HEADER HYDROLASE4/HYDROLASE INHIBITOR 21-APR-16 5JI6
TITLE POTENT, REVERSIBLE METAP2 INHIBITORS VIA FBDD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE AMINOPEPTIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 87-455;
COMPND 5 SYNONYM: METAP 2,INITIATION FACTOR 2-ASSOCIATED 67 KDA GLYCOPROTEIN,
COMPND 6 P67EIF2,PEPTIDASE M;
COMPND 7 EC: 3.4.11.18;
COMPND 8 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: METAP2, MNPEP, P67EIF2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9
KEYWDS HYDROLASE, PEPTIDASE, METAL ION BINDING, PROTEOLYSIS, HYDROLASE4-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DOUGAN,J.D.LAWSON
REVDAT 3 22-NOV-17 5JI6 1 JRNL REMARK
REVDAT 2 15-JUN-16 5JI6 1 JRNL
REVDAT 1 25-MAY-16 5JI6 0
JRNL AUTH Z.CHERUVALLATH,M.TANG,C.MCBRIDE,M.KOMANDLA,J.MIURA,T.TON-NU,
JRNL AUTH 2 P.ERIKSON,J.FENG,P.FARRELL,J.D.LAWSON,D.VANDERPOOL,Y.WU,
JRNL AUTH 3 D.R.DOUGAN,A.PLONOWSKI,C.HOLUB,C.LARSON
JRNL TITL DISCOVERY OF POTENT, REVERSIBLE METAP2 INHIBITORS VIA
JRNL TITL 2 FRAGMENT BASED DRUG DISCOVERY AND STRUCTURE BASED DRUG
JRNL TITL 3 DESIGN-PART 1.
JRNL REF BIOORG.MED.CHEM.LETT. V. 26 2774 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 27155900
JRNL DOI 10.1016/J.BMCL.2016.04.073
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23252
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
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 : 1250
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1660
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.87000
REMARK 3 B22 (A**2) : -3.85000
REMARK 3 B33 (A**2) : -0.02000
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): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.023
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2985 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4048 ; 1.178 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 368 ; 5.842 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;34.139 ;24.412
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 516 ;14.463 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;12.130 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2272 ; 0.004 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 8
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 110 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8932 12.2014 1.9128
REMARK 3 T TENSOR
REMARK 3 T11: 0.5925 T22: 0.1259
REMARK 3 T33: 0.2890 T12: 0.0368
REMARK 3 T13: -0.1175 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.0571 L22: 3.3868
REMARK 3 L33: 1.5589 L12: -0.2261
REMARK 3 L13: -0.0875 L23: -0.5191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0817 S12: -0.2263 S13: -0.6708
REMARK 3 S21: -1.2493 S22: -0.0729 S23: 0.5926
REMARK 3 S31: 0.6087 S32: 0.0861 S33: 0.1545
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 150 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5779 17.0729 2.7056
REMARK 3 T TENSOR
REMARK 3 T11: 0.3422 T22: 0.1259
REMARK 3 T33: 0.1782 T12: 0.0041
REMARK 3 T13: -0.1938 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.3480 L22: 3.2136
REMARK 3 L33: 1.1293 L12: 0.4219
REMARK 3 L13: -0.6110 L23: -0.5074
REMARK 3 S TENSOR
REMARK 3 S11: -0.1908 S12: 0.0712 S13: 0.0376
REMARK 3 S21: -0.8258 S22: 0.2144 S23: 0.6444
REMARK 3 S31: 0.3870 S32: -0.0588 S33: -0.0236
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 190 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6576 28.6705 14.0506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0190 T22: 0.1004
