HEADER SIGNALING PROTEIN 24-MAR-16 5IYV
TITLE CRYSTAL STRUCTURE OF THE ARABIDOPSIS RECEPTOR KINASE HAESA LRR
TITLE 2 ECTDOMAIN IN COMPLEX WITH THE PEPTIDE HORMONE IDL1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-LIKE PROTEIN KINASE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTODOMAIN, RESIDUES 20-620;
COMPND 5 SYNONYM: PROTEIN HAESA;
COMPND 6 EC: 2.7.10.1,2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN IDA-LIKE 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 67-78;
COMPND 12 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 ORGAN: FLOWERS;
SOURCE 6 TISSUE: ABSCISSION ZONE;
SOURCE 7 GENE: RLK5, HAE, AT4G28490, F21O9.180;
SOURCE 8 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: BTI38;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 13 MOL_ID: 2;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 16 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 17 ORGANISM_TAXID: 3702
KEYWDS MEMBRANE RECEPTOR KINASE, PEPTIDE HORMONE RECEPTOR, SIGNALING
KEYWDS 2 COMPLEX, PLANT DEVELOPMENT, ORGAN SHEDDING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SANTIAGO,M.HOTHORN
REVDAT 4 10-JAN-24 5IYV 1 HETSYN LINK
REVDAT 3 29-JUL-20 5IYV 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 28-SEP-16 5IYV 1
REVDAT 1 20-APR-16 5IYV 0
JRNL AUTH J.SANTIAGO,B.BRANDT,M.WILDHAGEN,U.HOHMANN,L.A.HOTHORN,
JRNL AUTH 2 M.A.BUTENKO,M.HOTHORN
JRNL TITL MECHANISTIC INSIGHT INTO A PEPTIDE HORMONE SIGNALING COMPLEX
JRNL TITL 2 MEDIATING FLORAL ORGAN ABSCISSION.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27058169
JRNL DOI 10.7554/ELIFE.15075
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 23835
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
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) : 2.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1685
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.3960
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 9
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.00000
REMARK 3 B22 (A**2) : -4.00000
REMARK 3 B33 (A**2) : 12.99000
REMARK 3 B12 (A**2) : -2.00000
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): 0.502
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.276
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.911
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4880 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4657 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6666 ; 1.479 ; 2.039
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10799 ; 1.047 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 613 ; 6.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;45.189 ;25.989
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 804 ;13.603 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;15.620 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 810 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5425 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 996 ; 0.002 ; 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): 2413 ; 2.216 ; 6.493
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2412 ; 2.216 ; 6.492
