HEADER OXIDOREDUCTASE 17-MAR-14 4PVD
TITLE CRYSTAL STRUCTURE OF YEAST METHYLGLYOXAL/ISOVALERALDEHYDE REDUCTASE
TITLE 2 GRE2 COMPLEXED WITH NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADPH-DEPENDENT METHYLGLYOXAL REDUCTASE GRE2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 3-METHYLBUTANAL REDUCTASE, GENES DE RESPUESTA A ESTRES
COMPND 5 PROTEIN 2, ISOVALERALDEHYDE REDUCTASE;
COMPND 6 EC: 1.1.1.283, 1.1.1.265;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: S288C;
SOURCE 6 GENE: GRE2, YOL151W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ROSSMANN FOLD, REDUCTASE, NADPH BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.GUO,Z.Z.BAO,W.F.LI,C.Z.ZHOU
REVDAT 2 08-NOV-23 4PVD 1 REMARK
REVDAT 1 22-OCT-14 4PVD 0
JRNL AUTH P.C.GUO,Z.Z.BAO,X.X.MA,Q.XIA,W.F.LI
JRNL TITL STRUCTURAL INSIGHTS INTO THE COFACTOR-ASSISTED SUBSTRATE
JRNL TITL 2 RECOGNITION OF YEAST METHYLGLYOXAL/ISOVALERALDEHYDE
JRNL TITL 3 REDUCTASE GRE2
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1844 1486 2014
JRNL REFN ISSN 0006-3002
JRNL PMID 24879127
JRNL DOI 10.1016/J.BBAPAP.2014.05.008
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 63099
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3358
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4638
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 220
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10193
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 3.37000
REMARK 3 B33 (A**2) : -3.48000
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): 0.414
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.287
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.382
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.007 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.105 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 5.282 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ;35.571 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;15.453 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ;17.636 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.082 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.004 ; NULL
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 342
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2318 7.7942 111.9829
REMARK 3 T TENSOR
REMARK 3 T11: 0.0514 T22: 0.1083
REMARK 3 T33: 0.0530 T12: 0.0292
REMARK 3 T13: 0.0168 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 1.1800 L22: 0.4732
REMARK 3 L33: 2.1193 L12: 0.2422
REMARK 3 L13: 0.3161 L23: -0.1577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.0164 S13: 0.0062
REMARK 3 S21: -0.0252 S22: 0.0265 S23: 0.0264
REMARK 3 S31: -0.0240 S32: 0.3687 S33: -0.0231