REMARK 3 T33: 0.0237 T12: 0.0016
REMARK 3 T13: 0.0047 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.5219 L22: 3.7030
REMARK 3 L33: 1.6098 L12: -0.0472
REMARK 3 L13: 0.3887 L23: -0.6104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0868 S12: 0.0150 S13: 0.0203
REMARK 3 S21: -0.1043 S22: -0.0331 S23: 0.0943
REMARK 3 S31: 0.0305 S32: 0.0983 S33: -0.0538
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 270 A 309
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9450 13.2437 23.4880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.1484
REMARK 3 T33: 0.3375 T12: -0.0697
REMARK 3 T13: 0.0541 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.6491 L22: 3.3976
REMARK 3 L33: 1.9017 L12: -0.1049
REMARK 3 L13: 0.2964 L23: -0.3300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.1275 S13: -0.1338
REMARK 3 S21: 0.2768 S22: 0.0984 S23: 0.9976
REMARK 3 S31: 0.1988 S32: -0.3178 S33: -0.0928
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 310 A 374
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8850 21.2816 22.8952
REMARK 3 T TENSOR
REMARK 3 T11: 0.1297 T22: 0.1677
REMARK 3 T33: 0.4614 T12: -0.0269
REMARK 3 T13: 0.1364 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.6637 L22: 2.8782
REMARK 3 L33: 3.5141 L12: -0.1030
REMARK 3 L13: 0.9769 L23: -0.9389
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: -0.1641 S13: -0.0165
REMARK 3 S21: 0.4061 S22: 0.0992 S23: 1.0949
REMARK 3 S31: 0.0437 S32: -0.5316 S33: -0.1256
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 375 A 394
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9571 41.4909 15.0949
REMARK 3 T TENSOR
REMARK 3 T11: 0.0473 T22: 0.1381
REMARK 3 T33: 0.3054 T12: 0.0322
REMARK 3 T13: 0.0711 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.0743 L22: 3.7707
REMARK 3 L33: 2.7664 L12: -0.4943
REMARK 3 L13: 0.0337 L23: -1.2870
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.0013 S13: -0.1367
REMARK 3 S21: 0.3149 S22: 0.1928 S23: 0.9857
REMARK 3 S31: -0.3254 S32: -0.2826 S33: -0.1665
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 395 A 414
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4886 47.9506 5.7046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1874 T22: 0.1212
REMARK 3 T33: 0.2363 T12: 0.0216
REMARK 3 T13: 0.0344 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2176 L22: 5.0454
REMARK 3 L33: 2.3898 L12: -1.0090
REMARK 3 L13: 0.0024 L23: -0.4214
REMARK 3 S TENSOR
REMARK 3 S11: 0.1108 S12: -0.0202 S13: -0.0761
REMARK 3 S21: -0.2428 S22: 0.1304 S23: 0.6033
REMARK 3 S31: -0.3473 S32: -0.1701 S33: -0.2413
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 415 A 478
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2194 31.6639 14.8877
REMARK 3 T TENSOR
REMARK 3 T11: 0.0389 T22: 0.0938
REMARK 3 T33: 0.1402 T12: -0.0104
REMARK 3 T13: 0.0281 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.3145 L22: 3.2962
REMARK 3 L33: 1.4970 L12: -0.2915
REMARK 3 L13: 0.2382 L23: -0.7249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0962 S12: -0.0205 S13: -0.0013
REMARK 3 S21: 0.0461 S22: 0.0233 S23: 0.6264
REMARK 3 S31: -0.0116 S32: -0.1259 S33: -0.1194
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5JI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XFIT
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24715
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.91600
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24.% PEG MME 2000, 0.05M MES PH 5.9,
REMARK 280 0.0175M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 49.73450