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3015 ; 3.368 ; 9.740
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3016 ; 3.367 ; 9.741
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2465 ; 3.317 ; 7.253
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2465 ; 3.315 ; 7.254
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3642 ; 5.209 ;10.770
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 19683 ; 8.164 ;63.745
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 19684 ; 8.164 ;63.746
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 : 7
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 18 A 56
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7476 86.4811 -15.5683
REMARK 3 T TENSOR
REMARK 3 T11: 0.1851 T22: 0.1449
REMARK 3 T33: 0.2425 T12: 0.1285
REMARK 3 T13: 0.0149 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 6.7425 L22: 5.7093
REMARK 3 L33: 5.8724 L12: -0.0721
REMARK 3 L13: 1.0638 L23: 1.5721
REMARK 3 S TENSOR
REMARK 3 S11: -0.2234 S12: -0.1680 S13: 0.8350
REMARK 3 S21: -0.0490 S22: 0.3111 S23: 0.7453
REMARK 3 S31: -0.8060 S32: -0.2356 S33: -0.0877
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 57 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5066 69.0545 -13.6705
REMARK 3 T TENSOR
REMARK 3 T11: 0.0528 T22: 0.1088
REMARK 3 T33: 0.1173 T12: 0.0198
REMARK 3 T13: -0.0187 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 2.1665 L22: 3.7723
REMARK 3 L33: 1.2457 L12: -2.3578
REMARK 3 L13: 0.8939 L23: -0.8497
REMARK 3 S TENSOR
REMARK 3 S11: 0.1944 S12: 0.3681 S13: 0.0453
REMARK 3 S21: -0.2650 S22: -0.2510 S23: -0.3040
REMARK 3 S31: -0.0582 S32: 0.1055 S33: 0.0566
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 245 A 355
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1373 52.0884 11.9488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1510 T22: 0.1591
REMARK 3 T33: 0.3337 T12: 0.0161
REMARK 3 T13: -0.1569 T23: 0.0914
REMARK 3 L TENSOR
REMARK 3 L11: 3.1102 L22: 2.4244
REMARK 3 L33: 4.9177 L12: 0.3569
REMARK 3 L13: -1.5692 L23: -0.7840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: -0.5980 S13: -0.2169
REMARK 3 S21: 0.3670 S22: -0.1126 S23: -0.4765
REMARK 3 S31: -0.0116 S32: 0.2086 S33: 0.0706
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 356 A 461
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5221 43.7919 26.2935
REMARK 3 T TENSOR
REMARK 3 T11: 0.5467 T22: 0.7212
REMARK 3 T33: 0.2895 T12: -0.0941
REMARK 3 T13: -0.0857 T23: 0.1595
REMARK 3 L TENSOR
REMARK 3 L11: 4.5293 L22: 1.9228
REMARK 3 L33: 1.5885 L12: 2.5924
REMARK 3 L13: 0.3621 L23: 0.4311
REMARK 3 S TENSOR
REMARK 3 S11: 0.3495 S12: -1.1097 S13: 0.0054
REMARK 3 S21: 0.6489 S22: -0.5427 S23: -0.0464
REMARK 3 S31: 0.2694 S32: -0.4849 S33: 0.1932
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 462 A 608
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8284 24.4863 20.8507
REMARK 3 T TENSOR
REMARK 3 T11: 0.4799 T22: 0.7950
REMARK 3 T33: 0.3933 T12: -0.2739
REMARK 3 T13: 0.1739 T23: 0.2444
REMARK 3 L TENSOR
REMARK 3 L11: 4.5156 L22: 4.7557
REMARK 3 L33: 2.2493 L12: 2.3223
REMARK 3 L13: 2.1807 L23: 0.5715