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 1 B 342
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2056 53.1748 120.7782
REMARK 3 T TENSOR
REMARK 3 T11: 0.1008 T22: 0.0637
REMARK 3 T33: 0.0349 T12: 0.0260
REMARK 3 T13: 0.0333 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.5470 L22: 0.4591
REMARK 3 L33: 3.4324 L12: 0.3488
REMARK 3 L13: 0.1393 L23: -0.6970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0954 S12: 0.0085 S13: -0.0171
REMARK 3 S21: 0.0997 S22: 0.0206 S23: 0.0480
REMARK 3 S31: -0.3725 S32: 0.1787 S33: -0.1160
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 : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9125 49.9042 115.0768
REMARK 3 T TENSOR
REMARK 3 T11: 0.1003 T22: 0.1596
REMARK 3 T33: 0.0909 T12: 0.0667
REMARK 3 T13: 0.0107 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 2.5498 L22: 3.0043
REMARK 3 L33: 3.5059 L12: 1.6553
REMARK 3 L13: 2.5793 L23: 0.3596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: -0.1159 S13: -0.0208
REMARK 3 S21: 0.1346 S22: 0.0030 S23: 0.0061
REMARK 3 S31: -0.1863 S32: -0.1440 S33: 0.0175
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 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8659 4.5718 106.1053
REMARK 3 T TENSOR
REMARK 3 T11: 0.0734 T22: 0.2266
REMARK 3 T33: 0.0763 T12: 0.0602
REMARK 3 T13: 0.0398 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 0.0395 L22: 3.9976
REMARK 3 L33: 1.0997 L12: 0.3926
REMARK 3 L13: -0.2060 L23: -2.0966
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0146 S13: 0.0171
REMARK 3 S21: 0.0149 S22: 0.0198 S23: 0.1402
REMARK 3 S31: -0.0057 S32: 0.0053 S33: -0.0449
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 : C 1 C 341
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4697 7.7066 64.0518
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.0493
REMARK 3 T33: 0.0520 T12: 0.0147
REMARK 3 T13: 0.0088 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.6718 L22: 0.3051
REMARK 3 L33: 3.6610 L12: -0.0335
REMARK 3 L13: 0.0487 L23: 0.6262
REMARK 3 S TENSOR
REMARK 3 S11: 0.1164 S12: 0.0617 S13: 0.0182
REMARK 3 S21: -0.0373 S22: -0.0464 S23: -0.0078
REMARK 3 S31: -0.0729 S32: -0.3283 S33: -0.0700
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 : D 1 D 341
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7427 53.3383 72.9533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0408 T22: 0.0527
REMARK 3 T33: 0.0464 T12: -0.0054
REMARK 3 T13: 0.0122 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 0.7097 L22: 0.3299
REMARK 3 L33: 4.1224 L12: -0.0383
REMARK 3 L13: -0.1216 L23: 0.7504
REMARK 3 S TENSOR
REMARK 3 S11: 0.0693 S12: 0.1248 S13: 0.0557
REMARK 3 S21: 0.0009 S22: -0.0694 S23: -0.0059
REMARK 3 S31: 0.0027 S32: -0.2570 S33: 0.0001
