HEADER ISOMERASE/ISOMERASE INHIBITOR 27-JUN-11 3SMC
TITLE MACROPHAGE MIGRATION INHIBITORY FACTOR (MIF) WITH COVALENTLY BOUND L-
TITLE 2 SULFORAPHANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE MIGRATION INHIBITORY FACTOR;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: MIF, GLYCOSYLATION-INHIBITING FACTOR, GIF, L-DOPACHROME
COMPND 5 ISOMERASE, L-DOPACHROME TAUTOMERASE, PHENYLPYRUVATE TAUTOMERASE;
COMPND 6 EC: 5.3.2.1, 5.3.3.12;
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: GLIF, MIF, MMIF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS CYTOKINE, RECEPTOR BINDING, SECRETED, ISOMERASE-ISOMERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.V.CRICHLOW,E.J.LOLIS
REVDAT 3 13-SEP-23 3SMC 1 REMARK LINK
REVDAT 2 20-FEB-13 3SMC 1 JRNL
REVDAT 1 03-OCT-12 3SMC 0
JRNL AUTH G.V.CRICHLOW,C.FAN,C.KEELER,M.HODSDON,E.J.LOLIS
JRNL TITL STRUCTURAL INTERACTIONS DICTATE THE KINETICS OF MACROPHAGE
JRNL TITL 2 MIGRATION INHIBITORY FACTOR INHIBITION BY DIFFERENT
JRNL TITL 3 CANCER-PREVENTIVE ISOTHIOCYANATES.
JRNL REF BIOCHEMISTRY V. 51 7506 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22931430
JRNL DOI 10.1021/BI3005494
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 110.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 50929
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 SET) : 0.172
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1051
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 184
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2586
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 446
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57200
REMARK 3 B22 (A**2) : -0.57200
REMARK 3 B33 (A**2) : 1.14400
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC, RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 54.41
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : SFN.PAR
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51163
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 110.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB EBTRY 3DJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 3% ISOPROPANOL,
REMARK 280 0.1 M TRIS(HYDROXYMETHYL)AMINOMETHANE; MIXED WITH PROTEIN:
REMARK 280 INHIBITOR COMPLEX IN A 1:1 RATIO, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 34.50533
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 69.01067
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 69.01067
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 34.50533
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 ARG A 88 NE CZ NH1 NH2
REMARK 470 ARG B 88 NE CZ NH1 NH2
REMARK 470 GLN C 28 CD OE1 NE2
REMARK 470 ARG C 88 NE CZ NH1 NH2
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 TRP A 108 142.72 -173.96
