HEADER HYDROLASE INHIBITOR 17-OCT-01 1K6U
TITLE CRYSTAL STRUCTURE OF CYCLIC BOVINE PANCREATIC TRYPSIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BPTI;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE WAS CHEMICALLY SYNTHESIZED. IT IS A 4-
SOURCE 4 POINT MUTANT OF THE NATURALLY OCCURING BPTI FROM BOS TAURUS.
KEYWDS BPTI, CYCLIC PROTEIN, ATOMIC RESOLUTION, HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BOTOS,Z.WU,W.LU,A.WLODAWER
REVDAT 4 16-AUG-23 1K6U 1 REMARK
REVDAT 3 27-OCT-21 1K6U 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1K6U 1 VERSN
REVDAT 1 19-DEC-01 1K6U 0
JRNL AUTH I.BOTOS,Z.WU,W.LU,A.WLODAWER
JRNL TITL CRYSTAL STRUCTURE OF A CYCLIC FORM OF BOVINE PANCREATIC
JRNL TITL 2 TRYPSIN INHIBITOR.
JRNL REF FEBS LETT. V. 509 90 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11734212
JRNL DOI 10.1016/S0014-5793(01)03113-1
REMARK 2
REMARK 2 RESOLUTION. 1.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.129
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.128
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3202
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 32215
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.120
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.118
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2634
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 26250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 451
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 604.03
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 407.37
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 8
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 6174
REMARK 3 NUMBER OF RESTRAINTS : 7248
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 ANGLE DISTANCES (A) : 0.036
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.031
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.083
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.102
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.064
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.056
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.102
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-22
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 728960
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: PDB ENTRY 1G6X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 2% PEG 400, 0.1M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 21.44800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 25.95200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 25.95200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.17200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 25.95200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 25.95200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 10.72400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 25.95200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 25.95200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.17200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 25.95200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 25.95200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 10.72400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 21.44800
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 61 LIES ON A SPECIAL POSITION.
REMARK 375 S SO4 A 65 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 170 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 181 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 189 LIES ON A SPECIAL POSITION.
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 ARG A 17 NH1
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 O2 EDO A 66 O HOH A 145 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 ARG A 1 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 17 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 CYS A 38 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 39 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 39 CD - NE - CZ ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 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 44 107.82 -161.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SO4 A 61
REMARK 610 SO4 A 65
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 61
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 62
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 63
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 64
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 65
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 67
DBREF 1K6U A 1 58 UNP P00974 BPT1_BOVIN 36 93
SEQADV 1K6U ALA A 11 UNP P00974 THR 46 ENGINEERED MUTATION
SEQADV 1K6U ALA A 13 UNP P00974 PRO 48 ENGINEERED MUTATION
SEQADV 1K6U ARG A 15 UNP P00974 LYS 50 ENGINEERED MUTATION
SEQADV 1K6U LEU A 52 UNP P00974 MET 87 ENGINEERED MUTATION
SEQRES 1 A 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR ALA GLY ALA
SEQRES 2 A 58 CYS ARG ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 A 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 A 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS LEU
SEQRES 5 A 58 ARG THR CYS GLY GLY ALA
HET SO4 A 59 5
HET SO4 A 60 5
HET SO4 A 61 3
HET SO4 A 62 5
HET SO4 A 63 5
HET SO4 A 64 5
HET SO4 A 65 3
HET EDO A 66 4
HET EDO A 67 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 7(O4 S 2-)
FORMUL 9 EDO 2(C2 H6 O2)
FORMUL 11 HOH *143(H2 O)
HELIX 1 1 PRO A 2 GLU A 7 5 6
HELIX 2 2 SER A 47 GLY A 56 1 10
SHEET 1 A 2 ILE A 18 ASN A 24 0
SHEET 2 A 2 LEU A 29 TYR A 35 -1 O TYR A 35 N ILE A 18
SSBOND 1 CYS A 5 CYS A 55 1555 1555 2.04
SSBOND 2 CYS A 14 CYS A 38 1555 1555 1.91
SSBOND 3 CYS A 30 CYS A 51 1555 1555 2.03
LINK N ARG A 1 C ALA A 58 1555 1555 1.33
SITE 1 AC1 8 PHE A 4 GLU A 7 ARG A 42 HOH A 109
SITE 2 AC1 8 HOH A 125 HOH A 137 HOH A 138 HOH A 209
SITE 1 AC2 11 ARG A 20 TYR A 35 GLY A 37 ALA A 40
SITE 2 AC2 11 ARG A 53 HOH A 124 HOH A 160 HOH A 188
SITE 3 AC2 11 HOH A 191 HOH A 199 HOH A 221
SITE 1 AC3 3 ARG A 15 HOH A 150 HOH A 234
SITE 1 AC4 8 CYS A 38 ARG A 39 HOH A 124 HOH A 154
SITE 2 AC4 8 HOH A 196 HOH A 207 HOH A 221 HOH A 244
SITE 1 AC5 4 ARG A 1 LYS A 26 HOH A 115 HOH A 219
SITE 1 AC6 8 PRO A 9 TYR A 10 ALA A 11 HOH A 101
SITE 2 AC6 8 HOH A 102 HOH A 103 HOH A 153 HOH A 216
SITE 1 AC7 2 PRO A 2 ASP A 3
SITE 1 AC8 4 ARG A 39 ALA A 40 LYS A 41 HOH A 145
SITE 1 AC9 3 ALA A 25 LEU A 52 HOH A 158
CRYST1 51.904 51.904 42.896 90.00 90.00 90.00 P 43 21 2 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 0.019266 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019266 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023312 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
