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HEADER SIGNALING PROTEIN 16-OCT-19 6L4H
TITLE CRYSTAL STRUCTURE OF HUMAN NDRG3 C30S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NDRG3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: N-MYC DOWNSTREAM-REGULATED GENE 3 PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: NDRG3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE FOLD, NDRG3, UNFOLDED HELIX, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.KIM,B.W.HAN
REVDAT 1 26-AUG-20 6L4H 0
JRNL AUTH K.R.KIM,K.A.KIM,J.S.PARK,J.Y.JANG,Y.CHOI,H.H.LEE,D.C.LEE,
JRNL AUTH 2 K.C.PARK,Y.I.YEOM,H.J.KIM,B.W.HAN
JRNL TITL STRUCTURAL AND BIOPHYSICAL ANALYSES OF HUMAN N-MYC
JRNL TITL 2 DOWNSTREAM-REGULATED GENE 3 (NDRG3) PROTEIN.
JRNL REF BIOMOLECULES V. 10 2020
JRNL REFN ESSN 2218-273X
JRNL PMID 31935861
JRNL DOI 10.3390/BIOM10010090
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 26570
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.013
REMARK 3 FREE R VALUE TEST SET COUNT : 1332
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1701
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8670
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 121.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.13400
REMARK 3 B22 (A**2) : -1.13400
REMARK 3 B33 (A**2) : 3.67800
REMARK 3 B12 (A**2) : -0.56700
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.568
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.464
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 69.859
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.873
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.831
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8855 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 8083 ; 0.036 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12041 ; 1.246 ; 1.635
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18851 ; 2.296 ; 1.567
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1110 ; 6.677 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 451 ;31.621 ;24.368
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1464 ;13.709 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;13.419 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1166 ; 0.046 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9942 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1662 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2026 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 40 ; 0.221 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4251 ; 0.154 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 123 ; 0.168 ; 0.200
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): 4461 ; 1.906 ; 7.732
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4460 ; 1.906 ; 7.731
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5564 ; 3.433 ;11.591
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5565 ; 3.433 ;11.593
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4394 ; 1.627 ; 7.837
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4395 ; 1.627 ; 7.838
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6477 ; 2.866 ;11.690
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6478 ; 2.866 ;11.691
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 : 4
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 29 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7830 -24.4557 -53.1431
