HEADER TRANSPORT PROTEIN 31-MAR-17 5NKN
TITLE CRYSTAL STRUCTURE OF AN ANTICALIN-COLCHICINE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NGAL,25 KDA ALPHA-2-MICROGLOBULIN-RELATED SUBUNIT OF MMP-9,
COMPND 5 LIPOCALIN-2,ONCOGENE 24P3,SIDEROCALIN LCN2,P25;
COMPND 6 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: LCN2, HNL, NGAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-BARREL, COLCHICINE, LCN2, LIPOCALIN, NGAL, PROTEIN ENGINEERING,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SKERRA,A.EICHINGER,M.BARKOVSKIY
REVDAT 4 17-JAN-24 5NKN 1 REMARK
REVDAT 3 20-FEB-19 5NKN 1 JRNL
REVDAT 2 19-DEC-18 5NKN 1 JRNL
REVDAT 1 04-APR-18 5NKN 0
JRNL AUTH M.BARKOVSKIY,E.ILYUKHINA,M.DAUNER,A.EICHINGER,A.SKERRA
JRNL TITL AN ENGINEERED LIPOCALIN THAT TIGHTLY COMPLEXES THE PLANT
JRNL TITL 2 POISON COLCHICINE FOR USE AS ANTIDOTE AND IN BIOANALYTICAL
JRNL TITL 3 APPLICATIONS.
JRNL REF BIOL. CHEM. V. 400 351 2019
JRNL REFN ISSN 1437-4315
JRNL PMID 30517073
JRNL DOI 10.1515/HSZ-2018-0342
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) : 46.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 7858
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 420
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) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 554
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 21
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1394
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : 0.39000
REMARK 3 B33 (A**2) : -0.79000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.376
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.257
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.195
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.490
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1464 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1378 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1986 ; 1.634 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3179 ; 0.974 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 171 ; 7.402 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 69 ;36.505 ;24.928
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 247 ;16.356 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;18.510 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 208 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1654 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 347 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 5 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8430 12.7490 -13.1330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0585 T22: 0.0348
REMARK 3 T33: 0.2815 T12: 0.0177
REMARK 3 T13: 0.0150 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 2.2299 L22: 1.6113
REMARK 3 L33: 2.7168 L12: 0.6316
REMARK 3 L13: -2.1459 L23: 0.2487
REMARK 3 S TENSOR
REMARK 3 S11: 0.2693 S12: 0.0726 S13: -0.1340
REMARK 3 S21: -0.0468 S22: -0.1483 S23: -0.1237
REMARK 3 S31: -0.3571 S32: -0.1238 S33: -0.1211
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
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 U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 5NKN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.89429
REMARK 200 MONOCHROMATOR : SI - 111 CRYSTAL
REMARK 200 OPTICS : COATED SI MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8323
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.811
REMARK 200 RESOLUTION RANGE LOW (A) : 46.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
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) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : 0.41000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 3DTQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M (NH4)2SO4, 200 MM LI2SO4, 100 MM
REMARK 280 TRIS/HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.42500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.21250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 102.63750
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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.42500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 102.63750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 34.21250
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 ASP A 177
