENSOR
REMARK 3 T11: 0.0406 T22: 0.0417
REMARK 3 T33: 0.0682 T12: -0.0043
REMARK 3 T13: -0.0392 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 3.3320 L22: 2.4556
REMARK 3 L33: 4.6513 L12: 0.3766
REMARK 3 L13: -2.2105 L23: -0.5566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: 0.1711 S13: 0.1375
REMARK 3 S21: 0.0242 S22: 0.0061 S23: -0.2011
REMARK 3 S31: -0.1750 S32: 0.1975 S33: -0.0392
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 148 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0441 20.8452 29.8915
REMARK 3 T TENSOR
REMARK 3 T11: 0.0911 T22: 0.1203
REMARK 3 T33: 0.1162 T12: 0.0029
REMARK 3 T13: -0.0700 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 4.3656 L22: 4.7598
REMARK 3 L33: 16.8570 L12: 3.6379
REMARK 3 L13: -8.0135 L23: -7.5670
REMARK 3 S TENSOR
REMARK 3 S11: 0.0925 S12: -0.5235 S13: -0.0806
REMARK 3 S21: 0.4196 S22: -0.2399 S23: -0.3254
REMARK 3 S31: -0.1568 S32: 0.6322 S33: 0.1474
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 166 A 211
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9333 9.7534 25.9527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0808 T22: 0.0491
REMARK 3 T33: 0.0705 T12: 0.0210
REMARK 3 T13: -0.0400 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 4.7314 L22: 3.2981
REMARK 3 L33: 2.2687 L12: 1.4590
REMARK 3 L13: -0.8863 L23: -1.3052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: -0.2156 S13: -0.1505
REMARK 3 S21: 0.1115 S22: -0.0587 S23: -0.2380
REMARK 3 S31: 0.0975 S32: 0.2174 S33: 0.0301
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 212 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9762 4.5267 22.0050
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.0106
REMARK 3 T33: 0.0566 T12: -0.0088
REMARK 3 T13: -0.0401 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 17.6239 L22: 3.0764
REMARK 3 L33: 6.9258 L12: 0.2541
REMARK 3 L13: -7.4868 L23: -0.1425
REMARK 3 S TENSOR
REMARK 3 S11: -0.1408 S12: 0.1401 S13: -0.2870
REMARK 3 S21: -0.0765 S22: 0.0874 S23: -0.1035
REMARK 3 S31: 0.1461 S32: 0.0469 S33: 0.0534
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4
REMARK 4 3UZD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24650
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 66.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.84500
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2B05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3M MG (OAC)2, 