HEADER HYDROLASE/HYDROLASE INHIBITOR 01-OCT-09 2WUC
TITLE CRYSTAL STRUCTURE OF HGFA IN COMPLEX WITH THE ALLOSTERIC NON-
TITLE 2 INHIBITORY ANTIBODY FAB40.DELTATRP AND AC-KQLR-CHLOROMETHYLKETONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR ACTIVATOR LONG CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N-GLYCOSYLATION AT ASN74;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HEPATOCYTE GROWTH FACTOR ACTIVATOR SHORT CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 EC: 3.4.21.-;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: FAB FRAGMENT FAB40.DELTATRP HEAVY CHAIN;
COMPND 14 CHAIN: H;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: ACE-KQLR-CHLOROMETHYLKETONE INHIBITOR;
COMPND 18 CHAIN: I;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: FAB FRAGMENT FAB40.DELTATRP LIGHT CHAIN;
COMPND 22 CHAIN: L;
COMPND 23 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: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: BACULOGOLD;
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: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: BACULOGOLD;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: 33D3;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 MOL_ID: 4;
SOURCE 28 SYNTHETIC: YES;
SOURCE 29 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 30 ORGANISM_TAXID: 32630;
SOURCE 31 MOL_ID: 5;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 37 EXPRESSION_SYSTEM_STRAIN: 33D3;
SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS SERINE PROTEASE, EGF-LIKE DOMAIN, ALLOSTERIC INHIBITOR, KRINGLE,
KEYWDS 2 ANTIBODY, HYDROLASE, FAB COMPLEX, GLYCOPROTEIN, IMMUNE SYSTEM,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GANESAN,C.EIGENBROT,S.SHIA
REVDAT 7 20-DEC-23 2WUC 1 HETSYN SHEET
REVDAT 6 29-JUL-20 2WUC 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 01-JUL-20 2WUC 1 REMARK LINK ATOM
REVDAT 4 21-DEC-16 2WUC 1 SOURCE
REVDAT 3 06-JUN-12 2WUC 1 JRNL
REVDAT 2 13-JUL-11 2WUC 1 VERSN
REVDAT 1 15-DEC-09 2WUC 0
JRNL AUTH R.GANESAN,C.EIGENBROT,Y.WU,W.C.LIANG,S.SHIA,M.T.LIPARI,
JRNL AUTH 2 D.KIRCHHOFER
JRNL TITL UNRAVELING THE ALLOSTERIC MECHANISM OF SERINE PROTEASE
JRNL TITL 2 INHIBITION BY AN ANTIBODY
JRNL REF STRUCTURE V. 17 1614 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 20004165
JRNL DOI 10.1016/J.STR.2009.09.014
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2076852.150
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 24111
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 SET) : 0.226
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2388
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3498
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 370
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.23000
REMARK 3 B22 (A**2) : -5.28000
REMARK 3 B33 (A**2) : 7.51000
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.38
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 22.22
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NAG.PAR
REMARK 3 PARAMETER FILE 5 : MAI.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NAG.TOP
REMARK 3 TOPOLOGY FILE 5 : MAI.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2WUC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97607
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24263
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2WUB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 10,000, 100 MM HEPES PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 73.18550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.18550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.17950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.94450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.17950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.94450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.18550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.17950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 73.94450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.18550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.17950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 73.94450
REMARK 290 SMTRY3 8 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I, L, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE UNBOUND FORM OF THE INHIBITOR IS ACE-KQLR-CHLOROMETHYLKETONE.
