HEADER HYDROLASE, IMMUNE SYSTEM 20-AUG-07 2R0K
TITLE PROTEASE DOMAIN OF HGFA WITH INHIBITOR FAB58
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HGFA PROTEASE DOMAIN;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANTIBODY LIGHT CHAIN OF FAB58;
COMPND 9 CHAIN: L;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ANTIBODY HEAVY CHAIN OF FAB58, FAB PORTION ONLY;
COMPND 13 CHAIN: H;
COMPND 14 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: HGFAC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 OTHER_DETAILS: THE PROTEIN WAS MADE USING A SYNTHETICALLY
SOURCE 18 DIVERSIFIED GENE LIBRARY AND SELECTED FOR TIGHT BINDING TO A
SOURCE 19 SPECIFIC TARGET ON A PLASTIC SURFACE. THE GENE LIBRARY USED CLONED
SOURCE 20 HUMAN GENES AS ITS BASIS;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 OTHER_DETAILS: THE PROTEIN WAS MADE USING A SYNTHETICALLY
SOURCE 29 DIVERSIFIED GENE LIBRARY AND SELECTED FOR TIGHT BINDING TO A
SOURCE 30 SPECIFIC TARGET ON A PLASTIC SURFACE. THE GENE LIBRARY USED CLONED
SOURCE 31 HUMAN GENES AS ITS BASIS.
KEYWDS SERINE PROTEASE, ANTIBODY, INHIBITOR, EGF-LIKE DOMAIN, GLYCOPROTEIN,
KEYWDS 2 HYDROLASE, KRINGLE, SECRETED, ZYMOGEN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,S.SHIA
REVDAT 6 30-AUG-23 2R0K 1 REMARK
REVDAT 5 25-OCT-17 2R0K 1 REMARK
REVDAT 4 05-FEB-14 2R0K 1 SOURCE
REVDAT 3 13-JUL-11 2R0K 1 VERSN
REVDAT 2 24-FEB-09 2R0K 1 VERSN
REVDAT 1 25-DEC-07 2R0K 0
JRNL AUTH Y.WU,C.EIGENBROT,W.C.LIANG,S.STAWICKI,S.SHIA,B.FAN,
JRNL AUTH 2 R.GANESAN,M.T.LIPARI,D.KIRCHHOFER
JRNL TITL STRUCTURAL INSIGHT INTO DISTINCT MECHANISMS OF PROTEASE
JRNL TITL 2 INHIBITION BY ANTIBODIES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 19784 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 18077410
JRNL DOI 10.1073/PNAS.0708251104
REMARK 2
REMARK 2 RESOLUTION. 3.51 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) : 3.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 3 NUMBER OF REFLECTIONS : 10827
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) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 526
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) : 3.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 675
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 9.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.59000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 2.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.90000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.813
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.585
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 81.710
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.830
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.746
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5174 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7051 ; 1.190 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 660 ; 6.159 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 203 ;34.584 ;23.793
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 787 ;17.899 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.680 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 783 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3937 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2321 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3405 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 178 ; 0.167 ; 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): 29 ; 0.267 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.462 ; 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): 3371 ; 1.907 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5339 ; 3.276 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2064 ; 1.544 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1712 ; 2.463 ; 5.000
