HEADER CELL ADHESION 20-JUL-16 5KX6
TITLE THE STRUCTURE OF ARABIDOPSIS THALIANA FUT1 MUTANT R284K IN COMPLEX
TITLE 2 WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALACTOSIDE 2-ALPHA-L-FUCOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 84-558;
COMPND 5 SYNONYM: XYLOGLUCAN ALPHA-(1,2)-FUCOSYLTRANSFERASE,ATFUT1;
COMPND 6 EC: 2.4.1.69;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: FUT1, FT1, MUR2, AT2G03220, T18E12.11;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293
KEYWDS ACETYL TRANSFERASE, GT37, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.ALAHUHTA,V.V.LUNIN
REVDAT 4 04-OCT-23 5KX6 1 REMARK
REVDAT 3 30-MAY-18 5KX6 1 JRNL REMARK
REVDAT 2 09-NOV-16 5KX6 1 DBREF ATOM
REVDAT 1 28-SEP-16 5KX6 0
JRNL AUTH B.R.URBANOWICZ,V.S.BHARADWAJ,M.ALAHUHTA,M.J.PENA,V.V.LUNIN,
JRNL AUTH 2 Y.J.BOMBLE,S.WANG,J.Y.YANG,S.T.TUOMIVAARA,M.E.HIMMEL,
JRNL AUTH 3 K.W.MOREMEN,W.S.YORK,M.F.CROWLEY
JRNL TITL STRUCTURAL, MUTAGENIC AND IN SILICO STUDIES OF XYLOGLUCAN
JRNL TITL 2 FUCOSYLATION IN ARABIDOPSIS THALIANA SUGGEST A
JRNL TITL 3 WATER-MEDIATED MECHANISM.
JRNL REF PLANT J. V. 91 931 2017
JRNL REFN ESSN 1365-313X
JRNL PMID 28670741
JRNL DOI 10.1111/TPJ.13628
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 45191
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) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.327
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2288
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3016
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.4800
REMARK 3 BIN FREE R VALUE SET COUNT : 156
REMARK 3 BIN FREE R VALUE : 0.4960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.77000
REMARK 3 B22 (A**2) : 3.59000
REMARK 3 B33 (A**2) : 2.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.451
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.317
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.337
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.604
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7595 ; 0.021 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6989 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10337 ; 2.094 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16182 ; 1.192 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 917 ; 7.580 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 338 ;39.661 ;23.905
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1255 ;17.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;19.772 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1092 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8483 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1762 ; 0.003 ; 0.020
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): 3641 ; 0.860 ; 0.661
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3640 ; 0.860 ; 0.661