REMARK 3 T TENSOR
REMARK 3 T11: 0.8222 T22: 0.3546
REMARK 3 T33: 0.4523 T12: -0.0576
REMARK 3 T13: 0.0541 T23: 0.2774
REMARK 3 L TENSOR
REMARK 3 L11: 1.8726 L22: 1.5377
REMARK 3 L33: 0.4454 L12: -1.0593
REMARK 3 L13: -0.6615 L23: 0.1831
REMARK 3 S TENSOR
REMARK 3 S11: 0.1664 S12: -0.0518 S13: 0.0809
REMARK 3 S21: -0.1900 S22: -0.0576 S23: -0.0895
REMARK 3 S31: -0.0203 S32: 0.0286 S33: -0.1088
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 : B 29 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4921 -26.4076 -48.5784
REMARK 3 T TENSOR
REMARK 3 T11: 0.7854 T22: 0.3693
REMARK 3 T33: 0.4897 T12: -0.0059
REMARK 3 T13: -0.0566 T23: 0.2254
REMARK 3 L TENSOR
REMARK 3 L11: 2.0372 L22: 1.6037
REMARK 3 L33: 0.9789 L12: 0.9341
REMARK 3 L13: 0.8847 L23: 0.4922
REMARK 3 S TENSOR
REMARK 3 S11: 0.2054 S12: -0.0457 S13: 0.0615
REMARK 3 S21: 0.0195 S22: -0.0914 S23: 0.0930
REMARK 3 S31: -0.0539 S32: -0.0052 S33: -0.1140
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 : C 29 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0444 -39.9732 -16.4747
REMARK 3 T TENSOR
REMARK 3 T11: 1.0885 T22: 0.5129
REMARK 3 T33: 0.3022 T12: -0.4415
REMARK 3 T13: -0.4244 T23: 0.3806
REMARK 3 L TENSOR
REMARK 3 L11: 0.7975 L22: 1.1543
REMARK 3 L33: 1.6427 L12: 0.0419
REMARK 3 L13: 0.7451 L23: -0.6119
REMARK 3 S TENSOR
REMARK 3 S11: 0.4252 S12: 0.0001 S13: -0.0421
REMARK 3 S21: 0.1767 S22: -0.3367 S23: -0.1579
REMARK 3 S31: 0.0924 S32: -0.0520 S33: -0.0885
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 : D 29 D 317
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4590 -69.3376 -12.7358
REMARK 3 T TENSOR
REMARK 3 T11: 1.0805 T22: 0.5408
REMARK 3 T33: 0.4981 T12: -0.7520
REMARK 3 T13: -0.6307 T23: 0.4621
REMARK 3 L TENSOR
REMARK 3 L11: 0.5117 L22: 2.6790
REMARK 3 L33: 0.9368 L12: 0.2709
REMARK 3 L13: 0.2802 L23: -0.5572
REMARK 3 S TENSOR
REMARK 3 S11: 0.1141 S12: -0.0288 S13: 0.0342
REMARK 3 S21: -0.0815 S22: 0.2319 S23: 0.0570
REMARK 3 S31: 0.2736 S32: -0.2356 S33: -0.3460
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 6L4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1300014175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-18
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26798
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.73200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHENIX
REMARK 200 STARTING MODEL: 6L4B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM CITRATE TRIBASIC
REMARK 280 DEHYDRATE, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 110.90333
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 221.80667
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 221.80667
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 110.90333
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: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 49.87950
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -86.39383
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -110.90333
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 99.75900
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLU A 3
REMARK 465 LEU A 4
REMARK 465 GLN A 5
REMARK 465 ASP A 6
REMARK 465 VAL A 7
REMARK 465 GLN A 8
REMARK 465 LEU A 9
REMARK 465 THR A 10
REMARK 465 GLU A 11
REMARK 465 ILE A 12
REMARK 465 LYS A 13
REMARK 465 PRO A 14
REMARK 465 LEU A 15
REMARK 465 LEU A 16
REMARK 465 ASN A 17
REMARK 465 ASP A 18
REMARK 465 LYS A 19
REMARK 465 ASN A 20
