HEADER HYDROLASE 10-DEC-13 4CIK
TITLE PLASMINOGEN KRINGLE 1 IN COMPLEX WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KRINGLE 1, RESIDUES 101-181;
COMPND 5 EC: 3.4.21.7;
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 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS HYDROLASE, FIBRINOLYSIS, PLASMINOGEN, PROTEIN-PROTEIN INTERACTION,
KEYWDS 2 KRINGLE LIGAND
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XUE,C.JOHANSSON,L.CHENG,D.PETTERSEN,D.GUSTAFSSON
REVDAT 2 20-DEC-23 4CIK 1 REMARK
REVDAT 1 18-JUN-14 4CIK 0
JRNL AUTH L.CHENG,D.PETTERSEN,B.OHLSSON,P.SCHELL,M.KARLE,E.EVERTSSON,
JRNL AUTH 2 S.PAHLEN,M.JONFORSEN,A.T.PLOWRIGHT,J.BOSTROM,T.FEX,A.THELIN,
JRNL AUTH 3 C.HILGENDORF,Y.XUE,G.WAHLUND,W.LINDBERG,L.LARSSON,
JRNL AUTH 4 D.GUSTAFSSON
JRNL TITL DISCOVERY OF THE FIBRINOLYSIS INHIBITOR AZD6564, ACTING VIA
JRNL TITL 2 INTERFERENCE OF A PROTEIN-PROTEIN INTERACTION.
JRNL REF ACS MED.CHEM.LETT. V. 5 538 2014
JRNL REFN ISSN 1948-5875
JRNL PMID 24900876
JRNL DOI 10.1021/ML400526D
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.5.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11798
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) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.740
REMARK 3 FREE R VALUE TEST SET COUNT : 559
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1865
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2821
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1774
REMARK 3 BIN R VALUE (WORKING SET) : 0.2821
REMARK 3 BIN FREE R VALUE : 0.2819
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.88
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
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 : 647
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57009
REMARK 3 B22 (A**2) : 0.32698
REMARK 3 B33 (A**2) : 0.24311
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 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1290059193.
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11799
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 28.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1CEB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 25.38850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.70700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.79700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.70700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.38850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.79700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.38850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.79700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.70700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.79700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.38850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 40.70700
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
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 LYS A -2
REMARK 465 ARG A -1
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 2144 O HOH A 2153 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 2010 O HOH A 2010 7555 2.03
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 GLU A 1 42.49 -102.56
REMARK 500 GLU A 48 -126.52 48.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2022 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A2025 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A2031 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A2035 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH A2043 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A2053 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A2055 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH A2060 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A2063 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A2066 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A2067 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A2136 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH A2137 DISTANCE = 8.28 ANGSTROMS
REMARK 525 HOH A2138 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH A2139 DISTANCE = 9.36 ANGSTROMS
REMARK 525 HOH A2140 DISTANCE = 9.38 ANGSTROMS
REMARK 525 HOH A2141 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH A2142 DISTANCE = 9.16 ANGSTROMS
REMARK 525 HOH A2143 DISTANCE = 9.20 ANGSTROMS
REMARK 525 HOH A2144 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH A2145 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH A2146 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH A2147 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A2148 DISTANCE = 8.50 ANGSTROMS
REMARK 525 HOH A2149 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH A2150 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A2151 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A2152 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH A2153 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A2154 DISTANCE = 8.48 ANGSTROMS
REMARK 525 HOH A2155 DISTANCE = 8.92 ANGSTROMS
REMARK 525 HOH A2156 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A2157 DISTANCE = 8.93 ANGSTROMS
REMARK 525 HOH A2158 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH A2159 DISTANCE = 8.67 ANGSTROMS
REMARK 525 HOH A2160 DISTANCE = 8.84 ANGSTROMS
REMARK 525 HOH A2161 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH A2162 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH A2163 DISTANCE = 9.96 ANGSTROMS
REMARK 525 HOH A2164 DISTANCE = 9.12 ANGSTROMS
REMARK 525 HOH A2165 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH A2166 DISTANCE = 8.61 ANGSTROMS
REMARK 525 HOH A2167 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A2168 DISTANCE = 9.18 ANGSTROMS
REMARK 525 HOH A2169 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A2170 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH A2171 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH A2172 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH A2173 DISTANCE = 8.93 ANGSTROMS
REMARK 525 HOH A2174 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A2175 DISTANCE = 8.70 ANGSTROMS
REMARK 525 HOH A2176 DISTANCE = 9.93 ANGSTROMS
REMARK 525 HOH A2177 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH A2178 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH A2179 DISTANCE = 9.67 ANGSTROMS
REMARK 525 HOH A2180 DISTANCE = 9.18 ANGSTROMS
REMARK 525 HOH A2181 DISTANCE = 13.13 ANGSTROMS
REMARK 525 HOH A2182 DISTANCE = 9.95 ANGSTROMS
REMARK 525 HOH A2183 DISTANCE = 9.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XO3 A 1081
DBREF 4CIK A 0 80 UNP P00747 PLMN_HUMAN 101 181
SEQADV 4CIK LYS A -2 UNP P00747 EXPRESSION TAG
SEQADV 4CIK ARG A -1 UNP P00747 EXPRESSION TAG
SEQRES 1 A 83 LYS ARG SER GLU CYS LYS THR GLY ASN GLY LYS ASN TYR
SEQRES 2 A 83 ARG GLY THR MET SER LYS THR LYS ASN GLY ILE THR CYS
SEQRES 3 A 83 GLN LYS TRP SER SER THR SER PRO HIS ARG PRO ARG PHE
SEQRES 4 A 83 SER PRO ALA THR HIS PRO SER GLU GLY LEU GLU GLU ASN
SEQRES 5 A 83 TYR CYS ARG ASN PRO ASP ASN ASP PRO GLN GLY PRO TRP
SEQRES 6 A 83 CYS TYR THR THR ASP PRO GLU LYS ARG TYR ASP TYR CYS
SEQRES 7 A 83 ASP ILE LEU GLU CYS
HET XO3 A1081 19
HETNAM XO3 5-[(2R,4S)-2-(PHENYLMETHYL)PIPERIDIN-4-YL]-1,2-OXAZOL-
HETNAM 2 XO3 3-ONE
FORMUL 2 XO3 C15 H18 N2 O2
FORMUL 3 HOH *183(H2 O)
SHEET 1 AA 2 TRP A 62 TYR A 64 0
SHEET 2 AA 2 TYR A 72 TYR A 74 -1 O ASP A 73 N CYS A 63
SSBOND 1 CYS A 2 CYS A 80 1555 1555 2.03
SSBOND 2 CYS A 23 CYS A 63 1555 1555 2.03
SSBOND 3 CYS A 51 CYS A 75 1555 1555 2.03
CISPEP 1 SER A 30 PRO A 31 0 5.61
SITE 1 AC1 7 ARG A 35 ASP A 55 ASP A 57 TRP A 62
SITE 2 AC1 7 TYR A 64 ARG A 71 TYR A 72
CRYST1 50.777 57.594 81.414 90.00 90.00 90.00 I 21 21 21 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 0.019694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012283 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
