HEADER HYDROLASE 22-JUL-11 3T2N
TITLE HUMAN HEPSIN PROTEASE IN COMPLEX WITH THE FAB FRAGMENT OF AN
TITLE 2 INHIBITORY ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE HEPSIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 46-417);
COMPND 5 SYNONYM: TRANSMEMBRANE PROTEASE SERINE 1, SERINE PROTEASE HEPSIN NON-
COMPND 6 CATALYTIC CHAIN, SERINE PROTEASE HEPSIN CATALYTIC CHAIN;
COMPND 7 EC: 3.4.21.106;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ANTIBODY, FAB FRAGMENT, LIGHT CHAIN;
COMPND 11 CHAIN: L, M;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ANTIBODY, FAB FRAGMENT, HEAVY CHAIN;
COMPND 15 CHAIN: H, I;
COMPND 16 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: HPN, TMPRSS1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE 293 CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTT5;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606
KEYWDS TYPE II TRANSMEMBRANE SERINE PROTEASE, SRCR DOMAIN, SUBSTRATES
KEYWDS 2 INCLUDE PRO-HEPSIN, PRO-HGF, LAMININ-332, TRANSMEMBRANE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KOSCHUBS,S.DENGL,H.DUERR,K.KALUZA,G.GEORGES,C.HARTL,S.JENNEWEIN,
AUTHOR 2 M.LANZENDOERFER,J.AUER,A.STERN,K.-S.HUANG,D.KOSTREWA,S.RIES,
AUTHOR 3 S.HANSEN,U.KOHNERT,P.CRAMER,O.MUNDIGL
REVDAT 3 25-JUL-12 3T2N 1 REMARK
REVDAT 2 18-APR-12 3T2N 1 JRNL
REVDAT 1 28-DEC-11 3T2N 0
JRNL AUTH T.KOSCHUBS,S.DENGL,H.DURR,K.KALUZA,G.GEORGES,C.HARTL,
JRNL AUTH 2 S.JENNEWEIN,M.LANZENDORFER,J.AUER,A.STERN,K.S.HUANG,
JRNL AUTH 3 K.PACKMAN,U.GUBLER,D.KOSTREWA,S.RIES,S.HANSEN,U.KOHNERT,
JRNL AUTH 4 P.CRAMER,O.MUNDIGL
JRNL TITL ALLOSTERIC ANTIBODY INHIBITION OF HUMAN HEPSIN PROTEASE.
JRNL REF BIOCHEM.J. V. 442 483 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22132769
JRNL DOI 10.1042/BJ20111317
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 54655
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2772
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.67
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4062
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2726
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3851
REMARK 3 BIN R VALUE (WORKING SET) : 0.2705
REMARK 3 BIN FREE R VALUE : 0.3126
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.19
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 211
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 : 11434
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.18470
REMARK 3 B22 (A**2) : -8.20360
REMARK 3 B33 (A**2) : -3.98110
REMARK 3 B12 (A**2) : 3.84320
REMARK 3 B13 (A**2) : 3.00410
REMARK 3 B23 (A**2) : -1.52950
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.48
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.67
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.31
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.77
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.33
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 : 0.866
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.836
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11739 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 16007 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5193 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 232 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1725 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11739 ; 20.000 ; HARMONIC
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 : 1526 ; 5.000 ; SEMIHARMONIC
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 : 13093 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.24
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.47
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4924 -36.9479 -7.5503
REMARK 3 T TENSOR
REMARK 3 T11: -0.1132 T22: -0.0299
REMARK 3 T33: -0.2184 T12: -0.0205
REMARK 3 T13: 0.0776 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.2421 L22: 1.4582
REMARK 3 L33: 1.8896 L12: 0.3169