REMARK 465 GLY A 21
REMARK 465 THR A 22
REMARK 465 ARG A 23
REMARK 465 ASN A 24
REMARK 465 PHE A 25
REMARK 465 GLN A 26
REMARK 465 ASP A 27
REMARK 465 PHE A 28
REMARK 465 SER A 318
REMARK 465 ALA A 319
REMARK 465 SER A 320
REMARK 465 MET A 321
REMARK 465 THR A 322
REMARK 465 ARG A 323
REMARK 465 LEU A 324
REMARK 465 ALA A 325
REMARK 465 ARG A 326
REMARK 465 SER A 327
REMARK 465 ARG A 328
REMARK 465 THR A 329
REMARK 465 HIS A 330
REMARK 465 SER A 331
REMARK 465 THR A 332
REMARK 465 SER A 333
REMARK 465 SER A 334
REMARK 465 SER A 335
REMARK 465 LEU A 336
REMARK 465 GLY A 337
REMARK 465 SER A 338
REMARK 465 GLY A 339
REMARK 465 GLU A 340
REMARK 465 SER A 341
REMARK 465 PRO A 342
REMARK 465 PHE A 343
REMARK 465 SER A 344
REMARK 465 ARG A 345
REMARK 465 SER A 346
REMARK 465 VAL A 347
REMARK 465 THR A 348
REMARK 465 SER A 349
REMARK 465 ASN A 350
REMARK 465 GLN A 351
REMARK 465 SER A 352
REMARK 465 ASP A 353
REMARK 465 GLY A 354
REMARK 465 THR A 355
REMARK 465 GLN A 356
REMARK 465 GLU A 357
REMARK 465 SER A 358
REMARK 465 CYS A 359
REMARK 465 GLU A 360
REMARK 465 SER A 361
REMARK 465 PRO A 362
REMARK 465 ASP A 363
REMARK 465 VAL A 364
REMARK 465 LEU A 365
REMARK 465 ASP A 366
REMARK 465 ARG A 367
REMARK 465 HIS A 368
REMARK 465 GLN A 369
REMARK 465 THR A 370
REMARK 465 MET A 371
REMARK 465 GLU A 372
REMARK 465 VAL A 373
REMARK 465 SER A 374
REMARK 465 CYS A 375
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 GLU B 3
REMARK 465 LEU B 4
REMARK 465 GLN B 5
REMARK 465 ASP B 6
REMARK 465 VAL B 7
REMARK 465 GLN B 8
REMARK 465 LEU B 9
REMARK 465 THR B 10
REMARK 465 GLU B 11
REMARK 465 ILE B 12
REMARK 465 LYS B 13
REMARK 465 PRO B 14
REMARK 465 LEU B 15
REMARK 465 LEU B 16
REMARK 465 ASN B 17
REMARK 465 ASP B 18
REMARK 465 LYS B 19
REMARK 465 ASN B 20
REMARK 465 GLY B 21
REMARK 465 THR B 22
REMARK 465 ARG B 23
REMARK 465 ASN B 24
REMARK 465 PHE B 25
REMARK 465 GLN B 26
REMARK 465 ASP B 27
REMARK 465 PHE B 28
REMARK 465 TRP B 170
REMARK 465 ILE B 171
REMARK 465 ASP B 172
REMARK 465 TRP B 173
REMARK 465 ALA B 174
REMARK 465 ALA B 175
REMARK 465 SER B 176
REMARK 465 LYS B 177
REMARK 465 LEU B 178
REMARK 465 SER B 179
REMARK 465 GLY B 180
REMARK 465 LEU B 181
REMARK 465 THR B 182
REMARK 465 SER B 318
REMARK 465 ALA B 319
REMARK 465 SER B 320
REMARK 465 MET B 321
REMARK 465 THR B 322
REMARK 465 ARG B 323
REMARK 465 LEU B 324
REMARK 465 ALA B 325
REMARK 465 ARG B 326
REMARK 465 SER B 327
REMARK 465 ARG B 328
REMARK 465 THR B 329
REMARK 465 HIS B 330
REMARK 465 SER B 331
REMARK 465 THR B 332
REMARK 465 SER B 333
REMARK 465 SER B 334
REMARK 465 SER B 335
REMARK 465 LEU B 336
REMARK 465 GLY B 337
REMARK 465 SER B 338
REMARK 465 GLY B 339
REMARK 465 GLU B 340
REMARK 465 SER B 341
REMARK 465 PRO B 342
REMARK 465 PHE B 343
REMARK 465 SER B 344
REMARK 465 ARG B 345
REMARK 465 SER B 346
REMARK 465 VAL B 347
REMARK 465 THR B 348
REMARK 465 SER B 349
REMARK 465 ASN B 350
REMARK 465 GLN B 351
REMARK 465 SER B 352
REMARK 465 ASP B 353
REMARK 465 GLY B 354
REMARK 465 THR B 355
REMARK 465 GLN B 356
REMARK 465 GLU B 357
REMARK 465 SER B 358
REMARK 465 CYS B 359
REMARK 465 GLU B 360
REMARK 465 SER B 361
REMARK 465 PRO B 362
REMARK 465 ASP B 363
REMARK 465 VAL B 364
REMARK 465 LEU B 365
REMARK 465 ASP B 366
REMARK 465 ARG B 367
REMARK 465 HIS B 368
REMARK 465 GLN B 369
REMARK 465 THR B 370
REMARK 465 MET B 371
REMARK 465 GLU B 372
REMARK 465 VAL B 373
REMARK 465 SER B 374