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 3 POSITIONS
REMARK 4
REMARK 4 4PVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67436
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9340
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46300
REMARK 200 R SYM FOR SHELL (I) : 0.46300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.515
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 4PVC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% POLYETHYLENE GLYCOL 2000 MME, 0.2M
REMARK 280 (NH4)2SO4, 0.1M SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 45.15450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.54700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.44550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.54700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.15450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.44550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: 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
REMARK 350 BIOMOLECULE: 3
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: 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
REMARK 350 BIOMOLECULE: 4
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: D
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 PHE C 85
REMARK 465 CYS C 86
REMARK 465 PHE C 87
REMARK 465 ASP C 88
REMARK 465 ILE C 89
REMARK 465 THR C 90
REMARK 465 ASP C 91
REMARK 465 SER C 92
REMARK 465 GLU C 93
REMARK 465 ARG C 94
REMARK 465 ASP C 95
REMARK 465 LEU C 96
REMARK 465 TRP C 154
REMARK 465 GLU C 155
REMARK 465 SER C 156
REMARK 465 CYS C 157
REMARK 465 GLN C 158
REMARK 465 SER C 159
REMARK 465 ASP C 160
REMARK 465 PRO C 161
REMARK 465 VAL C 162
REMARK 465 ASN C 163
REMARK 465 ALA C 164
REMARK 465 TYR C 165
REMARK 465 CYS C 166
REMARK 465 GLY C 167
REMARK 465 SER C 168
REMARK 465 HIS C 212
REMARK 465 LEU C 213
REMARK 465 ASN C 214
REMARK 465 THR C 215
REMARK 465 SER C 216
REMARK 465 CYS C 217
REMARK 465 ILE C 342
REMARK 465 PHE D 85
REMARK 465 CYS D 86
REMARK 465 PHE D 87
REMARK 465 ASP D 88
REMARK 465 ILE D 89
REMARK 465 THR D 90
REMARK 465 ASP D 91
REMARK 465 SER D 92
REMARK 465 GLU D 93
REMARK 465 ARG D 94
REMARK 465 ASP D 95
REMARK 465 MET D 134
REMARK 465 ALA D 135
REMARK 465 GLU D 146
REMARK 465 GLU D 147
REMARK 465 SER D 148
REMARK 465 TRP D 149
REMARK 465 TRP D 154
REMARK 465 GLU D 155
REMARK 465 SER D 156
REMARK 465 CYS D 157
REMARK 465 GLN D 158
REMARK 465 SER D 159
REMARK 465 ASP D 160
REMARK 465 PRO D 161
REMARK 465 VAL D 162
REMARK 465 ASN D 163
REMARK 465 ALA D 164
REMARK 465 TYR D 165
REMARK 465 CYS D 166
REMARK 465 GLY D 167
REMARK 465 HIS D 212
REMARK 465 LEU D 213
REMARK 465 ASN D 214
REMARK 465 THR D 215
REMARK 465 SER D 216
