HEADER LYASE 14-JUL-15 5CJF
TITLE THE CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE XIV IN COMPLEX
TITLE 2 WITH A 1,1'-BIPHENYL-4-SULFONAMIDE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 14;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 16-290;
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE XIV,CARBONIC ANHYDRASE XIV,CA-XIV;
COMPND 6 EC: 4.2.1.1;
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: CA14, UNQ690/PRO1335;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS 1, 1'-BIPHENYL-4-SULFONAMIDE, LYASE, GLYCOPROTEIN, ZINC-BINDING,
KEYWDS 2 COMPLEX, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR V.ALTERIO,G.DE SIMONE
REVDAT 5 10-JAN-24 5CJF 1 HETSYN LINK
REVDAT 4 29-JUL-20 5CJF 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 02-DEC-15 5CJF 1 JRNL
REVDAT 2 25-NOV-15 5CJF 1 JRNL
REVDAT 1 04-NOV-15 5CJF 0
JRNL AUTH G.LA REGINA,A.COLUCCIA,V.FAMIGLINI,S.PELLICCIA,L.MONTI,
JRNL AUTH 2 D.VULLO,E.NUTI,V.ALTERIO,G.DE SIMONE,S.M.MONTI,P.PAN,
JRNL AUTH 3 S.PARKKILA,C.T.SUPURAN,A.ROSSELLO,R.SILVESTRI
JRNL TITL DISCOVERY OF 1,1'-BIPHENYL-4-SULFONAMIDES AS A NEW CLASS OF
JRNL TITL 2 POTENT AND SELECTIVE CARBONIC ANHYDRASE XIV INHIBITORS.
JRNL REF J.MED.CHEM. V. 58 8564 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26497049
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01144
REMARK 2
REMARK 2 RESOLUTION. 1.83 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 36948
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 SELECTION
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1845
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) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3161
REMARK 3 BIN R VALUE (WORKING SET) : 0.2381
REMARK 3 BIN FREE R VALUE : 0.2685
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 170
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 : 2128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 104
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53300
REMARK 3 B22 (A**2) : -0.53300
REMARK 3 B33 (A**2) : 1.06700
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.247 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.949 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.979 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.059 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 42.92
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 : ION_PATCH_CA14.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : RS25NEW.PARAM
REMARK 3 PARAMETER FILE 7 : GLICEROLOCSD.PARAM
REMARK 3 PARAMETER FILE 8 : 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 TOPOLOGY FILE 8 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : D*TREK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38776
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.62100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 4LU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 -HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 54.36800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.24750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.24750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.18400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.24750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.24750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 81.55200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.24750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.24750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.18400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.24750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.24750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 81.55200
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 0.00000
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 54.36800
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: 1470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 496 LIES ON A SPECIAL POSITION.
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 ALA A -1
REMARK 465 ASP A 0
REMARK 465 GLY A 1
REMARK 465 GLY A 2
REMARK 465 GLN A 3
REMARK 465 GLY A 270
REMARK 465 GLU A 271
REMARK 465 MET A 272
REMARK 465 LEU A 273
REMARK 465 VAL A 274
REMARK 465 PRO A 275
REMARK 465 ARG A 276
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN A 188 OE1 GLN A 188 8665 2.01
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 ASP A 171 -7.31 81.76
REMARK 500 ASN A 244 51.49 -93.66
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 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 104.5
REMARK 620 3 HIS A 119 ND1 115.1 100.0
REMARK 620 4 520 A 302 N2 107.4 112.4 116.7
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LU3 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE HUMAN CARBONIC ANHYDRASE XIV IN
REMARK 900 COMPLEX WITH ACETAZOLAMIDE.