REMARK 3 L13: -0.6508 L23: -0.5575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0635 S12: 0.1489 S13: -0.0569
REMARK 3 S21: 0.0506 S22: -0.0518 S23: -0.0313
REMARK 3 S31: 0.0345 S32: 0.3520 S33: 0.1154
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9024 -36.0748 17.9916
REMARK 3 T TENSOR
REMARK 3 T11: -0.1372 T22: 0.0310
REMARK 3 T33: -0.2036 T12: -0.0075
REMARK 3 T13: 0.0966 T23: -0.0800
REMARK 3 L TENSOR
REMARK 3 L11: 1.3891 L22: 1.0664
REMARK 3 L33: 1.3322 L12: -0.5504
REMARK 3 L13: -0.3666 L23: 0.3022
REMARK 3 S TENSOR
REMARK 3 S11: -0.2023 S12: -0.1036 S13: 0.0109
REMARK 3 S21: -0.0905 S22: 0.0761 S23: 0.0487
REMARK 3 S31: 0.0320 S32: -0.3313 S33: 0.1263
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { H|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4298 -16.3837 -38.3121
REMARK 3 T TENSOR
REMARK 3 T11: -0.1278 T22: 0.0864
REMARK 3 T33: -0.2437 T12: -0.0468
REMARK 3 T13: 0.0818 T23: -0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 2.1839 L22: 0.6383
REMARK 3 L33: 1.3515 L12: -0.2116
REMARK 3 L13: 0.8070 L23: -0.3958
REMARK 3 S TENSOR
REMARK 3 S11: 0.1311 S12: 0.0270 S13: -0.1335
REMARK 3 S21: 0.0498 S22: -0.0339 S23: -0.0591
REMARK 3 S31: 0.0319 S32: -0.1297 S33: -0.0972
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { I|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4595 -15.5421 48.3280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1341 T22: 0.0837
REMARK 3 T33: -0.2164 T12: 0.0537
REMARK 3 T13: 0.0690 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 2.1410 L22: 0.2917
REMARK 3 L33: 0.9506 L12: 0.0543
REMARK 3 L13: 0.2203 L23: -0.1233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0806 S12: -0.0009 S13: -0.0762
REMARK 3 S21: 0.0756 S22: -0.0276 S23: 0.1365
REMARK 3 S31: -0.0358 S32: -0.0007 S33: -0.0530
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { L|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9257 -3.5204 -25.2884
REMARK 3 T TENSOR
REMARK 3 T11: -0.0797 T22: 0.0617
REMARK 3 T33: -0.1514 T12: -0.0777
REMARK 3 T13: 0.0836 T23: -0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 2.8583 L22: 0.3383
REMARK 3 L33: 0.4801 L12: -0.3848
REMARK 3 L13: 0.3758 L23: -0.1461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0556 S12: -0.0604 S13: 0.3548
REMARK 3 S21: 0.1086 S22: -0.0877 S23: -0.0061
REMARK 3 S31: 0.0349 S32: -0.0555 S33: 0.0321
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { M|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5915 -2.6784 35.6988
REMARK 3 T TENSOR
REMARK 3 T11: -0.1173 T22: 0.0748
REMARK 3 T33: -0.1787 T12: 0.1210
REMARK 3 T13: 0.0538 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 3.8583 L22: 0.3971
REMARK 3 L33: 0.5788 L12: 0.6350
REMARK 3 L13: -0.1401 L23: 0.2566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0637 S12: 0.1689 S13: 0.3036
REMARK 3 S21: -0.0151 S22: -0.0652 S23: -0.0069
REMARK 3 S31: -0.0480 S32: -0.0105 S33: 0.0014
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3T2N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54655
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 47.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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 : 7.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.15 M MGSO4 AND 0.01 M
REMARK 280 BARIUM CHLORIDE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 4980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
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: 4990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, M, I
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 SER A 46
REMARK 465 ASP A 47
REMARK 465 VAL A 160
REMARK 465 ASP A 161
REMARK 465 ARG A 162
REMARK 465 ILE A 163
REMARK 465 VAL A 164
REMARK 465 GLY A 165
REMARK 465 GLY A 166
REMARK 465 GLY A 297
REMARK 465 ASN A 298
REMARK 465 THR A 299
REMARK 465 GLN A 300
REMARK 465 TYR A 301
REMARK 465 TYR A 302