REMARK 400 UPON REACTION WITH PROTEIN IT FORMS TWO COVALENT BONDS: 1) A
REMARK 400 COVALENT BOND TO SER 195 FORMING A HEMIKETAL AR7 AND 2) A COVALENT
REMARK 400 BOND TO NE2 OF HIS 57
REMARK 400
REMARK 400 THE N-ACETYL-6-AMMONIO-L-NORLEUCYL-L-GLUTAMINYL-N-[(1S)-4-{
REMARK 400 [AMINO(IMINIO)METHYL]AMINO}-1-(CHLOROACETYL)BUTYL]-L-LEUCINAMIDE IS
REMARK 400 PEPTIDE-LIKE, A MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: N-ACETYL-6-AMMONIO-L-NORLEUCYL-L-GLUTAMINYL-N-[(1S)-4-{
REMARK 400 [AMINO(IMINIO)METHYL]AMINO}-1-(CHLOROACETYL)BUTYL]-L-
REMARK 400 LEUCINAMIDE
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 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 ALA A 253
REMARK 465 ALA A 254
REMARK 465 ALA A 255
REMARK 465 HIS A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 VAL B 372
REMARK 465 GLN B 373
REMARK 465 LEU B 374
REMARK 465 SER B 375
REMARK 465 PRO B 376
REMARK 465 ASP B 377
REMARK 465 LEU B 378
REMARK 465 LEU B 379
REMARK 465 ALA B 380
REMARK 465 THR B 381
REMARK 465 LEU B 382
REMARK 465 PRO B 383
REMARK 465 GLU B 384
REMARK 465 PRO B 385
REMARK 465 ALA B 386
REMARK 465 SER B 387
REMARK 465 PRO B 388
REMARK 465 GLY B 389
REMARK 465 ARG B 390
REMARK 465 GLN B 391
REMARK 465 LYS B 399
REMARK 465 ARG B 400
REMARK 465 THR B 401
REMARK 465 PHE B 402
REMARK 465 LEU B 403
REMARK 465 ARG B 404
REMARK 465 PRO B 405
REMARK 465 ARG B 406
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 LYS H 218
REMARK 465 THR H 219
REMARK 465 HIS H 220
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO A 244 CA C O CB CG CD
REMARK 470 LYS B 398 CA C O CB CG CD CE
REMARK 470 LYS B 398 NZ
REMARK 470 ASP H 217 CA C O CB CG OD1 OD2
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 ND2 ASN A 74 C2 NAG C 1 2.16
REMARK 500 CD2 HIS A 57 C1 0QE I 6 2.17
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 L 2002 O HOH L 2002 4545 2.14
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 CYS H 22 CA - CB - SG ANGL. DEV. = 7.0 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 ASN A 98 55.53 -164.44
REMARK 500 LYS A 111 53.18 -111.84
REMARK 500 ARG A 111C -158.45 -151.17
REMARK 500 CYS A 111D -91.31 -109.27
REMARK 500 ALA A 158 138.28 -172.67
REMARK 500 VAL A 171 -92.42 -87.16
REMARK 500 CYS A 187 47.90 73.03
REMARK 500 LYS A 188 -72.94 -84.81
REMARK 500 SER A 214 -64.23 -124.61
REMARK 500 ARG A 243 63.63 37.65
REMARK 500 ARG B 396 -140.67 -89.09
REMARK 500 HIS B 397 -65.25 -148.10
REMARK 500 PHE H 27 151.42 175.26
REMARK 500 PRO H 41 114.74 -37.16
REMARK 500 ALA H 88 170.77 170.43
REMARK 500 ALA H 100A -177.19 -176.89
REMARK 500 SER H 127 -119.40 -89.89
REMARK 500 SER H 132 118.93 -167.87
REMARK 500 ASP H 144 77.57 48.24
REMARK 500 SER L 30 -112.81 56.76
REMARK 500 ALA L 32 48.91 -77.37
REMARK 500 PRO L 40 129.54 -38.39
REMARK 500 ALA L 51 -40.43 67.19
REMARK 500 ALA L 84 -171.42 -178.95