REMARK 465 CYS B 375
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 GLU C 3
REMARK 465 LEU C 4
REMARK 465 GLN C 5
REMARK 465 ASP C 6
REMARK 465 VAL C 7
REMARK 465 GLN C 8
REMARK 465 LEU C 9
REMARK 465 THR C 10
REMARK 465 GLU C 11
REMARK 465 ILE C 12
REMARK 465 LYS C 13
REMARK 465 PRO C 14
REMARK 465 LEU C 15
REMARK 465 LEU C 16
REMARK 465 ASN C 17
REMARK 465 ASP C 18
REMARK 465 LYS C 19
REMARK 465 ASN C 20
REMARK 465 GLY C 21
REMARK 465 THR C 22
REMARK 465 ARG C 23
REMARK 465 ASN C 24
REMARK 465 PHE C 25
REMARK 465 GLN C 26
REMARK 465 ASP C 27
REMARK 465 PHE C 28
REMARK 465 TRP C 170
REMARK 465 ILE C 171
REMARK 465 ASP C 172
REMARK 465 TRP C 173
REMARK 465 ALA C 174
REMARK 465 ALA C 175
REMARK 465 SER C 176
REMARK 465 LYS C 177
REMARK 465 LEU C 178
REMARK 465 SER C 179
REMARK 465 GLY C 180
REMARK 465 LEU C 181
REMARK 465 THR C 182
REMARK 465 SER C 318
REMARK 465 ALA C 319
REMARK 465 SER C 320
REMARK 465 MET C 321
REMARK 465 THR C 322
REMARK 465 ARG C 323
REMARK 465 LEU C 324
REMARK 465 ALA C 325
REMARK 465 ARG C 326
REMARK 465 SER C 327
REMARK 465 ARG C 328
REMARK 465 THR C 329
REMARK 465 HIS C 330
REMARK 465 SER C 331
REMARK 465 THR C 332
REMARK 465 SER C 333
REMARK 465 SER C 334
REMARK 465 SER C 335
REMARK 465 LEU C 336
REMARK 465 GLY C 337
REMARK 465 SER C 338
REMARK 465 GLY C 339
REMARK 465 GLU C 340
REMARK 465 SER C 341
REMARK 465 PRO C 342
REMARK 465 PHE C 343
REMARK 465 SER C 344
REMARK 465 ARG C 345
REMARK 465 SER C 346
REMARK 465 VAL C 347
REMARK 465 THR C 348
REMARK 465 SER C 349
REMARK 465 ASN C 350
REMARK 465 GLN C 351
REMARK 465 SER C 352
REMARK 465 ASP C 353
REMARK 465 GLY C 354
REMARK 465 THR C 355
REMARK 465 GLN C 356
REMARK 465 GLU C 357
REMARK 465 SER C 358
REMARK 465 CYS C 359
REMARK 465 GLU C 360
REMARK 465 SER C 361
REMARK 465 PRO C 362
REMARK 465 ASP C 363
REMARK 465 VAL C 364
REMARK 465 LEU C 365
REMARK 465 ASP C 366
REMARK 465 ARG C 367
REMARK 465 HIS C 368
REMARK 465 GLN C 369
REMARK 465 THR C 370
REMARK 465 MET C 371
REMARK 465 GLU C 372
REMARK 465 VAL C 373
REMARK 465 SER C 374
REMARK 465 CYS C 375
REMARK 465 MET D 1
REMARK 465 ASP D 2
REMARK 465 GLU D 3
REMARK 465 LEU D 4
REMARK 465 GLN D 5
REMARK 465 ASP D 6
REMARK 465 VAL D 7
REMARK 465 GLN D 8
REMARK 465 LEU D 9
REMARK 465 THR D 10
REMARK 465 GLU D 11
REMARK 465 ILE D 12
REMARK 465 LYS D 13
REMARK 465 PRO D 14
REMARK 465 LEU D 15
REMARK 465 LEU D 16
REMARK 465 ASN D 17
REMARK 465 ASP D 18
REMARK 465 LYS D 19
REMARK 465 ASN D 20
REMARK 465 GLY D 21
REMARK 465 THR D 22
REMARK 465 ARG D 23
REMARK 465 ASN D 24
REMARK 465 PHE D 25
REMARK 465 GLN D 26
REMARK 465 ASP D 27
REMARK 465 PHE D 28
REMARK 465 TRP D 170
REMARK 465 ILE D 171
REMARK 465 ASP D 172
REMARK 465 TRP D 173
REMARK 465 ALA D 174
REMARK 465 ALA D 175
REMARK 465 SER D 176
REMARK 465 LYS D 177
REMARK 465 LEU D 178
REMARK 465 SER D 179
REMARK 465 GLY D 180
REMARK 465 LEU D 181
REMARK 465 THR D 182
REMARK 465 SER D 318
REMARK 465 ALA D 319
REMARK 465 SER D 320
REMARK 465 MET D 321
REMARK 465 THR D 322
REMARK 465 ARG D 323
REMARK 465 LEU D 324
REMARK 465 ALA D 325
REMARK 465 ARG D 326
REMARK 465 SER D 327
REMARK 465 ARG D 328
REMARK 465 THR D 329
REMARK 465 HIS D 330
REMARK 465 SER D 331
REMARK 465 THR D 332
REMARK 465 SER D 333
REMARK 465 SER D 334
REMARK 465 SER D 335
REMARK 465 LEU D 336
REMARK 465 GLY D 337
REMARK 465 SER D 338
REMARK 465 GLY D 339
REMARK 465 GLU D 340
REMARK 465 SER D 341
REMARK 465 PRO D 342