REMARK 465 GLY A 303
REMARK 465 GLN A 304
REMARK 465 GLN A 305
REMARK 465 ALA A 306
REMARK 465 GLU A 343
REMARK 465 GLY A 344
REMARK 465 GLY A 345
REMARK 465 ILE A 346
REMARK 465 ASP A 347
REMARK 465 ALA A 348
REMARK 465 CYS A 349
REMARK 465 GLN A 350
REMARK 465 TRP A 377
REMARK 465 GLY A 378
REMARK 465 THR A 379
REMARK 465 GLY A 380
REMARK 465 CYS A 381
REMARK 465 ALA A 382
REMARK 465 SER B 46
REMARK 465 ASP B 47
REMARK 465 PRO B 159
REMARK 465 VAL B 160
REMARK 465 ASP B 161
REMARK 465 ARG B 162
REMARK 465 ILE B 163
REMARK 465 VAL B 164
REMARK 465 GLY B 165
REMARK 465 GLY B 166
REMARK 465 ARG B 167
REMARK 465 ASP B 168
REMARK 465 GLY B 297
REMARK 465 ASN B 298
REMARK 465 THR B 299
REMARK 465 GLN B 300
REMARK 465 TYR B 301
REMARK 465 TYR B 302
REMARK 465 GLY B 303
REMARK 465 GLN B 304
REMARK 465 GLN B 305
REMARK 465 ALA B 306
REMARK 465 GLU B 343
REMARK 465 GLY B 344
REMARK 465 GLY B 345
REMARK 465 ILE B 346
REMARK 465 ASP B 347
REMARK 465 ALA B 348
REMARK 465 CYS B 349
REMARK 465 GLN B 350
REMARK 465 GLY B 378
REMARK 465 THR B 379
REMARK 465 GLY B 380
REMARK 465 CYS B 381
REMARK 465 ALA B 382
REMARK 465 LEU B 383
REMARK 465 LEU B 417
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 GLY H 134
REMARK 465 THR H 135
REMARK 465 ALA H 136
REMARK 465 LYS H 214
REMARK 465 SER H 215
REMARK 465 CYS H 216
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 465 CYS H 222
REMARK 465 PRO H 223
REMARK 465 PRO H 224
REMARK 465 CYS H 225
REMARK 465 SER I 127
REMARK 465 SER I 128
REMARK 465 LYS I 129
REMARK 465 SER I 130
REMARK 465 THR I 131
REMARK 465 SER I 132
REMARK 465 GLY I 133
REMARK 465 GLY I 134
REMARK 465 LYS I 214
REMARK 465 SER I 215
REMARK 465 CYS I 216
REMARK 465 ASP I 217
REMARK 465 LYS I 218
REMARK 465 THR I 219
REMARK 465 HIS I 220
REMARK 465 THR I 221
REMARK 465 CYS I 222
REMARK 465 PRO I 223
REMARK 465 PRO I 224
REMARK 465 CYS I 225
REMARK 465 THR L 210
REMARK 465 GLU L 211
REMARK 465 CYS L 212
REMARK 465 SER L 213
REMARK 465 GLU M 211
REMARK 465 CYS M 212
REMARK 465 SER M 213
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 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -3.5 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 PRO A 53 0.33 -68.92
REMARK 500 ALA A 111 32.49 -154.67
REMARK 500 LYS A 157 50.01 -97.74
REMARK 500 LEU A 187 -57.27 -122.02
REMARK 500 PHE A 205 68.83 -116.44
REMARK 500 ASN A 209 51.93 -115.57
REMARK 500 THR A 270 -163.36 -125.72
REMARK 500 GLN A 385 54.24 -114.66
REMARK 500 PRO B 53 0.94 -69.30
REMARK 500 ALA B 111 34.58 -153.18
REMARK 500 LEU B 187 -57.19 -121.61
REMARK 500 PHE B 205 70.21 -114.49
REMARK 500 ASN B 209 52.55 -113.27
REMARK 500 THR B 270 -165.58 -124.22
REMARK 500 GLN B 385 55.42 -113.75
REMARK 500 SER H 172 -3.63 -55.20
REMARK 500 ASN H 204 63.29 64.68
REMARK 500 SER I 172 -4.03 -56.17
REMARK 500 ASN I 204 63.85 64.93
REMARK 500 TYR L 32 53.36 35.13
REMARK 500 THR L 51 -58.79 65.90
REMARK 500 ALA L 84 -174.74 -173.09
REMARK 500 SER L 93 -58.51 66.86
REMARK 500 ASP L 152 -59.85 -126.38
REMARK 500 SER L 153 -3.55 -146.84
REMARK 500 ASN L 171 -1.92 69.25
REMARK 500 TYR M 32 53.65 33.45
REMARK 500 THR M 51 -59.42 66.41
REMARK 500 ALA M 84 -174.43 -173.07
REMARK 500 SER M 93 -50.14 68.04
REMARK 500 ASP M 152 -59.95 -129.51
REMARK 500 SER M 153 -11.95 -141.09
REMARK 500 ASN M 171 -1.66 68.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 167 0.16 SIDE CHAIN
REMARK 500 ASP B 257 0.07 SIDE CHAIN
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 H 314 DISTANCE = 6.31 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z8G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE
REMARK 900 TRANSMEMBRANE SERINE PROTEASE HEPSIN WITH COVALENTLY BOUND
REMARK 900 PREFERRED SUBSTRATE.
REMARK 900 RELATED ID: 1O5E RELATED DB: PDB
REMARK 900 DISSECTING AND DESIGNING INHIBITOR SELECTIVITY DETERMINANTS
REMARK 900 AT THE S1 SITE USING AN ARTIFICIAL ALA190 PROTEASE (ALA190