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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 107
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0305 11.2247 12.6755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0339 T22: -0.0933
REMARK 3 T33: -0.0684 T12: -0.0567
REMARK 3 T13: 0.0012 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 3.5155 L22: 1.7346
REMARK 3 L33: 0.8352 L12: -1.2845
REMARK 3 L13: -1.1853 L23: -0.3093
REMARK 3 S TENSOR
REMARK 3 S11: 0.2235 S12: 0.0433 S13: 0.2103
REMARK 3 S21: 0.0441 S22: 0.0981 S23: 0.0004
REMARK 3 S31: -0.1898 S32: 0.1477 S33: -0.3216
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 108 L 214
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6109 13.4558 25.6033
REMARK 3 T TENSOR
REMARK 3 T11: 0.0447 T22: -0.0455
REMARK 3 T33: -0.1285 T12: 0.0445
REMARK 3 T13: 0.0656 T23: 0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 2.4585 L22: 2.9899
REMARK 3 L33: 0.9877 L12: 1.2982
REMARK 3 L13: -1.0608 L23: -1.0804
REMARK 3 S TENSOR
REMARK 3 S11: 0.0936 S12: 0.1557 S13: 0.1850
REMARK 3 S21: 0.4300 S22: 0.1636 S23: 0.0142
REMARK 3 S31: -0.2971 S32: -0.3296 S33: -0.2572
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 119
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4592 -10.6299 17.4815
REMARK 3 T TENSOR
REMARK 3 T11: -0.0256 T22: -0.0765
REMARK 3 T33: 0.0613 T12: 0.0326
REMARK 3 T13: 0.0233 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.2534 L22: 0.4790
REMARK 3 L33: 1.4641 L12: 0.0165
REMARK 3 L13: -1.3545 L23: -0.0044
REMARK 3 S TENSOR
REMARK 3 S11: -0.1447 S12: -0.0867 S13: -0.1596
REMARK 3 S21: -0.0383 S22: 0.1192 S23: 0.0351
REMARK 3 S31: 0.0653 S32: 0.0394 S33: 0.0255
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 120 H 216
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8268 0.4684 16.2427
REMARK 3 T TENSOR
REMARK 3 T11: -0.0015 T22: 0.0093
REMARK 3 T33: -0.1727 T12: -0.0021
REMARK 3 T13: 0.0004 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 2.9689 L22: 3.2057
REMARK 3 L33: 0.2944 L12: -0.1729
REMARK 3 L13: 0.5092 L23: -0.8431
REMARK 3 S TENSOR
REMARK 3 S11: -0.1777 S12: 0.0937 S13: 0.0134
REMARK 3 S21: -0.2513 S22: 0.1577 S23: -0.2328
REMARK 3 S31: 0.0971 S32: -0.3483 S33: 0.0200
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 16 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1627 -18.7698 2.8051
REMARK 3 T TENSOR
REMARK 3 T11: -0.0811 T22: -0.0878
REMARK 3 T33: 0.0158 T12: -0.0021
REMARK 3 T13: 0.0171 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.5302 L22: 1.4294
REMARK 3 L33: 0.6404 L12: -0.8387
REMARK 3 L13: -0.2508 L23: 0.0272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: -0.0183 S13: -0.0286
REMARK 3 S21: -0.0293 S22: 0.0054 S23: 0.0001
REMARK 3 S31: 0.0029 S32: -0.0018 S33: -0.0468
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10827
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB 1YBW, PDB 1FVD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MIXTURE OF PROTEIN COMPLEX
REMARK 280 SOLUTION AND RESERVOIR CONTAINING 1.0M K/NA TARTRATE, CHES PH9.5,