REMARK 465 ILE D 342
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 ALA A 115 28.15 -150.65
REMARK 500 SER A 126 -142.60 -97.22
REMARK 500 GLU A 155 -55.32 95.24
REMARK 500 VAL A 197 -159.60 -84.87
REMARK 500 PHE B 85 45.34 -140.84
REMARK 500 ALA B 115 28.75 -158.40
REMARK 500 SER B 126 -141.02 -99.61
REMARK 500 ASN B 195 76.32 -119.91
REMARK 500 VAL B 197 -158.34 -83.07
REMARK 500 ALA C 115 27.86 -143.12
REMARK 500 SER C 126 -134.02 -109.56
REMARK 500 ASN C 145 -154.72 -128.54
REMARK 500 VAL C 197 -151.30 -91.96
REMARK 500 LYS C 207 0.13 -66.88
REMARK 500 ALA C 268 -165.66 -169.53
REMARK 500 ALA D 115 39.21 -153.44
REMARK 500 SER D 126 -147.95 -110.07
REMARK 500 VAL D 197 -153.29 -89.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PVC RELATED DB: PDB
DBREF 4PVD A 1 342 UNP Q12068 GRE2_YEAST 1 342
DBREF 4PVD B 1 342 UNP Q12068 GRE2_YEAST 1 342
DBREF 4PVD C 1 342 UNP Q12068 GRE2_YEAST 1 342
DBREF 4PVD D 1 342 UNP Q12068 GRE2_YEAST 1 342
SEQRES 1 A 342 MET SER VAL PHE VAL SER GLY ALA ASN GLY PHE ILE ALA
SEQRES 2 A 342 GLN HIS ILE VAL ASP LEU LEU LEU LYS GLU ASP TYR LYS
SEQRES 3 A 342 VAL ILE GLY SER ALA ARG SER GLN GLU LYS ALA GLU ASN
SEQRES 4 A 342 LEU THR GLU ALA PHE GLY ASN ASN PRO LYS PHE SER MET
SEQRES 5 A 342 GLU VAL VAL PRO ASP ILE SER LYS LEU ASP ALA PHE ASP
SEQRES 6 A 342 HIS VAL PHE GLN LYS HIS GLY LYS ASP ILE LYS ILE VAL
SEQRES 7 A 342 LEU HIS THR ALA SER PRO PHE CYS PHE ASP ILE THR ASP
SEQRES 8 A 342 SER GLU ARG ASP LEU LEU ILE PRO ALA VAL ASN GLY VAL
SEQRES 9 A 342 LYS GLY ILE LEU HIS SER ILE LYS LYS TYR ALA ALA ASP
SEQRES 10 A 342 SER VAL GLU ARG VAL VAL LEU THR SER SER TYR ALA ALA
SEQRES 11 A 342 VAL PHE ASP MET ALA LYS GLU ASN ASP LYS SER LEU THR
SEQRES 12 A 342 PHE ASN GLU GLU SER TRP ASN PRO ALA THR TRP GLU SER
SEQRES 13 A 342 CYS GLN SER ASP PRO VAL ASN ALA TYR CYS GLY SER LYS
SEQRES 14 A 342 LYS PHE ALA GLU LYS ALA ALA TRP GLU PHE LEU GLU GLU
SEQRES 15 A 342 ASN ARG ASP SER VAL LYS PHE GLU LEU THR ALA VAL ASN
SEQRES 16 A 342 PRO VAL TYR VAL PHE GLY PRO GLN MET PHE ASP LYS ASP
SEQRES 17 A 342 VAL LYS LYS HIS LEU ASN THR SER CYS GLU LEU VAL ASN
SEQRES 18 A 342 SER LEU MET HIS LEU SER PRO GLU ASP LYS ILE PRO GLU
SEQRES 19 A 342 LEU PHE GLY GLY TYR ILE ASP VAL ARG ASP VAL ALA LYS
SEQRES 20 A 342 ALA HIS LEU VAL ALA PHE GLN LYS ARG GLU THR ILE GLY
SEQRES 21 A 342 GLN ARG LEU ILE VAL SER GLU ALA ARG PHE THR MET GLN
SEQRES 22 A 342 ASP VAL LEU ASP ILE LEU ASN GLU ASP PHE PRO VAL LEU
SEQRES 23 A 342 LYS GLY ASN ILE PRO VAL GLY LYS PRO GLY SER GLY ALA
SEQRES 24 A 342 THR HIS ASN THR LEU GLY ALA THR LEU ASP ASN LYS LYS
SEQRES 25 A 342 SER LYS LYS LEU LEU GLY PHE LYS PHE ARG ASN LEU LYS
SEQRES 26 A 342 GLU THR ILE ASP ASP THR ALA SER GLN ILE LEU LYS PHE
