HEADER SIGNALING PROTEIN 23-MAR-16 5IXQ
TITLE CRYSTAL STRUCTURE OF THE ARABIDOPSIS RECEPTOR KINASE HAESA LRR
TITLE 2 ECTDOMAIN IN COMPLEX WITH THE PEPTIDE HORMONE IDA.
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;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 58-69;
COMPND 12 SYNONYM: PROTEIN INFLORESCENCE DEFICIENT IN ABSCISSION;
COMPND 13 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: FLOWER;
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_STRAIN: BTI38;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PBAC3MOD;
SOURCE 14 MOL_ID: 2;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 17 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 18 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 5IXQ 1 HETSYN LINK
REVDAT 3 29-JUL-20 5IXQ 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 28-SEP-16 5IXQ 1
REVDAT 1 20-APR-16 5IXQ 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. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 128.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 58551
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2988
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4295
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4611
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 182
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.22000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.940
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4923 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4694 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6715 ; 1.691 ; 2.035
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10883 ; 1.120 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 616 ; 6.349 ; 5.032
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 190 ;43.795 ;26.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 812 ;12.744 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;17.233 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 814 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5467 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1008 ; 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): 2435 ; 2.563 ; 6.412
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2434 ; 2.563 ; 6.412
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3041 ; 3.008 ; 9.596
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3042 ; 3.008 ; 9.596
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2486 ; 3.852 ; 7.073
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2486 ; 3.851 ; 7.073
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3667 ; 5.534 ;10.457
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5129 ; 6.205 ;51.477
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5130 ; 6.205 ;51.480
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): -12.7361 85.3549 -14.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0567
REMARK 3 T33: 0.1577 T12: 0.0329
REMARK 3 T13: -0.0330 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 4.2136 L22: 5.1423
REMARK 3 L33: 6.1871 L12: 0.7760
REMARK 3 L13: -0.4074 L23: 0.0934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: -0.1757 S13: 0.4409
REMARK 3 S21: -0.0967 S22: 0.0576 S23: 0.3517
REMARK 3 S31: -0.5366 S32: -0.1627 S33: -0.0052
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): 7.2493 67.7758 -13.5151
REMARK 3 T TENSOR
REMARK 3 T11: 0.0233 T22: 0.0234
REMARK 3 T33: 0.0640 T12: -0.0025
REMARK 3 T13: 0.0043 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 0.8385 L22: 1.6911
REMARK 3 L33: 0.7383 L12: -0.6414
REMARK 3 L13: 0.3475 L23: -0.2719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: 0.1318 S13: 0.0956
REMARK 3 S21: -0.1734 S22: -0.0580 S23: -0.0271
REMARK 3 S31: 0.0028 S32: 0.0307 S33: 0.0417
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): 16.8007 51.1229 12.0901
REMARK 3 T TENSOR
REMARK 3 T11: 0.0213 T22: 0.0382
REMARK 3 T33: 0.0767 T12: -0.0020
REMARK 3 T13: -0.0029 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.8753 L22: 1.8721
REMARK 3 L33: 2.4053 L12: 0.3307
REMARK 3 L13: -0.3775 L23: -0.1257
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: -0.1265 S13: 0.0342
