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Chemical substance (3) PDB-CCD (3) Gene (1) KEGG GENES (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) DNA sequence (1) EMBL (1) Protein domain (16) InterPro (10) PROSITE (6) All databases (25)
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HEADER CELL ADHESION 13-NOV-17 6EYJ
TITLE E-SELECTIN LECTIN, EGF-LIKE AND TWO SCR DOMAINS COMPLEXED WITH
TITLE 2 GLYCOMIMETIC LIGAND NV354
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E-SELECTIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CD62 ANTIGEN-LIKE FAMILY MEMBER E,ENDOTHELIAL LEUKOCYTE
COMPND 5 ADHESION MOLECULE 1,ELAM-1,LEUKOCYTE-ENDOTHELIAL CELL ADHESION
COMPND 6 MOLECULE 2,LECAM2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SELE, ELAM1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS CELL ADHESION, CELL-ADHESION MOLECULE, C-TYPE LECTIN, INFLAMMATION,
KEYWDS 2 LEUKOCYTE, GLYCOMIMETIC, CATCH-BOND
EXPDTA X-RAY DIFFRACTION
AUTHOR R.P.JAKOB,P.ZIHLMANN,R.C.PRESTON,N.VARGA,B.ERNST,T.MAIER
REVDAT 3 17-JAN-24 6EYJ 1 HETSYN
REVDAT 2 29-JUL-20 6EYJ 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 21-NOV-18 6EYJ 0
JRNL AUTH N.VARGA,P.ZIHLMANN,R.C.PRESTON,R.P.JAKOB,T.MAIER,B.ERNST
JRNL TITL E-SELECTIN LECTIN WITH DIFFERENT GLYCOMIMETIC LIGANDS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 33972
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1650
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.41
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2888
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2671
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2756
REMARK 3 BIN R VALUE (WORKING SET) : 0.2663
REMARK 3 BIN FREE R VALUE : 0.2837
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.57
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4358
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 284
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.48320
REMARK 3 B22 (A**2) : -3.90060
REMARK 3 B33 (A**2) : -8.58260
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.18620
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.370
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.286
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.216
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.280
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.216
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4792 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6564 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2172 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 134 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 680 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4792 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 682 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5302 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.89
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1 - A|52 }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2179 -52.8042 79.8190
REMARK 3 T TENSOR
REMARK 3 T11: -0.2593 T22: -0.0897
REMARK 3 T33: -0.1406 T12: 0.0761
REMARK 3 T13: -0.0380 T23: -0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 9.1645 L22: 3.4916
REMARK 3 L33: 3.9414 L12: -4.3259
REMARK 3 L13: -2.1315 L23: 1.1045
REMARK 3 S TENSOR