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4567 ; 1.597 ; 0.976
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4568 ; 1.597 ; 0.976
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3954 ; 0.723 ; 0.757
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3954 ; 0.723 ; 0.757
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5771 ; 1.350 ; 1.122
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8938 ; 6.265 ; 8.264
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8831 ; 6.146 ; 7.880
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 95 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2940 25.1930 -3.7320
REMARK 3 T TENSOR
REMARK 3 T11: 0.4903 T22: 0.0315
REMARK 3 T33: 0.0895 T12: 0.0735
REMARK 3 T13: 0.1962 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.9182 L22: 1.6038
REMARK 3 L33: 1.6581 L12: -0.6916
REMARK 3 L13: 0.3735 L23: -0.1619
REMARK 3 S TENSOR
REMARK 3 S11: -0.1324 S12: -0.0834 S13: -0.0303
REMARK 3 S21: 0.1534 S22: 0.1330 S23: 0.1216
REMARK 3 S31: -0.2541 S32: -0.1828 S33: -0.0006
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 339 A 424
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1480 4.7790 -19.5860
REMARK 3 T TENSOR
REMARK 3 T11: 0.4566 T22: 0.0277
REMARK 3 T33: 0.1079 T12: 0.0377
REMARK 3 T13: 0.2096 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.3204 L22: 1.8201
REMARK 3 L33: 1.5328 L12: -1.1095
REMARK 3 L13: -0.1239 L23: 0.1957
REMARK 3 S TENSOR
REMARK 3 S11: 0.0721 S12: 0.0510 S13: -0.0449
REMARK 3 S21: -0.1678 S22: -0.0880 S23: -0.0701
REMARK 3 S31: 0.1819 S32: 0.1785 S33: 0.0159
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 425 A 558
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2270 7.6980 -7.0520
REMARK 3 T TENSOR
REMARK 3 T11: 0.4014 T22: 0.0171
REMARK 3 T33: 0.0948 T12: 0.0212
REMARK 3 T13: 0.1701 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.4885 L22: 1.6154
REMARK 3 L33: 2.0663 L12: -0.7978
REMARK 3 L13: -0.8272 L23: 0.9647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: -0.0474 S13: -0.0333
REMARK 3 S21: 0.0568 S22: 0.0417 S23: -0.0033
REMARK 3 S31: 0.0623 S32: 0.0852 S33: 0.0263
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 : B 95 B 336
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8540 -7.8820 29.6280
REMARK 3 T TENSOR
REMARK 3 T11: 0.4336 T22: 0.0284
REMARK 3 T33: 0.0957 T12: 0.0013
REMARK 3 T13: 0.1886 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.3289 L22: 1.1773
REMARK 3 L33: 0.9508 L12: -0.4621
REMARK 3 L13: -0.3065 L23: 0.0294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: -0.1260 S13: 0.0302
REMARK 3 S21: -0.0314 S22: -0.0311 S23: -0.1382
REMARK 3 S31: 0.0401 S32: 0.1323 S33: 0.0293
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 : B 337 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3800 11.6350 45.8120
REMARK 3 T TENSOR
REMARK 3 T11: 0.4288 T22: 0.0268