REMARK 500 SER A 111 -155.96 -152.78
REMARK 500 SER B 111 -159.06 -154.77
REMARK 500 ASN C 109 67.44 36.00
REMARK 500 SER C 111 -160.63 -165.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE STARTING MATERIAL IS L-SULFORAPHANE. IT BINDS COVALENTLY TO PRO
REMARK 600 1. LE3 CORRESPONDS TO THE FINAL PRODUCT.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 LE3 C 200
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 NA A 802 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 100 O
REMARK 620 2 HOH A 238 O 91.8
REMARK 620 3 HOH A 390 O 80.6 94.8
REMARK 620 4 HOH A 549 O 171.8 89.7 91.2
REMARK 620 5 HOH A 576 O 97.0 80.3 174.5 91.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 804 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 288 O
REMARK 620 2 HOH A 345 O 85.6
REMARK 620 3 HOH B 280 O 82.1 167.2
REMARK 620 4 HOH B 349 O 93.8 100.9 83.6
REMARK 620 5 HOH C 313 O 83.1 89.8 85.1 168.6
REMARK 620 6 HOH C 372 O 165.7 100.3 90.8 97.8 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 803 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 100 O
REMARK 620 2 HOH B 262 O 91.2
REMARK 620 3 HOH B 453 O 79.3 82.6
REMARK 620 4 HOH B 504 O 90.2 87.9 165.7
REMARK 620 5 HOH C 458 O 169.5 80.8 92.9 96.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 801 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 100 O
REMARK 620 2 HOH C 353 O 95.6
REMARK 620 3 HOH C 409 O 82.8 88.9
REMARK 620 4 HOH C 432 O 170.5 81.8 88.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LE3 A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LE3 B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LE3 C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SMB RELATED DB: PDB
REMARK 900 MIF COVALENTLY BOUND TO THE ISOTHIOCYANATE PEITC
DBREF 3SMC A 1 114 UNP P14174 MIF_HUMAN 2 115
DBREF 3SMC B 1 114 UNP P14174 MIF_HUMAN 2 115
DBREF 3SMC C 1 114 UNP P14174 MIF_HUMAN 2 115
SEQRES 1 A 114 PRO MET PHE ILE VAL ASN THR ASN VAL PRO ARG ALA SER
SEQRES 2 A 114 VAL PRO ASP GLY PHE LEU SER GLU LEU THR GLN GLN LEU
SEQRES 3 A 114 ALA GLN ALA THR GLY LYS PRO PRO GLN TYR ILE ALA VAL
SEQRES 4 A 114 HIS VAL VAL PRO ASP GLN LEU MET ALA PHE GLY GLY SER
SEQRES 5 A 114 SER GLU PRO CYS ALA LEU CYS SER LEU HIS SER ILE GLY
SEQRES 6 A 114 LYS ILE GLY GLY ALA GLN ASN ARG SER TYR SER LYS LEU
SEQRES 7 A 114 LEU CYS GLY LEU LEU ALA GLU ARG LEU ARG ILE SER PRO
SEQRES 8 A 114 ASP ARG VAL TYR ILE ASN TYR TYR ASP MET ASN ALA ALA
SEQRES 9 A 114 ASN VAL GLY TRP ASN ASN SER THR PHE ALA
SEQRES 1 B 114 PRO MET PHE ILE VAL ASN THR ASN VAL PRO ARG ALA SER
SEQRES 2 B 114 VAL PRO ASP GLY PHE LEU SER GLU LEU THR GLN GLN LEU
SEQRES 3 B 114 ALA GLN ALA THR GLY LYS PRO PRO GLN TYR ILE ALA VAL