REMARK 3 S TENSOR
REMARK 3 S11: 0.4777 S12: -0.9177 S13: -0.5066
REMARK 3 S21: 0.5438 S22: -0.6090 S23: 0.0919
REMARK 3 S31: 0.2769 S32: -0.3211 S33: 0.1312
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 67 B 73
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9447 58.5023 -0.4199
REMARK 3 T TENSOR
REMARK 3 T11: 0.4289 T22: 0.5860
REMARK 3 T33: 0.3914 T12: 0.0033
REMARK 3 T13: -0.1179 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.6687 L22: 3.8513
REMARK 3 L33: 0.3624 L12: -3.7508
REMARK 3 L13: -1.1454 L23: 1.1639
REMARK 3 S TENSOR
REMARK 3 S11: 0.1401 S12: 0.2880 S13: -0.3445
REMARK 3 S21: -0.0820 S22: -0.2296 S23: 0.3389
REMARK 3 S31: -0.0681 S32: -0.1219 S33: 0.0895
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 74 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9407 47.1433 9.6086
REMARK 3 T TENSOR
REMARK 3 T11: 0.3658 T22: 0.4863
REMARK 3 T33: 0.5895 T12: -0.0560
REMARK 3 T13: 0.0265 T23: 0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 0.2020 L22: 1.0557
REMARK 3 L33: 14.5696 L12: -0.2353
REMARK 3 L13: 0.6090 L23: -3.8607
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -0.2664 S13: -0.1038
REMARK 3 S21: 0.1198 S22: 0.0875 S23: 0.1010
REMARK 3 S31: -0.5506 S32: 0.0610 S33: -0.1239
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 5IYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25124
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 14.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.910
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5IXO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 0.2 M MGCL2, 0.1 M
REMARK 280 CITRIC ACID PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 20.02333
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 40.04667
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 40.04667
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 20.02333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 ASP A 47
REMARK 465 ASN A 48
REMARK 465 ASN A 49
REMARK 465 LEU A 609
REMARK 465 ASP A 610
REMARK 465 GLY A 611
REMARK 465 LEU A 612
REMARK 465 CYS A 613
REMARK 465 ARG A 614
REMARK 465 LYS A 615
REMARK 465 ILE A 616
REMARK 465 THR A 617
REMARK 465 ARG A 618
REMARK 465 SER A 619
REMARK 465 LYS A 620
REMARK 465 LEU A 621
REMARK 465 GLU A 622
REMARK 465 GLY A 623
REMARK 465 SER A 624
REMARK 465 GLU A 625
REMARK 465 ASN A 626
REMARK 465 LEU A 627
REMARK 465 TYR A 628
REMARK 465 PHE A 629
REMARK 465 GLN A 630
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 MET A 18 CG SD CE
REMARK 470 SER A 46 OG
REMARK 470 ASP A 50 CG OD1 OD2
REMARK 470 HIS A 421 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 ASN A 469 CG OD1 ND2
REMARK 470 SER A 494 OG
REMARK 470 ARG A 517 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 593 CG CD CE NZ
REMARK 470 HIS A 597 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 608 CG OD1 OD2
REMARK 470 LEU B 67 CB CG CD1 CD2
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 72 40.48 -109.31
REMARK 500 ASN A 99 -161.91 -129.85
REMARK 500 ASP A 111 -48.80 -27.98
REMARK 500 ASN A 149 -162.87 -125.53
REMARK 500 ASP A 153 -168.96 57.71