REMARK 900 UPA)
REMARK 900 RELATED ID: 1P57 RELATED DB: PDB
REMARK 900 EXTRACELLULAR DOMAIN OF HUMAN HEPSIN
DBREF 3T2N A 46 417 UNP P05981 HEPS_HUMAN 46 417
DBREF 3T2N B 46 417 UNP P05981 HEPS_HUMAN 46 417
DBREF 3T2N L 1 213 PDB 3T2N 3T2N 1 213
DBREF 3T2N M 1 213 PDB 3T2N 3T2N 1 213
DBREF 3T2N H 1 225 PDB 3T2N 3T2N 1 225
DBREF 3T2N I 1 225 PDB 3T2N 3T2N 1 225
SEQRES 1 A 372 SER ASP GLN GLU PRO LEU TYR PRO VAL GLN VAL SER SER
SEQRES 2 A 372 ALA ASP ALA ARG LEU MET VAL PHE ASP LYS THR GLU GLY
SEQRES 3 A 372 THR TRP ARG LEU LEU CYS SER SER ARG SER ASN ALA ARG
SEQRES 4 A 372 VAL ALA GLY LEU SER CYS GLU GLU MET GLY PHE LEU ARG
SEQRES 5 A 372 ALA LEU THR HIS SER GLU LEU ASP VAL ARG THR ALA GLY
SEQRES 6 A 372 ALA ASN GLY THR SER GLY PHE PHE CYS VAL ASP GLU GLY
SEQRES 7 A 372 ARG LEU PRO HIS THR GLN ARG LEU LEU GLU VAL ILE SER
SEQRES 8 A 372 VAL CYS ASP CYS PRO ARG GLY ARG PHE LEU ALA ALA ILE
SEQRES 9 A 372 CYS GLN ASP CYS GLY ARG ARG LYS LEU PRO VAL ASP ARG
SEQRES 10 A 372 ILE VAL GLY GLY ARG ASP THR SER LEU GLY ARG TRP PRO
SEQRES 11 A 372 TRP GLN VAL SER LEU ARG TYR ASP GLY ALA HIS LEU CYS
SEQRES 12 A 372 GLY GLY SER LEU LEU SER GLY ASP TRP VAL LEU THR ALA
SEQRES 13 A 372 ALA HIS CYS PHE PRO GLU ARG ASN ARG VAL LEU SER ARG
SEQRES 14 A 372 TRP ARG VAL PHE ALA GLY ALA VAL ALA GLN ALA SER PRO
SEQRES 15 A 372 HIS GLY LEU GLN LEU GLY VAL GLN ALA VAL VAL TYR HIS
SEQRES 16 A 372 GLY GLY TYR LEU PRO PHE ARG ASP PRO ASN SER GLU GLU
SEQRES 17 A 372 ASN SER ASN ASP ILE ALA LEU VAL HIS LEU SER SER PRO
SEQRES 18 A 372 LEU PRO LEU THR GLU TYR ILE GLN PRO VAL CYS LEU PRO
SEQRES 19 A 372 ALA ALA GLY GLN ALA LEU VAL ASP GLY LYS ILE CYS THR
SEQRES 20 A 372 VAL THR GLY TRP GLY ASN THR GLN TYR TYR GLY GLN GLN
SEQRES 21 A 372 ALA GLY VAL LEU GLN GLU ALA ARG VAL PRO ILE ILE SER
SEQRES 22 A 372 ASN ASP VAL CYS ASN GLY ALA ASP PHE TYR GLY ASN GLN
SEQRES 23 A 372 ILE LYS PRO LYS MET PHE CYS ALA GLY TYR PRO GLU GLY
SEQRES 24 A 372 GLY ILE ASP ALA CYS GLN GLY ASP SER GLY GLY PRO PHE
SEQRES 25 A 372 VAL CYS GLU ASP SER ILE SER ARG THR PRO ARG TRP ARG
SEQRES 26 A 372 LEU CYS GLY ILE VAL SER TRP GLY THR GLY CYS ALA LEU
SEQRES 27 A 372 ALA GLN LYS PRO GLY VAL TYR THR LYS VAL SER ASP PHE
SEQRES 28 A 372 ARG GLU TRP ILE PHE GLN ALA ILE LYS THR HIS SER GLU
SEQRES 29 A 372 ALA SER GLY MET VAL THR GLN LEU
SEQRES 1 B 372 SER ASP GLN GLU PRO LEU TYR PRO VAL GLN VAL SER SER
SEQRES 2 B 372 ALA ASP ALA ARG LEU MET VAL PHE ASP LYS THR GLU GLY
SEQRES 3 B 372 THR TRP ARG LEU LEU CYS SER SER ARG SER ASN ALA ARG
SEQRES 4 B 372 VAL ALA GLY LEU SER CYS GLU GLU MET GLY PHE LEU ARG
SEQRES 5 B 372 ALA LEU THR HIS SER GLU LEU ASP VAL ARG THR ALA GLY
SEQRES 6 B 372 ALA ASN GLY THR SER GLY PHE PHE CYS VAL ASP GLU GLY
SEQRES 7 B 372 ARG LEU PRO HIS THR GLN ARG LEU LEU GLU VAL ILE SER
SEQRES 8 B 372 VAL CYS ASP CYS PRO ARG GLY ARG PHE LEU ALA ALA ILE
SEQRES 9 B 372 CYS GLN ASP CYS GLY ARG ARG LYS LEU PRO VAL ASP ARG
SEQRES 10 B 372 ILE VAL GLY GLY ARG ASP THR SER LEU GLY ARG TRP PRO
SEQRES 11 B 372 TRP GLN VAL SER LEU ARG TYR ASP GLY ALA HIS LEU CYS
SEQRES 12 B 372 GLY GLY SER LEU LEU SER GLY ASP TRP VAL LEU THR ALA
SEQRES 13 B 372 ALA HIS CYS PHE PRO GLU ARG ASN ARG VAL LEU SER ARG
SEQRES 14 B 372 TRP ARG VAL PHE ALA GLY ALA VAL ALA GLN ALA SER PRO
SEQRES 15 B 372 HIS GLY LEU GLN LEU GLY VAL GLN ALA VAL VAL TYR HIS
SEQRES 16 B 372 GLY GLY TYR LEU PRO PHE ARG ASP PRO ASN SER GLU GLU
SEQRES 17 B 372 ASN SER ASN ASP ILE ALA LEU VAL HIS LEU SER SER PRO
SEQRES 18 B 372 LEU PRO LEU THR GLU TYR ILE GLN PRO VAL CYS LEU PRO
SEQRES 19 B 372 ALA ALA GLY GLN ALA LEU VAL ASP GLY LYS ILE CYS THR
SEQRES 20 B 372 VAL THR GLY TRP GLY ASN THR GLN TYR TYR GLY GLN GLN
SEQRES 21 B 372 ALA GLY VAL LEU GLN GLU ALA ARG VAL PRO ILE ILE SER
SEQRES 22 B 372 ASN ASP VAL CYS ASN GLY ALA ASP PHE TYR GLY ASN GLN
SEQRES 23 B 372 ILE LYS PRO LYS MET PHE CYS ALA GLY TYR PRO GLU GLY
