HEADER HYDROLASE INHIBITOR/HYDROLASE 20-AUG-08 3E8L
TITLE THE CRYSTAL STRUCTURE OF THE DOUBLE-HEADED ARROWHEAD PROTEASE
TITLE 2 INHIBITOR A IN COMPLEX WITH TWO TRYPSINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEINASE INHIBITOR A;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: BETA-TREFOIL FOLD;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CATIONIC TRYPSIN;
COMPND 8 CHAIN: A, B;
COMPND 9 SYNONYM: BETA-TRYPSIN;
COMPND 10 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SAGITTARIA SAGITTIFOLIA;
SOURCE 3 ORGANISM_COMMON: ARROWHEAD;
SOURCE 4 ORGANISM_TAXID: 4451;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 12 ORGANISM_COMMON: BOVINE;
SOURCE 13 ORGANISM_TAXID: 9913
KEYWDS BETA-TREFOIL FOLD, PROTEASE INHIBITOR, TRYPSIN, COMPLEX, DIGESTION,
KEYWDS 2 HYDROLASE, METAL-BINDING, PROTEASE, SECRETED, SERINE PROTEASE,
KEYWDS 3 ZYMOGEN, HYDROLASE INHIBITOR-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BAO,C.-H.JIANG,C.W.CHI,S.X.LIN,Y.X.CHEN
REVDAT 5 01-NOV-23 3E8L 1 REMARK
REVDAT 4 10-NOV-21 3E8L 1 REMARK SEQADV LINK
REVDAT 3 18-SEP-13 3E8L 1 JRNL REMARK
REVDAT 2 13-JUL-11 3E8L 1 VERSN
REVDAT 1 28-JUL-09 3E8L 0
JRNL AUTH R.BAO,C.Z.ZHOU,C.-H.JIANG,S.X.LIN,C.W.CHI,Y.X.CHEN
JRNL TITL THE TERNARY STRUCTURE OF DOUBLE-HEADED ARROWHEAD PROTEASE
JRNL TITL 2 INHIBITOR API-A COMPLEXED WITH TWO TRYPSINS REVEALS A NOVEL
JRNL TITL 3 REACTIVE SITE CONFORMATION.
JRNL REF J.BIOL.CHEM. V. 284 26676 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19640842
JRNL DOI 10.1074/JBC.M109.022095
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.300
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 22030
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1396
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1585
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 101
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 45.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.91000
REMARK 3 B22 (A**2) : 0.86000
REMARK 3 B33 (A**2) : 1.05000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.692
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.292
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.991
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4808 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6509 ; 1.437 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 626 ; 8.558 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;37.875 ;25.345
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 750 ;16.602 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.201 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 716 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3569 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3105 ; 0.507 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4969 ; 0.951 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1703 ; 1.461 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1540 ; 2.444 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 16 A 238
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0900 25.1200 8.3130
REMARK 3 T TENSOR
REMARK 3 T11: -0.1318 T22: -0.1872
REMARK 3 T33: -0.1785 T12: 0.0016
REMARK 3 T13: 0.0013 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 2.5374 L22: 0.5783
REMARK 3 L33: 1.7221 L12: -0.0871
REMARK 3 L13: 0.2263 L23: -0.1584
REMARK 3 S TENSOR
REMARK 3 S11: -0.0212 S12: 0.0454 S13: -0.0486
REMARK 3 S21: -0.0477 S22: 0.0172 S23: -0.0133
REMARK 3 S31: -0.0923 S32: 0.0710 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 16 B 238
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3390 1.6550 -35.2380
REMARK 3 T TENSOR
REMARK 3 T11: -0.0055 T22: -0.0844
REMARK 3 T33: -0.1219 T12: -0.1017
REMARK 3 T13: -0.0576 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 1.3066 L22: 4.5364
REMARK 3 L33: 1.2963 L12: -0.4660
REMARK 3 L13: 0.2301 L23: -0.3590
REMARK 3 S TENSOR
REMARK 3 S11: -0.0478 S12: -0.0202 S13: -0.0900
REMARK 3 S21: -0.4722 S22: 0.2497 S23: 0.3230
REMARK 3 S31: 0.1523 S32: -0.1957 S33: -0.2018
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 177
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9140 26.5550 -20.6080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0454 T22: -0.0084
REMARK 3 T33: -0.0589 T12: -0.0019