SEQRES 27 A 342 GLU GLY ARG ILE
SEQRES 1 B 342 MET SER VAL PHE VAL SER GLY ALA ASN GLY PHE ILE ALA
SEQRES 2 B 342 GLN HIS ILE VAL ASP LEU LEU LEU LYS GLU ASP TYR LYS
SEQRES 3 B 342 VAL ILE GLY SER ALA ARG SER GLN GLU LYS ALA GLU ASN
SEQRES 4 B 342 LEU THR GLU ALA PHE GLY ASN ASN PRO LYS PHE SER MET
SEQRES 5 B 342 GLU VAL VAL PRO ASP ILE SER LYS LEU ASP ALA PHE ASP
SEQRES 6 B 342 HIS VAL PHE GLN LYS HIS GLY LYS ASP ILE LYS ILE VAL
SEQRES 7 B 342 LEU HIS THR ALA SER PRO PHE CYS PHE ASP ILE THR ASP
SEQRES 8 B 342 SER GLU ARG ASP LEU LEU ILE PRO ALA VAL ASN GLY VAL
SEQRES 9 B 342 LYS GLY ILE LEU HIS SER ILE LYS LYS TYR ALA ALA ASP
SEQRES 10 B 342 SER VAL GLU ARG VAL VAL LEU THR SER SER TYR ALA ALA
SEQRES 11 B 342 VAL PHE ASP MET ALA LYS GLU ASN ASP LYS SER LEU THR
SEQRES 12 B 342 PHE ASN GLU GLU SER TRP ASN PRO ALA THR TRP GLU SER
SEQRES 13 B 342 CYS GLN SER ASP PRO VAL ASN ALA TYR CYS GLY SER LYS
SEQRES 14 B 342 LYS PHE ALA GLU LYS ALA ALA TRP GLU PHE LEU GLU GLU
SEQRES 15 B 342 ASN ARG ASP SER VAL LYS PHE GLU LEU THR ALA VAL ASN
SEQRES 16 B 342 PRO VAL TYR VAL PHE GLY PRO GLN MET PHE ASP LYS ASP
SEQRES 17 B 342 VAL LYS LYS HIS LEU ASN THR SER CYS GLU LEU VAL ASN
SEQRES 18 B 342 SER LEU MET HIS LEU SER PRO GLU ASP LYS ILE PRO GLU
SEQRES 19 B 342 LEU PHE GLY GLY TYR ILE ASP VAL ARG ASP VAL ALA LYS
SEQRES 20 B 342 ALA HIS LEU VAL ALA PHE GLN LYS ARG GLU THR ILE GLY
SEQRES 21 B 342 GLN ARG LEU ILE VAL SER GLU ALA ARG PHE THR MET GLN
SEQRES 22 B 342 ASP VAL LEU ASP ILE LEU ASN GLU ASP PHE PRO VAL LEU
SEQRES 23 B 342 LYS GLY ASN ILE PRO VAL GLY LYS PRO GLY SER GLY ALA
SEQRES 24 B 342 THR HIS ASN THR LEU GLY ALA THR LEU ASP ASN LYS LYS
SEQRES 25 B 342 SER LYS LYS LEU LEU GLY PHE LYS PHE ARG ASN LEU LYS
SEQRES 26 B 342 GLU THR ILE ASP ASP THR ALA SER GLN ILE LEU LYS PHE
SEQRES 27 B 342 GLU GLY ARG ILE
SEQRES 1 C 342 MET SER VAL PHE VAL SER GLY ALA ASN GLY PHE ILE ALA
SEQRES 2 C 342 GLN HIS ILE VAL ASP LEU LEU LEU LYS GLU ASP TYR LYS
SEQRES 3 C 342 VAL ILE GLY SER ALA ARG SER GLN GLU LYS ALA GLU ASN
SEQRES 4 C 342 LEU THR GLU ALA PHE GLY ASN ASN PRO LYS PHE SER MET
SEQRES 5 C 342 GLU VAL VAL PRO ASP ILE SER LYS LEU ASP ALA PHE ASP
SEQRES 6 C 342 HIS VAL PHE GLN LYS HIS GLY LYS ASP ILE LYS ILE VAL
SEQRES 7 C 342 LEU HIS THR ALA SER PRO PHE CYS PHE ASP ILE THR ASP
SEQRES 8 C 342 SER GLU ARG ASP LEU LEU ILE PRO ALA VAL ASN GLY VAL
SEQRES 9 C 342 LYS GLY ILE LEU HIS SER ILE LYS LYS TYR ALA ALA ASP
SEQRES 10 C 342 SER VAL GLU ARG VAL VAL LEU THR SER SER TYR ALA ALA
SEQRES 11 C 342 VAL PHE ASP MET ALA LYS GLU ASN ASP LYS SER LEU THR
SEQRES 12 C 342 PHE ASN GLU GLU SER TRP ASN PRO ALA THR TRP GLU SER
SEQRES 13 C 342 CYS GLN SER ASP PRO VAL ASN ALA TYR CYS GLY SER LYS
