HEADER HYDROLASE 17-JUL-15 5A8X
TITLE CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A
TITLE 2 DIHYDROPYRIMIDONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL ELASTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BONE MARROW SERINE PROTEASE,ELASTASE-2,HUMAN LEUKOCYTE
COMPND 5 ELASTASE,HLE,MEDULLASIN,PMN ELASTASE;
COMPND 6 EC: 3.4.21.37;
COMPND 7 OTHER_DETAILS: PURCHASED COMERCIALLY
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRYPSIN FAMILY FOLD, PROTEASE, HYDROLASE, HYDROLASE- INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VONNUSSBAUM,V.M.LI,D.MEIBOM,S.ANLAUF,M.BECHEM,M.DELBECK,M.GERISCH,
AUTHOR 2 A.HARRENGA,D.KARTHAUS,D.LANG,K.LUSTIG,J.MITTENDORF,M.SCHAEFER,
AUTHOR 3 S.SCHAEFER,J.SCHAMBERGER
REVDAT 4 29-JUL-20 5A8X 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 12-DEC-18 5A8X 1 COMPND SOURCE JRNL REMARK
REVDAT 3 2 1 DBREF
REVDAT 2 28-JUN-17 5A8X 1 REMARK
REVDAT 1 03-AUG-16 5A8X 0
JRNL AUTH F.VON NUSSBAUM,V.M.LI,D.MEIBOM,S.ANLAUF,M.BECHEM,M.DELBECK,
JRNL AUTH 2 M.GERISCH,A.HARRENGA,D.KARTHAUS,D.LANG,K.LUSTIG,
JRNL AUTH 3 J.MITTENDORF,M.SCHAFER,S.SCHAFER,J.SCHAMBERGER
JRNL TITL POTENT AND SELECTIVE HUMAN NEUTROPHIL ELASTASE INHIBITORS
JRNL TITL 2 WITH NOVEL EQUATORIAL RING TOPOLOGY: IN VIVO EFFICACY OF THE
JRNL TITL 3 POLAR PYRIMIDOPYRIDAZINE BAY-8040 IN A PULMONARY ARTERIAL
JRNL TITL 4 HYPERTENSION RAT MODEL.
JRNL REF CHEMMEDCHEM V. 11 199 2016
JRNL REFN ESSN 1860-7187
JRNL PMID 26333652
JRNL DOI 10.1002/CMDC.201500269
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 10120
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 510
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) : 1.29
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 703
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1606
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 95
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.02000
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): 0.315
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1741 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2379 ; 1.349 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 213 ; 6.134 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;32.418 ;22.535
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 248 ;14.762 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.235 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 280 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1307 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 720 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1169 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 139 ; 0.145 ; 0.200
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): 24 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.165 ; 0.200
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): 1089 ; 0.715 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1694 ; 1.233 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 727 ; 1.755 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 685 ; 2.877 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 5A8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1290064401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 31.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 8.060
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.00500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.00500
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 35.00500
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 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 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 ARG A 147
REMARK 465 ASN A 148
REMARK 465 ARG A 149
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 O HOH A 2080 O HOH A 2081 1.88