REMARK 3 S21: 0.1328 S22: -0.1098 S23: -0.1648
REMARK 3 S31: -0.0231 S32: 0.1642 S33: 0.0476
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): -2.0038 43.0424 26.2988
REMARK 3 T TENSOR
REMARK 3 T11: 0.1214 T22: 0.1513
REMARK 3 T33: 0.0680 T12: -0.0965
REMARK 3 T13: 0.0607 T23: -0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 2.5465 L22: 2.0712
REMARK 3 L33: 1.5414 L12: 1.3762
REMARK 3 L13: 0.1833 L23: 0.1095
REMARK 3 S TENSOR
REMARK 3 S11: 0.2444 S12: -0.4200 S13: 0.1233
REMARK 3 S21: 0.3679 S22: -0.3008 S23: 0.2364
REMARK 3 S31: 0.0856 S32: -0.2607 S33: 0.0564
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 615
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9553 23.2362 20.0422
REMARK 3 T TENSOR
REMARK 3 T11: 0.1794 T22: 0.2466
REMARK 3 T33: 0.1094 T12: -0.1346
REMARK 3 T13: 0.0656 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 3.0718 L22: 2.8314
REMARK 3 L33: 2.2446 L12: 2.0307
REMARK 3 L13: 1.0639 L23: 0.4865
REMARK 3 S TENSOR
REMARK 3 S11: 0.3833 S12: -0.3937 S13: 0.0971
REMARK 3 S21: 0.2262 S22: -0.3773 S23: 0.2991
REMARK 3 S31: 0.2291 S32: -0.3306 S33: -0.0060
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 58 B 64
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0438 57.3302 -0.2876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1341 T22: 0.5350
REMARK 3 T33: 0.2512 T12: -0.0426
REMARK 3 T13: 0.0267 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 8.4834 L22: 10.1351
REMARK 3 L33: 1.5477 L12: 1.3701
REMARK 3 L13: -2.3070 L23: 2.6037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1746 S12: 1.0928 S13: 0.1130
REMARK 3 S21: -0.5539 S22: -0.0735 S23: 1.0021
REMARK 3 S31: -0.1078 S32: -0.4744 S33: 0.2481
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 65 B 69
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5258 46.7859 8.4915
REMARK 3 T TENSOR
REMARK 3 T11: 0.1135 T22: 0.1120
REMARK 3 T33: 0.1252 T12: 0.0096
REMARK 3 T13: 0.0110 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 4.4790 L22: 6.5909
REMARK 3 L33: 2.8358 L12: 4.5857
REMARK 3 L13: -2.2431 L23: -2.7108
REMARK 3 S TENSOR
REMARK 3 S11: -0.1438 S12: 0.1908 S13: -0.0161
REMARK 3 S21: -0.1776 S22: 0.1448 S23: 0.0975
REMARK 3 S31: 0.0629 S32: -0.2668 S33: -0.0010
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 5IXQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219630.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-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) : 1.000010
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 : 61813
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 128.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 19.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 (%): 54.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% 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 19.31000
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 38.62000
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 38.62000
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 19.31000
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: 5040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 17.0 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 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 ARG A 517 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 593 CG CD CE NZ
REMARK 470 LEU A 609 CG CD1 CD2
REMARK 470 ASP A 610 CG OD1 OD2
REMARK 470 LEU A 612 CB CG CD1 CD2
REMARK 470 ARG A 614 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 615 CG CD CE NZ
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 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.6 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 ASN A 98 62.09 62.96
REMARK 500 ASN A 99 -157.13 -131.04
REMARK 500 ASN A 124 -156.95 -129.86
REMARK 500 ASN A 149 -161.20 -120.41
REMARK 500 ASP A 153 -164.20 69.92
REMARK 500 SER A 176 -164.79 -128.60
REMARK 500 TYR A 196 60.59 65.56
REMARK 500 ASN A 269 70.24 59.18
REMARK 500 ASN A 270 -159.38 -140.20
REMARK 500 ASN A 294 -155.93 -131.63
REMARK 500 ASP A 302 -168.05 -108.17
REMARK 500 ASP A 388 63.13 60.57
REMARK 500 ASN A 413 -157.33 -124.88