SEQRES 24 B 372 GLY ILE ASP ALA CYS GLN GLY ASP SER GLY GLY PRO PHE
SEQRES 25 B 372 VAL CYS GLU ASP SER ILE SER ARG THR PRO ARG TRP ARG
SEQRES 26 B 372 LEU CYS GLY ILE VAL SER TRP GLY THR GLY CYS ALA LEU
SEQRES 27 B 372 ALA GLN LYS PRO GLY VAL TYR THR LYS VAL SER ASP PHE
SEQRES 28 B 372 ARG GLU TRP ILE PHE GLN ALA ILE LYS THR HIS SER GLU
SEQRES 29 B 372 ALA SER GLY MET VAL THR GLN LEU
SEQRES 1 L 215 GLN THR VAL VAL THR GLN GLU PRO SER LEU THR VAL SER
SEQRES 2 L 215 PRO GLY GLY THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 L 215 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN
SEQRES 4 L 215 GLN LYS PRO GLY GLN ALA PHE ARG GLY LEU ILE GLY ASP
SEQRES 5 L 215 THR ASN ASN ARG ALA PRO TRP THR PRO ALA ARG PHE SER
SEQRES 6 L 215 GLY SER LEU LEU GLY GLY LYS ALA ALA LEU THR LEU SER
SEQRES 7 L 215 GLY VAL GLN PRO GLU ASP GLU ALA GLU TYR TYR CYS ALA
SEQRES 8 L 215 LEU TRP TYR SER ASN HIS PHE ILE PHE GLY SER GLY THR
SEQRES 9 L 215 LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER
SEQRES 10 L 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA
SEQRES 11 L 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR
SEQRES 12 L 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER
SEQRES 13 L 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS
SEQRES 14 L 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER
SEQRES 15 L 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER
SEQRES 16 L 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR
SEQRES 17 L 215 VAL ALA PRO THR GLU CYS SER
SEQRES 1 H 225 GLN VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS
SEQRES 2 H 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 225 TYR THR PHE THR ASP TYR SER MET ARG TRP VAL ARG GLN
SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN
SEQRES 5 H 225 THR GLU THR GLY SER PRO THR TYR ALA ASP ASP PHE LYS
SEQRES 6 H 225 GLY ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR
SEQRES 7 H 225 ALA TYR LEU GLN ILE SER SER LEU LYS ALA GLU ASP THR
SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLY PHE ALA TYR TRP GLY
SEQRES 9 H 225 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS
SEQRES 10 H 225 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 11 H 225 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 12 H 225 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 13 H 225 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 14 H 225 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL
SEQRES 15 H 225 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 16 H 225 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 17 H 225 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR
SEQRES 18 H 225 CYS PRO PRO CYS
SEQRES 1 M 215 GLN THR VAL VAL THR GLN GLU PRO SER LEU THR VAL SER
SEQRES 2 M 215 PRO GLY GLY THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 M 215 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN
SEQRES 4 M 215 GLN LYS PRO GLY GLN ALA PHE ARG GLY LEU ILE GLY ASP
SEQRES 5 M 215 THR ASN ASN ARG ALA PRO TRP THR PRO ALA ARG PHE SER
SEQRES 6 M 215 GLY SER LEU LEU GLY GLY LYS ALA ALA LEU THR LEU SER
SEQRES 7 M 215 GLY VAL GLN PRO GLU ASP GLU ALA GLU TYR TYR CYS ALA
SEQRES 8 M 215 LEU TRP TYR SER ASN HIS PHE ILE PHE GLY SER GLY THR
SEQRES 9 M 215 LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER
SEQRES 10 M 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA
SEQRES 11 M 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR
SEQRES 12 M 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER
SEQRES 13 M 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS
SEQRES 14 M 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER
SEQRES 15 M 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER
SEQRES 16 M 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR
SEQRES 17 M 215 VAL ALA PRO THR GLU CYS SER
SEQRES 1 I 225 GLN VAL GLN LEU VAL GLN SER GLY SER GLU LEU LYS LYS