20% PEG3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.25550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.61500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.11600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.25550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.61500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.11600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.25550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.61500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.11600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.25550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.61500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.11600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 401 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 ALA A 72
REMARK 465 ASP A 73
REMARK 465 GLY A 74
REMARK 465 LYS A 77
REMARK 465 SER A 235
REMARK 465 ASP A 236
REMARK 465 GLN A 237
REMARK 465 GLN A 238
REMARK 465 ASP A 239
REMARK 465 ASP A 240
REMARK 465 ASP A 241
REMARK 465 GLY A 242
REMARK 465 GLY A 243
REMARK 465 GLU A 244
REMARK 465 GLY A 245
REMARK 465 ASN A 246
REMARK 465 ASN A 247
REMARK 465 SER A 248
REMARK 465 LEU B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 TYR B 4
REMARK 465 THR B 5
REMARK 465 GLY B 15
REMARK 465 LEU B 16
REMARK 465 PRO B 17
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 VAL A 2 CG1 CG2
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 GLU A 5 CG CD OE1 OE2
REMARK 470 LYS A 10 CE NZ
REMARK 470 GLN A 68 CG CD OE1 NE2
REMARK 470 LYS A 69 CG CD CE NZ
REMARK 470 THR A 70 OG1 CG2
REMARK 470 SER A 71 CB OG
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 ILE A 79 CG1 CD1
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 ARG A 83 CD NE CZ NH1 NH2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 LYS A 91 CD CE NZ
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 LYS A 152 CE NZ
REMARK 470 LYS A 162 CD CE NZ
REMARK 470 GLU A 163 OE1 OE2
REMARK 470 GLU A 213 CD OE1 OE2
REMARK 470 LEU B 14 CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 42 N CA C O CB CG CD
REMARK 480 ARG A 42 NE CZ NH2
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 O HOH A 528 O HOH A 528 2565 1.88
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 ASN A 34 36.66 76.26
REMARK 500 TYR A 107 -66.23 -133.58
REMARK 500 ALA A 189 75.08 -118.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 513 DISTANCE = 7.20 ANGSTROMS
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 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 480 O
REMARK 620 2 HOH A 459 O 136.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 101
DBREF 3UZD A 1 247 UNP P61981 1433G_HUMAN 1 247
DBREF 3UZD B 1 17 UNP P56524 HDAC4_HUMAN 343 359
SEQADV 3UZD SER A 248 UNP P61981 EXPRESSION TAG
SEQRES 1 A 248 MET VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU
SEQRES 2 A 248 ALA GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA
SEQRES 3 A 248 MET LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN
SEQRES 4 A 248 GLU GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL
SEQRES 5 A 248 VAL GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER
SEQRES 6 A 248 ILE GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS
SEQRES 7 A 248 ILE GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS
SEQRES 8 A 248 GLU LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU
SEQRES 9 A 248 ASP ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR
SEQRES 10 A 248 GLU SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR
SEQRES 11 A 248 TYR ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG
SEQRES 12 A 248 ALA THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU
SEQRES 13 A 248 ALA HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS
SEQRES 14 A 248 PRO ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE
SEQRES 15 A 248 TYR TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS
SEQRES 16 A 248 LEU ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU
SEQRES 17 A 248 ASP THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU
SEQRES 18 A 248 ILE MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR
SEQRES 19 A 248 SER ASP GLN GLN ASP ASP ASP GLY GLY GLU GLY ASN ASN
SEQRES 20 A 248 SER
SEQRES 1 B 17 LEU PRO LEU TYR THR SER PRO SEP LEU PRO ASN ILE THR
SEQRES 2 B 17 LEU GLY LEU PRO
MODRES 3UZD SEP B 8 SER PHOSPHOSERINE
HET SEP B 8 10
HET NO3 A 301 4
HET NO3 A 302 4
HET MG A 303 1
HET NO3 B 101 4
HETNAM SEP PHOSPHOSERINE
HETNAM NO3 NITRATE ION
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 3 NO3 3(N O3 1-)
FORMUL 5 MG MG 2+
FORMUL 7 HOH *138(H2 O)
HELIX 1 1 ASP A 3 ALA A 17 1 15
HELIX 2 2 ARG A 19 GLU A 32 1 14
HELIX 3 3 SER A 38 SER A 71 1 34
HELIX 4 4 ASN A 75 GLU A 76 1 2
HELIX 5 5 LYS A 78 LYS A 78 1 1
HELIX 6 6 ILE A 79 ASN A 106 1 28
HELIX 7 7 TYR A 107 CYS A 112 1 6
HELIX 8 8 GLN A 116 ALA A 138 1 23
HELIX 9 9 THR A 139 MET A 165 1 27
HELIX 10 10 HIS A 169 ILE A 186 1 18
HELIX 11 11 ALA A 189 GLU A 207 1 19
HELIX 12 12 LEU A 208 LEU A 211 1 4
HELIX 13 13 SER A 215 THR A 234 1 20
LINK MG MG A 303 O HOH A 480 1555 1555 2.41
LINK MG MG A 303 O HOH A 459 1555 1555 2.74
SITE 1 AC1 7 SER A 113 GLU A 114 THR A 115 ALA A 189
SITE 2 AC1 7 PRO A 190 GLU A 191 GLN A 192
SITE 1 AC2 6 ASP A 214 SER A 215 TYR A 216 LYS A 217
SITE 2 AC2 6 ASP A 218 HOH A 429
SITE 1 AC3 2 HOH A 459 HOH A 480
SITE 1 AC4 2 GLU A 185 PRO B 7
CRYST1 60.511 79.230 122.232 90.00 90.00 90.00 I 2 2 2 8
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 0.016526 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008181 0.00000
MODEL 1
ATOM 1 N VAL A 2 19.310 -20.549 3.371 1.00 63.94 N
ANISOU 1 N VAL A 2 7763 8058 8472 2580 -821 -227 N
ATOM 2 CA VAL A 2 18.790 -20.376 2.036 1.00 61.99 C
ANISOU 2 CA VAL A 2 7067 8211 8273 2250 -550 -315 C
ATOM 3 C VAL A 2 19.634 -19.402 1.238 1.00 60.83 C
ANISOU 3 C VAL A 2 6746 8187 8179 2080 -293 -445 C