SEQRES 4 B 114 HIS VAL VAL PRO ASP GLN LEU MET ALA PHE GLY GLY SER
SEQRES 5 B 114 SER GLU PRO CYS ALA LEU CYS SER LEU HIS SER ILE GLY
SEQRES 6 B 114 LYS ILE GLY GLY ALA GLN ASN ARG SER TYR SER LYS LEU
SEQRES 7 B 114 LEU CYS GLY LEU LEU ALA GLU ARG LEU ARG ILE SER PRO
SEQRES 8 B 114 ASP ARG VAL TYR ILE ASN TYR TYR ASP MET ASN ALA ALA
SEQRES 9 B 114 ASN VAL GLY TRP ASN ASN SER THR PHE ALA
SEQRES 1 C 114 PRO MET PHE ILE VAL ASN THR ASN VAL PRO ARG ALA SER
SEQRES 2 C 114 VAL PRO ASP GLY PHE LEU SER GLU LEU THR GLN GLN LEU
SEQRES 3 C 114 ALA GLN ALA THR GLY LYS PRO PRO GLN TYR ILE ALA VAL
SEQRES 4 C 114 HIS VAL VAL PRO ASP GLN LEU MET ALA PHE GLY GLY SER
SEQRES 5 C 114 SER GLU PRO CYS ALA LEU CYS SER LEU HIS SER ILE GLY
SEQRES 6 C 114 LYS ILE GLY GLY ALA GLN ASN ARG SER TYR SER LYS LEU
SEQRES 7 C 114 LEU CYS GLY LEU LEU ALA GLU ARG LEU ARG ILE SER PRO
SEQRES 8 C 114 ASP ARG VAL TYR ILE ASN TYR TYR ASP MET ASN ALA ALA
SEQRES 9 C 114 ASN VAL GLY TRP ASN ASN SER THR PHE ALA
HET LE3 A 200 10
HET CL A 702 1
HET CL A 704 1
HET CL A 707 1
HET NA A 802 1
HET NA A 804 1
HET SO4 A 901 5
HET LE3 B 200 10
HET CL B 701 1
HET CL B 706 1
HET NA B 803 1
HET LE3 C 200 7
HET CL C 703 1
HET CL C 705 1
HET NA C 801 1
HETNAM LE3 N-{4-[(R)-METHYLSULFINYL]BUTYL}THIOFORMAMIDE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM SO4 SULFATE ION
HETSYN LE3 L-SULFORAPHANE, BOUND FORM
FORMUL 4 LE3 3(C6 H13 N O S2)
FORMUL 5 CL 7(CL 1-)
FORMUL 8 NA 4(NA 1+)
FORMUL 10 SO4 O4 S 2-
FORMUL 19 HOH *446(H2 O)
HELIX 1 1 PRO A 10 VAL A 14 5 5
HELIX 2 2 GLY A 17 GLY A 31 1 15
HELIX 3 3 PRO A 33 TYR A 36 5 4
HELIX 4 4 GLY A 68 ARG A 88 1 21
HELIX 5 5 SER A 90 ASP A 92 5 3
HELIX 6 6 ASN A 102 ALA A 104 5 3
HELIX 7 7 PRO B 10 VAL B 14 5 5
HELIX 8 8 GLY B 17 GLY B 31 1 15
HELIX 9 9 PRO B 33 TYR B 36 5 4
HELIX 10 10 GLY B 68 ARG B 88 1 21
HELIX 11 11 SER B 90 ASP B 92 5 3
HELIX 12 12 ASN B 102 ALA B 104 5 3
HELIX 13 13 PRO C 10 VAL C 14 5 5
HELIX 14 14 GLY C 17 GLY C 31 1 15
HELIX 15 15 PRO C 33 TYR C 36 5 4
HELIX 16 16 GLY C 68 ARG C 88 1 21
HELIX 17 17 SER C 90 ASP C 92 5 3
HELIX 18 18 ASN C 102 ALA C 104 5 3
SHEET 1 A 7 SER B 111 THR B 112 0
SHEET 2 A 7 VAL B 106 TRP B 108 -1 N TRP B 108 O SER B 111
SHEET 3 A 7 VAL A 94 ASP A 100 -1 N ILE A 96 O GLY B 107
SHEET 4 A 7 ALA A 57 SER A 63 1 N CYS A 59 O TYR A 95
SHEET 5 A 7 MET A 2 THR A 7 -1 N MET A 2 O HIS A 62
SHEET 6 A 7 ALA A 38 VAL A 42 1 O VAL A 42 N VAL A 5
SHEET 7 A 7 LEU C 46 PHE C 49 -1 O ALA C 48 N VAL A 39
SHEET 1 B 7 LEU A 46 PHE A 49 0
SHEET 2 B 7 ALA B 38 VAL B 42 -1 O VAL B 41 N LEU A 46
SHEET 3 B 7 MET B 2 THR B 7 1 N VAL B 5 O VAL B 42
SHEET 4 B 7 ALA B 57 SER B 63 -1 O HIS B 62 N MET B 2
SHEET 5 B 7 VAL B 94 ASP B 100 1 O TYR B 95 N CYS B 59
SHEET 6 B 7 VAL C 106 TRP C 108 -1 O GLY C 107 N ILE B 96