REMARK 500 TYR A 196 61.11 64.94
REMARK 500 LEU A 198 52.02 -115.46
REMARK 500 GLN A 247 55.63 -116.81
REMARK 500 PHE A 268 130.57 -37.66
REMARK 500 SER A 326 0.53 -66.70
REMARK 500 ASN A 340 46.96 72.79
REMARK 500 ASN A 365 -167.23 -129.43
REMARK 500 CYS A 376 52.03 -102.32
REMARK 500 ASN A 389 -157.71 -121.86
REMARK 500 SER A 438 41.48 -109.00
REMARK 500 ASN A 485 -157.13 -137.14
REMARK 500 GLN A 510 40.60 -106.72
REMARK 500 GLN A 558 53.17 -115.11
REMARK 500 HIS A 581 30.85 -96.62
REMARK 500 TYR A 590 31.30 -93.58
REMARK 500 MET B 75 41.93 -102.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5IYV A 20 620 UNP P47735 RLK5_ARATH 20 620
DBREF 5IYV B 67 78 UNP Q29PV4 IDL1_ARATH 67 78
SEQADV 5IYV GLY A 15 UNP P47735 EXPRESSION TAG
SEQADV 5IYV SER A 16 UNP P47735 EXPRESSION TAG
SEQADV 5IYV SER A 17 UNP P47735 EXPRESSION TAG
SEQADV 5IYV MET A 18 UNP P47735 EXPRESSION TAG
SEQADV 5IYV GLY A 19 UNP P47735 EXPRESSION TAG
SEQADV 5IYV LEU A 621 UNP P47735 EXPRESSION TAG
SEQADV 5IYV GLU A 622 UNP P47735 EXPRESSION TAG
SEQADV 5IYV GLY A 623 UNP P47735 EXPRESSION TAG
SEQADV 5IYV SER A 624 UNP P47735 EXPRESSION TAG
SEQADV 5IYV GLU A 625 UNP P47735 EXPRESSION TAG
SEQADV 5IYV ASN A 626 UNP P47735 EXPRESSION TAG
SEQADV 5IYV LEU A 627 UNP P47735 EXPRESSION TAG
SEQADV 5IYV TYR A 628 UNP P47735 EXPRESSION TAG
SEQADV 5IYV PHE A 629 UNP P47735 EXPRESSION TAG
SEQADV 5IYV GLN A 630 UNP P47735 EXPRESSION TAG
SEQRES 1 A 616 GLY SER SER MET GLY SER LEU ASN GLN ASP ALA THR ILE
SEQRES 2 A 616 LEU ARG GLN ALA LYS LEU GLY LEU SER ASP PRO ALA GLN
SEQRES 3 A 616 SER LEU SER SER TRP SER ASP ASN ASN ASP VAL THR PRO
SEQRES 4 A 616 CYS LYS TRP LEU GLY VAL SER CYS ASP ALA THR SER ASN
SEQRES 5 A 616 VAL VAL SER VAL ASP LEU SER SER PHE MET LEU VAL GLY
SEQRES 6 A 616 PRO PHE PRO SER ILE LEU CYS HIS LEU PRO SER LEU HIS
SEQRES 7 A 616 SER LEU SER LEU TYR ASN ASN SER ILE ASN GLY SER LEU
SEQRES 8 A 616 SER ALA ASP ASP PHE ASP THR CYS HIS ASN LEU ILE SER
SEQRES 9 A 616 LEU ASP LEU SER GLU ASN LEU LEU VAL GLY SER ILE PRO
SEQRES 10 A 616 LYS SER LEU PRO PHE ASN LEU PRO ASN LEU LYS PHE LEU
SEQRES 11 A 616 GLU ILE SER GLY ASN ASN LEU SER ASP THR ILE PRO SER
SEQRES 12 A 616 SER PHE GLY GLU PHE ARG LYS LEU GLU SER LEU ASN LEU
SEQRES 13 A 616 ALA GLY ASN PHE LEU SER GLY THR ILE PRO ALA SER LEU
SEQRES 14 A 616 GLY ASN VAL THR THR LEU LYS GLU LEU LYS LEU ALA TYR
SEQRES 15 A 616 ASN LEU PHE SER PRO SER GLN ILE PRO SER GLN LEU GLY
SEQRES 16 A 616 ASN LEU THR GLU LEU GLN VAL LEU TRP LEU ALA GLY CYS
SEQRES 17 A 616 ASN LEU VAL GLY PRO ILE PRO PRO SER LEU SER ARG LEU
SEQRES 18 A 616 THR SER LEU VAL ASN LEU ASP LEU THR PHE ASN GLN LEU
SEQRES 19 A 616 THR GLY SER ILE PRO SER TRP ILE THR GLN LEU LYS THR
SEQRES 20 A 616 VAL GLU GLN ILE GLU LEU PHE ASN ASN SER PHE SER GLY
SEQRES 21 A 616 GLU LEU PRO GLU SER MET GLY ASN MET THR THR LEU LYS
SEQRES 22 A 616 ARG PHE ASP ALA SER MET ASN LYS LEU THR GLY LYS ILE
SEQRES 23 A 616 PRO ASP ASN LEU ASN LEU LEU ASN LEU GLU SER LEU ASN
SEQRES 24 A 616 LEU PHE GLU ASN MET LEU GLU GLY PRO LEU PRO GLU SER
SEQRES 25 A 616 ILE THR ARG SER LYS THR LEU SER GLU LEU LYS LEU PHE