ATOM 4 O VAL A 2 20.327 -18.567 1.787 1.00 62.52 O
ANISOU 4 O VAL A 2 7214 8140 8402 2116 -271 -381 O
ATOM 5 CB VAL A 2 17.360 -19.856 2.076 1.00 58.88 C
ANISOU 5 CB VAL A 2 6822 7719 7829 1848 -408 -19 C
ATOM 6 N ASP A 3 19.579 -19.538 -0.070 1.00 57.54 N
ANISOU 6 N ASP A 3 5923 8174 7766 1858 -94 -639 N
ATOM 7 CA ASP A 3 20.094 -18.513 -0.973 1.00 52.08 C
ANISOU 7 CA ASP A 3 5141 7589 7057 1555 191 -703 C
ATOM 8 C ASP A 3 18.933 -17.577 -1.317 1.00 45.19 C
ANISOU 8 C ASP A 3 4478 6566 6128 1131 356 -406 C
ATOM 9 O ASP A 3 17.778 -17.798 -0.925 1.00 44.89 O
ANISOU 9 O ASP A 3 4572 6405 6078 1075 274 -207 O
ATOM 10 CB ASP A 3 20.628 -19.154 -2.255 1.00 54.17 C
ANISOU 10 CB ASP A 3 4914 8377 7290 1454 339 -1093 C
ATOM 11 N ARG A 4 19.234 -16.529 -2.059 1.00 40.97 N
ANISOU 11 N ARG A 4 3988 6041 5539 855 566 -398 N
ATOM 12 CA ARG A 4 18.222 -15.526 -2.419 1.00 35.03 C
ANISOU 12 CA ARG A 4 3477 5117 4717 532 664 -157 C
ATOM 13 C ARG A 4 17.215 -16.148 -3.393 1.00 35.67 C
ANISOU 13 C ARG A 4 3444 5386 4724 276 727 -175 C
ATOM 14 O ARG A 4 16.004 -15.962 -3.272 1.00 34.25 O
ANISOU 14 O ARG A 4 3435 5052 4527 178 677 14 O
ATOM 15 CB ARG A 4 18.949 -14.359 -3.066 1.00 36.46 C
ANISOU 15 CB ARG A 4 3760 5273 4819 341 829 -185 C
ATOM 16 CG ARG A 4 18.108 -13.141 -3.301 1.00 29.10 C
ANISOU 16 CG ARG A 4 3131 4116 3809 125 854 33 C
ATOM 17 CD ARG A 4 18.854 -12.174 -4.263 1.00 32.32 C
ANISOU 17 CD ARG A 4 3654 4551 4074 -102 1009 -29 C
ATOM 18 NE ARG A 4 18.072 -10.946 -4.358 1.00 33.12 N
ANISOU 18 NE ARG A 4 4083 4404 4099 -201 948 162 N
ATOM 19 CZ ARG A 4 18.154 -9.906 -3.526 1.00 30.57 C
ANISOU 19 CZ ARG A 4 3901 3891 3823 -63 859 246 C
ATOM 20 NH1 ARG A 4 19.074 -9.840 -2.546 1.00 30.59 N
ANISOU 20 NH1 ARG A 4 3826 3867 3930 124 848 192 N
ATOM 21 NH2 ARG A 4 17.342 -8.890 -3.720 1.00 28.27 N
ANISOU 21 NH2 ARG A 4 3848 3440 3452 -115 769 353 N
ATOM 22 N GLU A 5 17.697 -16.922 -4.344 1.00 37.04 N
ANISOU 22 N GLU A 5 3317 5918 4840 152 840 -441 N
ATOM 23 CA GLU A 5 16.846 -17.539 -5.342 1.00 36.81 C
ANISOU 23 CA GLU A 5 3190 6089 4708 -167 929 -500 C
ATOM 24 C GLU A 5 15.803 -18.446 -4.722 1.00 36.38 C
ANISOU 24 C GLU A 5 3088 6010 4725 -4 745 -414 C
ATOM 25 O GLU A 5 14.688 -18.495 -5.120 1.00 32.32 O
ANISOU 25 O GLU A 5 2696 5436 4150 -223 760 -301 O
ATOM 26 CB GLU A 5 17.678 -18.303 -6.375 1.00 40.17 C
ANISOU 26 CB GLU A 5 3225 6997 5042 -360 1106 -885 C
ATOM 27 N GLN A 6 16.218 -19.156 -3.690 1.00 36.30 N
ANISOU 27 N GLN A 6 2948 6017 4828 407 548 -471 N
ATOM 28 CA GLN A 6 15.342 -20.015 -2.935 1.00 36.94 C
ANISOU 28 CA GLN A 6 3042 6046 4946 596 342 -378 C
ATOM 29 C GLN A 6 14.282 -19.234 -2.130 1.00 31.26 C
ANISOU 29 C GLN A 6 2705 4943 4229 554 287 -39 C
ATOM 30 O GLN A 6 13.177 -19.623 -2.096 1.00 30.89 O
ANISOU 30 O GLN A 6 2698 4886 4153 468 239 48 O