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 49.73450
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 44.48100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.05000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.48100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.05000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.73450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.48100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.05000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.73450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.48100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.05000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 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 GLY A 349
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 SER A 117 -14.16 -149.94
REMARK 500 CYS A 223 39.14 -143.46
REMARK 500 ASN A 226 -114.86 59.68
REMARK 500 ASP A 294 -0.89 74.51
REMARK 500 MET A 378 -178.93 69.44
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 MN A 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 251 OD1
REMARK 620 2 ASP A 251 OD2 57.3
REMARK 620 3 ASP A 262 OD2 88.3 145.3
REMARK 620 4 GLU A 459 OE2 102.7 98.5 84.2
REMARK 620 5 HOH A 605 O 84.7 87.3 94.0 172.3
REMARK 620 6 HOH A 620 O 138.6 82.5 132.1 91.8 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 262 OD1
REMARK 620 2 HIS A 331 NE2 96.1
REMARK 620 3 GLU A 364 OE1 159.7 81.8
REMARK 620 4 GLU A 459 OE1 75.7 109.0 85.8
REMARK 620 5 6KN A 504 N15 95.4 80.9 104.2 167.1
REMARK 620 6 HOH A 620 O 101.1 158.4 86.5 88.0 84.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6KN A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JHU RELATED DB: PDB
REMARK 900 RELATED ID: 5JFR RELATED DB: PDB
DBREF 5JI6 A 110 478 UNP P50579 MAP2_HUMAN 87 455
SEQRES 1 A 369 LYS VAL GLN THR ASP PRO PRO SER VAL PRO ILE CYS ASP
SEQRES 2 A 369 LEU TYR PRO ASN GLY VAL PHE PRO LYS GLY GLN GLU CYS
SEQRES 3 A 369 GLU TYR PRO PRO THR GLN ASP GLY ARG THR ALA ALA TRP
SEQRES 4 A 369 ARG THR THR SER GLU GLU LYS LYS ALA LEU ASP GLN ALA
SEQRES 5 A 369 SER GLU GLU ILE TRP ASN ASP PHE ARG GLU ALA ALA GLU
SEQRES 6 A 369 ALA HIS ARG GLN VAL ARG LYS TYR VAL MET SER TRP ILE
SEQRES 7 A 369 LYS PRO GLY MET THR MET ILE GLU ILE CYS GLU LYS LEU
SEQRES 8 A 369 GLU ASP CYS SER ARG LYS LEU ILE LYS GLU ASN GLY LEU
SEQRES 9 A 369 ASN ALA GLY LEU ALA PHE PRO THR GLY CYS SER LEU ASN
SEQRES 10 A 369 ASN CYS ALA ALA HIS TYR THR PRO ASN ALA GLY ASP THR
SEQRES 11 A 369 THR VAL LEU GLN TYR ASP ASP ILE CYS LYS ILE ASP PHE
SEQRES 12 A 369 GLY THR HIS ILE SER GLY ARG ILE ILE ASP CYS ALA PHE
SEQRES 13 A 369 THR VAL THR PHE ASN PRO LYS TYR ASP THR LEU LEU LYS
SEQRES 14 A 369 ALA VAL LYS ASP ALA THR ASN THR GLY ILE LYS CYS ALA
SEQRES 15 A 369 GLY ILE ASP VAL ARG LEU CYS ASP VAL GLY GLU ALA ILE
SEQRES 16 A 369 GLN GLU VAL MET GLU SER TYR GLU VAL GLU ILE ASP GLY
SEQRES 17 A 369 LYS THR TYR GLN VAL LYS PRO ILE ARG ASN LEU ASN GLY
SEQRES 18 A 369 HIS SER ILE GLY GLN TYR ARG ILE HIS ALA GLY LYS THR
SEQRES 19 A 369 VAL PRO ILE VAL LYS GLY GLY GLU ALA THR ARG MET GLU
SEQRES 20 A 369 GLU GLY GLU VAL TYR ALA ILE GLU THR PHE GLY SER THR
SEQRES 21 A 369 GLY LYS GLY VAL VAL HIS ASP ASP MET GLU CYS SER HIS
SEQRES 22 A 369 TYR MET LYS ASN PHE ASP VAL GLY HIS VAL PRO ILE ARG
SEQRES 23 A 369 LEU PRO ARG THR LYS HIS LEU LEU ASN VAL ILE ASN GLU
SEQRES 24 A 369 ASN PHE GLY THR LEU ALA PHE CYS ARG ARG TRP LEU ASP
