HEADER HYDROLASE INHIBITOR/HYDROLASE 25-NOV-14 4X1S
TITLE THE CRYSTAL STRUCTURE OF MUPAIN-1-16-D9A IN COMPLEX WITH MURINISED
TITLE 2 HUMAN UPA AT PH7.4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUPAIN-1-16;
COMPND 3 CHAIN: P;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;
COMPND 7 CHAIN: U;
COMPND 8 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 179-425);
COMPND 9 SYNONYM: UPA;
COMPND 10 EC: 3.4.21.73;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: PLAU;
SOURCE 10 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS SERINE PROTEASE, PEPTIDIC INHIBITOR, UPA, HYDROLASE INHIBITOR-
KEYWDS 2 HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JIANG,B.ZHAO,P.XU,P.ANDREASEN,M.HUANG
REVDAT 2 08-NOV-23 4X1S 1 REMARK
REVDAT 1 28-OCT-15 4X1S 0
JRNL AUTH B.ZHAO,P.XU,L.JIANG,B.PAASKE,T.KROMANN-HANSEN,J.K.JENSEN,
JRNL AUTH 2 H.P.SRENSEN,Z.LIU,J.T.NIELSEN,A.CHRISTENSEN,M.HOSSEINI,
JRNL AUTH 3 K.K.SRENSEN,N.C.NIELSEN,K.J.JENSEN,M.HUANG,P.A.ANDREASEN
JRNL TITL A CYCLIC PEPTIDIC SERINE PROTEASE INHIBITOR: INCREASING
JRNL TITL 2 AFFINITY BY INCREASING PEPTIDE FLEXIBILITY.
JRNL REF PLOS ONE V. 9 15872 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 25545505
JRNL DOI 10.1371/JOURNAL.PONE.0115872
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 18052
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 925
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.1089 - 3.6247 0.90 2274 123 0.1806 0.2270
REMARK 3 2 3.6247 - 2.8785 0.99 2493 141 0.2000 0.2220
REMARK 3 3 2.8785 - 2.5151 0.99 2490 135 0.2227 0.2709
REMARK 3 4 2.5151 - 2.2853 0.98 2496 140 0.2246 0.3102
REMARK 3 5 2.2853 - 2.1216 0.98 2485 119 0.2293 0.2767
REMARK 3 6 2.1216 - 1.9966 0.98 2479 133 0.2395 0.3020
REMARK 3 7 1.9966 - 1.8967 0.96 2410 134 0.2623 0.2824
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2081
REMARK 3 ANGLE : 1.111 2809
REMARK 3 CHIRALITY : 0.047 303
REMARK 3 PLANARITY : 0.006 355
REMARK 3 DIHEDRAL : 14.783 760
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4X1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000204916.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18056
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.897
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.4000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2NWN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 50MM SODIUM
REMARK 280 CITRATE PH 4.6, 5% PEG 400, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 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 60.65000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.01629
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.30867
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 60.65000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 35.01629
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.30867
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 60.65000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 35.01629
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 14.30867
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.03259
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 28.61733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.03259
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 28.61733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.03259
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 28.61733
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, U
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 GLU U 244
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA P 6 CA ALA P 6 C -0.183
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA P 6 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU P 8 CB - CG - CD2 ANGL. DEV. = -10.4 DEGREES
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 GLN U 27 61.60 -150.34
REMARK 500 CYS U 111 -159.55 -91.84
REMARK 500 TYR U 171 -102.60 -96.52
REMARK 500 GLN U 204 -117.75 52.22
REMARK 500 SER U 214 -62.60 -124.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER P 5 ALA P 6 149.85