ATOM 31 CB GLN A 6 16.129 -20.955 -2.024 1.00 38.64 C
ANISOU 31 CB GLN A 6 3124 6325 5231 1073 95 -528 C
ATOM 32 CG GLN A 6 16.954 -22.040 -2.743 1.00 48.59 C
ANISOU 32 CG GLN A 6 3889 8079 6494 1202 80 -964 C
ATOM 33 CD GLN A 6 17.689 -22.948 -1.783 1.00 58.60 C
ANISOU 33 CD GLN A 6 5088 9357 7822 1785 -253 -1130 C
ATOM 34 OE1 GLN A 6 18.503 -22.512 -1.004 1.00 60.47 O
ANISOU 34 OE1 GLN A 6 5548 9326 8102 2067 -360 -1082 O
ATOM 35 NE2 GLN A 6 17.391 -24.231 -1.846 1.00 66.90 N
ANISOU 35 NE2 GLN A 6 5860 10702 8857 1979 -446 -1341 N
ATOM 36 N LEU A 7 14.644 -18.129 -1.507 1.00 30.89 N
ANISOU 36 N LEU A 7 2902 4627 4207 599 304 105 N
ATOM 37 CA LEU A 7 13.624 -17.312 -0.820 1.00 29.18 C
ANISOU 37 CA LEU A 7 2968 4143 3976 516 282 340 C
ATOM 38 C LEU A 7 12.590 -16.825 -1.821 1.00 28.35 C
ANISOU 38 C LEU A 7 2912 4049 3809 232 384 380 C
ATOM 39 O LEU A 7 11.369 -16.811 -1.552 1.00 27.08 O
ANISOU 39 O LEU A 7 2850 3812 3626 178 332 478 O
ATOM 40 CB LEU A 7 14.282 -16.125 -0.100 1.00 27.89 C
ANISOU 40 CB LEU A 7 3006 3755 3834 566 305 420 C
ATOM 41 CG LEU A 7 15.129 -16.526 1.135 1.00 32.70 C
ANISOU 41 CG LEU A 7 3724 4230 4471 834 169 423 C
ATOM 42 CD1 LEU A 7 16.152 -15.421 1.471 1.00 36.96 C
ANISOU 42 CD1 LEU A 7 4401 4612 5029 849 233 419 C
ATOM 43 CD2 LEU A 7 14.255 -16.813 2.329 1.00 34.18 C
ANISOU 43 CD2 LEU A 7 4131 4253 4602 845 52 579 C
ATOM 44 N VAL A 8 13.062 -16.395 -2.978 1.00 28.92 N
ANISOU 44 N VAL A 8 2966 4196 3824 42 520 295 N
ATOM 45 CA VAL A 8 12.137 -15.858 -3.972 1.00 28.52 C
ANISOU 45 CA VAL A 8 3098 4068 3669 -224 579 344 C
ATOM 46 C VAL A 8 11.248 -16.976 -4.542 1.00 30.43 C
ANISOU 46 C VAL A 8 3232 4464 3865 -370 574 283 C
ATOM 47 O VAL A 8 10.024 -16.808 -4.681 1.00 29.74 O
ANISOU 47 O VAL A 8 3319 4245 3737 -450 520 366 O
ATOM 48 CB VAL A 8 12.902 -15.129 -5.093 1.00 28.40 C
ANISOU 48 CB VAL A 8 3199 4056 3537 -450 723 283 C
ATOM 49 CG1 VAL A 8 11.979 -14.758 -6.221 1.00 29.46 C
ANISOU 49 CG1 VAL A 8 3623 4062 3507 -741 749 329 C
ATOM 50 CG2 VAL A 8 13.555 -13.866 -4.508 1.00 28.40 C
ANISOU 50 CG2 VAL A 8 3348 3872 3571 -306 700 358 C
ATOM 51 N GLN A 9 11.835 -18.134 -4.797 1.00 30.24 N
ANISOU 51 N GLN A 9 2900 4740 3849 -372 608 102 N
ATOM 52 CA GLN A 9 11.042 -19.290 -5.167 1.00 33.38 C
ANISOU 52 CA GLN A 9 3141 5332 4211 -484 581 13 C
ATOM 53 C GLN A 9 10.025 -19.649 -4.085 1.00 32.10 C
ANISOU 53 C GLN A 9 3037 5047 4111 -272 404 154 C
ATOM 54 O GLN A 9 8.920 -19.948 -4.393 1.00 29.66 O
ANISOU 54 O GLN A 9 2795 4724 3750 -413 386 178 O
ATOM 55 CB GLN A 9 11.900 -20.483 -5.529 1.00 36.64 C
ANISOU 55 CB GLN A 9 3136 6161 4624 -467 615 -275 C
ATOM 56 CG GLN A 9 11.139 -21.642 -6.141 1.00 49.45 C
ANISOU 56 CG GLN A 9 4559 8053 6177 -664 618 -428 C
ATOM 57 CD GLN A 9 10.200 -21.219 -7.260 1.00 57.58 C