REMARK 280 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 94.32900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.80500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 94.32900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.80500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 3440 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H
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 VAL A -19
REMARK 465 GLN A -18
REMARK 465 LEU A -17
REMARK 465 SER A -16
REMARK 465 PRO A -15
REMARK 465 ASP A -14
REMARK 465 LEU A -13
REMARK 465 LEU A -12
REMARK 465 ALA A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 PRO A -8
REMARK 465 GLU A -7
REMARK 465 PRO A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 GLN A 0
REMARK 465 ALA A 1
REMARK 465 CYS A 2
REMARK 465 GLY A 3
REMARK 465 ARG A 4
REMARK 465 ARG A 5
REMARK 465 HIS A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 ARG A 9
REMARK 465 THR A 10
REMARK 465 PHE A 11
REMARK 465 LEU A 12
REMARK 465 ARG A 13
REMARK 465 PRO A 14
REMARK 465 ARG A 15
REMARK 465 PRO A 244
REMARK 465 PRO A 245
REMARK 465 ARG A 246
REMARK 465 ARG A 247
REMARK 465 LEU A 248
REMARK 465 VAL A 249
REMARK 465 ALA A 250
REMARK 465 PRO A 251
REMARK 465 SER A 252
REMARK 465 SER H 127
REMARK 465 SER H 128
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 GLY H 133
REMARK 465 ASP H 217
REMARK 465 LYS H 218
REMARK 465 THR H 219
REMARK 465 HIS H 220
REMARK 465 THR H 221
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU H 1 N CA CB CG CD OE1 OE2
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 GLU H 1 N GLU H 1 CA -0.366
REMARK 500 GLN H 192 CB GLN H 192 CG 0.235
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 SER A 60B 59.28 35.54
REMARK 500 THR A 77 -164.46 -119.36
REMARK 500 ASN A 98 61.50 -150.71
REMARK 500 LYS A 111 75.07 -105.83
REMARK 500 CYS A 111D -79.96 -103.97
REMARK 500 HIS A 166 -73.18 -59.09
REMARK 500 VAL A 171 -113.28 -95.16
REMARK 500 ALA A 174 1.25 -68.40
REMARK 500 PRO A 178 1.08 -58.34
REMARK 500 LEU A 181 149.11 178.29
REMARK 500 CYS A 187 109.22 5.70
REMARK 500 LYS A 188 -114.51 -148.42
REMARK 500 LEU A 199 77.88 -102.02
REMARK 500 SER A 214 -61.18 -127.45
REMARK 500 LEU A 222 133.05 -37.37
REMARK 500 SER L 30 -128.43 39.02
REMARK 500 SER L 50 52.13 29.99
REMARK 500 ALA L 51 -32.34 56.68
REMARK 500 PRO L 59 115.55 -25.28
REMARK 500 SER L 67 118.68 -167.06
REMARK 500 THR L 69 -25.02 -144.85
REMARK 500 GLU L 81 -5.46 -55.79
REMARK 500 ALA L 84 171.32 178.11
REMARK 500 THR L 102 103.91 -161.71
REMARK 500 ASN L 138 74.87 60.94
REMARK 500 ASN L 152 -13.83 70.95
REMARK 500 SER L 156 113.13 -163.79
REMARK 500 ASP L 170 11.67 -148.65
REMARK 500 PRO L 204 120.39 -34.24
REMARK 500 GLU L 213 9.39 -59.87
REMARK 500 GLN H 3 140.63 -175.10
REMARK 500 SER H 32 116.69 175.23
REMARK 500 ARG H 66 -43.06 -137.54
REMARK 500 ALA H 96 -74.34 -145.33
REMARK 500 PHE H 98 5.57 44.40
REMARK 500 PHE H 100 92.48 -61.80
REMARK 500 ASP H 144 74.79 52.42
REMARK 500 SER H 153 143.36 153.86
REMARK 500 TRP H 154 66.47 146.44
REMARK 500 SER H 156 46.18 -161.79
REMARK 500 THR H 191 -66.37 -94.42
REMARK 500 GLN H 192 -163.14 -107.43
REMARK 500 ASN H 204 20.03 40.82
REMARK 500 LYS H 214 -135.99 -130.02
REMARK 500 SER H 215 -29.89 -145.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YBW RELATED DB: PDB
REMARK 900 PROTEASE DOMAIN OF HGFA WITH NO INHIBITOR
REMARK 900 RELATED ID: 1YC0 RELATED DB: PDB
REMARK 900 SHORT FORM HGFA WITH KUNITZ DOMAIN 1 FROM HAI-1