REMARK 3 T13: 0.0144 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.6015 L22: 1.7210
REMARK 3 L33: 1.9881 L12: -0.2749
REMARK 3 L13: 0.0677 L23: 0.4776
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: 0.1750 S13: 0.1920
REMARK 3 S21: -0.1599 S22: -0.0279 S23: 0.0146
REMARK 3 S31: -0.1552 S32: -0.0541 S33: 0.0244
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3E8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000049011.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22790
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12460
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 2J9N, 1AVA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE PH6.5, 0.2M
REMARK 280 (NH4)2SO4 20% PEG 8000, EVAPORATION, TEMPERATURE 291K
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 76.49550
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 76.49550
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 38.31700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.43150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.31700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.43150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.49550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.31700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.43150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.49550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.31700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.43150
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A, 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 MET C -7
REMARK 465 GLY C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
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 ILE C 29 CB CG1 CG2 CD1
REMARK 480 PHE C 31 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 ARG C 32 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU C 52 CB CG CD OE1 OE2
REMARK 480 THR C 53 CB OG1 CG2
REMARK 480 ASP C 54 CB CG OD1 OD2
REMARK 480 ARG C 55 CG CD NE CZ NH1 NH2
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 O ACT A 6 O HOH A 315 1.34
REMARK 500 NA NA A 7 CH3 ACT A 6 1.63
REMARK 500 O GLU C 52 CG2 THR C 53 1.74
REMARK 500 O ARG C 32 OE2 GLU C 49 1.83
REMARK 500 OD2 ASP B 160 C1 EDO B 8 1.88
REMARK 500 OE2 GLU A 77 O HOH A 314 1.91
REMARK 500 O PRO C 2 O2 GOL C 179 1.92
REMARK 500 NH2 ARG C 76 O CYS C 144 2.14
REMARK 500 CB CYS C 43 SG CYS C 89 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE C 29 C ILE C 29 O 0.171
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 ILE C 29 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 GLY C 33 N - CA - C ANGL. DEV. = -19.2 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 ARG C 32 -75.43 -117.33
REMARK 500 LYS C 40 -65.85 -106.38
REMARK 500 ASP C 41 148.44 -170.56
REMARK 500 ALA C 42 -125.79 48.64
REMARK 500 THR C 53 -1.72 77.59
REMARK 500 ALA C 65 157.46 -44.09
REMARK 500 THR C 66 -11.15 81.18
REMARK 500 VAL A 27 73.86 -119.45
REMARK 500 ASP A 68 -73.19 -120.75
REMARK 500 LEU A 96 17.90 59.73
REMARK 500 SER A 142 75.95 -105.53
REMARK 500 SER A 207 -70.54 -120.27
REMARK 500 ASN A 216 19.90 56.96
REMARK 500 ASP B 68 -63.93 -120.89
REMARK 500 ASN B 98 39.82 72.41
REMARK 500 SER B 207 -73.32 -122.30
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 ILE C 29 18.76
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 NA A 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 122 OG1
REMARK 620 2 HOH A 293 O 126.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 3 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 170 OE1
REMARK 620 2 SER A 210 OG 127.4
REMARK 620 3 HOH A 250 O 173.6 54.8
REMARK 620 4 HOH A 289 O 86.0 108.3 99.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 5 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 40 O
REMARK 620 2 HOH A 253 O 92.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 239
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 239
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2
DBREF 3E8L C 2 177 UNP Q7M1P4 Q7M1P4_SAGSA 26 201
DBREF 3E8L A 16 238 UNP P00760 TRY1_BOVIN 21 243
DBREF 3E8L B 16 238 UNP P00760 TRY1_BOVIN 21 243