ANISOU 57 CD GLN A 9 5872 8954 7051 -1132 762 -367 C
ATOM 58 OE1 GLN A 9 10.557 -20.448 -8.142 1.00 66.80 O
ANISOU 58 OE1 GLN A 9 7246 10039 8096 -1435 930 -370 O
ATOM 59 NE2 GLN A 9 9.014 -21.737 -7.237 1.00 52.38 N
ANISOU 59 NE2 GLN A 9 5276 8256 6370 -1193 682 -318 N
ATOM 60 N LYS A 10 10.417 -19.584 -2.821 1.00 31.79 N
ANISOU 60 N LYS A 10 3019 4906 4154 31 284 239 N
ATOM 61 CA LYS A 10 9.450 -19.830 -1.726 1.00 29.77 C
ANISOU 61 CA LYS A 10 2885 4527 3901 155 146 377 C
ATOM 62 C LYS A 10 8.346 -18.786 -1.776 1.00 27.93 C
ANISOU 62 C LYS A 10 2879 4095 3637 9 192 491 C
ATOM 63 O LYS A 10 7.213 -19.120 -1.549 1.00 27.43 O
ANISOU 63 O LYS A 10 2856 4030 3538 -30 139 520 O
ATOM 64 CB LYS A 10 10.112 -19.715 -0.348 1.00 31.20 C
ANISOU 64 CB LYS A 10 3179 4562 4116 414 36 466 C
ATOM 65 CG LYS A 10 9.153 -20.026 0.825 1.00 34.49 C
ANISOU 65 CG LYS A 10 3770 4867 4468 457 -80 598 C
ATOM 66 CD LYS A 10 9.862 -19.893 2.166 1.00 44.00 C
ANISOU 66 CD LYS A 10 5198 5877 5645 628 -176 693 C
ATOM 67 N ALA A 11 8.668 -17.518 -2.045 1.00 25.86 N
ANISOU 67 N ALA A 11 2760 3683 3382 -39 265 525 N
ATOM 68 CA ALA A 11 7.601 -16.514 -2.115 1.00 24.36 C
ANISOU 68 CA ALA A 11 2765 3331 3160 -96 250 569 C
ATOM 69 C ALA A 11 6.612 -16.834 -3.230 1.00 24.85 C
ANISOU 69 C ALA A 11 2908 3390 3145 -273 250 521 C
ATOM 70 O ALA A 11 5.412 -16.623 -3.050 1.00 25.41 O
ANISOU 70 O ALA A 11 3076 3386 3193 -255 181 518 O
ATOM 71 CB ALA A 11 8.163 -15.081 -2.262 1.00 21.09 C
ANISOU 71 CB ALA A 11 2498 2768 2748 -73 279 584 C
ATOM 72 N ARG A 12 7.112 -17.278 -4.390 1.00 25.37 N
ANISOU 72 N ARG A 12 2954 3538 3147 -473 337 455 N
ATOM 73 CA ARG A 12 6.249 -17.579 -5.528 1.00 27.61 C
ANISOU 73 CA ARG A 12 3394 3784 3314 -725 356 405 C
ATOM 74 C ARG A 12 5.331 -18.760 -5.211 1.00 27.11 C
ANISOU 74 C ARG A 12 3170 3870 3262 -727 299 362 C
ATOM 75 O ARG A 12 4.182 -18.784 -5.627 1.00 29.00 O
ANISOU 75 O ARG A 12 3586 3999 3434 -826 253 348 O
ATOM 76 CB ARG A 12 7.061 -17.897 -6.791 1.00 28.03 C
ANISOU 76 CB ARG A 12 3444 3955 3249 -1044 511 307 C
ATOM 77 CG ARG A 12 7.928 -16.746 -7.355 1.00 31.76 C
ANISOU 77 CG ARG A 12 4154 4271 3642 -1129 583 342 C
ATOM 78 CD ARG A 12 8.591 -17.221 -8.670 1.00 37.75 C
ANISOU 78 CD ARG A 12 4918 5203 4222 -1562 781 205 C
ATOM 79 NE ARG A 12 9.668 -16.341 -9.133 1.00 49.63 N
ANISOU 79 NE ARG A 12 6576 6651 5632 -1670 885 208 N
ATOM 80 CZ ARG A 12 10.970 -16.662 -9.187 1.00 54.70 C
ANISOU 80 CZ ARG A 12 6902 7591 6289 -1721 1038 60 C
ATOM 81 NH1 ARG A 12 11.415 -17.838 -8.722 1.00 52.77 N
ANISOU 81 NH1 ARG A 12 6154 7722 6174 -1594 1061 -115 N
ATOM 82 NH2 ARG A 12 11.842 -15.798 -9.717 1.00 52.39 N
ANISOU 82 NH2 ARG A 12 6810 7228 5867 -1874 1144 61 N
ATOM 83 N LEU A 13 5.848 -19.745 -4.490 1.00 26.10 N