REMARK 500 ASN L 138 92.20 33.47
REMARK 500 ASN L 152 -15.52 70.95
REMARK 500 SER L 156 142.00 -171.37
REMARK 500 GLN L 166 135.40 -39.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU I 4 -15.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
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 FIRST KUNITZ DOMAIN FROM HAI-1
REMARK 900 RELATED ID: 2WUB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HGFA IN COMPLEX WITH THE ALLOSTERIC NON-
REMARK 900 INHIBITORY ANTIBODY FAB40. DELTATRP
DBREF 2WUC A 16 251 UNP Q04756 HGFA_HUMAN 408 655
DBREF 2WUC A 252 260 PDB 2WUC 2WUC 252 260
DBREF 2WUC B 372 406 UNP Q04756 HGFA_HUMAN 373 407
DBREF 2WUC H 1 220 PDB 2WUC 2WUC 1 220
DBREF 2WUC I 1 6 PDB 2WUC 2WUC 1 6
DBREF 2WUC L 1 214 PDB 2WUC 2WUC 1 214
SEQRES 1 A 257 ILE ILE GLY GLY SER SER SER LEU PRO GLY SER HIS PRO
SEQRES 2 A 257 TRP LEU ALA ALA ILE TYR ILE GLY ASP SER PHE CYS ALA
SEQRES 3 A 257 GLY SER LEU VAL HIS THR CYS TRP VAL VAL SER ALA ALA
SEQRES 4 A 257 HIS CYS PHE SER HIS SER PRO PRO ARG ASP SER VAL SER
SEQRES 5 A 257 VAL VAL LEU GLY GLN HIS PHE PHE ASN ARG THR THR ASP
SEQRES 6 A 257 VAL THR GLN THR PHE GLY ILE GLU LYS TYR ILE PRO TYR
SEQRES 7 A 257 THR LEU TYR SER VAL PHE ASN PRO SER ASP HIS ASP LEU
SEQRES 8 A 257 VAL LEU ILE ARG LEU LYS LYS LYS GLY ASP ARG CYS ALA
SEQRES 9 A 257 THR ARG SER GLN PHE VAL GLN PRO ILE CYS LEU PRO GLU
SEQRES 10 A 257 PRO GLY SER THR PHE PRO ALA GLY HIS LYS CYS GLN ILE
SEQRES 11 A 257 ALA GLY TRP GLY HIS LEU ASP GLU ASN VAL SER GLY TYR
SEQRES 12 A 257 SER SER SER LEU ARG GLU ALA LEU VAL PRO LEU VAL ALA
SEQRES 13 A 257 ASP HIS LYS CYS SER SER PRO GLU VAL TYR GLY ALA ASP
SEQRES 14 A 257 ILE SER PRO ASN MET LEU CYS ALA GLY TYR PHE ASP CYS
SEQRES 15 A 257 LYS SER ASP ALA CYS GLN GLY ASP SER GLY GLY PRO LEU
SEQRES 16 A 257 ALA CYS GLU LYS ASN GLY VAL ALA TYR LEU TYR GLY ILE
SEQRES 17 A 257 ILE SER TRP GLY ASP GLY CYS GLY ARG LEU HIS LYS PRO
SEQRES 18 A 257 GLY VAL TYR THR ARG VAL ALA ASN TYR VAL ASP TRP ILE
SEQRES 19 A 257 ASN ASP ARG ILE ARG PRO PRO ARG ARG LEU VAL ALA PRO
SEQRES 20 A 257 SER ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 35 VAL GLN LEU SER PRO ASP LEU LEU ALA THR LEU PRO GLU
SEQRES 2 B 35 PRO ALA SER PRO GLY ARG GLN ALA CYS GLY ARG ARG HIS
SEQRES 3 B 35 LYS LYS ARG THR PHE LEU ARG PRO ARG
SEQRES 1 H 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 224 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 224 PHE THR ILE ASN GLY THR TYR ILE HIS TRP VAL ARG GLN
SEQRES 4 H 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY GLY ILE TYR
SEQRES 5 H 224 PRO ALA GLY GLY ALA THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 H 224 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 H 224 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA LYS TRP ALA TRP PRO ALA PHE