REMARK 3 S11: -0.2648 S12: -0.3476 S13: -0.2836
REMARK 3 S21: -0.1984 S22: 0.0732 S23: 0.1802
REMARK 3 S31: -0.2966 S32: -0.4181 S33: 0.1916
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|53 - A|115 }
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3631 -42.2551 87.3866
REMARK 3 T TENSOR
REMARK 3 T11: -0.0907 T22: 0.0370
REMARK 3 T33: 0.1080 T12: 0.1559
REMARK 3 T13: -0.0460 T23: -0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 3.7340 L22: 2.0432
REMARK 3 L33: 7.4436 L12: -1.3699
REMARK 3 L13: 0.5975 L23: 2.3472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: -0.3325 S13: 0.4730
REMARK 3 S21: -0.3386 S22: -0.1664 S23: 0.3194
REMARK 3 S31: -1.0634 S32: -0.2681 S33: 0.0938
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|116 - A|167 }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1857 -66.3442 76.9954
REMARK 3 T TENSOR
REMARK 3 T11: -0.3896 T22: -0.1036
REMARK 3 T33: 0.4012 T12: 0.0439
REMARK 3 T13: 0.0017 T23: 0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 7.7062 L22: 2.0239
REMARK 3 L33: 0.7059 L12: -5.4244
REMARK 3 L13: -0.1517 L23: 0.3677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0822 S12: -0.1297 S13: -0.2208
REMARK 3 S21: 0.1755 S22: -0.0123 S23: -0.0917
REMARK 3 S31: -0.0870 S32: 0.1928 S33: 0.0945
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|168 - A|218 }
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5237 -77.2349 78.4086
REMARK 3 T TENSOR
REMARK 3 T11: -0.4270 T22: -0.0207
REMARK 3 T33: 0.3398 T12: 0.0712
REMARK 3 T13: 0.0684 T23: 0.2303
REMARK 3 L TENSOR
REMARK 3 L11: 10.4039 L22: 0.0000
REMARK 3 L33: 0.4578 L12: -3.4975
REMARK 3 L13: 3.3771 L23: 1.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0509 S12: -0.1061 S13: -0.0595
REMARK 3 S21: 0.0269 S22: 0.0560 S23: 0.2876
REMARK 3 S31: 0.0267 S32: 0.3409 S33: -0.0051
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|219 - A|280 }
REMARK 3 ORIGIN FOR THE GROUP (A): 72.3941 -90.5511 77.0689
REMARK 3 T TENSOR
REMARK 3 T11: -0.3981 T22: -0.2842
REMARK 3 T33: 0.5096 T12: 0.0617
REMARK 3 T13: 0.0950 T23: 0.1812
REMARK 3 L TENSOR
REMARK 3 L11: 12.3672 L22: 8.4119
REMARK 3 L33: 3.8578 L12: -0.0867
REMARK 3 L13: 3.1553 L23: 2.9391
REMARK 3 S TENSOR
REMARK 3 S11: 0.2356 S12: -0.3439 S13: -1.2190
REMARK 3 S21: -0.0599 S22: 0.3805 S23: -1.6401
REMARK 3 S31: 0.3191 S32: -0.0139 S33: -0.6161
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|1 - B|52 }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2700 -51.2507 59.9256
REMARK 3 T TENSOR
REMARK 3 T11: -0.2167 T22: -0.2977
REMARK 3 T33: -0.1407 T12: -0.0383
REMARK 3 T13: -0.0304 T23: 0.1354
REMARK 3 L TENSOR
REMARK 3 L11: 9.3481 L22: 3.2186
REMARK 3 L33: 3.0856 L12: 2.8803
REMARK 3 L13: -2.0186 L23: -0.0666
REMARK 3 S TENSOR
REMARK 3 S11: 0.1425 S12: 0.0457 S13: 0.1607
REMARK 3 S21: 0.2919 S22: -0.1662 S23: -0.3496
REMARK 3 S31: -0.1304 S32: 0.0246 S33: 0.0237
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { B|53 - B|115 }
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5288 -40.0409 53.6483
REMARK 3 T TENSOR
REMARK 3 T11: -0.0374 T22: -0.2643
REMARK 3 T33: 0.0499 T12: -0.0259
REMARK 3 T13: 0.0797 T23: 0.1327
REMARK 3 L TENSOR
REMARK 3 L11: 4.0315 L22: 5.4054
REMARK 3 L33: 7.8467 L12: 0.9011
REMARK 3 L13: -1.1812 L23: -0.6674
REMARK 3 S TENSOR