SHEET 7 B 7 SER C 111 THR C 112 -1 O SER C 111 N TRP C 108
SHEET 1 C 7 SER A 111 THR A 112 0
SHEET 2 C 7 VAL A 106 TRP A 108 -1 N TRP A 108 O SER A 111
SHEET 3 C 7 VAL C 94 ASP C 100 -1 O ILE C 96 N GLY A 107
SHEET 4 C 7 ALA C 57 SER C 63 1 N CYS C 59 O TYR C 95
SHEET 5 C 7 MET C 2 THR C 7 -1 N MET C 2 O HIS C 62
SHEET 6 C 7 ALA C 38 VAL C 42 1 O VAL C 42 N VAL C 5
SHEET 7 C 7 LEU B 46 PHE B 49 -1 N ALA B 48 O VAL C 39
LINK N PRO A 1 C LE3 A 200 1555 1555 1.34
LINK N PRO B 1 C LE3 B 200 1555 1555 1.34
LINK N PRO C 1 C LE3 C 200 1555 1555 1.34
LINK O ASP A 100 NA NA A 802 1555 1555 2.61
LINK O HOH A 238 NA NA A 802 1555 1555 2.49
LINK O HOH A 288 NA NA A 804 1555 1555 2.49
LINK O HOH A 345 NA NA A 804 1555 1555 2.56
LINK O HOH A 390 NA NA A 802 1555 1555 2.12
LINK O HOH A 549 NA NA A 802 1555 1555 2.95
LINK O HOH A 576 NA NA A 802 1555 1555 2.35
LINK NA NA A 804 O HOH B 280 1555 1555 2.59
LINK NA NA A 804 O HOH B 349 1555 1555 2.53
LINK NA NA A 804 O HOH C 313 1555 1555 2.51
LINK NA NA A 804 O HOH C 372 1555 1555 2.52
LINK O ASP B 100 NA NA B 803 1555 1555 2.66
LINK O HOH B 262 NA NA B 803 1555 1555 2.46
LINK O HOH B 453 NA NA B 803 1555 1555 2.47
LINK O HOH B 504 NA NA B 803 1555 1555 2.49
LINK NA NA B 803 O HOH C 458 1555 1555 3.13
LINK O ASP C 100 NA NA C 801 1555 1555 2.57
LINK O HOH C 353 NA NA C 801 1555 1555 2.47
LINK O HOH C 409 NA NA C 801 1555 1555 2.46
LINK O HOH C 432 NA NA C 801 1555 1555 3.04
SITE 1 AC1 9 PRO A 1 MET A 2 LYS A 32 TYR A 36
SITE 2 AC1 9 ILE A 64 ASP A 92 PHE A 113 HOH A 366
SITE 3 AC1 9 TYR C 95
SITE 1 AC2 3 ASN A 102 ASN A 105 HOH C 264
SITE 1 AC3 3 GLN A 24 HOH A 431 HOH B 258
SITE 1 AC4 4 GLY A 68 GLY A 69 ALA A 70 GLN A 71
SITE 1 AC5 5 ASP A 100 HOH A 238 HOH A 390 HOH A 549
SITE 2 AC5 5 HOH A 576
SITE 1 AC6 6 HOH A 288 HOH A 345 HOH B 280 HOH B 349
SITE 2 AC6 6 HOH C 313 HOH C 372
SITE 1 AC7 7 PRO A 15 ASP A 16 HOH A 568 HOH A 599
SITE 2 AC7 7 ARG B 73 HOH C 263 HOH C 616
SITE 1 AC8 9 TYR A 95 ASN A 109 PRO B 1 MET B 2
SITE 2 AC8 9 TYR B 36 ILE B 64 PHE B 113 HOH B 463
SITE 3 AC8 9 HOH B 500
SITE 1 AC9 3 HOH A 221 ASN B 102 ASN B 105
SITE 1 BC1 3 GLY B 68 ALA B 70 GLN B 71
SITE 1 BC2 4 ASP B 100 HOH B 262 HOH B 453 HOH B 504
SITE 1 BC3 7 TYR B 95 PRO C 1 MET C 2 TYR C 36
SITE 2 BC3 7 PHE C 113 HOH C 376 HOH C 612
SITE 1 BC4 3 HOH B 268 ASN C 102 ASN C 105
SITE 1 BC5 4 GLY C 68 ALA C 70 GLN C 71 HOH C 613
SITE 1 BC6 4 ASP C 100 HOH C 353 HOH C 409 HOH C 432
CRYST1 95.638 95.638 103.516 90.00 90.00 120.00 P 31 2 1 18
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 0.010456 0.006037 0.000000 0.00000
SCALE2 0.000000 0.012074 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009660 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
