HEADER HYDROLASE 26-NOV-04 1Y3X
TITLE TRYPSIN INHIBITOR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSINOGEN, CATIONIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN, FRAGMENT;
COMPND 5 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 TISSUE: BLOOD
KEYWDS TRYPSIN, INHIBITOR COMPLEX, BARREL, 6 STRANDED BETA-SHEET, BETA
KEYWDS 2 HAIRPIN, GREEK KEY MOTIVE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FOKKENS,G.KLEBE
REVDAT 6 23-AUG-23 1Y3X 1 REMARK LINK
REVDAT 5 24-JUL-19 1Y3X 1 REMARK
REVDAT 4 11-OCT-17 1Y3X 1 REMARK
REVDAT 3 24-FEB-09 1Y3X 1 VERSN
REVDAT 2 03-OCT-06 1Y3X 1 JRNL
REVDAT 1 06-DEC-05 1Y3X 0
JRNL AUTH J.FOKKENS,G.KLEBE
JRNL TITL A SIMPLE PROTOCOL TO ESTIMATE DIFFERENCES IN PROTEIN BINDING
JRNL TITL 2 AFFINITY FOR ENANTIOMERS WITHOUT PRIOR RESOLUTION OF
JRNL TITL 3 RACEMATES.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 985 2006
JRNL REFN ESSN 0570-0833
JRNL PMID 16374786
JRNL DOI 10.1002/ANIE.200502302
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
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) : 0.154
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.152
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2926
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29157
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.136
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.134
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2132
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 21370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1622
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 150
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1806.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1581.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 14
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 7445
REMARK 3 NUMBER OF RESTRAINTS : 7103
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.029
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.051
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.063
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.029
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.071
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 4
REMARK 4 1Y3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031084.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 6.00
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : OSMICS MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTAL CLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31574
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 2.720
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
REMARK 200 R SYM FOR SHELL (I) : 0.22900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1MTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, CALCIUM
REMARK 280 CHLORIDE, BENZAMIDINIUM HYDROCHLORIDE, PH 6.00, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.95500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.95500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 SER A 147 OG
REMARK 470 THR A 149 OG1 CG2
REMARK 470 LYS A 222 CG CD CE NZ
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 HIS A 40 CG - ND1 - CE1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 HIS A 40 ND1 - CE1 - NE2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU A 99 O - C - N ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG A 117 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 PHE A 181 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 CYS A 182 CA - CB - SG ANGL. DEV. = 6.7 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 ASP A 71 -79.47 -126.36
REMARK 500 ASN A 79 -5.95 81.35
REMARK 500 ASN A 115 -169.63 -160.91
REMARK 500 ASN A 223 19.21 59.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A3394 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 90.7
REMARK 620 3 VAL A 75 O 161.5 82.6
REMARK 620 4 GLU A 80 OE2 104.3 157.3 87.7
REMARK 620 5 HOH A3415 O 79.3 104.2 85.6 95.4
REMARK 620 6 HOH A3424 O 83.4 85.3 113.0 79.7 160.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UIB A 1994
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y3U RELATED DB: PDB
REMARK 900 TRYPSIN INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1Y3V RELATED DB: PDB
REMARK 900 TRYPSIN INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1Y3W RELATED DB: PDB
REMARK 900 TRYPSIN INHIBITOR COMPLEX
DBREF 1Y3X A 16 238 UNP P00760 TRY1_BOVIN 21 243
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A3394 1
HET UIB A1994 33
HETNAM CA CALCIUM ION
HETNAM UIB (1R,3AS,4R,8AS,8BR)-4-{5-(PHENYL[1,3]DIOXOL-5-
HETNAM 2 UIB YLMETHYL)-4-ETHYL-2,3,3-TRIMETHYL-6-OXO-OCTAHYDRO-
HETNAM 3 UIB PYRROLO[3,4-C]PYRROL-1-YL}-BENZAMIDINE
FORMUL 2 CA CA 2+
FORMUL 3 UIB C26 H32 N4 O3
FORMUL 4 HOH *150(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 TYR A 172 1 9
HELIX 3 3 TYR A 234 SER A 244 1 11
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 A 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 A 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 GLN A 64 LEU A 67 -1 N VAL A 65 O ILE A 83
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.02
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.05
SSBOND 4 CYS A 136 CYS A 201 1555 1555 1.99
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.00
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.05
LINK OE1 GLU A 70 CA CA A3394 1555 1555 2.32
LINK O ASN A 72 CA CA A3394 1555 1555 2.34
LINK O VAL A 75 CA CA A3394 1555 1555 2.30
LINK OE2 GLU A 80 CA CA A3394 1555 1555 2.30
LINK CA CA A3394 O HOH A3415 1555 1555 2.40
LINK CA CA A3394 O HOH A3424 1555 1555 2.29
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A3415 HOH A3424
SITE 1 AC2 14 ASN A 97 THR A 98 LEU A 99 GLN A 175
SITE 2 AC2 14 ASP A 189 SER A 190 GLN A 192 SER A 214
SITE 3 AC2 14 TRP A 215 GLY A 216 GLY A 219 HOH A3416
SITE 4 AC2 14 HOH A3474 HOH A3487
CRYST1 63.250 69.300 63.910 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015647 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