SEQRES 14 C 342 LYS PHE ALA GLU LYS ALA ALA TRP GLU PHE LEU GLU GLU
SEQRES 15 C 342 ASN ARG ASP SER VAL LYS PHE GLU LEU THR ALA VAL ASN
SEQRES 16 C 342 PRO VAL TYR VAL PHE GLY PRO GLN MET PHE ASP LYS ASP
SEQRES 17 C 342 VAL LYS LYS HIS LEU ASN THR SER CYS GLU LEU VAL ASN
SEQRES 18 C 342 SER LEU MET HIS LEU SER PRO GLU ASP LYS ILE PRO GLU
SEQRES 19 C 342 LEU PHE GLY GLY TYR ILE ASP VAL ARG ASP VAL ALA LYS
SEQRES 20 C 342 ALA HIS LEU VAL ALA PHE GLN LYS ARG GLU THR ILE GLY
SEQRES 21 C 342 GLN ARG LEU ILE VAL SER GLU ALA ARG PHE THR MET GLN
SEQRES 22 C 342 ASP VAL LEU ASP ILE LEU ASN GLU ASP PHE PRO VAL LEU
SEQRES 23 C 342 LYS GLY ASN ILE PRO VAL GLY LYS PRO GLY SER GLY ALA
SEQRES 24 C 342 THR HIS ASN THR LEU GLY ALA THR LEU ASP ASN LYS LYS
SEQRES 25 C 342 SER LYS LYS LEU LEU GLY PHE LYS PHE ARG ASN LEU LYS
SEQRES 26 C 342 GLU THR ILE ASP ASP THR ALA SER GLN ILE LEU LYS PHE
SEQRES 27 C 342 GLU GLY ARG ILE
SEQRES 1 D 342 MET SER VAL PHE VAL SER GLY ALA ASN GLY PHE ILE ALA
SEQRES 2 D 342 GLN HIS ILE VAL ASP LEU LEU LEU LYS GLU ASP TYR LYS
SEQRES 3 D 342 VAL ILE GLY SER ALA ARG SER GLN GLU LYS ALA GLU ASN
SEQRES 4 D 342 LEU THR GLU ALA PHE GLY ASN ASN PRO LYS PHE SER MET
SEQRES 5 D 342 GLU VAL VAL PRO ASP ILE SER LYS LEU ASP ALA PHE ASP
SEQRES 6 D 342 HIS VAL PHE GLN LYS HIS GLY LYS ASP ILE LYS ILE VAL
SEQRES 7 D 342 LEU HIS THR ALA SER PRO PHE CYS PHE ASP ILE THR ASP
SEQRES 8 D 342 SER GLU ARG ASP LEU LEU ILE PRO ALA VAL ASN GLY VAL
SEQRES 9 D 342 LYS GLY ILE LEU HIS SER ILE LYS LYS TYR ALA ALA ASP
SEQRES 10 D 342 SER VAL GLU ARG VAL VAL LEU THR SER SER TYR ALA ALA
SEQRES 11 D 342 VAL PHE ASP MET ALA LYS GLU ASN ASP LYS SER LEU THR
SEQRES 12 D 342 PHE ASN GLU GLU SER TRP ASN PRO ALA THR TRP GLU SER
SEQRES 13 D 342 CYS GLN SER ASP PRO VAL ASN ALA TYR CYS GLY SER LYS
SEQRES 14 D 342 LYS PHE ALA GLU LYS ALA ALA TRP GLU PHE LEU GLU GLU
SEQRES 15 D 342 ASN ARG ASP SER VAL LYS PHE GLU LEU THR ALA VAL ASN
SEQRES 16 D 342 PRO VAL TYR VAL PHE GLY PRO GLN MET PHE ASP LYS ASP
SEQRES 17 D 342 VAL LYS LYS HIS LEU ASN THR SER CYS GLU LEU VAL ASN
SEQRES 18 D 342 SER LEU MET HIS LEU SER PRO GLU ASP LYS ILE PRO GLU
SEQRES 19 D 342 LEU PHE GLY GLY TYR ILE ASP VAL ARG ASP VAL ALA LYS
SEQRES 20 D 342 ALA HIS LEU VAL ALA PHE GLN LYS ARG GLU THR ILE GLY
SEQRES 21 D 342 GLN ARG LEU ILE VAL SER GLU ALA ARG PHE THR MET GLN
SEQRES 22 D 342 ASP VAL LEU ASP ILE LEU ASN GLU ASP PHE PRO VAL LEU
SEQRES 23 D 342 LYS GLY ASN ILE PRO VAL GLY LYS PRO GLY SER GLY ALA
SEQRES 24 D 342 THR HIS ASN THR LEU GLY ALA THR LEU ASP ASN LYS LYS
SEQRES 25 D 342 SER LYS LYS LEU LEU GLY PHE LYS PHE ARG ASN LEU LYS
SEQRES 26 D 342 GLU THR ILE ASP ASP THR ALA SER GLN ILE LEU LYS PHE
SEQRES 27 D 342 GLU GLY ARG ILE
HET NDP A 401 48