DBREF 5CJF A -1 272 UNP Q9ULX7 CAH14_HUMAN 16 290
SEQADV 5CJF LEU A 273 UNP Q9ULX7 EXPRESSION TAG
SEQADV 5CJF VAL A 274 UNP Q9ULX7 EXPRESSION TAG
SEQADV 5CJF PRO A 275 UNP Q9ULX7 EXPRESSION TAG
SEQADV 5CJF ARG A 276 UNP Q9ULX7 EXPRESSION TAG
SEQRES 1 A 279 ALA ASP GLY GLY GLN HIS TRP THR TYR GLU GLY PRO HIS
SEQRES 2 A 279 GLY GLN ASP HIS TRP PRO ALA SER TYR PRO GLU CYS GLY
SEQRES 3 A 279 ASN ASN ALA GLN SER PRO ILE ASP ILE GLN THR ASP SER
SEQRES 4 A 279 VAL THR PHE ASP PRO ASP LEU PRO ALA LEU GLN PRO HIS
SEQRES 5 A 279 GLY TYR ASP GLN PRO GLY THR GLU PRO LEU ASP LEU HIS
SEQRES 6 A 279 ASN ASN GLY HIS THR VAL GLN LEU SER LEU PRO SER THR
SEQRES 7 A 279 LEU TYR LEU GLY GLY LEU PRO ARG LYS TYR VAL ALA ALA
SEQRES 8 A 279 GLN LEU HIS LEU HIS TRP GLY GLN LYS GLY SER PRO GLY
SEQRES 9 A 279 GLY SER GLU HIS GLN ILE ASN SER GLU ALA THR PHE ALA
SEQRES 10 A 279 GLU LEU HIS ILE VAL HIS TYR ASP SER ASP SER TYR ASP
SEQRES 11 A 279 SER LEU SER GLU ALA ALA GLU ARG PRO GLN GLY LEU ALA
SEQRES 12 A 279 VAL LEU GLY ILE LEU ILE GLU VAL GLY GLU THR LYS ASN
SEQRES 13 A 279 ILE ALA TYR GLU HIS ILE LEU SER HIS LEU HIS GLU VAL
SEQRES 14 A 279 ARG HIS LYS ASP GLN LYS THR SER VAL PRO PRO PHE ASN
SEQRES 15 A 279 LEU ARG GLU LEU LEU PRO LYS GLN LEU GLY GLN TYR PHE
SEQRES 16 A 279 ARG TYR ASN GLY SER LEU THR THR PRO PRO CYS TYR GLN
SEQRES 17 A 279 SER VAL LEU TRP THR VAL PHE TYR ARG ARG SER GLN ILE
SEQRES 18 A 279 SER MET GLU GLN LEU GLU LYS LEU GLN GLY THR LEU PHE
SEQRES 19 A 279 SER THR GLU GLU GLU PRO SER LYS LEU LEU VAL GLN ASN
SEQRES 20 A 279 TYR ARG ALA LEU GLN PRO LEU ASN GLN ARG MET VAL PHE
SEQRES 21 A 279 ALA SER PHE ILE GLN ALA GLY SER SER TYR THR THR GLY
SEQRES 22 A 279 GLU MET LEU VAL PRO ARG
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET MAN B 5 11
HET ZN A 301 1
HET 520 A 302 25
HET GOL A 303 6
HET GOL A 304 6
HET SO4 A 305 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM 520 4'-(4-AMINOBENZOYL)BIPHENYL-4-SULFONAMIDE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE 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
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 3 ZN ZN 2+
FORMUL 4 520 C19 H16 N2 O3 S
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *228(H2 O)
HELIX 1 AA1 GLY A 12 ASP A 14 5 3
HELIX 2 AA2 HIS A 15 TYR A 20 1 6
HELIX 3 AA3 PRO A 21 ASN A 25 5 5
HELIX 4 AA4 GLN A 34 VAL A 38 5 5
HELIX 5 AA5 SER A 130 ALA A 135 1 6
HELIX 6 AA6 ASN A 154 SER A 162 1 9
HELIX 7 AA7 HIS A 163 VAL A 167 5 5
HELIX 8 AA8 ASN A 180 LEU A 185 5 6
HELIX 9 AA9 MET A 220 GLY A 227A 1 9
SHEET 1 AA1 2 ASP A 32 ILE A 33 0
SHEET 2 AA1 2 GLN A 108 ILE A 109 1 O GLN A 108 N ILE A 33
SHEET 1 AA210 THR A 39 PHE A 40 0
SHEET 2 AA210 PHE A 257 ALA A 258 1 O ALA A 258 N THR A 39
SHEET 3 AA210 TYR A 191 GLY A 196 -1 N ARG A 193 O PHE A 257
SHEET 4 AA210 VAL A 207 PHE A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AA210 LEU A 141 GLY A 151 1 N GLY A 145 O THR A 210
SHEET 6 AA210 ALA A 116 ASP A 124 -1 N ALA A 116 O ILE A 148
SHEET 7 AA210 TYR A 88 TRP A 97 -1 N GLN A 92 O VAL A 121
SHEET 8 AA210 VAL A 66 SER A 69 -1 N LEU A 68 O LEU A 93
SHEET 9 AA210 LEU A 57 ASN A 61 -1 N HIS A 60 O GLN A 67
SHEET 10 AA210 LYS A 173 VAL A 176 -1 O VAL A 176 N LEU A 57
SHEET 1 AA3 6 PRO A 49 HIS A 50 0
SHEET 2 AA3 6 TYR A 78 LEU A 79 -1 O TYR A 78 N HIS A 50
SHEET 3 AA3 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AA3 6 ALA A 116 ASP A 124 -1 O VAL A 121 N GLN A 92
SHEET 5 AA3 6 LEU A 141 GLY A 151 -1 O ILE A 148 N ALA A 116
SHEET 6 AA3 6 SER A 216 SER A 219 1 O SER A 216 N GLU A 149
SSBOND 1 CYS A 23 CYS A 203 1555 1555 2.04
LINK ND2 ASN A 195 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.39
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.40
LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.40
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 1.99
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.00
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.02
LINK ZN ZN A 301 N2 520 A 302 1555 1555 2.01
CISPEP 1 SER A 29 PRO A 30 0 0.29
CISPEP 2 PRO A 201 PRO A 202 0 0.36
CISPEP 3 GLU A 236 PRO A 237 0 -0.23
CRYST1 88.495 88.495 108.736 90.00 90.00 90.00 P 41 21 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 0.011300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