SEQRES 26 A 616 ASN ASN ARG LEU THR GLY VAL LEU PRO SER GLN LEU GLY
SEQRES 27 A 616 ALA ASN SER PRO LEU GLN TYR VAL ASP LEU SER TYR ASN
SEQRES 28 A 616 ARG PHE SER GLY GLU ILE PRO ALA ASN VAL CYS GLY GLU
SEQRES 29 A 616 GLY LYS LEU GLU TYR LEU ILE LEU ILE ASP ASN SER PHE
SEQRES 30 A 616 SER GLY GLU ILE SER ASN ASN LEU GLY LYS CYS LYS SER
SEQRES 31 A 616 LEU THR ARG VAL ARG LEU SER ASN ASN LYS LEU SER GLY
SEQRES 32 A 616 GLN ILE PRO HIS GLY PHE TRP GLY LEU PRO ARG LEU SER
SEQRES 33 A 616 LEU LEU GLU LEU SER ASP ASN SER PHE THR GLY SER ILE
SEQRES 34 A 616 PRO LYS THR ILE ILE GLY ALA LYS ASN LEU SER ASN LEU
SEQRES 35 A 616 ARG ILE SER LYS ASN ARG PHE SER GLY SER ILE PRO ASN
SEQRES 36 A 616 GLU ILE GLY SER LEU ASN GLY ILE ILE GLU ILE SER GLY
SEQRES 37 A 616 ALA GLU ASN ASP PHE SER GLY GLU ILE PRO GLU SER LEU
SEQRES 38 A 616 VAL LYS LEU LYS GLN LEU SER ARG LEU ASP LEU SER LYS
SEQRES 39 A 616 ASN GLN LEU SER GLY GLU ILE PRO ARG GLU LEU ARG GLY
SEQRES 40 A 616 TRP LYS ASN LEU ASN GLU LEU ASN LEU ALA ASN ASN HIS
SEQRES 41 A 616 LEU SER GLY GLU ILE PRO LYS GLU VAL GLY ILE LEU PRO
SEQRES 42 A 616 VAL LEU ASN TYR LEU ASP LEU SER SER ASN GLN PHE SER
SEQRES 43 A 616 GLY GLU ILE PRO LEU GLU LEU GLN ASN LEU LYS LEU ASN
SEQRES 44 A 616 VAL LEU ASN LEU SER TYR ASN HIS LEU SER GLY LYS ILE
SEQRES 45 A 616 PRO PRO LEU TYR ALA ASN LYS ILE TYR ALA HIS ASP PHE
SEQRES 46 A 616 ILE GLY ASN PRO GLY LEU CYS VAL ASP LEU ASP GLY LEU
SEQRES 47 A 616 CYS ARG LYS ILE THR ARG SER LYS LEU GLU GLY SER GLU
SEQRES 48 A 616 ASN LEU TYR PHE GLN
SEQRES 1 B 12 LEU VAL PRO PRO SER GLY HYP SER MET ARG HIS ASN
MODRES 5IYV HYP B 73 PRO MODIFIED RESIDUE
HET HYP B 73 8
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG A 703 14
HET NAG A 706 14
HET NAG A 711 14
HET EDO B2000 4
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HYP HYDROXYPROLINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 HYP C5 H9 N O3
FORMUL 3 NAG 11(C8 H15 N O6)
FORMUL 5 BMA C6 H12 O6
FORMUL 5 MAN C6 H12 O6
FORMUL 10 EDO C2 H6 O2
FORMUL 11 HOH *9(H2 O)
HELIX 1 AA1 MET A 18 GLY A 34 1 17
HELIX 2 AA2 LEU A 42 SER A 46 5 5
HELIX 3 AA3 THR A 52 TRP A 56 5 5
HELIX 4 AA4 PRO A 82 LEU A 88 5 7
HELIX 5 AA5 ALA A 107 ASP A 111 5 5
HELIX 6 AA6 SER A 133 LEU A 138 1 6
HELIX 7 AA7 PRO A 156 PHE A 162 5 7
HELIX 8 AA8 PRO A 180 VAL A 186 5 7
HELIX 9 AA9 PRO A 205 LEU A 211 5 7
HELIX 10 AB1 PRO A 229 LEU A 235 5 7
HELIX 11 AB2 PRO A 253 LEU A 259 5 7
HELIX 12 AB3 PRO A 277 MET A 283 5 7
HELIX 13 AB4 PRO A 324 SER A 330 5 7
HELIX 14 AB5 ASN A 398 CYS A 402 5 5
HELIX 15 AB6 PRO A 420 GLY A 425 5 6
HELIX 16 AB7 PRO A 444 ALA A 450 5 7
HELIX 17 AB8 PRO A 468 LEU A 474 5 7
HELIX 18 AB9 PRO A 492 LYS A 497 5 6
HELIX 19 AC1 PRO A 540 LEU A 546 5 7
HELIX 20 AC2 PRO A 564 LEU A 570 5 7
HELIX 21 AC3 PRO A 587 ALA A 591 5 5
HELIX 22 AC4 ASN A 592 PHE A 599 5 8
SHEET 1 AA123 VAL A 59 CYS A 61 0
SHEET 2 AA123 VAL A 67 ASP A 71 -1 O VAL A 68 N SER A 60
SHEET 3 AA123 SER A 93 SER A 95 1 O SER A 95 N VAL A 70
SHEET 4 AA123 SER A 118 ASP A 120 1 O ASP A 120 N LEU A 94
SHEET 5 AA123 PHE A 143 GLU A 145 1 O PHE A 143 N LEU A 119