REMARK 465 PHE D 343
REMARK 465 SER D 344
REMARK 465 ARG D 345
REMARK 465 SER D 346
REMARK 465 VAL D 347
REMARK 465 THR D 348
REMARK 465 SER D 349
REMARK 465 ASN D 350
REMARK 465 GLN D 351
REMARK 465 SER D 352
REMARK 465 ASP D 353
REMARK 465 GLY D 354
REMARK 465 THR D 355
REMARK 465 GLN D 356
REMARK 465 GLU D 357
REMARK 465 SER D 358
REMARK 465 CYS D 359
REMARK 465 GLU D 360
REMARK 465 SER D 361
REMARK 465 PRO D 362
REMARK 465 ASP D 363
REMARK 465 VAL D 364
REMARK 465 LEU D 365
REMARK 465 ASP D 366
REMARK 465 ARG D 367
REMARK 465 HIS D 368
REMARK 465 GLN D 369
REMARK 465 THR D 370
REMARK 465 MET D 371
REMARK 465 GLU D 372
REMARK 465 VAL D 373
REMARK 465 SER D 374
REMARK 465 CYS D 375
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 CD1 LEU D 310 CD1 ILE D 316 1.84
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 TYR A 108 127.79 -39.42
REMARK 500 THR A 182 52.27 -144.73
REMARK 500 GLU A 236 -5.65 88.21
REMARK 500 ILE B 316 58.74 38.83
REMARK 500 PHE D 77 140.70 -39.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6L4H A 1 375 UNP Q9UGV2 NDRG3_HUMAN 1 375
DBREF 6L4H B 1 375 UNP Q9UGV2 NDRG3_HUMAN 1 375
DBREF 6L4H C 1 375 UNP Q9UGV2 NDRG3_HUMAN 1 375
DBREF 6L4H D 1 375 UNP Q9UGV2 NDRG3_HUMAN 1 375
SEQADV 6L4H SER A 30 UNP Q9UGV2 CYS 30 ENGINEERED MUTATION
SEQADV 6L4H SER B 30 UNP Q9UGV2 CYS 30 ENGINEERED MUTATION
SEQADV 6L4H SER C 30 UNP Q9UGV2 CYS 30 ENGINEERED MUTATION
SEQADV 6L4H SER D 30 UNP Q9UGV2 CYS 30 ENGINEERED MUTATION
SEQRES 1 A 375 MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS
SEQRES 2 A 375 PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN
SEQRES 3 A 375 ASP PHE ASP SER GLN GLU HIS ASP ILE GLU THR THR HIS
SEQRES 4 A 375 GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY
SEQRES 5 A 375 ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU
SEQRES 6 A 375 ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU
SEQRES 7 A 375 ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS
SEQRES 8 A 375 VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE
SEQRES 9 A 375 PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA
SEQRES 10 A 375 GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS
SEQRES 11 A 375 SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE
SEQRES 12 A 375 LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU
SEQRES 13 A 375 GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY
SEQRES 14 A 375 TRP ILE ASP TRP ALA ALA SER LYS LEU SER GLY LEU THR
SEQRES 15 A 375 THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY
SEQRES 16 A 375 GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR
SEQRES 17 A 375 TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN
SEQRES 18 A 375 LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP
SEQRES 19 A 375 LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN
SEQRES 20 A 375 LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL
SEQRES 21 A 375 GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS
SEQRES 22 A 375 ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS
SEQRES 23 A 375 MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO
SEQRES 24 A 375 GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY
SEQRES 25 A 375 MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA
SEQRES 26 A 375 ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER
SEQRES 27 A 375 GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN
SEQRES 28 A 375 SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL
SEQRES 29 A 375 LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS
SEQRES 1 B 375 MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS
SEQRES 2 B 375 PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN
SEQRES 3 B 375 ASP PHE ASP SER GLN GLU HIS ASP ILE GLU THR THR HIS
SEQRES 4 B 375 GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY
SEQRES 5 B 375 ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU
SEQRES 6 B 375 ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU
SEQRES 7 B 375 ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS
SEQRES 8 B 375 VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE
SEQRES 9 B 375 PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA
SEQRES 10 B 375 GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS
SEQRES 11 B 375 SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE
SEQRES 12 B 375 LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU
SEQRES 13 B 375 GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY
SEQRES 14 B 375 TRP ILE ASP TRP ALA ALA SER LYS LEU SER GLY LEU THR
SEQRES 15 B 375 THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY
SEQRES 16 B 375 GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR
SEQRES 17 B 375 TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN
SEQRES 18 B 375 LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP
SEQRES 19 B 375 LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN
SEQRES 20 B 375 LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL
SEQRES 21 B 375 GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS
SEQRES 22 B 375 ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS
SEQRES 23 B 375 MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO
SEQRES 24 B 375 GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY
SEQRES 25 B 375 MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA
SEQRES 26 B 375 ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER
SEQRES 27 B 375 GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN
SEQRES 28 B 375 SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL
SEQRES 29 B 375 LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS
SEQRES 1 C 375 MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS
SEQRES 2 C 375 PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN
SEQRES 3 C 375 ASP PHE ASP SER GLN GLU HIS ASP ILE GLU THR THR HIS
SEQRES 4 C 375 GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY
SEQRES 5 C 375 ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU
SEQRES 6 C 375 ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU
SEQRES 7 C 375 ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS
SEQRES 8 C 375 VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE
SEQRES 9 C 375 PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA
SEQRES 10 C 375 GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS
SEQRES 11 C 375 SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE
SEQRES 12 C 375 LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU
SEQRES 13 C 375 GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY
SEQRES 14 C 375 TRP ILE ASP TRP ALA ALA SER LYS LEU SER GLY LEU THR
SEQRES 15 C 375 THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY
SEQRES 16 C 375 GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR
SEQRES 17 C 375 TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN
SEQRES 18 C 375 LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP
SEQRES 19 C 375 LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN
SEQRES 20 C 375 LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL
SEQRES 21 C 375 GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS
SEQRES 22 C 375 ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS
SEQRES 23 C 375 MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO
SEQRES 24 C 375 GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY
SEQRES 25 C 375 MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA
SEQRES 26 C 375 ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER
SEQRES 27 C 375 GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN
SEQRES 28 C 375 SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL
SEQRES 29 C 375 LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS
SEQRES 1 D 375 MET ASP GLU LEU GLN ASP VAL GLN LEU THR GLU ILE LYS
SEQRES 2 D 375 PRO LEU LEU ASN ASP LYS ASN GLY THR ARG ASN PHE GLN
SEQRES 3 D 375 ASP PHE ASP SER GLN GLU HIS ASP ILE GLU THR THR HIS
SEQRES 4 D 375 GLY VAL VAL HIS VAL THR ILE ARG GLY LEU PRO LYS GLY
SEQRES 5 D 375 ASN ARG PRO VAL ILE LEU THR TYR HIS ASP ILE GLY LEU
SEQRES 6 D 375 ASN HIS LYS SER CYS PHE ASN ALA PHE PHE ASN PHE GLU
SEQRES 7 D 375 ASP MET GLN GLU ILE THR GLN HIS PHE ALA VAL CYS HIS
SEQRES 8 D 375 VAL ASP ALA PRO GLY GLN GLN GLU GLY ALA PRO SER PHE
SEQRES 9 D 375 PRO THR GLY TYR GLN TYR PRO THR MET ASP GLU LEU ALA
SEQRES 10 D 375 GLU MET LEU PRO PRO VAL LEU THR HIS LEU SER LEU LYS
SEQRES 11 D 375 SER ILE ILE GLY ILE GLY VAL GLY ALA GLY ALA TYR ILE
SEQRES 12 D 375 LEU SER ARG PHE ALA LEU ASN HIS PRO GLU LEU VAL GLU
SEQRES 13 D 375 GLY LEU VAL LEU ILE ASN VAL ASP PRO CYS ALA LYS GLY
SEQRES 14 D 375 TRP ILE ASP TRP ALA ALA SER LYS LEU SER GLY LEU THR
SEQRES 15 D 375 THR ASN VAL VAL ASP ILE ILE LEU ALA HIS HIS PHE GLY
SEQRES 16 D 375 GLN GLU GLU LEU GLN ALA ASN LEU ASP LEU ILE GLN THR
SEQRES 17 D 375 TYR ARG MET HIS ILE ALA GLN ASP ILE ASN GLN ASP ASN
SEQRES 18 D 375 LEU GLN LEU PHE LEU ASN SER TYR ASN GLY ARG ARG ASP
SEQRES 19 D 375 LEU GLU ILE GLU ARG PRO ILE LEU GLY GLN ASN ASP ASN
SEQRES 20 D 375 LYS SER LYS THR LEU LYS CYS SER THR LEU LEU VAL VAL
SEQRES 21 D 375 GLY ASP ASN SER PRO ALA VAL GLU ALA VAL VAL GLU CYS
SEQRES 22 D 375 ASN SER ARG LEU ASN PRO ILE ASN THR THR LEU LEU LYS
SEQRES 23 D 375 MET ALA ASP CYS GLY GLY LEU PRO GLN VAL VAL GLN PRO
SEQRES 24 D 375 GLY LYS LEU THR GLU ALA PHE LYS TYR PHE LEU GLN GLY
SEQRES 25 D 375 MET GLY TYR ILE PRO SER ALA SER MET THR ARG LEU ALA
SEQRES 26 D 375 ARG SER ARG THR HIS SER THR SER SER SER LEU GLY SER
SEQRES 27 D 375 GLY GLU SER PRO PHE SER ARG SER VAL THR SER ASN GLN
SEQRES 28 D 375 SER ASP GLY THR GLN GLU SER CYS GLU SER PRO ASP VAL
SEQRES 29 D 375 LEU ASP ARG HIS GLN THR MET GLU VAL SER CYS
HELIX 1 AA1 ASN A 66 ASN A 76 1 11
HELIX 2 AA2 PHE A 77 PHE A 87 1 11
HELIX 3 AA3 THR A 112 GLU A 118 1 7
HELIX 4 AA4 MET A 119 LEU A 127 1 9
HELIX 5 AA5 GLY A 138 HIS A 151 1 14
HELIX 6 AA6 ASN A 184 PHE A 194 1 11
HELIX 7 AA7 GLY A 195 ASN A 202 1 8
HELIX 8 AA8 LEU A 203 ASP A 216 1 14
HELIX 9 AA9 ASN A 218 GLY A 231 1 14
HELIX 10 AB1 ALA A 266 SER A 275 1 10
HELIX 11 AB2 ARG A 276 LEU A 277 5 2
HELIX 12 AB3 ASN A 278 ILE A 280 5 3
HELIX 13 AB4 LEU A 293 GLN A 298 1 6
HELIX 14 AB5 GLN A 298 GLY A 314 1 17
HELIX 15 AB6 ASN B 66 PHE B 77 1 12
HELIX 16 AB7 PHE B 77 GLN B 85 1 9
HELIX 17 AB8 THR B 112 MET B 119 1 8
HELIX 18 AB9 MET B 119 LEU B 127 1 9