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 ARG A 36 53.53 17.95
REMARK 500 HIS A 71 -59.33 -138.61
REMARK 500 ASN A 92 50.66 -143.47
REMARK 500 ASN A 115 -157.38 -139.11
REMARK 500 LEU A 223 -56.99 -120.81
REMARK 500
REMARK 500 REMARK: NULL
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 NAG A 403
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A
REMARK 900 DIHYDROPYRIMIDONE INHIBITOR
REMARK 900 RELATED ID: 5A8Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A
REMARK 900 DIHYDROPYRIMIDONE INHIBITOR
DBREF 5A8X A 16 243 UNP P08246 ELNE_HUMAN 30 247
SEQRES 1 A 218 ILE VAL GLY GLY ARG ARG ALA ARG PRO HIS ALA TRP PRO
SEQRES 2 A 218 PHE MET VAL SER LEU GLN LEU ARG GLY GLY HIS PHE CYS
SEQRES 3 A 218 GLY ALA THR LEU ILE ALA PRO ASN PHE VAL MET SER ALA
SEQRES 4 A 218 ALA HIS CYS VAL ALA ASN VAL ASN VAL ARG ALA VAL ARG
SEQRES 5 A 218 VAL VAL LEU GLY ALA HIS ASN LEU SER ARG ARG GLU PRO
SEQRES 6 A 218 THR ARG GLN VAL PHE ALA VAL GLN ARG ILE PHE GLU ASN
SEQRES 7 A 218 GLY TYR ASP PRO VAL ASN LEU LEU ASN ASP ILE VAL ILE
SEQRES 8 A 218 LEU GLN LEU ASN GLY SER ALA THR ILE ASN ALA ASN VAL
SEQRES 9 A 218 GLN VAL ALA GLN LEU PRO ALA GLN GLY ARG ARG LEU GLY
SEQRES 10 A 218 ASN GLY VAL GLN CYS LEU ALA MET GLY TRP GLY LEU LEU
SEQRES 11 A 218 GLY ARG ASN ARG GLY ILE ALA SER VAL LEU GLN GLU LEU
SEQRES 12 A 218 ASN VAL THR VAL VAL THR SER LEU CYS ARG ARG SER ASN
SEQRES 13 A 218 VAL CYS THR LEU VAL ARG GLY ARG GLN ALA GLY VAL CYS
SEQRES 14 A 218 PHE GLY ASP SER GLY SER PRO LEU VAL CYS ASN GLY LEU
SEQRES 15 A 218 ILE HIS GLY ILE ALA SER PHE VAL ARG GLY GLY CYS ALA
SEQRES 16 A 218 SER GLY LEU TYR PRO ASP ALA PHE ALA PRO VAL ALA GLN
SEQRES 17 A 218 PHE VAL ASN TRP ILE ASP SER ILE ILE GLN
MODRES 5A8X ASN A 109 ASN GLYCOSYLATION SITE
MODRES 5A8X ASN A 159 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET FUC B 2 10
HET NAG C 1 14
HET FUC C 2 10
HET NAG A 403 14
HET IUY A1001 33
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM IUY ETHYL (5R)-5-(4-CYANOPHENYL)-7-METHYL-8-[3-
HETNAM 2 IUY (TRIFLUOROMETHYL)PHENYL]-1,5-DIHYDROIMIDAZO[1,2-
HETNAM 3 IUY A]PYRIMIDIN-4-IUM-6-CARBOXYLATE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 FUC 2(C6 H12 O5)
FORMUL 5 IUY C24 H20 F3 N4 O2 1+
FORMUL 6 HOH *118(H2 O)
HELIX 1 1 ALA A 55 ALA A 60 1 6
HELIX 2 2 ASN A 63 ALA A 63C 5 4
HELIX 3 3 PHE A 234 GLN A 243 1 10
SHEET 1 AA 8 ARG A 20 ARG A 21 0
SHEET 2 AA 8 GLN A 156 VAL A 163 -1 O GLU A 157 N ARG A 20
SHEET 3 AA 8 VAL A 181 LEU A 184 -1 O CYS A 182 N VAL A 163
SHEET 4 AA 8 ASP A 226 PRO A 230 -1 O ASP A 226 N THR A 183
SHEET 5 AA 8 LEU A 208 PHE A 215 -1 O ILE A 212 N ALA A 229
SHEET 6 AA 8 PRO A 198 CYS A 201 -1 O LEU A 199 N HIS A 210
SHEET 7 AA 8 GLN A 135 GLY A 140 -1 O LEU A 137 N VAL A 200
SHEET 8 AA 8 ARG A 20 ARG A 21 0
SHEET 1 AB 7 MET A 30 LEU A 35 0
SHEET 2 AB 7 GLY A 39 ALA A 48 -1 O GLY A 39 N LEU A 35
SHEET 3 AB 7 PHE A 51 SER A 54 -1 O PHE A 51 N ILE A 47
SHEET 4 AB 7 VAL A 104 LEU A 108 -1 O VAL A 104 N SER A 54
SHEET 5 AB 7 GLN A 81 GLU A 90 -1 N GLN A 86 O GLN A 107
SHEET 6 AB 7 ARG A 65 LEU A 68 -1 O VAL A 66 N PHE A 83
SHEET 7 AB 7 MET A 30 LEU A 35 -1 O SER A 32 N VAL A 67
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.04
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.10
LINK ND2 ASN A 109 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 159 C1 NAG B 1 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 2 1555 1555 1.45
LINK O6 NAG C 1 C1 FUC C 2 1555 1555 1.45
CRYST1 73.795 73.795 70.010 90.00 90.00 120.00 P 63 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 0.013551 0.007824 0.000000 0.00000
SCALE2 0.000000 0.015647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