HET NDP B 401 48
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 5 NDP 2(C21 H30 N7 O17 P3)
FORMUL 7 HOH *127(H2 O)
HELIX 1 1 GLY A 10 GLU A 23 1 14
HELIX 2 2 SER A 33 PHE A 44 1 12
HELIX 3 3 PHE A 64 GLY A 72 1 9
HELIX 4 4 ASP A 91 LEU A 96 1 6
HELIX 5 5 LEU A 96 ALA A 115 1 20
HELIX 6 6 SER A 127 VAL A 131 5 5
HELIX 7 7 ASP A 133 GLU A 137 5 5
HELIX 8 8 GLU A 155 SER A 159 5 5
HELIX 9 9 ASP A 160 ASN A 183 1 24
HELIX 10 10 PHE A 205 VAL A 209 5 5
HELIX 11 11 ASN A 214 MET A 224 1 11
HELIX 12 12 VAL A 242 LYS A 255 1 14
HELIX 13 13 MET A 272 PHE A 283 1 12
HELIX 14 14 ASN A 310 GLY A 318 1 9
HELIX 15 15 ASN A 323 GLY A 340 1 18
HELIX 16 16 GLY B 10 GLU B 23 1 14
HELIX 17 17 SER B 33 PHE B 44 1 12
HELIX 18 18 PHE B 64 GLY B 72 1 9
HELIX 19 19 ASP B 91 LEU B 96 1 6
HELIX 20 20 LEU B 96 ALA B 115 1 20
HELIX 21 21 SER B 127 VAL B 131 5 5
HELIX 22 22 ASP B 133 GLU B 137 5 5
HELIX 23 23 GLU B 155 SER B 159 5 5
HELIX 24 24 ASP B 160 ASN B 183 1 24
HELIX 25 25 PHE B 205 VAL B 209 5 5
HELIX 26 26 ASN B 214 HIS B 225 1 12
HELIX 27 27 VAL B 242 LYS B 255 1 14
HELIX 28 28 MET B 272 PHE B 283 1 12
HELIX 29 29 ASN B 310 GLY B 318 1 9
HELIX 30 30 ASN B 323 GLU B 339 1 17
HELIX 31 31 GLY C 10 GLU C 23 1 14
HELIX 32 32 SER C 33 PHE C 44 1 12
HELIX 33 33 PHE C 64 GLY C 72 1 9
HELIX 34 34 ILE C 98 ALA C 115 1 18
HELIX 35 35 SER C 127 VAL C 131 5 5
HELIX 36 36 ALA C 135 ASP C 139 5 5
HELIX 37 37 LYS C 170 ARG C 184 1 15
HELIX 38 38 PHE C 205 VAL C 209 5 5
HELIX 39 39 LEU C 219 HIS C 225 1 7
HELIX 40 40 VAL C 242 LYS C 255 1 14
HELIX 41 41 MET C 272 PHE C 283 1 12
HELIX 42 42 ASN C 310 GLY C 318 1 9
HELIX 43 43 ASN C 323 ARG C 341 1 19
HELIX 44 44 GLY D 10 GLU D 23 1 14
HELIX 45 45 SER D 33 PHE D 44 1 12
HELIX 46 46 PHE D 64 GLY D 72 1 9
HELIX 47 47 LEU D 97 ALA D 115 1 19
HELIX 48 48 SER D 127 VAL D 131 5 5
HELIX 49 49 LYS D 169 ASN D 183 1 15
HELIX 50 50 PHE D 205 VAL D 209 5 5
HELIX 51 51 GLU D 218 HIS D 225 1 8
HELIX 52 52 VAL D 242 LYS D 255 1 14
HELIX 53 53 MET D 272 PHE D 283 1 12
HELIX 54 54 ASN D 310 GLY D 318 1 9
HELIX 55 55 ASN D 323 ARG D 341 1 19
SHEET 1 A 7 PHE A 50 VAL A 54 0
SHEET 2 A 7 LYS A 26 ALA A 31 1 N GLY A 29 O SER A 51
SHEET 3 A 7 SER A 2 SER A 6 1 N VAL A 5 O ILE A 28
SHEET 4 A 7 ILE A 75 HIS A 80 1 O LEU A 79 N PHE A 4
SHEET 5 A 7 ARG A 121 THR A 125 1 O ARG A 121 N VAL A 78
SHEET 6 A 7 GLU A 190 PRO A 196 1 O VAL A 194 N LEU A 124
SHEET 7 A 7 ARG A 262 VAL A 265 1 O LEU A 263 N ASN A 195
SHEET 1 B 2 THR A 143 PHE A 144 0
SHEET 2 B 2 THR A 307 LEU A 308 1 O THR A 307 N PHE A 144
SHEET 1 C 3 TYR A 198 PHE A 200 0
SHEET 2 C 3 PHE A 236 ASP A 241 1 O ILE A 240 N PHE A 200
SHEET 3 C 3 ALA A 268 THR A 271 -1 O PHE A 270 N GLY A 237
SHEET 1 D 7 PHE B 50 VAL B 54 0