REMARK 3 T33: 0.0752 T12: 0.0237
REMARK 3 T13: 0.1515 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.6244 L22: 2.5189
REMARK 3 L33: 0.6455 L12: -1.2232
REMARK 3 L13: -0.4182 L23: -0.3590
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.1400 S13: 0.0666
REMARK 3 S21: -0.0028 S22: 0.1462 S23: 0.1087
REMARK 3 S31: -0.0891 S32: -0.0403 S33: -0.1430
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 : B 430 B 558
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2000 11.6380 34.2690
REMARK 3 T TENSOR
REMARK 3 T11: 0.4092 T22: 0.0081
REMARK 3 T33: 0.0962 T12: 0.0117
REMARK 3 T13: 0.1713 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.0049 L22: 0.5677
REMARK 3 L33: 1.6942 L12: -0.6585
REMARK 3 L13: -1.0217 L23: 0.5571
REMARK 3 S TENSOR
REMARK 3 S11: 0.1153 S12: 0.0080 S13: 0.1530
REMARK 3 S21: -0.1281 S22: -0.0387 S23: -0.1469
REMARK 3 S31: -0.1434 S32: 0.0220 S33: -0.0766
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5KX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : HELIOS MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47518
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 85.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 2.710
REMARK 200 R MERGE (I) : 0.10770
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48090
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.140
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5KOE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7 MG/ML PROTEIN IN 0.1 M MES PH 6.0 TO
REMARK 280 7.0 AND 16% TO 23% W/V PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 56.47850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -21.95969
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 85.03427
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 83
REMARK 465 GLY A 84
REMARK 465 VAL A 85
REMARK 465 PHE A 86
REMARK 465 PRO A 87
REMARK 465 ASN A 88
REMARK 465 VAL A 89
REMARK 465 THR A 90
REMARK 465 ASN A 91
REMARK 465 ILE A 92
REMARK 465 ASN A 93
REMARK 465 SER A 94
REMARK 465 HIS A 164
REMARK 465 ILE A 165
REMARK 465 ASP A 166
REMARK 465 GLY A 167
REMARK 465 ASP A 168
REMARK 465 ILE A 256
REMARK 465 ASP A 257
REMARK 465 THR A 258
REMARK 465 GLU A 259
REMARK 465 GLY A 260
REMARK 465 GLU A 400
REMARK 465 ARG A 401
REMARK 465 SER A 402
REMARK 465 ARG A 403
REMARK 465 HIS A 404
REMARK 465 VAL A 405
REMARK 465 ASN A 406
REMARK 465 TYR A 451
REMARK 465 GLN A 452
REMARK 465 GLN A 453
REMARK 465 THR A 454
REMARK 465 GLU A 455
REMARK 465 LYS A 456
REMARK 465 LYS A 457
REMARK 465 GLY B 83
REMARK 465 GLY B 84
REMARK 465 VAL B 85
REMARK 465 PHE B 86
REMARK 465 PRO B 87
REMARK 465 ASN B 88
REMARK 465 VAL B 89
REMARK 465 THR B 90
REMARK 465 ASN B 91
REMARK 465 ILE B 92
REMARK 465 ASN B 93
REMARK 465 SER B 94
REMARK 465 GLU B 400
REMARK 465 ARG B 401
REMARK 465 SER B 402
REMARK 465 ARG B 403
REMARK 465 HIS B 404
REMARK 465 VAL B 405