SEQRES 2 I 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 I 225 TYR THR PHE THR ASP TYR SER MET ARG TRP VAL ARG GLN
SEQRES 4 I 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN
SEQRES 5 I 225 THR GLU THR GLY SER PRO THR TYR ALA ASP ASP PHE LYS
SEQRES 6 I 225 GLY ARG PHE VAL PHE SER LEU ASP THR SER VAL SER THR
SEQRES 7 I 225 ALA TYR LEU GLN ILE SER SER LEU LYS ALA GLU ASP THR
SEQRES 8 I 225 ALA VAL TYR TYR CYS ALA ARG GLY PHE ALA TYR TRP GLY
SEQRES 9 I 225 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS
SEQRES 10 I 225 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 11 I 225 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 12 I 225 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 13 I 225 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 14 I 225 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL
SEQRES 15 I 225 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 16 I 225 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 17 I 225 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR
SEQRES 18 I 225 CYS PRO PRO CYS
FORMUL 7 HOH *315(H2 O)
HELIX 1 1 SER A 81 MET A 93 1 13
HELIX 2 2 VAL A 106 GLY A 110 1 5
HELIX 3 3 ARG A 124 THR A 128 5 5
HELIX 4 4 ALA A 201 PHE A 205 5 5
HELIX 5 5 PRO A 206 ARG A 210 5 5
HELIX 6 6 VAL A 211 SER A 213 5 3
HELIX 7 7 TYR A 243 ARG A 247 5 5
HELIX 8 8 SER A 318 ASP A 326 1 9
HELIX 9 9 PHE A 396 HIS A 407 1 12
HELIX 10 10 SER B 81 MET B 93 1 13
HELIX 11 11 VAL B 106 GLY B 110 1 5
HELIX 12 12 ARG B 124 THR B 128 5 5
HELIX 13 13 ALA B 201 PHE B 205 5 5
HELIX 14 14 PRO B 206 ARG B 210 5 5
HELIX 15 15 VAL B 211 SER B 213 5 3
HELIX 16 16 TYR B 243 ARG B 247 5 5
HELIX 17 17 SER B 318 ASP B 326 1 9
HELIX 18 18 PHE B 396 HIS B 407 1 12
HELIX 19 19 THR H 28 TYR H 32 5 5
HELIX 20 20 ASP H 61 LYS H 64 5 4
HELIX 21 21 THR H 73 VAL H 75 5 3
HELIX 22 22 LYS H 83 THR H 87 5 5
HELIX 23 23 SER H 156 ALA H 158 5 3
HELIX 24 24 PRO H 185 LEU H 189 5 5
HELIX 25 25 THR I 28 TYR I 32 5 5
HELIX 26 26 ASP I 61 LYS I 64 5 4
HELIX 27 27 THR I 73 VAL I 75 5 3
HELIX 28 28 LYS I 83 THR I 87 5 5
HELIX 29 29 SER I 156 ALA I 158 5 3
HELIX 30 30 PRO I 185 LEU I 189 5 5
HELIX 31 31 THR L 28 TYR L 32 5 5
HELIX 32 32 GLN L 79 GLU L 83 5 5
HELIX 33 33 SER L 122 GLN L 127 1 6
HELIX 34 34 THR L 182 LYS L 187 1 6
HELIX 35 35 THR M 28 TYR M 32 5 5
HELIX 36 36 GLN M 79 GLU M 83 5 5
HELIX 37 37 SER M 122 GLN M 127 1 6
HELIX 38 38 THR M 182 HIS M 189 1 8
SHEET 1 A 5 VAL A 54 VAL A 56 0
SHEET 2 A 5 LEU A 63 ASP A 67 -1 O MET A 64 N GLN A 55
SHEET 3 A 5 THR A 72 LEU A 76 -1 O THR A 72 N ASP A 67
SHEET 4 A 5 PHE A 117 VAL A 120 1 O PHE A 118 N LEU A 75
SHEET 5 A 5 ILE A 135 CYS A 138 -1 O SER A 136 N CYS A 119
SHEET 1 B 2 ALA A 98 ASP A 105 0
SHEET 2 B 2 ARG A 144 CYS A 150 -1 O ALA A 147 N SER A 102
SHEET 1 C 8 LEU A 230 LEU A 232 0
SHEET 2 C 8 TRP A 215 ALA A 219 -1 N VAL A 217 O LEU A 232
SHEET 3 C 8 GLN A 177 TYR A 182 -1 N SER A 179 O PHE A 218
SHEET 4 C 8 ALA A 185 SER A 194 -1 O CYS A 188 N LEU A 180
SHEET 5 C 8 TRP A 197 THR A 200 -1 O LEU A 199 N SER A 191
SHEET 6 C 8 ALA A 259 LEU A 263 -1 O VAL A 261 N VAL A 198
SHEET 7 C 8 VAL A 234 HIS A 240 -1 N VAL A 238 O LEU A 260
SHEET 8 C 8 GLY A 412 GLN A 416 1 O VAL A 414 N TYR A 239
SHEET 1 D 7 ILE A 290 GLY A 295 0
SHEET 2 D 7 GLN A 310 ILE A 317 -1 O GLN A 310 N GLY A 295
SHEET 3 D 7 MET A 336 ALA A 339 -1 O CYS A 338 N ILE A 317
SHEET 4 D 7 GLY A 388 LYS A 392 -1 O TYR A 390 N PHE A 337
SHEET 5 D 7 ARG A 368 VAL A 375 -1 N ILE A 374 O THR A 391
SHEET 6 D 7 PRO A 356 ASP A 361 -1 N CYS A 359 O ARG A 370
SHEET 7 D 7 ILE A 290 GLY A 295 -1 N THR A 292 O VAL A 358
SHEET 1 E 5 VAL B 54 VAL B 56 0
SHEET 2 E 5 LEU B 63 ASP B 67 -1 O MET B 64 N GLN B 55
SHEET 3 E 5 THR B 72 LEU B 76 -1 O THR B 72 N ASP B 67
SHEET 4 E 5 PHE B 117 VAL B 120 1 O PHE B 118 N LEU B 75
SHEET 5 E 5 ILE B 135 CYS B 138 -1 O SER B 136 N CYS B 119
SHEET 1 F 2 ALA B 98 ASP B 105 0