ANISOU 83 N LEU A 13 2741 3976 3202 -596 275 329 N
ATOM 84 CA LEU A 13 5.054 -20.937 -4.128 1.00 28.49 C
ANISOU 84 CA LEU A 13 2894 4440 3491 -575 191 286 C
ATOM 85 C LEU A 13 4.017 -20.558 -3.078 1.00 28.11 C
ANISOU 85 C LEU A 13 2979 4244 3455 -428 97 388 C
ATOM 86 O LEU A 13 2.858 -20.965 -3.169 1.00 28.78 O
ANISOU 86 O LEU A 13 3109 4339 3487 -501 56 356 O
ATOM 87 CB LEU A 13 5.980 -22.019 -3.563 1.00 29.07 C
ANISOU 87 CB LEU A 13 2665 4771 3609 -393 124 212 C
ATOM 88 CG LEU A 13 6.926 -22.711 -4.529 1.00 30.26 C
ANISOU 88 CG LEU A 13 2539 5220 3739 -523 209 -3 C
ATOM 89 CD1 LEU A 13 7.912 -23.573 -3.749 1.00 30.79 C
ANISOU 89 CD1 LEU A 13 2333 5497 3869 -187 67 -102 C
ATOM 90 CD2 LEU A 13 6.139 -23.560 -5.549 1.00 36.74 C
ANISOU 90 CD2 LEU A 13 3263 6240 4455 -842 263 -158 C
ATOM 91 N ALA A 14 4.418 -19.678 -2.159 1.00 27.59 N
ANISOU 91 N ALA A 14 2985 4057 3442 -264 87 477 N
ATOM 92 CA ALA A 14 3.549 -19.290 -1.038 1.00 25.60 C
ANISOU 92 CA ALA A 14 2813 3743 3173 -181 39 521 C
ATOM 93 C ALA A 14 2.392 -18.526 -1.615 1.00 27.09 C
ANISOU 93 C ALA A 14 3141 3819 3333 -239 33 449 C
ATOM 94 O ALA A 14 1.256 -18.693 -1.178 1.00 27.47 O
ANISOU 94 O ALA A 14 3197 3906 3336 -238 -5 395 O
ATOM 95 CB ALA A 14 4.351 -18.418 -0.042 1.00 24.65 C
ANISOU 95 CB ALA A 14 2739 3538 3091 -69 61 589 C
ATOM 96 N GLU A 15 2.660 -17.684 -2.596 1.00 26.23 N
ANISOU 96 N GLU A 15 3179 3560 3227 -276 51 429 N
ATOM 97 CA GLU A 15 1.632 -16.969 -3.316 1.00 27.24 C
ANISOU 97 CA GLU A 15 3535 3513 3303 -279 -19 348 C
ATOM 98 C GLU A 15 0.622 -17.877 -3.961 1.00 27.76 C
ANISOU 98 C GLU A 15 3660 3590 3296 -421 -47 286 C
ATOM 99 O GLU A 15 -0.526 -17.669 -3.813 1.00 27.56 O
ANISOU 99 O GLU A 15 3713 3513 3246 -344 -127 193 O
ATOM 100 CB GLU A 15 2.232 -16.063 -4.375 1.00 26.03 C
ANISOU 100 CB GLU A 15 3632 3150 3107 -325 -23 367 C
ATOM 101 CG GLU A 15 1.365 -14.932 -4.808 1.00 33.63 C
ANISOU 101 CG GLU A 15 4896 3868 4013 -186 -175 281 C
ATOM 102 CD GLU A 15 0.552 -15.220 -6.048 1.00 47.42 C
ANISOU 102 CD GLU A 15 6990 5401 5626 -340 -246 242 C
ATOM 103 OE1 GLU A 15 0.833 -16.169 -6.773 1.00 56.39 O
ANISOU 103 OE1 GLU A 15 8146 6586 6694 -639 -134 283 O
ATOM 104 OE2 GLU A 15 -0.409 -14.521 -6.300 1.00 45.15 O
ANISOU 104 OE2 GLU A 15 6965 4903 5287 -166 -424 137 O
ATOM 105 N GLN A 16 1.083 -18.854 -4.690 1.00 27.25 N
ANISOU 105 N GLN A 16 3538 3622 3193 -633 23 298 N
ATOM 106 CA GLN A 16 0.171 -19.725 -5.341 1.00 29.90 C
ANISOU 106 CA GLN A 16 3930 3985 3446 -817 9 219 C
ATOM 107 C GLN A 16 -0.657 -20.498 -4.327 1.00 27.90 C
ANISOU 107 C GLN A 16 3482 3910 3211 -715 -45 189 C
ATOM 108 O GLN A 16 -1.756 -20.810 -4.584 1.00 29.72 O
ANISOU 108 O GLN A 16 3805 4106 3380 -776 -93 106 O
ATOM 109 CB GLN A 16 0.911 -20.647 -6.280 1.00 31.52 C
ANISOU 109 CB GLN A 16 4035 4350 3589 -1110 118 178 C