REMARK 465 ASN B 406
REMARK 465 TYR B 451
REMARK 465 GLN B 452
REMARK 465 GLN B 453
REMARK 465 THR B 454
REMARK 465 GLU B 455
REMARK 465 LYS B 456
REMARK 465 LYS B 457
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 GLN B 162 CG CD OE1 NE2
REMARK 470 GLN B 341 CD OE1 NE2
REMARK 470 GLU B 370 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 183 N GLY A 183 CA 0.092
REMARK 500 GLU B 424 CD GLU B 424 OE2 0.067
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 201 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 333 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 185 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU B 187 CB - CG - CD2 ANGL. DEV. = 10.8 DEGREES
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 LEU A 98 49.21 71.78
REMARK 500 ASP A 161 -77.68 -93.36
REMARK 500 GLN A 162 75.53 -69.64
REMARK 500 SER A 180 167.07 81.64
REMARK 500 ASP A 206 102.60 -37.30
REMARK 500 ASP A 210 5.80 -153.60
REMARK 500 MET A 222 132.57 -174.42
REMARK 500 GLN A 254 100.02 13.12
REMARK 500 THR A 397 -71.79 -74.89
REMARK 500 HIS A 444 119.51 -161.43
REMARK 500 TRP A 481 -9.21 84.59
REMARK 500 ARG B 114 -74.70 -13.25
REMARK 500 SER B 180 -162.45 70.11
REMARK 500 ASP B 210 2.28 -156.04
REMARK 500 PHE B 280 -31.83 -37.94
REMARK 500 VAL B 304 -47.41 -26.61
REMARK 500 LEU B 398 66.87 -159.71
REMARK 500 CYS B 548 152.99 -40.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1008 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A1009 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 6.06 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KWK RELATED DB: PDB
DBREF 5KX6 A 84 558 UNP Q9SWH5 FUT1_ARATH 84 558
DBREF 5KX6 B 84 558 UNP Q9SWH5 FUT1_ARATH 84 558
SEQADV 5KX6 GLY A 83 UNP Q9SWH5 EXPRESSION TAG
SEQADV 5KX6 LYS A 366 UNP Q9SWH5 ARG 366 ENGINEERED MUTATION
SEQADV 5KX6 GLY B 83 UNP Q9SWH5 EXPRESSION TAG
SEQADV 5KX6 LYS B 366 UNP Q9SWH5 ARG 366 ENGINEERED MUTATION
SEQRES 1 A 476 GLY GLY VAL PHE PRO ASN VAL THR ASN ILE ASN SER ASP
SEQRES 2 A 476 LYS LEU LEU GLY GLY LEU LEU ALA SER GLY PHE ASP GLU
SEQRES 3 A 476 ASP SER CYS LEU SER ARG TYR GLN SER VAL HIS TYR ARG
SEQRES 4 A 476 LYS PRO SER PRO TYR LYS PRO SER SER TYR LEU ILE SER
SEQRES 5 A 476 LYS LEU ARG ASN TYR GLU LYS LEU HIS LYS ARG CYS GLY
SEQRES 6 A 476 PRO GLY THR GLU SER TYR LYS LYS ALA LEU LYS GLN LEU
SEQRES 7 A 476 ASP GLN GLU HIS ILE ASP GLY ASP GLY GLU CYS LYS TYR
SEQRES 8 A 476 VAL VAL TRP ILE SER PHE SER GLY LEU GLY ASN ARG ILE
SEQRES 9 A 476 LEU SER LEU ALA SER VAL PHE LEU TYR ALA LEU LEU THR
SEQRES 10 A 476 ASP ARG VAL LEU LEU VAL ASP ARG GLY LYS ASP MET ASP
SEQRES 11 A 476 ASP LEU PHE CYS GLU PRO PHE LEU GLY MET SER TRP LEU
SEQRES 12 A 476 LEU PRO LEU ASP PHE PRO MET THR ASP GLN PHE ASP GLY
SEQRES 13 A 476 LEU ASN GLN GLU SER SER ARG CYS TYR GLY TYR MET VAL
SEQRES 14 A 476 LYS ASN GLN VAL ILE ASP THR GLU GLY THR LEU SER HIS