REMARK 900 RELATED ID: 2R0L RELATED DB: PDB
DBREF 2R0K A -19 252 UNP Q04756 HGFA_HUMAN 373 655
DBREF 2R0K L 1 214 PDB 2R0K 2R0K 1 214
DBREF 2R0K H 1 221 PDB 2R0K 2R0K 1 221
SEQRES 1 A 283 VAL GLN LEU SER PRO ASP LEU LEU ALA THR LEU PRO GLU
SEQRES 2 A 283 PRO ALA SER PRO GLY ARG GLN ALA CYS GLY ARG ARG HIS
SEQRES 3 A 283 LYS LYS ARG THR PHE LEU ARG PRO ARG ILE ILE GLY GLY
SEQRES 4 A 283 SER SER SER LEU PRO GLY SER HIS PRO TRP LEU ALA ALA
SEQRES 5 A 283 ILE TYR ILE GLY ASP SER PHE CYS ALA GLY SER LEU VAL
SEQRES 6 A 283 HIS THR CYS TRP VAL VAL SER ALA ALA HIS CYS PHE SER
SEQRES 7 A 283 HIS SER PRO PRO ARG ASP SER VAL SER VAL VAL LEU GLY
SEQRES 8 A 283 GLN HIS PHE PHE ASN ARG THR THR ASP VAL THR GLN THR
SEQRES 9 A 283 PHE GLY ILE GLU LYS TYR ILE PRO TYR THR LEU TYR SER
SEQRES 10 A 283 VAL PHE ASN PRO SER ASP HIS ASP LEU VAL LEU ILE ARG
SEQRES 11 A 283 LEU LYS LYS LYS GLY ASP ARG CYS ALA THR ARG SER GLN
SEQRES 12 A 283 PHE VAL GLN PRO ILE CYS LEU PRO GLU PRO GLY SER THR
SEQRES 13 A 283 PHE PRO ALA GLY HIS LYS CYS GLN ILE ALA GLY TRP GLY
SEQRES 14 A 283 HIS LEU ASP GLU ASN VAL SER GLY TYR SER SER SER LEU
SEQRES 15 A 283 ARG GLU ALA LEU VAL PRO LEU VAL ALA ASP HIS LYS CYS
SEQRES 16 A 283 SER SER PRO GLU VAL TYR GLY ALA ASP ILE SER PRO ASN
SEQRES 17 A 283 MET LEU CYS ALA GLY TYR PHE ASP CYS LYS SER ASP ALA
SEQRES 18 A 283 CYS GLN GLY ASP SER GLY GLY PRO LEU ALA CYS GLU LYS
SEQRES 19 A 283 ASN GLY VAL ALA TYR LEU TYR GLY ILE ILE SER TRP GLY
SEQRES 20 A 283 ASP GLY CYS GLY ARG LEU HIS LYS PRO GLY VAL TYR THR
SEQRES 21 A 283 ARG VAL ALA ASN TYR VAL ASP TRP ILE ASN ASP ARG ILE
SEQRES 22 A 283 ARG PRO PRO ARG ARG LEU VAL ALA PRO SER
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 L 214 PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 L 214 TYR THR THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 225 PHE THR ILE THR GLY SER ALA ILE HIS TRP VAL ARG GLN
SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE ASN
SEQRES 5 H 225 PRO ASN GLY GLY TYR THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 H 225 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 H 225 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG SER ALA ARG PHE SER PHE
SEQRES 9 H 225 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 10 H 225 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 H 225 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 H 225 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 225 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 H 225 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 H 225 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 H 225 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 H 225 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP
SEQRES 18 H 225 LYS THR HIS THR
HELIX 1 1 ALA A 55 PHE A 59 5 5
HELIX 2 2 PRO A 60D ASP A 62 5 3
HELIX 3 3 ALA A 164 SER A 170 1 7
HELIX 4 4 TYR A 172 ILE A 176 5 5
HELIX 5 5 TYR A 234 ASP A 240 1 7
HELIX 6 6 GLN L 79 PHE L 83 5 5
HELIX 7 7 SER L 121 SER L 127 1 7
HELIX 8 8 SER L 182 LYS L 188 1 7
HELIX 9 9 ARG H 83 THR H 87 5 5
HELIX 10 10 LYS H 201 ASN H 204 5 4
SHEET 1 A 7 SER A 20 SER A 21 0
SHEET 2 A 7 ARG A 156 PRO A 161 -1 O GLU A 157 N SER A 20
SHEET 3 A 7 LYS A 135 GLY A 140 -1 N CYS A 136 O VAL A 160
SHEET 4 A 7 PRO A 198 LYS A 203 -1 O ALA A 200 N GLN A 137
SHEET 5 A 7 VAL A 206 TRP A 215 -1 O TYR A 208 N CYS A 201
SHEET 6 A 7 GLY A 226 ARG A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 CYS A 182 ALA A 183 -1 N ALA A 183 O GLY A 226