REMARK 465 GLY A 178
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 ASP A 61 5.96 -69.15
REMARK 500 PRO A 72 32.51 -94.48
REMARK 500 TYR A 115 -44.29 70.33
REMARK 500 GLN A 117 -66.78 -137.22
REMARK 500 ASN A 129 50.53 -107.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LOC A 201
DBREF 5NKN A 5 178 UNP P80188 NGAL_HUMAN 25 198
SEQADV 5NKN HIS A 28 UNP P80188 GLN 48 ENGINEERED MUTATION
SEQADV 5NKN VAL A 36 UNP P80188 LEU 56 ENGINEERED MUTATION
SEQADV 5NKN GLY A 40 UNP P80188 ALA 60 ENGINEERED MUTATION
SEQADV 5NKN PHE A 41 UNP P80188 ILE 61 ENGINEERED MUTATION
SEQADV 5NKN ILE A 49 UNP P80188 GLN 69 ENGINEERED MUTATION
SEQADV 5NKN ALA A 52 UNP P80188 TYR 72 ENGINEERED MUTATION
SEQADV 5NKN PHE A 68 UNP P80188 SER 88 ENGINEERED MUTATION
SEQADV 5NKN GLN A 69 UNP P80188 VAL 89 ENGINEERED MUTATION
SEQADV 5NKN LYS A 70 UNP P80188 LEU 90 ENGINEERED MUTATION
SEQADV 5NKN PRO A 72 UNP P80188 ARG 92 ENGINEERED MUTATION
SEQADV 5NKN MET A 73 UNP P80188 LYS 93 ENGINEERED MUTATION
SEQADV 5NKN GLN A 77 UNP P80188 ASP 97 ENGINEERED MUTATION
SEQADV 5NKN MET A 79 UNP P80188 TRP 99 ENGINEERED MUTATION
SEQADV 5NKN THR A 80 UNP P80188 ILE 100 ENGINEERED MUTATION
SEQADV 5NKN ASP A 81 UNP P80188 ARG 101 ENGINEERED MUTATION
SEQADV 5NKN LEU A 83 UNP P80188 PHE 103 ENGINEERED MUTATION
SEQADV 5NKN SER A 87 UNP P80188 CYS 107 ENGINEERED MUTATION
SEQADV 5NKN GLU A 100 UNP P80188 TYR 120 ENGINEERED MUTATION
SEQADV 5NKN TYR A 103 UNP P80188 LEU 123 ENGINEERED MUTATION
SEQADV 5NKN TRP A 106 UNP P80188 TYR 126 ENGINEERED MUTATION
SEQADV 5NKN ALA A 125 UNP P80188 LYS 145 ENGINEERED MUTATION
SEQADV 5NKN GLN A 127 UNP P80188 SER 147 ENGINEERED MUTATION
SEQADV 5NKN ASP A 132 UNP P80188 TYR 152 ENGINEERED MUTATION
SEQADV 5NKN PHE A 134 UNP P80188 LYS 154 ENGINEERED MUTATION
SEQRES 1 A 174 SER ASP LEU ILE PRO ALA PRO PRO LEU SER LYS VAL PRO
SEQRES 2 A 174 LEU GLN GLN ASN PHE GLN ASP ASN GLN PHE HIS GLY LYS
SEQRES 3 A 174 TRP TYR VAL VAL GLY VAL ALA GLY ASN GLY PHE LEU ARG
SEQRES 4 A 174 GLU ASP LYS ASP PRO ILE LYS MET ALA ALA THR ILE TYR
SEQRES 5 A 174 GLU LEU LYS GLU ASP LYS SER TYR ASN VAL THR PHE GLN
SEQRES 6 A 174 LYS PHE PRO MET LYS LYS CYS GLN TYR MET THR ASP THR
SEQRES 7 A 174 LEU VAL PRO GLY SER GLN PRO GLY GLU PHE THR LEU GLY
SEQRES 8 A 174 ASN ILE LYS SER GLU PRO GLY TYR THR SER TRP LEU VAL
SEQRES 9 A 174 ARG VAL VAL SER THR ASN TYR ASN GLN HIS ALA MET VAL
SEQRES 10 A 174 PHE PHE LYS ALA VAL GLN GLN ASN ARG GLU ASP PHE PHE
SEQRES 11 A 174 ILE THR LEU TYR GLY ARG THR LYS GLU LEU THR SER GLU
SEQRES 12 A 174 LEU LYS GLU ASN PHE ILE ARG PHE SER LYS SER LEU GLY
SEQRES 13 A 174 LEU PRO GLU ASN HIS ILE VAL PHE PRO VAL PRO ILE ASP
SEQRES 14 A 174 GLN CYS ILE ASP GLY
HET LOC A 201 29
HETNAM LOC N-[(7S)-1,2,3,10-TETRAMETHOXY-9-OXO-6,7-DIHYDRO-5H-
HETNAM 2 LOC BENZO[D]HEPTALEN-7-YL]ETHANAMIDE
HETSYN LOC COLCHICINE
FORMUL 2 LOC C22 H25 N O6
FORMUL 3 HOH *36(H2 O)
HELIX 1 AA1 PRO A 12 VAL A 16 5 5
HELIX 2 AA2 GLN A 23 HIS A 28 1 6
HELIX 3 AA3 THR A 145 LEU A 159 1 15
HELIX 4 AA4 PRO A 162 ASN A 164 5 3
SHEET 1 AA110 ILE A 166 VAL A 167 0
SHEET 2 AA110 GLY A 29 GLY A 38 -1 N VAL A 36 O VAL A 167
SHEET 3 AA110 PHE A 133 GLY A 139 -1 O LEU A 137 N GLY A 35
SHEET 4 AA110 HIS A 118 ALA A 125 -1 N ALA A 119 O TYR A 138
SHEET 5 AA110 TRP A 106 THR A 113 -1 N LEU A 107 O LYS A 124
SHEET 6 AA110 GLU A 91 GLY A 95 -1 N PHE A 92 O VAL A 108
SHEET 7 AA110 TYR A 78 PRO A 85 -1 N VAL A 84 O THR A 93
SHEET 8 AA110 TYR A 64 GLN A 69 -1 N PHE A 68 O MET A 79
SHEET 9 AA110 THR A 54 LEU A 58 -1 N GLU A 57 O ASN A 65
SHEET 10 AA110 GLY A 29 GLY A 38 -1 N GLY A 29 O TYR A 56
SHEET 1 AA2 2 LYS A 50 ALA A 52 0
SHEET 2 AA2 2 VAL A 170 ILE A 172 1 O ILE A 172 N MET A 51
SSBOND 1 CYS A 76 CYS A 175 1555 1555 2.06
CISPEP 1 PHE A 71 PRO A 72 0 2.20
SITE 1 AC1 11 PHE A 41 VAL A 66 PHE A 68 GLN A 69
SITE 2 AC1 11 LYS A 70 PHE A 71 TRP A 106 PHE A 134
SITE 3 AC1 11 THR A 136 HOH A 301 HOH A 314
CRYST1 46.680 46.680 136.850 90.00 90.00 90.00 P 41 2 2 8
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 0.021423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021423 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007307 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