SEQRES 15 A 476 LEU TYR LEU HIS LEU VAL HIS ASP TYR GLY ASP HIS ASP
SEQRES 16 A 476 LYS MET PHE PHE CYS GLU GLY ASP GLN THR PHE ILE GLY
SEQRES 17 A 476 LYS VAL PRO TRP LEU ILE VAL LYS THR ASP ASN TYR PHE
SEQRES 18 A 476 VAL PRO SER LEU TRP LEU ILE PRO GLY PHE ASP ASP GLU
SEQRES 19 A 476 LEU ASN LYS LEU PHE PRO GLN LYS ALA THR VAL PHE HIS
SEQRES 20 A 476 HIS LEU GLY ARG TYR LEU PHE HIS PRO THR ASN GLN VAL
SEQRES 21 A 476 TRP GLY LEU VAL THR ARG TYR TYR GLU ALA TYR LEU SER
SEQRES 22 A 476 HIS ALA ASP GLU LYS ILE GLY ILE GLN VAL LYS VAL PHE
SEQRES 23 A 476 ASP GLU ASP PRO GLY PRO PHE GLN HIS VAL MET ASP GLN
SEQRES 24 A 476 ILE SER SER CYS THR GLN LYS GLU LYS LEU LEU PRO GLU
SEQRES 25 A 476 VAL ASP THR LEU VAL GLU ARG SER ARG HIS VAL ASN THR
SEQRES 26 A 476 PRO LYS HIS LYS ALA VAL LEU VAL THR SER LEU ASN ALA
SEQRES 27 A 476 GLY TYR ALA GLU ASN LEU LYS SER MET TYR TRP GLU TYR
SEQRES 28 A 476 PRO THR SER THR GLY GLU ILE ILE GLY VAL HIS GLN PRO
SEQRES 29 A 476 SER GLN GLU GLY TYR GLN GLN THR GLU LYS LYS MET HIS
SEQRES 30 A 476 ASN GLY LYS ALA LEU ALA GLU MET TYR LEU LEU SER LEU
SEQRES 31 A 476 THR ASP ASN LEU VAL THR SER ALA TRP SER THR PHE GLY
SEQRES 32 A 476 TYR VAL ALA GLN GLY LEU GLY GLY LEU LYS PRO TRP ILE
SEQRES 33 A 476 LEU TYR ARG PRO GLU ASN ARG THR THR PRO ASP PRO SER
SEQRES 34 A 476 CYS GLY ARG ALA MET SER MET GLU PRO CYS PHE HIS SER
SEQRES 35 A 476 PRO PRO PHE TYR ASP CYS LYS ALA LYS THR GLY ILE ASP
SEQRES 36 A 476 THR GLY THR LEU VAL PRO HIS VAL ARG HIS CYS GLU ASP
SEQRES 37 A 476 ILE SER TRP GLY LEU LYS LEU VAL
SEQRES 1 B 476 GLY GLY VAL PHE PRO ASN VAL THR ASN ILE ASN SER ASP
SEQRES 2 B 476 LYS LEU LEU GLY GLY LEU LEU ALA SER GLY PHE ASP GLU
SEQRES 3 B 476 ASP SER CYS LEU SER ARG TYR GLN SER VAL HIS TYR ARG
SEQRES 4 B 476 LYS PRO SER PRO TYR LYS PRO SER SER TYR LEU ILE SER
SEQRES 5 B 476 LYS LEU ARG ASN TYR GLU LYS LEU HIS LYS ARG CYS GLY
SEQRES 6 B 476 PRO GLY THR GLU SER TYR LYS LYS ALA LEU LYS GLN LEU
SEQRES 7 B 476 ASP GLN GLU HIS ILE ASP GLY ASP GLY GLU CYS LYS TYR
SEQRES 8 B 476 VAL VAL TRP ILE SER PHE SER GLY LEU GLY ASN ARG ILE
SEQRES 9 B 476 LEU SER LEU ALA SER VAL PHE LEU TYR ALA LEU LEU THR
SEQRES 10 B 476 ASP ARG VAL LEU LEU VAL ASP ARG GLY LYS ASP MET ASP
SEQRES 11 B 476 ASP LEU PHE CYS GLU PRO PHE LEU GLY MET SER TRP LEU
SEQRES 12 B 476 LEU PRO LEU ASP PHE PRO MET THR ASP GLN PHE ASP GLY
SEQRES 13 B 476 LEU ASN GLN GLU SER SER ARG CYS TYR GLY TYR MET VAL
SEQRES 14 B 476 LYS ASN GLN VAL ILE ASP THR GLU GLY THR LEU SER HIS
SEQRES 15 B 476 LEU TYR LEU HIS LEU VAL HIS ASP TYR GLY ASP HIS ASP
SEQRES 16 B 476 LYS MET PHE PHE CYS GLU GLY ASP GLN THR PHE ILE GLY
SEQRES 17 B 476 LYS VAL PRO TRP LEU ILE VAL LYS THR ASP ASN TYR PHE
SEQRES 18 B 476 VAL PRO SER LEU TRP LEU ILE PRO GLY PHE ASP ASP GLU
SEQRES 19 B 476 LEU ASN LYS LEU PHE PRO GLN LYS ALA THR VAL PHE HIS