SEQRES 25 A 369 ARG LEU GLY GLU SER LYS TYR LEU MET ALA LEU LYS ASN
SEQRES 26 A 369 LEU CYS ASP LEU GLY ILE VAL ASP PRO TYR PRO PRO LEU
SEQRES 27 A 369 CYS ASP ILE LYS GLY SER TYR THR ALA GLN PHE GLU HIS
SEQRES 28 A 369 THR ILE LEU LEU ARG PRO THR CYS LYS GLU VAL VAL SER
SEQRES 29 A 369 ARG GLY ASP ASP TYR
HET MN A 501 1
HET MN A 502 1
HET SO4 A 503 5
HET 6KN A 504 20
HETNAM MN MANGANESE (II) ION
HETNAM SO4 SULFATE ION
HETNAM 6KN 4-(3-METHYLPYRIDIN-4-YL)-6-(TRIFLUOROMETHYL)-1H-
HETNAM 2 6KN INDAZOLE
FORMUL 2 MN 2(MN 2+)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 6KN C14 H10 F3 N3
FORMUL 6 HOH *132(H2 O)
HELIX 1 AA1 PRO A 119 TYR A 124 1 6
HELIX 2 AA2 ALA A 147 SER A 152 1 6
HELIX 3 AA3 SER A 152 SER A 162 1 11
HELIX 4 AA4 SER A 162 ILE A 187 1 26
HELIX 5 AA5 THR A 192 LYS A 209 1 18
HELIX 6 AA6 ASN A 211 LEU A 213 5 3
HELIX 7 AA7 ASN A 270 LYS A 272 5 3
HELIX 8 AA8 TYR A 273 ALA A 291 1 19
HELIX 9 AA9 ARG A 296 GLU A 309 1 14
HELIX 10 AB1 LEU A 396 PHE A 410 1 15
HELIX 11 AB2 ARG A 417 LEU A 423 1 7
HELIX 12 AB3 TYR A 428 LEU A 438 1 11
SHEET 1 AA1 5 GLN A 133 CYS A 135 0
SHEET 2 AA1 5 LYS A 469 VAL A 471 -1 O LYS A 469 N CYS A 135
SHEET 3 AA1 5 THR A 455 LEU A 464 -1 N LEU A 463 O GLU A 470
SHEET 4 AA1 5 VAL A 360 SER A 368 -1 N TYR A 361 O ILE A 462
SHEET 5 AA1 5 LYS A 323 PRO A 324 -1 N LYS A 323 O SER A 368
SHEET 1 AA2 6 GLN A 133 CYS A 135 0
SHEET 2 AA2 6 LYS A 469 VAL A 471 -1 O LYS A 469 N CYS A 135
SHEET 3 AA2 6 THR A 455 LEU A 464 -1 N LEU A 463 O GLU A 470
SHEET 4 AA2 6 VAL A 360 SER A 368 -1 N TYR A 361 O ILE A 462
SHEET 5 AA2 6 GLY A 330 SER A 332 -1 N HIS A 331 O ALA A 362
SHEET 6 AA2 6 THR A 343 VAL A 344 -1 O VAL A 344 N GLY A 330
SHEET 1 AA3 3 ALA A 215 LEU A 225 0
SHEET 2 AA3 3 CYS A 248 ILE A 256 -1 O ASP A 251 N GLY A 222
SHEET 3 AA3 3 ARG A 259 VAL A 267 -1 O VAL A 267 N CYS A 248
SHEET 1 AA4 3 CYS A 228 ALA A 230 0
SHEET 2 AA4 3 LEU A 447 CYS A 448 -1 O LEU A 447 N ALA A 229
SHEET 3 AA4 3 HIS A 375 ASP A 376 -1 N HIS A 375 O CYS A 448
SHEET 1 AA5 2 GLU A 312 ILE A 315 0
SHEET 2 AA5 2 LYS A 318 GLN A 321 -1 O TYR A 320 N VAL A 313
SHEET 1 AA6 3 PHE A 415 CYS A 416 0
SHEET 2 AA6 3 HIS A 382 LYS A 385 -1 N TYR A 383 O PHE A 415
SHEET 3 AA6 3 VAL A 441 TYR A 444 -1 O TYR A 444 N HIS A 382
SSBOND 1 CYS A 228 CYS A 448 1555 1555 2.07
LINK OD1 ASP A 251 MN MN A 501 1555 1555 2.30
LINK OD2 ASP A 251 MN MN A 501 1555 1555 2.20
LINK OD1 ASP A 262 MN MN A 502 1555 1555 2.01
LINK OD2 ASP A 262 MN MN A 501 1555 1555 1.87
LINK NE2 HIS A 331 MN MN A 502 1555 1555 2.18
LINK OE1 GLU A 364 MN MN A 502 1555 1555 2.17
LINK OE1 GLU A 459 MN MN A 502 1555 1555 2.13
LINK OE2 GLU A 459 MN MN A 501 1555 1555 1.99
LINK MN MN A 501 O HOH A 605 1555 1555 2.21
LINK MN MN A 501 O HOH A 620 1555 1555 1.94
LINK MN MN A 502 N15 6KN A 504 1555 1555 2.15
LINK MN MN A 502 O HOH A 620 1555 1555 2.34
CISPEP 1 ASP A 114 PRO A 115 0 -1.03
SITE 1 AC1 6 ASP A 251 ASP A 262 GLU A 459 MN A 502
SITE 2 AC1 6 HOH A 605 HOH A 620
SITE 1 AC2 7 ASP A 262 HIS A 331 GLU A 364 GLU A 459
SITE 2 AC2 7 MN A 501 6KN A 504 HOH A 620
SITE 1 AC3 2 HIS A 391 HOH A 668
SITE 1 AC4 13 HIS A 231 ASP A 262 HIS A 331 ILE A 338
SITE 2 AC4 13 HIS A 339 GLU A 364 HIS A 382 MET A 384
SITE 3 AC4 13 ALA A 414 TYR A 444 MN A 502 HOH A 605
SITE 4 AC4 13 HOH A 620
CRYST1 88.962 100.100 99.469 90.00 90.00 90.00 C 2 2 21 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 0.011241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010053 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