SHEET 2 F 2 ARG B 144 CYS B 150 -1 O ALA B 147 N SER B 102
SHEET 1 G 8 LEU B 230 LEU B 232 0
SHEET 2 G 8 TRP B 215 ALA B 219 -1 N VAL B 217 O LEU B 232
SHEET 3 G 8 GLN B 177 TYR B 182 -1 N SER B 179 O PHE B 218
SHEET 4 G 8 ALA B 185 SER B 194 -1 O CYS B 188 N LEU B 180
SHEET 5 G 8 TRP B 197 THR B 200 -1 O LEU B 199 N SER B 191
SHEET 6 G 8 ALA B 259 LEU B 263 -1 O VAL B 261 N VAL B 198
SHEET 7 G 8 VAL B 234 HIS B 240 -1 N VAL B 238 O LEU B 260
SHEET 8 G 8 GLY B 412 GLN B 416 1 O VAL B 414 N TYR B 239
SHEET 1 H 7 ILE B 290 GLY B 295 0
SHEET 2 H 7 GLN B 310 ILE B 317 -1 O GLN B 310 N GLY B 295
SHEET 3 H 7 MET B 336 ALA B 339 -1 O CYS B 338 N ILE B 317
SHEET 4 H 7 GLY B 388 LYS B 392 -1 O TYR B 390 N PHE B 337
SHEET 5 H 7 ARG B 368 VAL B 375 -1 N ILE B 374 O THR B 391
SHEET 6 H 7 PRO B 356 ASP B 361 -1 N CYS B 359 O ARG B 370
SHEET 7 H 7 ILE B 290 GLY B 295 -1 N THR B 292 O VAL B 358
SHEET 1 I 4 GLN H 3 GLN H 6 0
SHEET 2 I 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5
SHEET 3 I 4 THR H 77 ILE H 82 -1 O LEU H 80 N VAL H 20
SHEET 4 I 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 J 6 GLU H 10 LYS H 12 0
SHEET 2 J 6 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10
SHEET 3 J 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107
SHEET 4 J 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 J 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36
SHEET 6 J 6 PRO H 57 TYR H 59 -1 O THR H 58 N TRP H 50
SHEET 1 K 4 GLU H 10 LYS H 12 0
SHEET 2 K 4 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10
SHEET 3 K 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107
SHEET 4 K 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 L 4 SER H 120 LEU H 124 0
SHEET 2 L 4 LEU H 138 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 L 4 TYR H 176 VAL H 182 -1 O TYR H 176 N TYR H 145
SHEET 4 L 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 M 4 SER H 120 LEU H 124 0
SHEET 2 M 4 LEU H 138 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 M 4 TYR H 176 VAL H 182 -1 O TYR H 176 N TYR H 145
SHEET 4 M 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 N 3 THR H 151 TRP H 154 0
SHEET 2 N 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 N 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200
SHEET 1 O 4 GLN I 3 GLN I 6 0
SHEET 2 O 4 VAL I 18 SER I 25 -1 O LYS I 23 N VAL I 5
SHEET 3 O 4 THR I 77 ILE I 82 -1 O LEU I 80 N VAL I 20
SHEET 4 O 4 PHE I 67 ASP I 72 -1 N SER I 70 O TYR I 79
SHEET 1 P 6 GLU I 10 LYS I 12 0
SHEET 2 P 6 THR I 107 VAL I 111 1 O LEU I 108 N GLU I 10
SHEET 3 P 6 ALA I 88 ARG I 94 -1 N TYR I 90 O THR I 107
SHEET 4 P 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 91
SHEET 5 P 6 LEU I 45 ILE I 51 -1 O MET I 48 N TRP I 36
SHEET 6 P 6 PRO I 57 TYR I 59 -1 O THR I 58 N TRP I 50
SHEET 1 Q 4 GLU I 10 LYS I 12 0
SHEET 2 Q 4 THR I 107 VAL I 111 1 O LEU I 108 N GLU I 10
SHEET 3 Q 4 ALA I 88 ARG I 94 -1 N TYR I 90 O THR I 107
SHEET 4 Q 4 TYR I 102 TRP I 103 -1 O TYR I 102 N ARG I 94
SHEET 1 R 4 SER I 120 LEU I 124 0
SHEET 2 R 4 ALA I 136 TYR I 145 -1 O LEU I 141 N PHE I 122
SHEET 3 R 4 TYR I 176 VAL I 184 -1 O VAL I 184 N ALA I 136
SHEET 4 R 4 VAL I 163 THR I 165 -1 N HIS I 164 O VAL I 181
SHEET 1 S 4 SER I 120 LEU I 124 0
SHEET 2 S 4 ALA I 136 TYR I 145 -1 O LEU I 141 N PHE I 122
SHEET 3 S 4 TYR I 176 VAL I 184 -1 O VAL I 184 N ALA I 136
SHEET 4 S 4 VAL I 169 LEU I 170 -1 N VAL I 169 O SER I 177
SHEET 1 T 3 THR I 151 TRP I 154 0
SHEET 2 T 3 ILE I 195 HIS I 200 -1 O ASN I 197 N SER I 153
SHEET 3 T 3 THR I 205 LYS I 210 -1 O THR I 205 N HIS I 200
SHEET 1 U 4 VAL L 4 GLN L 6 0
SHEET 2 U 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5
SHEET 3 U 4 ALA L 71 LEU L 75 -1 O LEU L 75 N VAL L 19
SHEET 4 U 4 PHE L 62 LEU L 66 -1 N SER L 63 O THR L 74
SHEET 1 V 6 SER L 9 VAL L 13 0
SHEET 2 V 6 THR L 102 VAL L 106 1 O LYS L 103 N LEU L 11
SHEET 3 V 6 ALA L 84 TYR L 92 -1 N ALA L 84 O VAL L 104