HELIX 19 AC1 GLY B 138 HIS B 151 1 14
HELIX 20 AC2 ASN B 184 PHE B 194 1 11
HELIX 21 AC3 GLY B 195 ASN B 202 1 8
HELIX 22 AC4 LEU B 203 ASP B 216 1 14
HELIX 23 AC5 ASN B 218 GLY B 231 1 14
HELIX 24 AC6 ALA B 266 ARG B 276 1 11
HELIX 25 AC7 LEU B 277 ILE B 280 5 4
HELIX 26 AC8 LEU B 293 GLN B 298 1 6
HELIX 27 AC9 GLN B 298 MET B 313 1 16
HELIX 28 AD1 ASN C 66 PHE C 71 1 6
HELIX 29 AD2 PHE C 71 PHE C 77 1 7
HELIX 30 AD3 PHE C 77 PHE C 87 1 11
HELIX 31 AD4 THR C 112 GLU C 118 1 7
HELIX 32 AD5 MET C 119 LEU C 127 1 9
HELIX 33 AD6 GLY C 138 HIS C 151 1 14
HELIX 34 AD7 ASN C 184 PHE C 194 1 11
HELIX 35 AD8 GLY C 195 ASN C 202 1 8
HELIX 36 AD9 LEU C 203 ASP C 216 1 14
HELIX 37 AE1 ASN C 218 GLY C 231 1 14
HELIX 38 AE2 ALA C 266 ARG C 276 1 11
HELIX 39 AE3 LEU C 293 GLN C 298 1 6
HELIX 40 AE4 GLN C 298 GLY C 314 1 17
HELIX 41 AE5 ASN D 66 PHE D 77 1 12
HELIX 42 AE6 PHE D 77 PHE D 87 1 11
HELIX 43 AE7 THR D 112 MET D 119 1 8
HELIX 44 AE8 MET D 119 LEU D 127 1 9
HELIX 45 AE9 GLY D 138 HIS D 151 1 14
HELIX 46 AF1 ASN D 184 PHE D 194 1 11
HELIX 47 AF2 GLY D 195 ASN D 202 1 8
HELIX 48 AF3 LEU D 203 ILE D 217 1 15
HELIX 49 AF4 ASN D 218 ARG D 232 1 15
HELIX 50 AF5 ALA D 266 LEU D 277 1 12
HELIX 51 AF6 LEU D 293 GLN D 298 1 6
HELIX 52 AF7 GLN D 298 GLY D 312 1 15
SHEET 1 AA1 8 GLU A 32 THR A 37 0
SHEET 2 AA1 8 GLY A 40 ARG A 47 -1 O VAL A 44 N HIS A 33
SHEET 3 AA1 8 VAL A 89 ASP A 93 -1 O HIS A 91 N THR A 45
SHEET 4 AA1 8 VAL A 56 TYR A 60 1 N THR A 59 O VAL A 92
SHEET 5 AA1 8 ILE A 132 VAL A 137 1 O ILE A 133 N VAL A 56
SHEET 6 AA1 8 VAL A 155 ILE A 161 1 O ILE A 161 N GLY A 136
SHEET 7 AA1 8 SER A 255 GLY A 261 1 O LEU A 257 N LEU A 158
SHEET 8 AA1 8 THR A 282 MET A 287 1 O MET A 287 N VAL A 260
SHEET 1 AA2 8 SER B 30 THR B 37 0
SHEET 2 AA2 8 GLY B 40 ARG B 47 -1 O ILE B 46 N GLN B 31
SHEET 3 AA2 8 VAL B 89 ASP B 93 -1 O HIS B 91 N THR B 45
SHEET 4 AA2 8 VAL B 56 TYR B 60 1 N THR B 59 O VAL B 92
SHEET 5 AA2 8 ILE B 132 VAL B 137 1 O ILE B 135 N LEU B 58
SHEET 6 AA2 8 VAL B 155 ILE B 161 1 O VAL B 159 N GLY B 134
SHEET 7 AA2 8 SER B 255 GLY B 261 1 O LEU B 257 N LEU B 158
SHEET 8 AA2 8 THR B 282 MET B 287 1 O MET B 287 N VAL B 260
SHEET 1 AA3 8 GLU C 32 THR C 37 0
SHEET 2 AA3 8 GLY C 40 ARG C 47 -1 O VAL C 42 N ILE C 35
SHEET 3 AA3 8 VAL C 89 ASP C 93 -1 O HIS C 91 N THR C 45
SHEET 4 AA3 8 VAL C 56 TYR C 60 1 N ILE C 57 O CYS C 90
SHEET 5 AA3 8 ILE C 132 VAL C 137 1 O ILE C 135 N LEU C 58
SHEET 6 AA3 8 VAL C 155 ILE C 161 1 O ILE C 161 N GLY C 136
SHEET 7 AA3 8 SER C 255 GLY C 261 1 O LEU C 257 N LEU C 158
SHEET 8 AA3 8 THR C 282 MET C 287 1 O MET C 287 N VAL C 260
SHEET 1 AA4 8 SER D 30 ILE D 35 0
SHEET 2 AA4 8 VAL D 42 ARG D 47 -1 O VAL D 44 N HIS D 33
SHEET 3 AA4 8 VAL D 89 ASP D 93 -1 O HIS D 91 N THR D 45
SHEET 4 AA4 8 VAL D 56 TYR D 60 1 N THR D 59 O VAL D 92
SHEET 5 AA4 8 ILE D 132 VAL D 137 1 O ILE D 135 N LEU D 58
SHEET 6 AA4 8 VAL D 155 ILE D 161 1 O ILE D 161 N GLY D 136
SHEET 7 AA4 8 SER D 255 GLY D 261 1 O LEU D 257 N LEU D 158
SHEET 8 AA4 8 THR D 282 MET D 287 1 O LEU D 285 N LEU D 258
CRYST1 99.759 99.759 332.710 90.00 90.00 120.00 P 31 2 1 24
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 0.010024 0.005787 0.000000 0.00000
SCALE2 0.000000 0.011575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003006 0.00000
TER 2245 PRO A 317
TER 4388 PRO B 317
TER 6531 PRO C 317
TER 8674 PRO D 317
MASTER 752 0 0 52 32 0 0 6 8670 4 0 116
END |