SHEET 1 B 7 GLN A 81 PHE A 83 0
SHEET 2 B 7 VAL A 64 LEU A 68 -1 N VAL A 66 O PHE A 83
SHEET 3 B 7 LEU A 30 ILE A 35 -1 N TYR A 34 O SER A 65
SHEET 4 B 7 SER A 40 LEU A 46 -1 O CYS A 42 N ILE A 33
SHEET 5 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 6 B 7 VAL A 104 LEU A 108 -1 O VAL A 104 N SER A 54
SHEET 7 B 7 ILE A 85 PRO A 90 -1 N ILE A 89 O LEU A 105
SHEET 1 C 4 MET L 4 SER L 7 0
SHEET 2 C 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 C 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19
SHEET 4 C 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74
SHEET 1 D 6 SER L 10 SER L 14 0
SHEET 2 D 6 LYS L 103 LYS L 107 1 O GLU L 105 N ALA L 13
SHEET 3 D 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 D 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 D 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 D 6 PHE L 53 LEU L 54 -1 O PHE L 53 N TYR L 49
SHEET 1 E 4 SER L 114 PHE L 118 0
SHEET 2 E 4 ALA L 130 PHE L 139 -1 O ASN L 137 N SER L 114
SHEET 3 E 4 TYR L 173 LEU L 181 -1 O LEU L 175 N LEU L 136
SHEET 4 E 4 GLU L 161 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 F 4 ALA L 153 LEU L 154 0
SHEET 2 F 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 F 4 VAL L 191 THR L 197 -1 O THR L 197 N LYS L 145
SHEET 4 F 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SHEET 1 G 4 GLN H 3 SER H 7 0
SHEET 2 G 4 SER H 17 SER H 25 -1 O SER H 21 N SER H 7
SHEET 3 G 4 THR H 77 ASN H 82A-1 O MET H 82 N LEU H 18
SHEET 4 G 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 H 6 LEU H 11 VAL H 12 0
SHEET 2 H 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 H 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 H 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 H 6 LEU H 45 ASN H 52 -1 O GLU H 46 N ARG H 38
SHEET 6 H 6 TYR H 56 TYR H 59 -1 O TYR H 58 N ILE H 50
SHEET 1 I 4 LEU H 11 VAL H 12 0
SHEET 2 I 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 I 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 I 4 PHE H 100 TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 J 4 PRO H 123 LEU H 124 0
SHEET 2 J 4 THR H 135 CYS H 140 -1 O GLY H 139 N LEU H 124
SHEET 3 J 4 SER H 180 PRO H 185 -1 O VAL H 182 N LEU H 138
SHEET 4 J 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 K 3 LYS H 143 TYR H 145 0
SHEET 2 K 3 LEU H 175 SER H 177 -1 O TYR H 176 N TYR H 145
SHEET 3 K 3 VAL H 169 GLN H 171 -1 N VAL H 169 O SER H 177
SHEET 1 L 3 THR H 151 TRP H 154 0
SHEET 2 L 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151
SHEET 3 L 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 50 CYS A 111D 1555 1555 2.05
SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.03
SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 7 CYS L 134 CYS L 194 1555 1555 2.04
SSBOND 8 CYS L 214 CYS H 216 1555 1555 2.03
SSBOND 9 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 10 CYS H 140 CYS H 196 1555 1555 2.04
CISPEP 1 SER L 7 PRO L 8 0 5.73
CISPEP 2 THR L 94 PRO L 95 0 -13.49
CISPEP 3 TYR L 140 PRO L 141 0 14.42
CISPEP 4 PHE H 146 PRO H 147 0 -9.08
CISPEP 5 GLU H 148 PRO H 149 0 2.83
CISPEP 6 SER H 153 TRP H 154 0 -22.22
CISPEP 7 ASN H 155 SER H 156 0 5.85
CRYST1 188.658 75.610 69.139 90.00 92.67 90.00 C 1 2 1 4
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 0.005301 0.000000 0.000247 0.00000
SCALE2 0.000000 0.013226 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014479 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