SHEET 4 V 6 ASN L 34 GLN L 38 -1 N VAL L 36 O TYR L 87
SHEET 5 V 6 PHE L 44 GLY L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 V 6 ASN L 53 ARG L 54 -1 O ASN L 53 N GLY L 49
SHEET 1 W 4 SER L 9 VAL L 13 0
SHEET 2 W 4 THR L 102 VAL L 106 1 O LYS L 103 N LEU L 11
SHEET 3 W 4 ALA L 84 TYR L 92 -1 N ALA L 84 O VAL L 104
SHEET 4 W 4 HIS L 95 PHE L 98 -1 O HIS L 95 N TYR L 92
SHEET 1 X 4 SER L 115 PHE L 119 0
SHEET 2 X 4 ALA L 131 PHE L 140 -1 O VAL L 134 N PHE L 119
SHEET 3 X 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135
SHEET 4 X 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178
SHEET 1 Y 4 SER L 115 PHE L 119 0
SHEET 2 Y 4 ALA L 131 PHE L 140 -1 O VAL L 134 N PHE L 119
SHEET 3 Y 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135
SHEET 4 Y 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174
SHEET 1 Z 4 PRO L 155 VAL L 156 0
SHEET 2 Z 4 THR L 146 LYS L 150 -1 N TRP L 149 O VAL L 156
SHEET 3 Z 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 Z 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196
SHEET 1 AA 4 VAL M 4 GLN M 6 0
SHEET 2 AA 4 VAL M 19 SER M 25 -1 O ARG M 24 N THR M 5
SHEET 3 AA 4 ALA M 71 LEU M 75 -1 O LEU M 75 N VAL M 19
SHEET 4 AA 4 PHE M 62 LEU M 66 -1 N SER M 63 O THR M 74
SHEET 1 AB 6 SER M 9 VAL M 13 0
SHEET 2 AB 6 THR M 102 VAL M 106 1 O LYS M 103 N LEU M 11
SHEET 3 AB 6 ALA M 84 TRP M 91 -1 N ALA M 84 O VAL M 104
SHEET 4 AB 6 ASN M 34 GLN M 38 -1 N VAL M 36 O TYR M 87
SHEET 5 AB 6 PHE M 44 GLY M 49 -1 O LEU M 47 N TRP M 35
SHEET 6 AB 6 ASN M 53 ARG M 54 -1 O ASN M 53 N GLY M 49
SHEET 1 AC 4 SER M 9 VAL M 13 0
SHEET 2 AC 4 THR M 102 VAL M 106 1 O LYS M 103 N LEU M 11
SHEET 3 AC 4 ALA M 84 TRP M 91 -1 N ALA M 84 O VAL M 104
SHEET 4 AC 4 PHE M 96 PHE M 98 -1 O ILE M 97 N LEU M 90
SHEET 1 AD 4 SER M 115 PHE M 119 0
SHEET 2 AD 4 ALA M 131 PHE M 140 -1 O VAL M 134 N PHE M 119
SHEET 3 AD 4 TYR M 173 LEU M 181 -1 O SER M 177 N CYS M 135
SHEET 4 AD 4 VAL M 160 THR M 162 -1 N GLU M 161 O TYR M 178
SHEET 1 AE 4 SER M 115 PHE M 119 0
SHEET 2 AE 4 ALA M 131 PHE M 140 -1 O VAL M 134 N PHE M 119
SHEET 3 AE 4 TYR M 173 LEU M 181 -1 O SER M 177 N CYS M 135
SHEET 4 AE 4 SER M 166 LYS M 167 -1 N SER M 166 O ALA M 174
SHEET 1 AF 4 PRO M 155 VAL M 156 0
SHEET 2 AF 4 THR M 146 LYS M 150 -1 N TRP M 149 O VAL M 156
SHEET 3 AF 4 TYR M 192 HIS M 198 -1 O GLN M 195 N ALA M 148
SHEET 4 AF 4 SER M 201 VAL M 207 -1 O VAL M 203 N VAL M 196
SSBOND 1 CYS A 77 CYS A 140 1555 1555 2.05
SSBOND 2 CYS A 90 CYS A 150 1555 1555 2.04
SSBOND 3 CYS A 119 CYS A 138 1555 1555 2.03
SSBOND 4 CYS A 153 CYS A 277 1555 1555 2.04
SSBOND 5 CYS A 188 CYS A 204 1555 1555 2.05
SSBOND 6 CYS A 291 CYS A 359 1555 1555 2.04
SSBOND 7 CYS A 322 CYS A 338 1555 1555 2.04
SSBOND 8 CYS B 77 CYS B 140 1555 1555 2.02
SSBOND 9 CYS B 90 CYS B 150 1555 1555 2.05
SSBOND 10 CYS B 119 CYS B 138 1555 1555 2.04
SSBOND 11 CYS B 153 CYS B 277 1555 1555 2.04
SSBOND 12 CYS B 188 CYS B 204 1555 1555 2.02
SSBOND 13 CYS B 291 CYS B 359 1555 1555 2.05
SSBOND 14 CYS B 322 CYS B 338 1555 1555 2.03
SSBOND 15 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 16 CYS H 140 CYS H 196 1555 1555 2.05
SSBOND 17 CYS I 22 CYS I 92 1555 1555 2.06
SSBOND 18 CYS I 140 CYS I 196 1555 1555 2.05
SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 20 CYS L 135 CYS L 194 1555 1555 2.03
SSBOND 21 CYS M 23 CYS M 88 1555 1555 2.03
SSBOND 22 CYS M 135 CYS M 194 1555 1555 2.04
CISPEP 1 PHE H 146 PRO H 147 0 -5.06
CISPEP 2 GLU H 148 PRO H 149 0 4.57
CISPEP 3 PHE I 146 PRO I 147 0 -4.27
CISPEP 4 GLU I 148 PRO I 149 0 5.86
CISPEP 5 TYR L 141 PRO L 142 0 -2.25
CISPEP 6 TYR M 141 PRO M 142 0 -1.49
CISPEP 7 PRO M 209 THR M 210 0 21.23
CRYST1 62.980 66.580 108.330 88.71 94.30 104.53 P 1 2
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 0.015878 0.004115 0.001178 0.00000
SCALE2 0.000000 0.015516 -0.000059 0.00000
SCALE3 0.000000 0.000000 0.009257 0.00000
(ATOM LINES ARE NOT SHOWN.)
END