REMARK 3 S11: 0.3841 S12: 0.2387 S13: 0.8302
REMARK 3 S21: 0.3484 S22: -0.1718 S23: 0.0308
REMARK 3 S31: -1.3003 S32: -0.2117 S33: -0.2122
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { B|116 - B|167 }
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1718 -65.1554 60.7764
REMARK 3 T TENSOR
REMARK 3 T11: -0.2830 T22: -0.2058
REMARK 3 T33: 0.4721 T12: -0.0588
REMARK 3 T13: -0.0221 T23: 0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 12.9702 L22: 1.2791
REMARK 3 L33: 0.3103 L12: 5.8571
REMARK 3 L13: 1.1830 L23: 0.2752
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -0.0347 S13: -0.6111
REMARK 3 S21: -0.0710 S22: 0.0873 S23: 0.1074
REMARK 3 S31: -0.0828 S32: -0.1798 S33: -0.1455
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { B|168 - B|218 }
REMARK 3 ORIGIN FOR THE GROUP (A): -46.5701 -75.5701 57.8292
REMARK 3 T TENSOR
REMARK 3 T11: -0.2997 T22: -0.1823
REMARK 3 T33: 0.4508 T12: -0.0584
REMARK 3 T13: 0.0216 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 5.2574 L22: 0.0000
REMARK 3 L33: 0.2084 L12: 1.2473
REMARK 3 L13: 1.7700 L23: 0.0489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: -0.4772 S13: -0.5143
REMARK 3 S21: -0.1403 S22: -0.2215 S23: -0.4642
REMARK 3 S31: 0.0070 S32: -0.1933 S33: 0.2098
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { B|219 - B|280 }
REMARK 3 ORIGIN FOR THE GROUP (A): -81.5180 -89.0114 56.4812
REMARK 3 T TENSOR
REMARK 3 T11: -0.1564 T22: -0.1971
REMARK 3 T33: 0.5098 T12: -0.0427
REMARK 3 T13: 0.0939 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 10.5731 L22: 9.0205
REMARK 3 L33: 4.6886 L12: 0.5220
REMARK 3 L13: 5.4958 L23: 0.1564
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: 0.1694 S13: -1.0967
REMARK 3 S21: 0.1337 S22: 0.1863 S23: 1.5164
REMARK 3 S31: 0.2475 S32: -0.2620 S33: -0.2451
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6EYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00003
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33972
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 56.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
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) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4C16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1 M MOPS PH 6.2, 11-14%
REMARK 280 PEG8000, AFTER MICROSEEDING, 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 35.52000
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
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 SG CYS B 234 SG CYS B 247 1.67
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 ILE A 29 -79.58 -96.22
REMARK 500 GLN A 30 106.42 73.46
REMARK 500 TYR A 48 -160.74 69.38
REMARK 500 LYS A 86 156.28 64.71
REMARK 500 SER A 128 19.35 57.43
REMARK 500 ASN A 139 -129.60 -158.62
REMARK 500 HIS A 167 23.68 83.73
REMARK 500 ASN A 244 -4.12 90.60
REMARK 500 ALA B 28 -100.24 -110.79
REMARK 500 ILE B 29 99.98 -22.84
REMARK 500 TYR B 48 -167.27 66.58
REMARK 500 LYS B 86 155.44 65.32
REMARK 500 SER B 128 16.56 58.36
REMARK 500 ASN B 139 -130.17 -158.10
REMARK 500 HIS B 167 21.47 83.11
REMARK 500 TYR B 181 129.43 -39.62
REMARK 500 ASN B 244 -5.64 91.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 309 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 80 OE1
REMARK 620 2 ASN A 82 OD1 68.4
REMARK 620 3 GLU A 88 OE1 136.8 79.4