SHEET 6 AA123 SER A 167 ASN A 169 1 O ASN A 169 N LEU A 144
SHEET 7 AA123 GLU A 191 LYS A 193 1 O LYS A 193 N LEU A 168
SHEET 8 AA123 VAL A 216 TRP A 218 1 O TRP A 218 N LEU A 192
SHEET 9 AA123 ASN A 240 ASP A 242 1 O ASP A 242 N LEU A 217
SHEET 10 AA123 GLN A 264 GLU A 266 1 O GLU A 266 N LEU A 241
SHEET 11 AA123 ARG A 288 ASP A 290 1 O ARG A 288 N ILE A 265
SHEET 12 AA123 SER A 311 ASN A 313 1 O SER A 311 N PHE A 289
SHEET 13 AA123 GLU A 335 LYS A 337 1 O GLU A 335 N LEU A 312
SHEET 14 AA123 TYR A 359 ASP A 361 1 O TYR A 359 N LEU A 336
SHEET 15 AA123 TYR A 383 ILE A 385 1 O ILE A 385 N VAL A 360
SHEET 16 AA123 ARG A 407 ARG A 409 1 O ARG A 407 N LEU A 384
SHEET 17 AA123 LEU A 431 GLU A 433 1 O GLU A 433 N VAL A 408
SHEET 18 AA123 ASN A 455 ARG A 457 1 O ARG A 457 N LEU A 432
SHEET 19 AA123 GLU A 479 SER A 481 1 O SER A 481 N LEU A 456
SHEET 20 AA123 ARG A 503 ASP A 505 1 O ARG A 503 N ILE A 480
SHEET 21 AA123 GLU A 527 ASN A 529 1 O ASN A 529 N LEU A 504
SHEET 22 AA123 TYR A 551 ASP A 553 1 O TYR A 551 N LEU A 528
SHEET 23 AA123 VAL A 574 ASN A 576 1 O ASN A 576 N LEU A 552
SHEET 1 AA2 4 VAL A 78 GLY A 79 0
SHEET 2 AA2 4 SER A 100 SER A 104 1 O ASN A 102 N GLY A 79
SHEET 3 AA2 4 LEU A 125 SER A 129 1 O LEU A 125 N ILE A 101
SHEET 4 AA2 4 ASN A 150 SER A 152 1 O ASN A 150 N LEU A 126
SHEET 1 AA3 3 VAL A 225 GLY A 226 0
SHEET 2 AA3 3 GLN A 247 GLY A 250 1 O THR A 249 N GLY A 226
SHEET 3 AA3 3 SER A 271 PHE A 272 1 O SER A 271 N LEU A 248
SHEET 1 AA4 4 GLU A 320 GLY A 321 0
SHEET 2 AA4 4 ARG A 342 GLY A 345 1 O THR A 344 N GLY A 321
SHEET 3 AA4 4 ARG A 366 GLY A 369 1 O ARG A 366 N LEU A 343
SHEET 4 AA4 4 SER A 390 PHE A 391 1 O SER A 390 N PHE A 367
SHEET 1 AA5 4 SER A 416 GLN A 418 0
SHEET 2 AA5 4 SER A 438 GLY A 441 1 O THR A 440 N GLY A 417
SHEET 3 AA5 4 ARG A 462 GLY A 465 1 O SER A 464 N GLY A 441
SHEET 4 AA5 4 ASP A 486 PHE A 487 1 O ASP A 486 N PHE A 463
SHEET 1 AA6 5 SER A 512 GLY A 513 0
SHEET 2 AA6 5 HIS A 534 GLY A 537 1 O SER A 536 N GLY A 513
SHEET 3 AA6 5 GLN A 558 GLY A 561 1 O GLN A 558 N LEU A 535
SHEET 4 AA6 5 HIS A 581 LYS A 585 1 O SER A 583 N GLY A 561
SHEET 5 AA6 5 GLY A 604 CYS A 606 1 O GLY A 604 N GLY A 584
SSBOND 1 CYS A 54 CYS A 61 1555 1555 2.07
SSBOND 2 CYS A 86 CYS A 113 1555 1555 2.00
SSBOND 3 CYS A 376 CYS A 402 1555 1555 2.05
LINK ND2 ASN A 98 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 102 C1 NAG A 703 1555 1555 1.46
LINK ND2 ASN A 150 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 185 C1 NAG A 706 1555 1555 1.44
LINK ND2 ASN A 269 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 282 C1 NAG A 711 1555 1555 1.46
LINK ND2 ASN A 576 C1 NAG F 1 1555 1555 1.44
LINK C GLY B 72 N HYP B 73 1555 1555 1.35
LINK C HYP B 73 N SER B 74 1555 1555 1.34
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.46
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
CRYST1 150.181 150.181 60.070 90.00 90.00 120.00 P 31 2 1 6
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 0.006659 0.003844 0.000000 0.00000
SCALE2 0.000000 0.007689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016647 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