SEQRES 20 B 476 HIS LEU GLY ARG TYR LEU PHE HIS PRO THR ASN GLN VAL
SEQRES 21 B 476 TRP GLY LEU VAL THR ARG TYR TYR GLU ALA TYR LEU SER
SEQRES 22 B 476 HIS ALA ASP GLU LYS ILE GLY ILE GLN VAL LYS VAL PHE
SEQRES 23 B 476 ASP GLU ASP PRO GLY PRO PHE GLN HIS VAL MET ASP GLN
SEQRES 24 B 476 ILE SER SER CYS THR GLN LYS GLU LYS LEU LEU PRO GLU
SEQRES 25 B 476 VAL ASP THR LEU VAL GLU ARG SER ARG HIS VAL ASN THR
SEQRES 26 B 476 PRO LYS HIS LYS ALA VAL LEU VAL THR SER LEU ASN ALA
SEQRES 27 B 476 GLY TYR ALA GLU ASN LEU LYS SER MET TYR TRP GLU TYR
SEQRES 28 B 476 PRO THR SER THR GLY GLU ILE ILE GLY VAL HIS GLN PRO
SEQRES 29 B 476 SER GLN GLU GLY TYR GLN GLN THR GLU LYS LYS MET HIS
SEQRES 30 B 476 ASN GLY LYS ALA LEU ALA GLU MET TYR LEU LEU SER LEU
SEQRES 31 B 476 THR ASP ASN LEU VAL THR SER ALA TRP SER THR PHE GLY
SEQRES 32 B 476 TYR VAL ALA GLN GLY LEU GLY GLY LEU LYS PRO TRP ILE
SEQRES 33 B 476 LEU TYR ARG PRO GLU ASN ARG THR THR PRO ASP PRO SER
SEQRES 34 B 476 CYS GLY ARG ALA MET SER MET GLU PRO CYS PHE HIS SER
SEQRES 35 B 476 PRO PRO PHE TYR ASP CYS LYS ALA LYS THR GLY ILE ASP
SEQRES 36 B 476 THR GLY THR LEU VAL PRO HIS VAL ARG HIS CYS GLU ASP
SEQRES 37 B 476 ILE SER TRP GLY LEU LYS LEU VAL
HET GDP A 601 28
HET GDP B 601 28
HET GOL B 602 6
HET EDO B 603 4
HET MES B 604 12
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 EDO C2 H6 O2
FORMUL 7 MES C6 H13 N O4 S
FORMUL 8 HOH *610(H2 O)
HELIX 1 AA1 LEU A 112 SER A 117 1 6
HELIX 2 AA2 VAL A 118 TYR A 120 5 3
HELIX 3 AA3 SER A 129 GLY A 147 1 19
HELIX 4 AA4 THR A 150 GLN A 159 1 10
HELIX 5 AA5 GLY A 181 THR A 199 1 19
HELIX 6 AA6 ASP A 210 PHE A 215 1 6
HELIX 7 AA7 PHE A 230 PHE A 236 5 7
HELIX 8 AA8 CYS A 246 ASN A 253 1 8
HELIX 9 AA9 ASP A 277 PHE A 281 5 5
HELIX 10 AB1 CYS A 282 GLY A 290 1 9
HELIX 11 AB2 PHE A 303 TRP A 308 1 6
HELIX 12 AB3 GLY A 312 PHE A 321 1 10
HELIX 13 AB4 GLN A 323 ALA A 325 5 3
HELIX 14 AB5 THR A 326 PHE A 336 1 11
HELIX 15 AB6 THR A 339 LEU A 354 1 16
HELIX 16 AB7 PHE A 375 GLU A 389 1 15
HELIX 17 AB8 ALA A 420 TYR A 433 1 14
HELIX 18 AB9 HIS A 459 LEU A 472 1 14
HELIX 19 AC1 SER A 482 GLY A 493 1 12
HELIX 20 AC2 ASP A 537 LEU A 541 5 5
HELIX 21 AC3 LEU B 112 ARG B 121 1 10
HELIX 22 AC4 SER B 129 GLY B 147 1 19
HELIX 23 AC5 THR B 150 LYS B 158 1 9
HELIX 24 AC6 GLN B 159 ASP B 161 5 3
HELIX 25 AC7 GLY B 181 THR B 199 1 19
HELIX 26 AC8 ASP B 210 PHE B 215 1 6
HELIX 27 AC9 MET B 232 PHE B 236 5 5
HELIX 28 AD1 CYS B 246 GLN B 254 1 9
HELIX 29 AD2 HIS B 276 PHE B 281 5 6
HELIX 30 AD3 CYS B 282 GLY B 290 1 9
HELIX 31 AD4 PHE B 303 TRP B 308 1 6
HELIX 32 AD5 GLY B 312 PHE B 321 1 10
HELIX 33 AD6 GLN B 323 ALA B 325 5 3
HELIX 34 AD7 THR B 326 PHE B 336 1 11
HELIX 35 AD8 THR B 339 LEU B 354 1 16
HELIX 36 AD9 PHE B 375 GLU B 389 1 15
HELIX 37 AE1 ALA B 420 TYR B 433 1 14
HELIX 38 AE2 HIS B 459 LEU B 472 1 14
HELIX 39 AE3 SER B 482 GLY B 493 1 12