REMARK 620 4 ASN A 105 OD1 67.6 131.0 149.5
REMARK 620 5 ASP A 106 O 129.3 153.7 74.9 74.6
REMARK 620 6 ASP A 106 OD1 72.1 93.8 82.4 92.5 77.1
REMARK 620 7 C5H A 308 OBB 67.2 70.6 128.0 73.4 131.4 139.4
REMARK 620 8 C5H A 308 OBD 128.9 114.2 90.0 79.1 72.0 149.2 66.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 309 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 80 OE1
REMARK 620 2 ASN B 82 OD1 72.6
REMARK 620 3 GLU B 88 OE1 140.2 81.1
REMARK 620 4 ASN B 105 OD1 67.3 138.0 139.5
REMARK 620 5 ASP B 106 O 127.6 143.8 64.7 74.8
REMARK 620 6 ASP B 106 OD1 73.4 90.9 77.7 89.4 71.3
REMARK 620 7 C5H B 308 OBB 69.8 74.8 131.2 80.1 137.0 143.1
REMARK 620 8 C5H B 308 OBD 134.2 118.4 84.6 83.3 71.7 143.0 71.1
REMARK 620 N 1 2 3 4 5 6 7
DBREF 6EYJ A 1 280 UNP P16581 LYAM2_HUMAN 22 301
DBREF 6EYJ B 1 280 UNP P16581 LYAM2_HUMAN 22 301
SEQRES 1 A 280 TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP
SEQRES 2 A 280 GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU
SEQRES 3 A 280 VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN
SEQRES 4 A 280 SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY
SEQRES 5 A 280 ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR
SEQRES 6 A 280 GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO
SEQRES 7 A 280 GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL
SEQRES 8 A 280 GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP
SEQRES 9 A 280 ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS
SEQRES 10 A 280 TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS
SEQRES 11 A 280 GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS
SEQRES 12 A 280 CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE
SEQRES 13 A 280 VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER
SEQRES 14 A 280 LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN
SEQRES 15 A 280 SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO
SEQRES 16 A 280 SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU
SEQRES 17 A 280 TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS
SEQRES 18 A 280 ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS
SEQRES 19 A 280 PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS
SEQRES 20 A 280 THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA
SEQRES 21 A 280 GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN
SEQRES 22 A 280 GLU LYS PRO THR CYS LYS ALA
SEQRES 1 B 280 TRP SER TYR ASN THR SER THR GLU ALA MET THR TYR ASP
SEQRES 2 B 280 GLU ALA SER ALA TYR CYS GLN GLN ARG TYR THR HIS LEU
SEQRES 3 B 280 VAL ALA ILE GLN ASN LYS GLU GLU ILE GLU TYR LEU ASN
SEQRES 4 B 280 SER ILE LEU SER TYR SER PRO SER TYR TYR TRP ILE GLY
SEQRES 5 B 280 ILE ARG LYS VAL ASN ASN VAL TRP VAL TRP VAL GLY THR
SEQRES 6 B 280 GLN LYS PRO LEU THR GLU GLU ALA LYS ASN TRP ALA PRO
SEQRES 7 B 280 GLY GLU PRO ASN ASN ARG GLN LYS ASP GLU ASP CYS VAL
SEQRES 8 B 280 GLU ILE TYR ILE LYS ARG GLU LYS ASP VAL GLY MET TRP
SEQRES 9 B 280 ASN ASP GLU ARG CYS SER LYS LYS LYS LEU ALA LEU CYS
SEQRES 10 B 280 TYR THR ALA ALA CYS THR ASN THR SER CYS SER GLY HIS
SEQRES 11 B 280 GLY GLU CYS VAL GLU THR ILE ASN ASN TYR THR CYS LYS
SEQRES 12 B 280 CYS ASP PRO GLY PHE SER GLY LEU LYS CYS GLU GLN ILE
SEQRES 13 B 280 VAL ASN CYS THR ALA LEU GLU SER PRO GLU HIS GLY SER
