HEADER HYDROLASE 05-FEB-02 1KYN
TITLE CATHEPSIN-G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN G;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CG;
COMPND 5 EC: 3.4.21.20
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS SERINE PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.N.GRECO,M.J.HAWKINS,E.T.POWELL,H.R.ALMOND JR.,
AUTHOR 2 T.W.CORCORAN,L.DE GARAVILLA,J.A.KAUFFMAN,R.RECACHA,
AUTHOR 3 D.CHATTOPADHYAY,P.ANDRADE-GORDON,B.E.MARYANOFF
REVDAT 3 01-APR-08 1KYN 1 COMPND SEQRES ATOM SOURCE
REVDAT 3 2 1 VERSN
REVDAT 2 01-APR-03 1KYN 1 JRNL
REVDAT 1 01-MAY-02 1KYN 0
JRNL AUTH M.N.GRECO,M.J.HAWKINS,E.T.POWELL,H.R.ALMOND JR.,
JRNL AUTH 2 T.W.CORCORAN,L.DE GARAVILLA,J.A.KAUFFMAN,R.RECACHA,
JRNL AUTH 3 D.CHATTOPADHYAY,P.ANDRADE-GORDON,B.E.MARYANOFF
JRNL TITL NONPEPTIDE INHIBITORS OF CATHEPSIN G: OPTIMIZATION
JRNL TITL 2 OF A NOVEL BETA-KETOPHOSPHONIC ACID LEAD BY
JRNL TITL 3 STRUCTURE-BASED DRUG DESIGN.
JRNL REF J.AM.CHEM.SOC. V. 124 3810 2002
JRNL REFN ISSN 0002-7863
JRNL PMID 11942800
JRNL DOI 10.1021/JA017506H
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1184420.360
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 72.6
REMARK 3 NUMBER OF REFLECTIONS : 4111
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) : 0.258
REMARK 3 FREE R VALUE : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.000
REMARK 3 FREE R VALUE TEST SET COUNT : 453
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.015
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) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 603
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3553
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.39
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.57
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.61
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73
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 NCS MODEL : NULL
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 : PAR.TXT
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-02.
REMARK 100 THE RCSB ID CODE IS RCSB015474.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 65.31000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.65500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 97.96500
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 244
REMARK 465 PHE A 245
REMARK 465 LYS A 246
REMARK 465 LEU A 247
REMARK 465 LEU A 248
REMARK 465 ASP A 249
REMARK 465 GLN A 250
REMARK 465 MET A 251
REMARK 465 GLU A 252
REMARK 465 THR A 253
REMARK 465 PRO A 254
REMARK 465 LEU A 255
REMARK 465 LYS B 546
REMARK 465 LEU B 547
REMARK 465 LEU B 548
REMARK 465 ASP B 549
REMARK 465 GLN B 550
REMARK 465 MET B 551
REMARK 465 GLU B 552
REMARK 465 THR B 553
REMARK 465 PRO B 554
REMARK 465 LEU B 555
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 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 339 CB CG CD OE1 NE2
REMARK 470 ARG B 539 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 545 CB CG CD1 CD2 CE1 CE2 CZ
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 24 117.75 -33.82
REMARK 500 ILE A 35 0.46 -66.66
REMARK 500 GLN A 36 78.32 -65.05
REMARK 500 SER A 36A -61.58 177.23
REMARK 500 ALA A 37 82.21 -151.89