REMARK 500 ASP A 436 60.14 62.41
REMARK 500 ASN A 437 -154.28 -135.50
REMARK 500 ASN A 485 -159.87 -129.59
REMARK 500 ASN A 509 -159.21 -135.50
REMARK 500 ASN A 533 -158.17 -134.69
REMARK 500 ASN A 557 -154.91 -134.81
REMARK 500 HYP B 64 140.69 -38.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5IXQ A 20 620 UNP P47735 RLK5_ARATH 20 620
DBREF 5IXQ B 58 69 UNP Q8LAD7 IDA_ARATH 58 69
SEQADV 5IXQ GLY A 15 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ SER A 16 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ SER A 17 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ MET A 18 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ GLY A 19 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ LEU A 621 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ GLU A 622 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ GLY A 623 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ SER A 624 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ GLU A 625 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ ASN A 626 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ LEU A 627 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ TYR A 628 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ PHE A 629 UNP P47735 EXPRESSION TAG
SEQADV 5IXQ 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 PRO ILE PRO PRO SER ALA HYP SER LYS ARG HIS ASN
MODRES 5IXQ HYP B 64 PRO MODIFIED RESIDUE
HET HYP B 64 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 MG A 714 1
HET MG A 715 1
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 MG MAGNESIUM ION
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 MG 2(MG 2+)
FORMUL 12 EDO C2 H6 O2
FORMUL 13 HOH *39(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 SER A 396 CYS A 402 5 7
HELIX 15 AB6 PRO A 420 LEU A 426 5 7
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 LEU A 498 5 7
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 SER A 167 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 ASN A 313 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 LEU A 431 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 ASP A 505 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 VAL A 574 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 4 VAL A 225 GLY A 226 0
SHEET 2 AA3 4 GLN A 247 GLY A 250 1 O THR A 249 N GLY A 226
SHEET 3 AA3 4 SER A 271 GLY A 274 1 O SER A 271 N LEU A 248
SHEET 4 AA3 4 LYS A 295 LEU A 296 1 O LYS A 295 N PHE A 272
SHEET 1 AA410 GLU A 320 GLY A 321 0
SHEET 2 AA410 ARG A 342 VAL A 346 1 O THR A 344 N GLY A 321
SHEET 3 AA410 ARG A 366 GLY A 369 1 O ARG A 366 N LEU A 343
SHEET 4 AA410 SER A 390 GLY A 393 1 O SER A 390 N PHE A 367
SHEET 5 AA410 LYS A 414 GLN A 418 1 O LYS A 414 N PHE A 391
SHEET 6 AA410 SER A 438 GLY A 441 1 O SER A 438 N LEU A 415
SHEET 7 AA410 ARG A 462 GLY A 465 1 O SER A 464 N GLY A 441
SHEET 8 AA410 ASP A 486 GLU A 490 1 O ASP A 486 N PHE A 463
SHEET 9 AA410 GLN A 510 GLY A 513 1 O GLN A 510 N PHE A 487
SHEET 10 AA410 HIS A 534 LEU A 535 1 O HIS A 534 N LEU A 511
SHEET 1 AA5 4 SER A 560 GLU A 562 0
SHEET 2 AA5 4 HIS A 581 LYS A 585 1 O SER A 583 N GLY A 561
SHEET 3 AA5 4 LEU A 605 LEU A 609 1 O CYS A 606 N GLY A 584
SHEET 4 AA5 4 LEU A 612 ARG A 614 -1 O ARG A 614 N VAL A 607
SSBOND 1 CYS A 54 CYS A 61 1555 1555 2.10
SSBOND 2 CYS A 86 CYS A 113 1555 1555 2.03
SSBOND 3 CYS A 376 CYS A 402 1555 1555 2.04
SSBOND 4 CYS A 606 CYS A 613 1555 1555 2.04
LINK ND2 ASN A 98 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 102 C1 NAG A 703 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG D 1 1555 1555 1.45
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 1.45
LINK ND2 ASN A 576 C1 NAG F 1 1555 1555 1.44
LINK C ALA B 63 N HYP B 64 1555 1555 1.33
LINK C HYP B 64 N SER B 65 1555 1555 1.35
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
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 1.45
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
CRYST1 148.282 148.282 57.930 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 0.006744 0.003894 0.000000 0.00000
SCALE2 0.000000 0.007787 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