SEQRES 14 B 280 LEU VAL CYS SER HIS PRO LEU GLY ASN PHE SER TYR ASN
SEQRES 15 B 280 SER SER CYS SER ILE SER CYS ASP ARG GLY TYR LEU PRO
SEQRES 16 B 280 SER SER MET GLU THR MET GLN CYS MET SER SER GLY GLU
SEQRES 17 B 280 TRP SER ALA PRO ILE PRO ALA CYS ASN VAL VAL GLU CYS
SEQRES 18 B 280 ASP ALA VAL THR ASN PRO ALA ASN GLY PHE VAL GLU CYS
SEQRES 19 B 280 PHE GLN ASN PRO GLY SER PHE PRO TRP ASN THR THR CYS
SEQRES 20 B 280 THR PHE ASP CYS GLU GLU GLY PHE GLU LEU MET GLY ALA
SEQRES 21 B 280 GLN SER LEU GLN CYS THR SER SER GLY ASN TRP ASP ASN
SEQRES 22 B 280 GLU LYS PRO THR CYS LYS ALA
HET NAG A 301 14
HET NAG A 302 14
HET NAG A 303 14
HET NAG A 304 14
HET NAG A 305 14
HET NAG A 306 14
HET NAG A 307 14
HET C5H A 308 43
HET CA A 309 1
HET NAG B 301 14
HET NAG B 302 14
HET NAG B 303 14
HET NAG B 304 14
HET NAG B 305 14
HET NAG B 306 14
HET NAG B 307 14
HET C5H B 308 43
HET CA B 309 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM C5H (2~{S})-3-CYCLOHEXYL-2-[(2~{R},3~{S},4~{S},5~{R},
HETNAM 2 C5H 6~{R})-2-(HYDROXYMETHYL)-3,5-BIS(OXIDANYL)-6-[(1~{R},
HETNAM 3 C5H 2~{R})-2-[(2~{R},3~{S},4~{R},5~{S},6~{R})-3,4,5-
HETNAM 4 C5H TRIS(OXIDANYL)-6-(TRIFLUOROMETHYL)OXAN-2-
HETNAM 5 C5H YL]OXYCYCLOHEXYL]OXY-OXAN-4-YL]OXY-PROPANOIC ACID
HETNAM CA CALCIUM ION
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
FORMUL 3 NAG 14(C8 H15 N O6)
FORMUL 10 C5H 2(C27 H43 F3 O13)
FORMUL 11 CA 2(CA 2+)
FORMUL 21 HOH *252(H2 O)
HELIX 1 AA1 THR A 11 ARG A 22 1 12
HELIX 2 AA2 ASN A 31 LEU A 42 1 12
HELIX 3 AA3 THR B 11 ARG B 22 1 12
HELIX 4 AA4 ASN B 31 LEU B 42 1 12
SHEET 1 AA1 5 SER A 2 THR A 5 0
SHEET 2 AA1 5 LEU A 114 THR A 119 -1 O CYS A 117 N ASN A 4
SHEET 3 AA1 5 TYR A 49 VAL A 56 1 N TRP A 50 O LEU A 114
SHEET 4 AA1 5 VAL A 59 TRP A 62 -1 O VAL A 59 N VAL A 56
SHEET 5 AA1 5 LYS A 67 PRO A 68 -1 O LYS A 67 N TRP A 62
SHEET 1 AA2 5 HIS A 25 LEU A 26 0
SHEET 2 AA2 5 LEU A 114 THR A 119 -1 O TYR A 118 N HIS A 25
SHEET 3 AA2 5 TYR A 49 VAL A 56 1 N TRP A 50 O LEU A 114
SHEET 4 AA2 5 CYS A 90 ILE A 93 -1 O ILE A 93 N TYR A 49
SHEET 5 AA2 5 TRP A 104 GLU A 107 -1 O GLU A 107 N CYS A 90
SHEET 1 AA3 2 GLY A 131 GLU A 135 0
SHEET 2 AA3 2 TYR A 140 CYS A 144 -1 O THR A 141 N VAL A 134
SHEET 1 AA4 2 PHE A 148 SER A 149 0
SHEET 2 AA4 2 GLN A 155 ILE A 156 -1 O GLN A 155 N SER A 149
SHEET 1 AA5 3 GLY A 168 SER A 173 0
SHEET 2 AA5 3 SER A 184 CYS A 189 -1 O SER A 184 N SER A 173
SHEET 3 AA5 3 MET A 201 GLN A 202 -1 O MET A 201 N CYS A 185
SHEET 1 AA6 2 TYR A 193 PRO A 195 0
SHEET 2 AA6 2 CYS A 216 VAL A 218 -1 O ASN A 217 N LEU A 194
SHEET 1 AA7 3 GLY A 230 GLU A 233 0
SHEET 2 AA7 3 THR A 246 CYS A 251 -1 O THR A 248 N GLU A 233
SHEET 3 AA7 3 SER A 262 GLN A 264 -1 O LEU A 263 N CYS A 247
SHEET 1 AA8 2 GLU A 256 MET A 258 0
SHEET 2 AA8 2 THR A 277 LYS A 279 -1 O THR A 277 N MET A 258
SHEET 1 AA9 4 SER B 2 THR B 5 0
SHEET 2 AA9 4 LEU B 114 THR B 119 -1 O CYS B 117 N ASN B 4
SHEET 3 AA9 4 TYR B 49 VAL B 56 1 N TRP B 50 O LEU B 114
SHEET 4 AA9 4 VAL B 59 TRP B 62 -1 O VAL B 59 N VAL B 56
SHEET 1 AB1 5 HIS B 25 LEU B 26 0
SHEET 2 AB1 5 LEU B 114 THR B 119 -1 O TYR B 118 N HIS B 25
SHEET 3 AB1 5 TYR B 49 VAL B 56 1 N TRP B 50 O LEU B 114
SHEET 4 AB1 5 CYS B 90 ILE B 93 -1 O ILE B 93 N TYR B 49
SHEET 5 AB1 5 TRP B 104 GLU B 107 -1 O GLU B 107 N CYS B 90
SHEET 1 AB2 2 GLY B 131 GLU B 135 0