ATOM 110 CG GLN A 16 1.533 -19.904 -7.420 1.00 38.34 C
ANISOU 110 CG GLN A 16 5181 5026 4361 -1318 197 189 C
ATOM 111 CD GLN A 16 2.366 -20.766 -8.297 1.00 43.66 C
ANISOU 111 CD GLN A 16 5693 5946 4950 -1666 356 89 C
ATOM 112 OE1 GLN A 16 3.552 -20.872 -8.106 1.00 44.59 O
ANISOU 112 OE1 GLN A 16 5552 6265 5124 -1625 436 71 O
ATOM 113 NE2 GLN A 16 1.755 -21.365 -9.276 1.00 48.38 N
ANISOU 113 NE2 GLN A 16 6440 6545 5398 -2025 408 -13 N
ATOM 114 N ALA A 17 -0.102 -20.773 -3.173 1.00 25.99 N
ANISOU 114 N ALA A 17 3024 3827 3023 -573 -43 258 N
ATOM 115 CA ALA A 17 -0.783 -21.504 -2.114 1.00 28.23 C
ANISOU 115 CA ALA A 17 3194 4264 3268 -512 -94 255 C
ATOM 116 C ALA A 17 -1.647 -20.603 -1.203 1.00 29.46 C
ANISOU 116 C ALA A 17 3418 4366 3409 -404 -104 211 C
ATOM 117 O ALA A 17 -2.296 -21.094 -0.246 1.00 29.57 O
ANISOU 117 O ALA A 17 3375 4514 3345 -410 -116 193 O
ATOM 118 CB ALA A 17 0.228 -22.270 -1.288 1.00 29.73 C
ANISOU 118 CB ALA A 17 3223 4606 3466 -422 -121 347 C
ATOM 119 N GLU A 18 -1.700 -19.328 -1.521 1.00 27.81 N
ANISOU 119 N GLU A 18 3326 3994 3246 -320 -105 156 N
ATOM 120 CA GLU A 18 -2.399 -18.350 -0.717 1.00 28.68 C
ANISOU 120 CA GLU A 18 3420 4126 3349 -197 -116 30 C
ATOM 121 C GLU A 18 -1.939 -18.386 0.716 1.00 26.78 C
ANISOU 121 C GLU A 18 3053 4044 3080 -220 -39 95 C
ATOM 122 O GLU A 18 -2.704 -18.198 1.616 1.00 25.86 O
ANISOU 122 O GLU A 18 2870 4069 2886 -249 -4 -24 O
ATOM 123 CB GLU A 18 -3.891 -18.507 -0.827 1.00 29.41 C
ANISOU 123 CB GLU A 18 3541 4258 3377 -184 -172 -158 C
ATOM 124 CG GLU A 18 -4.422 -18.079 -2.130 1.00 36.54 C
ANISOU 124 CG GLU A 18 4684 4917 4283 -123 -282 -255 C
ATOM 125 CD GLU A 18 -5.867 -18.438 -2.313 1.00 44.57 C
ANISOU 125 CD GLU A 18 5760 5946 5230 -108 -354 -448 C
ATOM 126 OE1 GLU A 18 -6.688 -17.871 -1.638 1.00 45.57 O
ANISOU 126 OE1 GLU A 18 5782 6191 5343 43 -383 -661 O
ATOM 127 OE2 GLU A 18 -6.179 -19.302 -3.107 1.00 45.92 O
ANISOU 127 OE2 GLU A 18 6057 6040 5351 -264 -372 -420 O
ATOM 128 N ARG A 19 -0.659 -18.584 0.904 1.00 24.95 N
ANISOU 128 N ARG A 19 2816 3777 2887 -225 -11 261 N
ATOM 129 CA ARG A 19 -0.080 -18.512 2.244 1.00 26.51 C
ANISOU 129 CA ARG A 19 3006 4035 3032 -258 43 340 C
ATOM 130 C ARG A 19 0.707 -17.212 2.362 1.00 26.25 C
ANISOU 130 C ARG A 19 2978 3920 3076 -195 89 324 C
ATOM 131 O ARG A 19 1.918 -17.206 2.111 1.00 25.41 O
ANISOU 131 O ARG A 19 2904 3713 3037 -146 88 445 O
ATOM 132 CB ARG A 19 0.812 -19.730 2.481 1.00 27.36 C
ANISOU 132 CB ARG A 19 3146 4139 3110 -252 -10 512 C
ATOM 133 CG ARG A 19 -0.050 -21.000 2.646 1.00 29.00 C
ANISOU 133 CG ARG A 19 3351 4468 3199 -315 -78 507 C
ATOM 134 CD ARG A 19 0.756 -22.267 2.664 1.00 27.92 C
ANISOU 134 CD ARG A 19 3213 4357 3036 -229 -201 613 C
ATOM 135 NE ARG A 19 1.668 -22.243 3.809 1.00 28.05 N