REMARK 500 GLN A 39 66.47 -151.60
REMARK 500 ARG A 41 155.23 -44.26
REMARK 500 ASN A 63 87.86 -174.31
REMARK 500 HIS A 71 -54.71 -136.60
REMARK 500 ARG A 87 117.77 -160.05
REMARK 500 PRO A 120 160.12 -44.22
REMARK 500 GLN A 127 11.15 59.96
REMARK 500 LEU A 130 78.37 -155.12
REMARK 500 GLN A 167 -71.62 -51.75
REMARK 500 ILE A 171 -64.02 -123.33
REMARK 500 ARG A 188A 47.50 -79.18
REMARK 500 ALA A 189 170.38 176.52
REMARK 500 PHE A 191 -155.76 -149.06
REMARK 500 ASN A 202 41.48 71.30
REMARK 500 ALA A 209 98.50 -56.51
REMARK 500 SER A 214 -83.17 -95.53
REMARK 500 SER A 218 -1.32 -56.96
REMARK 500 PRO B 324 117.59 -33.79
REMARK 500 GLN B 334 70.85 -119.13
REMARK 500 ILE B 335 62.25 -170.03
REMARK 500 GLN B 336 34.92 -78.15
REMARK 500 ALA B 337 -2.88 -177.60
REMARK 500 ARG B 341 113.81 177.14
REMARK 500 ASN B 363 89.02 -173.10
REMARK 500 HIS B 371 -54.49 -136.67
REMARK 500 PRO B 420 160.07 -44.68
REMARK 500 GLN B 427 11.18 59.79
REMARK 500 LEU B 430 77.72 -155.04
REMARK 500 GLN B 467 -71.37 -51.96
REMARK 500 ILE B 471 -63.69 -123.17
REMARK 500 ARG B 488A 47.75 -79.54
REMARK 500 ALA B 489 170.34 176.62
REMARK 500 PHE B 491 -155.60 -148.97
REMARK 500 ASN B 502 41.60 71.10
REMARK 500 ALA B 509 98.67 -56.59
REMARK 500 SER B 514 -83.33 -95.57
REMARK 500 SER B 518 -1.09 -57.12
REMARK 500 ARG B 543 -149.43 -82.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KTP A 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KTP B 701
DBREF 1KYN A 16 255 UNP P08311 CATG_HUMAN 21 255
DBREF 1KYN B 316 555 UNP P08311 CATG_HUMAN 21 255
SEQRES 1 A 235 ILE ILE GLY GLY ARG GLU SER ARG PRO HIS SER ARG PRO
SEQRES 2 A 235 TYR MET ALA TYR LEU GLN ILE GLN SER PRO ALA GLY GLN
SEQRES 3 A 235 SER ARG CYS GLY GLY PHE LEU VAL ARG GLU ASP PHE VAL
SEQRES 4 A 235 LEU THR ALA ALA HIS CYS TRP GLY SER ASN ILE ASN VAL
SEQRES 5 A 235 THR LEU GLY ALA HIS ASN ILE GLN ARG ARG GLU ASN THR
SEQRES 6 A 235 GLN GLN HIS ILE THR ALA ARG ARG ALA ILE ARG HIS PRO
SEQRES 7 A 235 GLN TYR ASN GLN ARG THR ILE GLN ASN ASP ILE MET LEU
SEQRES 8 A 235 LEU GLN LEU SER ARG ARG VAL ARG ARG ASN ARG ASN VAL
SEQRES 9 A 235 ASN PRO VAL ALA LEU PRO ARG ALA GLN GLU GLY LEU ARG
SEQRES 10 A 235 PRO GLY THR LEU CYS THR VAL ALA GLY TRP GLY ARG VAL
SEQRES 11 A 235 SER MET ARG ARG GLY THR ASP THR LEU ARG GLU VAL GLN
SEQRES 12 A 235 LEU ARG VAL GLN ARG ASP ARG GLN CYS LEU ARG ILE PHE
SEQRES 13 A 235 GLY SER TYR ASP PRO ARG ARG GLN ILE CYS VAL GLY ASP
SEQRES 14 A 235 ARG ARG GLU ARG LYS ALA ALA PHE LYS GLY ASP SER GLY
SEQRES 15 A 235 GLY PRO LEU LEU CYS ASN ASN VAL ALA HIS GLY ILE VAL
SEQRES 16 A 235 SER TYR GLY LYS SER SER GLY VAL PRO PRO GLU VAL PHE
SEQRES 17 A 235 THR ARG VAL SER SER PHE LEU PRO TRP ILE ARG THR THR
SEQRES 18 A 235 MET ARG SER PHE LYS LEU LEU ASP GLN MET GLU THR PRO
SEQRES 19 A 235 LEU
SEQRES 1 B 235 ILE ILE GLY GLY ARG GLU SER ARG PRO HIS SER ARG PRO
SEQRES 2 B 235 TYR MET ALA TYR LEU GLN ILE GLN SER PRO ALA GLY GLN
SEQRES 3 B 235 SER ARG CYS GLY GLY PHE LEU VAL ARG GLU ASP PHE VAL
SEQRES 4 B 235 LEU THR ALA ALA HIS CYS TRP GLY SER ASN ILE ASN VAL
SEQRES 5 B 235 THR LEU GLY ALA HIS ASN ILE GLN ARG ARG GLU ASN THR
SEQRES 6 B 235 GLN GLN HIS ILE THR ALA ARG ARG ALA ILE ARG HIS PRO
SEQRES 7 B 235 GLN TYR ASN GLN ARG THR ILE GLN ASN ASP ILE MET LEU