HELIX 40 AE4 ASP B 537 LEU B 541 5 5
SHEET 1 AA1 4 VAL A 202 VAL A 205 0
SHEET 2 AA1 4 TYR A 173 TRP A 176 1 N VAL A 174 O VAL A 202
SHEET 3 AA1 4 TRP A 294 THR A 299 1 O LEU A 295 N VAL A 175
SHEET 4 AA1 4 HIS A 264 LEU A 269 1 N LEU A 267 O ILE A 296
SHEET 1 AA2 6 ILE A 440 HIS A 444 0
SHEET 2 AA2 6 HIS A 410 THR A 416 1 N LYS A 411 O ILE A 440
SHEET 3 AA2 6 GLU A 359 GLN A 364 1 N ILE A 361 O LEU A 414
SHEET 4 AA2 6 ASN A 475 SER A 479 1 O ASN A 475 N GLY A 362
SHEET 5 AA2 6 TRP A 497 LEU A 499 1 O LEU A 499 N THR A 478
SHEET 6 AA2 6 CYS A 512 ARG A 514 -1 O GLY A 513 N ILE A 498
SHEET 1 AA3 2 TYR A 528 ASP A 529 0
SHEET 2 AA3 2 THR A 534 GLY A 535 -1 O THR A 534 N ASP A 529
SHEET 1 AA4 2 VAL A 545 HIS A 547 0
SHEET 2 AA4 2 LEU A 555 LEU A 557 -1 O LYS A 556 N ARG A 546
SHEET 1 AA5 4 VAL B 202 VAL B 205 0
SHEET 2 AA5 4 TYR B 173 TRP B 176 1 N VAL B 174 O LEU B 204
SHEET 3 AA5 4 TRP B 294 THR B 299 1 O VAL B 297 N VAL B 175
SHEET 4 AA5 4 HIS B 264 LEU B 269 1 N LEU B 267 O ILE B 296
SHEET 1 AA6 6 ILE B 440 HIS B 444 0
SHEET 2 AA6 6 HIS B 410 THR B 416 1 N LYS B 411 O ILE B 440
SHEET 3 AA6 6 GLU B 359 GLN B 364 1 N ILE B 361 O LEU B 414
SHEET 4 AA6 6 ASN B 475 SER B 479 1 O VAL B 477 N GLY B 362
SHEET 5 AA6 6 TRP B 497 LEU B 499 1 O TRP B 497 N THR B 478
SHEET 6 AA6 6 CYS B 512 ARG B 514 -1 O GLY B 513 N ILE B 498
SHEET 1 AA7 2 VAL B 545 HIS B 547 0
SHEET 2 AA7 2 LEU B 555 LEU B 557 -1 O LYS B 556 N ARG B 546
SSBOND 1 CYS A 111 CYS A 216 1555 1555 2.07
SSBOND 2 CYS A 146 CYS A 171 1555 1555 2.02
SSBOND 3 CYS A 282 CYS A 530 1555 1555 2.05
SSBOND 4 CYS A 385 CYS A 512 1555 1555 2.14
SSBOND 5 CYS A 521 CYS A 548 1555 1555 2.05
SSBOND 6 CYS B 111 CYS B 216 1555 1555 2.08
SSBOND 7 CYS B 146 CYS B 171 1555 1555 2.07
SSBOND 8 CYS B 282 CYS B 530 1555 1555 2.02
SSBOND 9 CYS B 385 CYS B 512 1555 1555 2.09
SSBOND 10 CYS B 521 CYS B 548 1555 1555 2.03
CISPEP 1 GLY A 373 PRO A 374 0 1.98
CISPEP 2 ASP A 509 PRO A 510 0 -5.63
CISPEP 3 GLY B 373 PRO B 374 0 4.11
CISPEP 4 ASP B 509 PRO B 510 0 4.24
SITE 1 AC1 10 LYS A 366 PHE A 368 THR A 416 SER A 417
SITE 2 AC1 10 LEU A 418 SER A 447 ALA A 463 GLU A 466
SITE 3 AC1 10 PHE A 484 HOH A 749
SITE 1 AC2 9 LYS B 366 THR B 416 SER B 417 SER B 447
SITE 2 AC2 9 GLU B 466 PHE B 484 HOH B 713 HOH B 718
SITE 3 AC2 9 HOH B 841
SITE 1 AC3 9 LYS B 366 VAL B 378 GLN B 381 SER B 479
SITE 2 AC3 9 ALA B 480 LEU B 499 TYR B 500 PRO B 502
SITE 3 AC3 9 HOH B 855
SITE 1 AC4 6 ALA A 352 HIS B 410 LYS B 411 GLY B 442
SITE 2 AC4 6 HIS B 444 HOH B 899
SITE 1 AC5 4 TYR B 247 GLY B 284 ASP B 285 HOH B 701
CRYST1 54.224 112.957 87.824 90.00 104.48 90.00 P 1 21 1 4
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 0.018442 0.000000 0.004764 0.00000
SCALE2 0.000000 0.008853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011760 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