SHEET 2 D 7 LYS B 26 ALA B 31 1 N GLY B 29 O SER B 51
SHEET 3 D 7 SER B 2 SER B 6 1 N VAL B 5 O ILE B 28
SHEET 4 D 7 ILE B 75 HIS B 80 1 O ILE B 77 N PHE B 4
SHEET 5 D 7 ARG B 121 THR B 125 1 O VAL B 123 N VAL B 78
SHEET 6 D 7 GLU B 190 PRO B 196 1 O VAL B 194 N LEU B 124
SHEET 7 D 7 ARG B 262 VAL B 265 1 O LEU B 263 N ASN B 195
SHEET 1 E 2 THR B 143 ASN B 145 0
SHEET 2 E 2 THR B 307 ASP B 309 1 O ASP B 309 N PHE B 144
SHEET 1 F 3 TYR B 198 PHE B 200 0
SHEET 2 F 3 PHE B 236 ASP B 241 1 O ILE B 240 N PHE B 200
SHEET 3 F 3 ALA B 268 THR B 271 -1 O PHE B 270 N GLY B 237
SHEET 1 G 7 PHE C 50 VAL C 54 0
SHEET 2 G 7 LYS C 26 ALA C 31 1 N GLY C 29 O GLU C 53
SHEET 3 G 7 SER C 2 VAL C 5 1 N VAL C 5 O ILE C 28
SHEET 4 G 7 ILE C 75 HIS C 80 1 O LEU C 79 N PHE C 4
SHEET 5 G 7 ARG C 121 THR C 125 1 O ARG C 121 N VAL C 78
SHEET 6 G 7 GLU C 190 PRO C 196 1 O GLU C 190 N VAL C 122
SHEET 7 G 7 ARG C 262 VAL C 265 1 O LEU C 263 N ASN C 195
SHEET 1 H 2 THR C 143 PHE C 144 0
SHEET 2 H 2 THR C 307 LEU C 308 1 O THR C 307 N PHE C 144
SHEET 1 I 3 TYR C 198 PHE C 200 0
SHEET 2 I 3 PHE C 236 ASP C 241 1 O ILE C 240 N PHE C 200
SHEET 3 I 3 ALA C 268 THR C 271 -1 O PHE C 270 N GLY C 237
SHEET 1 J 7 PHE D 50 VAL D 54 0
SHEET 2 J 7 LYS D 26 ALA D 31 1 N GLY D 29 O SER D 51
SHEET 3 J 7 SER D 2 SER D 6 1 N VAL D 3 O LYS D 26
SHEET 4 J 7 ILE D 75 HIS D 80 1 O LEU D 79 N PHE D 4
SHEET 5 J 7 ARG D 121 THR D 125 1 O VAL D 123 N VAL D 78
SHEET 6 J 7 GLU D 190 PRO D 196 1 O THR D 192 N LEU D 124
SHEET 7 J 7 ARG D 262 VAL D 265 1 O LEU D 263 N ASN D 195
SHEET 1 K 2 THR D 143 PHE D 144 0
SHEET 2 K 2 THR D 307 LEU D 308 1 O THR D 307 N PHE D 144
SHEET 1 L 3 TYR D 198 PHE D 200 0
SHEET 2 L 3 PHE D 236 ASP D 241 1 O ILE D 240 N PHE D 200
SHEET 3 L 3 ALA D 268 THR D 271 -1 O PHE D 270 N GLY D 237
SITE 1 AC1 25 GLY A 7 ASN A 9 GLY A 10 PHE A 11
SITE 2 AC1 25 ILE A 12 ARG A 32 LYS A 36 ASP A 57
SITE 3 AC1 25 ILE A 58 THR A 81 ALA A 82 SER A 83
SITE 4 AC1 25 PRO A 84 PHE A 85 THR A 125 SER A 126
SITE 5 AC1 25 SER A 127 TYR A 165 LYS A 169 PRO A 196
SITE 6 AC1 25 VAL A 197 TYR A 198 VAL A 199 SER A 216
SITE 7 AC1 25 HOH A 532
SITE 1 AC2 26 GLY B 7 ASN B 9 GLY B 10 PHE B 11
SITE 2 AC2 26 ILE B 12 ARG B 32 LYS B 36 ASP B 57
SITE 3 AC2 26 ILE B 58 THR B 81 ALA B 82 SER B 83
SITE 4 AC2 26 PRO B 84 PHE B 85 THR B 125 SER B 126
SITE 5 AC2 26 SER B 127 TYR B 165 LYS B 169 PRO B 196
SITE 6 AC2 26 VAL B 197 TYR B 198 VAL B 199 SER B 216
SITE 7 AC2 26 HOH B 511 HOH B 513
CRYST1 90.309 92.891 201.094 90.00 90.00 90.00 P 21 21 21 16
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 0.011073 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004973 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