SEQRES 8 B 235 LEU GLN LEU SER ARG ARG VAL ARG ARG ASN ARG ASN VAL
SEQRES 9 B 235 ASN PRO VAL ALA LEU PRO ARG ALA GLN GLU GLY LEU ARG
SEQRES 10 B 235 PRO GLY THR LEU CYS THR VAL ALA GLY TRP GLY ARG VAL
SEQRES 11 B 235 SER MET ARG ARG GLY THR ASP THR LEU ARG GLU VAL GLN
SEQRES 12 B 235 LEU ARG VAL GLN ARG ASP ARG GLN CYS LEU ARG ILE PHE
SEQRES 13 B 235 GLY SER TYR ASP PRO ARG ARG GLN ILE CYS VAL GLY ASP
SEQRES 14 B 235 ARG ARG GLU ARG LYS ALA ALA PHE LYS GLY ASP SER GLY
SEQRES 15 B 235 GLY PRO LEU LEU CYS ASN ASN VAL ALA HIS GLY ILE VAL
SEQRES 16 B 235 SER TYR GLY LYS SER SER GLY VAL PRO PRO GLU VAL PHE
SEQRES 17 B 235 THR ARG VAL SER SER PHE LEU PRO TRP ILE ARG THR THR
SEQRES 18 B 235 MET ARG SER PHE LYS LEU LEU ASP GLN MET GLU THR PRO
SEQRES 19 B 235 LEU
HET KTP A 601 27
HET KTP B 701 27
HETNAM KTP (2-NAPHTHALEN-2-YL-1-NAPHTHALEN-1-YL-2-OXO-ETHYL)-
HETNAM 2 KTP PHOSPHONIC ACID
HETSYN KTP BIS-NAPTHYL BETA-KETOPHOSPHONIC ACID
FORMUL 3 KTP 2(C22 H17 O4 P)
HELIX 1 1 ARG A 164 ARG A 170 1 7
HELIX 2 2 PHE A 234 ARG A 243 1 10
HELIX 3 3 ARG B 464 ARG B 470 1 7
HELIX 4 4 PHE B 534 ARG B 543 1 10
SHEET 1 A 7 ARG A 20 GLU A 21 0
SHEET 2 A 7 ARG A 156 ARG A 161 -1 O GLU A 157 N ARG A 20
SHEET 3 A 7 LEU A 135 GLY A 140 -1 N VAL A 138 O VAL A 158
SHEET 4 A 7 PRO A 198 LEU A 200 -1 O LEU A 200 N THR A 137
SHEET 5 A 7 ALA A 209 TYR A 215 -1 O GLY A 211 N LEU A 199
SHEET 6 A 7 GLU A 226 ARG A 230 -1 O THR A 229 N ILE A 212
SHEET 7 A 7 GLN A 180 VAL A 183 -1 N VAL A 183 O GLU A 226
SHEET 1 B 5 PHE A 45 LEU A 46 0
SHEET 2 B 5 PHE A 51 THR A 54 -1 O LEU A 53 N PHE A 45
SHEET 3 B 5 MET A 104 LEU A 108 -1 O MET A 104 N THR A 54
SHEET 4 B 5 GLN A 81 ARG A 90 -1 N ARG A 87 O GLN A 107
SHEET 5 B 5 ASN A 65 LEU A 68 -1 N LEU A 68 O GLN A 81
SHEET 1 C 7 ARG B 320 GLU B 321 0
SHEET 2 C 7 ARG B 456 ARG B 461 -1 O GLU B 457 N ARG B 320
SHEET 3 C 7 LEU B 435 GLY B 440 -1 N VAL B 438 O VAL B 458
SHEET 4 C 7 PRO B 498 LEU B 500 -1 O LEU B 500 N THR B 437
SHEET 5 C 7 ALA B 509 TYR B 515 -1 O GLY B 511 N LEU B 499
SHEET 6 C 7 GLU B 526 ARG B 530 -1 O THR B 529 N ILE B 512
SHEET 7 C 7 GLN B 480 VAL B 483 -1 N VAL B 483 O GLU B 526
SHEET 1 D 5 PHE B 345 LEU B 346 0
SHEET 2 D 5 PHE B 351 THR B 354 -1 O LEU B 353 N PHE B 345
SHEET 3 D 5 MET B 404 LEU B 408 -1 O MET B 404 N THR B 354
SHEET 4 D 5 GLN B 381 ARG B 390 -1 N ARG B 387 O GLN B 407
SHEET 5 D 5 ASN B 365 LEU B 368 -1 N LEU B 368 O GLN B 381
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 4 CYS B 342 CYS B 358 1555 1555 2.03
SSBOND 5 CYS B 436 CYS B 501 1555 1555 2.03
SSBOND 6 CYS B 468 CYS B 482 1555 1555 2.03
CISPEP 1 PRO A 224 PRO A 225 0 -0.02
CISPEP 2 PRO B 524 PRO B 525 0 -0.07
SITE 1 AC1 12 CYS A 42 HIS A 57 ARG A 114 ASN A 115
SITE 2 AC1 12 ARG A 116 ALA A 190 PHE A 191 LYS A 192
SITE 3 AC1 12 GLY A 193 SER A 195 GLY A 216 LYS A 217
SITE 1 AC2 10 HIS B 357 ILE B 399 PHE B 491 LYS B 492
SITE 2 AC2 10 GLY B 493 ASP B 494 SER B 495 SER B 514
SITE 3 AC2 10 TYR B 515 GLY B 516
CRYST1 59.440 59.440 130.620 90.00 90.00 90.00 P 41 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 0.016824 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016824 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