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 MRZ P 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X0W RELATED DB: PDB
REMARK 900 RELATED ID: 4X1N RELATED DB: PDB
REMARK 900 RELATED ID: 4N1P RELATED DB: PDB
REMARK 900 RELATED ID: 4N1Q RELATED DB: PDB
REMARK 900 RELATED ID: 4N1R RELATED DB: PDB
DBREF 4X1S P 1 10 PDB 4X1S 4X1S 1 10
DBREF 4X1S U 16 244 UNP P00749 UROK_HUMAN 179 425
SEQADV 4X1S TYR U 99 UNP P00749 HIS 272 ENGINEERED MUTATION
SEQADV 4X1S ALA U 122 UNP P00749 CYS 299 ENGINEERED MUTATION
SEQADV 4X1S GLN U 145 UNP P00749 ASN 322 ENGINEERED MUTATION
SEQRES 1 P 10 CYS PRO ALA TYR SER ALA TYR LEU ALA CYS
SEQRES 1 U 247 ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO
SEQRES 2 U 247 TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER
SEQRES 3 U 247 VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS
SEQRES 4 U 247 TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO
SEQRES 5 U 247 LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG
SEQRES 6 U 247 LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL
SEQRES 7 U 247 GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR
SEQRES 8 U 247 LEU ALA TYR HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG
SEQRES 9 U 247 SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE
SEQRES 10 U 247 GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN
SEQRES 11 U 247 PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU
SEQRES 12 U 247 GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET
SEQRES 13 U 247 THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN
SEQRES 14 U 247 PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU
SEQRES 15 U 247 CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN
SEQRES 16 U 247 GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY
SEQRES 17 U 247 ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY
SEQRES 18 U 247 CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL
SEQRES 19 U 247 SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU
HET MRZ P 100 9
HETNAM MRZ PIPERIDINE-1-CARBOXIMIDAMIDE
FORMUL 3 MRZ C6 H13 N3
FORMUL 4 HOH *67(H2 O)
HELIX 1 AA1 THR U 23 GLN U 27 5 5
HELIX 2 AA2 ALA U 55 PHE U 59 5 5
HELIX 3 AA3 LYS U 61 GLU U 62A 5 3
HELIX 4 AA4 SER U 164 GLN U 169 1 6
HELIX 5 AA5 TYR U 172 VAL U 176 5 5
HELIX 6 AA6 PHE U 234 LYS U 243 1 10
SHEET 1 AA1 8 GLU U 20 PHE U 21 0
SHEET 2 AA1 8 LYS U 156 ILE U 163 -1 O MET U 157 N GLU U 20
SHEET 3 AA1 8 MET U 180 ALA U 184 -1 O CYS U 182 N ILE U 163
SHEET 4 AA1 8 GLY U 226 ARG U 230 -1 O TYR U 228 N LEU U 181
SHEET 5 AA1 8 ARG U 206 TRP U 215 -1 N TRP U 215 O VAL U 227
SHEET 6 AA1 8 PRO U 198 LEU U 203 -1 N LEU U 199 O GLY U 211
SHEET 7 AA1 8 SER U 135 GLY U 140 -1 N GLU U 137 O VAL U 200
SHEET 8 AA1 8 LYS U 156 ILE U 163 -1 O VAL U 160 N CYS U 136
SHEET 1 AA2 7 PHE U 30 ARG U 36 0
SHEET 2 AA2 7 VAL U 38 SER U 48 -1 O VAL U 41 N ILE U 33
SHEET 3 AA2 7 TRP U 51 SER U 54 -1 O ILE U 53 N SER U 45
SHEET 4 AA2 7 ALA U 104 ARG U 109 -1 O LEU U 106 N VAL U 52
SHEET 5 AA2 7 MET U 81 LEU U 90 -1 N ILE U 89 O LEU U 105
SHEET 6 AA2 7 TYR U 64 LEU U 68 -1 N VAL U 66 O PHE U 83
SHEET 7 AA2 7 PHE U 30 ARG U 36 -1 N TYR U 34 O ILE U 65
SHEET 1 AA3 2 SER U 95 ALA U 96 0
SHEET 2 AA3 2 TYR U 99 HIS U 100 -1 O HIS U 100 N SER U 95
SSBOND 1 CYS P 1 CYS P 10 1555 1555 1.98
SSBOND 2 CYS U 42 CYS U 58 1555 1555 2.04
SSBOND 3 CYS U 50 CYS U 111 1555 1555 2.03
SSBOND 4 CYS U 136 CYS U 201 1555 1555 2.04
SSBOND 5 CYS U 168 CYS U 182 1555 1555 2.03
SSBOND 6 CYS U 191 CYS U 220 1555 1555 2.06
LINK CB ALA P 6 C1 MRZ P 100 1555 1555 1.54
SITE 1 AC1 9 ALA P 6 ASP U 189 SER U 190 VAL U 213
SITE 2 AC1 9 TRP U 215 GLY U 216 GLY U 219 CYS U 220
SITE 3 AC1 9 GLY U 226
CRYST1 121.300 121.300 42.926 90.00 90.00 120.00 H 3 9
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 0.008244 0.004760 0.000000 0.00000
SCALE2 0.000000 0.009519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023296 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