SEQRES 9 H 224 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 10 H 224 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO
SEQRES 11 H 224 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY
SEQRES 12 H 224 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 224 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR
SEQRES 14 H 224 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU
SEQRES 15 H 224 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR
SEQRES 16 H 224 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN
SEQRES 17 H 224 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP
SEQRES 18 H 224 LYS THR HIS
SEQRES 1 I 6 ACE LYS GLN LEU AR7 0QE
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 ASN ARG ALA PRO ALA 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
MODRES 2WUC ASN A 74 ASN GLYCOSYLATION SITE
MODRES 2WUC AR7 I 5 ARG
HET ACE I 1 3
HET AR7 I 5 11
HET 0QE I 6 1
HET NAG C 1 14
HET NAG C 2 14
HETNAM ACE ACETYL GROUP
HETNAM AR7 AMINO{[(4S)-4-AMINO-5,5-
HETNAM 2 AR7 DIHYDROXYPENTYL]AMINO}METHANIMINIUM
HETNAM 0QE CHLOROMETHANE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN 0QE CHLORO METHYL GROUP
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 4 ACE C2 H4 O
FORMUL 4 AR7 C6 H17 N4 O2 1+
FORMUL 4 0QE C H3 CL
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 HOH *131(H2 O)
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 169 1 6
HELIX 4 4 TYR A 172 ILE A 176 5 5
HELIX 5 5 VAL A 231 ASN A 233 5 3
HELIX 6 6 TYR A 234 ARG A 243 1 10
HELIX 7 7 ASP H 61 LYS H 64 5 4
HELIX 8 8 ARG H 83 THR H 87 5 5
HELIX 9 9 SER H 156 ALA H 158 5 3
HELIX 10 10 LYS H 201 ASN H 204 5 4
HELIX 11 11 GLN L 79 PHE L 83 5 5
HELIX 12 12 GLN L 124 SER L 127 5 4
HELIX 13 13 LYS L 183 LYS L 188 1 6
SHEET 1 AA 7 SER A 20 SER A 21 0
SHEET 2 AA 7 ARG A 156 PRO A 161 -1 O GLU A 157 N SER A 20
SHEET 3 AA 7 LYS A 135 GLY A 140 -1 O CYS A 136 N VAL A 160
SHEET 4 AA 7 PRO A 198 LYS A 203 -1 O ALA A 200 N GLN A 137
SHEET 5 AA 7 VAL A 206 TRP A 215 -1 O VAL A 206 N LYS A 203
SHEET 6 AA 7 GLY A 226 THR A 229 -1 O VAL A 227 N TRP A 215
SHEET 7 AA 7 MET A 180 ALA A 183 -1 O LEU A 181 N TYR A 228
SHEET 1 AB 7 LEU A 30 ILE A 35 0
SHEET 2 AB 7 SER A 40 HIS A 48 -1 O SER A 40 N ILE A 35
SHEET 3 AB 7 TRP A 51 SER A 54 -1 O TRP A 51 N VAL A 47
SHEET 4 AB 7 VAL A 104 LEU A 108 -1 O VAL A 104 N SER A 54
SHEET 5 AB 7 GLN A 81 PRO A 90 -1 N GLU A 86 O ARG A 107
SHEET 6 AB 7 VAL A 64 LEU A 68 -1 O VAL A 64 N ILE A 85
SHEET 7 AB 7 LEU A 30 ILE A 35 -1 O ALA A 32 N VAL A 67
SHEET 1 HA 4 GLN H 3 SER H 7 0
SHEET 2 HA 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7
SHEET 3 HA 4 THR H 77 MET H 82 -1 O ALA H 78 N CYS H 22
SHEET 4 HA 4 PHE H 67 ASP H 72 -1 O THR H 68 N GLN H 81
SHEET 1 HB 8 GLY H 10 VAL H 12 0
SHEET 2 HB 8 THR H 107 VAL H 111 1 O LEU H 108 N GLY H 10
SHEET 3 HB 8 ALA H 88 TYR H 91 -1 O ALA H 88 N VAL H 109