SHEET 2 AB2 2 TYR B 140 CYS B 144 -1 O THR B 141 N VAL B 134
SHEET 1 AB3 2 PHE B 148 SER B 149 0
SHEET 2 AB3 2 GLN B 155 ILE B 156 -1 O GLN B 155 N SER B 149
SHEET 1 AB4 3 GLY B 168 SER B 173 0
SHEET 2 AB4 3 SER B 184 CYS B 189 -1 O SER B 184 N SER B 173
SHEET 3 AB4 3 MET B 201 GLN B 202 -1 O MET B 201 N CYS B 185
SHEET 1 AB5 2 TYR B 193 PRO B 195 0
SHEET 2 AB5 2 CYS B 216 VAL B 218 -1 O ASN B 217 N LEU B 194
SHEET 1 AB6 3 GLY B 230 GLU B 233 0
SHEET 2 AB6 3 THR B 246 CYS B 251 -1 O THR B 248 N GLU B 233
SHEET 3 AB6 3 SER B 262 GLN B 264 -1 O LEU B 263 N CYS B 247
SHEET 1 AB7 2 GLU B 256 MET B 258 0
SHEET 2 AB7 2 THR B 277 LYS B 279 -1 O THR B 277 N MET B 258
SSBOND 1 CYS A 19 CYS A 117 1555 1555 2.05
SSBOND 2 CYS A 90 CYS A 109 1555 1555 2.04
SSBOND 3 CYS A 122 CYS A 133 1555 1555 2.05
SSBOND 4 CYS A 127 CYS A 142 1555 1555 2.04
SSBOND 5 CYS A 144 CYS A 153 1555 1555 2.05
SSBOND 6 CYS A 159 CYS A 203 1555 1555 2.03
SSBOND 7 CYS A 172 CYS A 185 1555 1555 2.05
SSBOND 8 CYS A 189 CYS A 216 1555 1555 2.05
SSBOND 9 CYS A 221 CYS A 265 1555 1555 2.03
SSBOND 10 CYS A 234 CYS A 247 1555 1555 2.04
SSBOND 11 CYS A 251 CYS A 278 1555 1555 2.04
SSBOND 12 CYS B 19 CYS B 117 1555 1555 2.04
SSBOND 13 CYS B 90 CYS B 109 1555 1555 2.04
SSBOND 14 CYS B 122 CYS B 133 1555 1555 2.04
SSBOND 15 CYS B 127 CYS B 142 1555 1555 2.04
SSBOND 16 CYS B 144 CYS B 153 1555 1555 2.06
SSBOND 17 CYS B 159 CYS B 203 1555 1555 2.03
SSBOND 18 CYS B 172 CYS B 185 1555 1555 2.05
SSBOND 19 CYS B 189 CYS B 216 1555 1555 2.04
SSBOND 20 CYS B 221 CYS B 265 1555 1555 2.01
SSBOND 21 CYS B 251 CYS B 278 1555 1555 2.04
LINK ND2 ASN A 4 C1 NAG A 305 1555 1555 1.43
LINK ND2 ASN A 124 C1 NAG A 306 1555 1555 1.43
LINK ND2 ASN A 139 C1 NAG A 302 1555 1555 1.43
LINK ND2 ASN A 158 C1 NAG A 303 1555 1555 1.44
LINK ND2 ASN A 178 C1 NAG A 304 1555 1555 1.43
LINK ND2 ASN A 182 C1 NAG A 301 1555 1555 1.43
LINK ND2 ASN A 244 C1 NAG A 307 1555 1555 1.43
LINK ND2 ASN B 4 C1 NAG B 305 1555 1555 1.44
LINK ND2 ASN B 124 C1 NAG B 306 1555 1555 1.43
LINK ND2 ASN B 139 C1 NAG B 302 1555 1555 1.43
LINK ND2 ASN B 158 C1 NAG B 303 1555 1555 1.43
LINK ND2 ASN B 178 C1 NAG B 304 1555 1555 1.44
LINK ND2 ASN B 182 C1 NAG B 301 1555 1555 1.43
LINK ND2 ASN B 244 C1 NAG B 307 1555 1555 1.43
LINK OE1 GLU A 80 CA CA A 309 1555 1555 2.79
LINK OD1 ASN A 82 CA CA A 309 1555 1555 2.60
LINK OE1 GLU A 88 CA CA A 309 1555 1555 2.38
LINK OD1 ASN A 105 CA CA A 309 1555 1555 2.59
LINK O ASP A 106 CA CA A 309 1555 1555 2.53
LINK OD1 ASP A 106 CA CA A 309 1555 1555 2.25
LINK OBB C5H A 308 CA CA A 309 1555 1555 2.63
LINK OBD C5H A 308 CA CA A 309 1555 1555 2.28
LINK OE1 GLU B 80 CA CA B 309 1555 1555 2.67
LINK OD1 ASN B 82 CA CA B 309 1555 1555 2.56
LINK OE1 GLU B 88 CA CA B 309 1555 1555 2.41
LINK OD1 ASN B 105 CA CA B 309 1555 1555 2.54
LINK O ASP B 106 CA CA B 309 1555 1555 2.64
LINK OD1 ASP B 106 CA CA B 309 1555 1555 2.43
LINK OBB C5H B 308 CA CA B 309 1555 1555 2.43
LINK OBD C5H B 308 CA CA B 309 1555 1555 2.21
CISPEP 1 GLU A 80 PRO A 81 0 -5.92
CISPEP 2 GLU B 80 PRO B 81 0 -3.19
CRYST1 52.580 71.040 92.160 90.00 93.73 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 0.019019 0.000000 0.001240 0.00000
SCALE2 0.000000 0.014077 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010874 0.00000
(ATOM LINES ARE NOT SHOWN.)
END