SHEET 4 HB 8 TYR H 33 GLN H 39 -1 O VAL H 37 N TYR H 91
SHEET 5 HB 8 ALA H 56 TYR H 59 0
SHEET 6 HB 8 GLU H 46 TYR H 52 -1 O GLY H 50 N TYR H 58
SHEET 7 HB 8 LYS H 94 TRP H 95 -1 O TRP H 95 N TYR H 33
SHEET 8 HB 8 TYR H 33 GLN H 39 -1 O TYR H 33 N TRP H 95
SHEET 1 HC 6 SER H 120 LEU H 124 0
SHEET 2 HC 6 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 HC 6 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 HC 6 VAL H 163 THR H 165 -1 O HIS H 164 N VAL H 181
SHEET 5 HC 6 VAL H 169 LEU H 170 -1 O VAL H 169 N SER H 177
SHEET 6 HC 6 TYR H 176 PRO H 185 -1 O SER H 177 N VAL H 169
SHEET 1 HD 3 THR H 151 TRP H 154 0
SHEET 2 HD 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 HD 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200
SHEET 1 LA 4 MET L 4 SER L 7 0
SHEET 2 LA 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 LA 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 LA 4 PHE L 62 GLY L 66 -1 O SER L 63 N THR L 74
SHEET 1 LB 8 SER L 10 SER L 14 0
SHEET 2 LB 8 THR L 102 LYS L 107 1 O LYS L 103 N LEU L 11
SHEET 3 LB 8 ALA L 84 GLN L 90 -1 O ALA L 84 N VAL L 104
SHEET 4 LB 8 PHE L 53 LEU L 54 0
SHEET 5 LB 8 LYS L 45 TYR L 49 -1 O TYR L 49 N PHE L 53
SHEET 6 LB 8 VAL L 33 GLN L 38 -1 O TRP L 35 N LEU L 47
SHEET 7 LB 8 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 8 LB 8 ALA L 84 GLN L 90 -1 O GLN L 90 N THR L 97
SHEET 1 LC 4 SER L 114 PHE L 118 0
SHEET 2 LC 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 LC 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139
SHEET 4 LC 4 SER L 159 VAL L 163 -1 O GLN L 160 N THR L 178
SHEET 1 LD 4 ALA L 153 LEU L 154 0
SHEET 2 LD 4 LYS L 145 VAL L 150 -1 O VAL L 150 N ALA L 153
SHEET 3 LD 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149
SHEET 4 LD 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.04
SSBOND 2 CYS A 50 CYS A 111D 1555 1555 2.04
SSBOND 3 CYS A 122 CYS B 393 1555 1555 2.03
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.04
SSBOND 7 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 8 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 9 CYS H 216 CYS L 214 1555 1555 2.03
SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.06
SSBOND 11 CYS L 134 CYS L 194 1555 1555 2.04
LINK NE2 HIS A 57 C1 0QE I 6 1555 1555 1.43
LINK ND2 ASN A 74 C1 NAG C 1 1555 1555 1.52
LINK OG SER A 195 C AR7 I 5 1555 1555 1.46
LINK C ACE I 1 N LYS I 2 1555 1555 1.34
LINK C LEU I 4 N AR7 I 5 1555 1555 1.33
LINK C AR7 I 5 C1 0QE I 6 1555 1555 1.55
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.59
CISPEP 1 PHE H 146 PRO H 147 0 0.08
CISPEP 2 GLU H 148 PRO H 149 0 0.70
CISPEP 3 SER L 7 PRO L 8 0 -1.11
CISPEP 4 ALA L 94 PRO L 95 0 1.17
CISPEP 5 TYR L 140 PRO L 141 0 2.12
CRYST1 80.359 147.889 146.371 90.00 90.00 90.00 C 2 2 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 0.012444 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