SEQADV 3E8L MET C -7 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L GLY C -6 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C -5 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C -4 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C -3 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C -2 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C -1 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L HIS C 0 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L MET C 1 UNP Q7M1P4 EXPRESSION TAG
SEQADV 3E8L ARG C 39 UNP Q7M1P4 HIS 63 ENGINEERED MUTATION
SEQADV 3E8L GLN C 172 UNP Q7M1P4 ARG 196 ENGINEERED MUTATION
SEQRES 1 C 185 MET GLY HIS HIS HIS HIS HIS HIS MET PRO VAL VAL ASP
SEQRES 2 C 185 SER ASP GLY ASP ALA VAL GLN LEU ASN LEU GLY GLY ASN
SEQRES 3 C 185 TYR PRO LEU TYR THR ILE GLN SER ALA ALA ILE GLY PHE
SEQRES 4 C 185 ARG GLY GLY LEU SER THR LEU ARG LYS ASP ALA CYS LYS
SEQRES 5 C 185 SER TYR VAL TYR GLU ALA PRO GLU THR ASP ARG GLY LEU
SEQRES 6 C 185 PRO VAL GLY PHE SER ALA SER ALA THR SER GLN PRO VAL
SEQRES 7 C 185 MET GLN LEU GLY SER ARG TYR LYS PHE SER PHE SER MET
SEQRES 8 C 185 PRO VAL PRO LEU ILE CYS ASP THR ALA TRP SER ILE GLY
SEQRES 9 C 185 LYS SER GLU THR ASN GLY GLY ILE SER PHE GLN PRO ILE
SEQRES 10 C 185 THR ALA GLY ASP TYR PHE TYR LEU ASN ASN PHE SER TRP
SEQRES 11 C 185 PHE GLU ALA ARG SER THR GLU GLU THR GLY VAL TYR LYS
SEQRES 12 C 185 LEU ALA ALA CYS SER CYS GLU PHE CYS LYS ILE ALA CYS
SEQRES 13 C 185 PRO GLU VAL GLY SER PHE ASN VAL ASN GLY ARG THR LEU
SEQRES 14 C 185 LEU GLY ILE GLY GLY GLU HIS PHE THR VAL GLN PHE GLN
SEQRES 15 C 185 LYS PHE ASP
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
SEQRES 1 B 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 B 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 B 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 B 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 B 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 B 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 B 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 B 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 B 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 B 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 B 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 B 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 B 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 B 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 B 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 B 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 B 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 B 223 SER ASN
HET GOL C 178 6
HET GOL C 179 6
HET GOL C 180 6
HET ACT C 181 4
HET ACT C 182 4
HET SO4 C 183 5
HET NA A 1 1
HET NA A 3 1
HET CA A 4 1
HET CA A 5 1
HET NA A 7 1
HET CA A 8 1
HET CA A 9 1
HET CA A 10 1
HET GOL A 2 6
HET GOL A 239 6
HET GOL A 12 6
HET SO4 A 240 5
HET ACT A 6 4
HET CA B 6 1
HET CA B 11 1
HET GOL B 1 6
HET EDO B 3 4
HET EDO B 239 4
HET EDO B 7 8
HET EDO B 8 4
HET PEG B 240 7
HET ACT B 2 4
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 GOL 7(C3 H8 O3)
FORMUL 7 ACT 4(C2 H3 O2 1-)
FORMUL 9 SO4 2(O4 S 2-)
FORMUL 10 NA 3(NA 1+)
FORMUL 12 CA 7(CA 2+)
FORMUL 26 EDO 4(C2 H6 O2)
FORMUL 30 PEG C4 H10 O3
FORMUL 32 HOH *160(H2 O)
HELIX 1 1 TYR C 114 ASN C 118 5 5
HELIX 2 2 ALA A 53 TYR A 57 5 5
HELIX 3 3 SER A 159 TYR A 167 1 9
HELIX 4 4 TYR A 227 SER A 237 1 11
HELIX 5 5 ALA B 53 TYR B 57 5 5
HELIX 6 6 SER B 159 TYR B 167 1 9
HELIX 7 7 TYR B 227 ASN B 238 1 12
SHEET 1 A 2 TYR C 22 SER C 26 0
SHEET 2 A 2 VAL C 171 LYS C 175 -1 O GLN C 172 N GLN C 25
SHEET 1 B 4 LEU C 35 ASP C 41 0
SHEET 2 B 4 LYS C 44 GLU C 49 -1 O LYS C 44 N ASP C 41
SHEET 3 B 4 ILE C 109 ALA C 111 -1 O ILE C 109 N VAL C 47
SHEET 4 B 4 TRP C 93 ILE C 95 -1 N SER C 94 O THR C 110
SHEET 1 C 4 VAL C 59 SER C 62 0
SHEET 2 C 4 ARG C 76 PHE C 81 -1 O SER C 80 N GLY C 60
SHEET 3 C 4 TRP C 122 SER C 127 -1 O PHE C 123 N TYR C 77
SHEET 4 C 4 TYR C 134 CYS C 139 -1 O CYS C 139 N TRP C 122
SHEET 1 D 6 PRO C 84 PRO C 86 0
SHEET 2 D 6 LYS B 201 SER B 210 -1 O GLY B 209 N VAL C 85
SHEET 3 D 6 PRO B 195 CYS B 198 -1 N CYS B 198 O LYS B 201
SHEET 4 D 6 GLN B 130 GLY B 135 -1 N LEU B 132 O VAL B 197
SHEET 5 D 6 LYS B 151 PRO B 156 -1 O LEU B 153 N ILE B 133
SHEET 6 D 6 TYR B 20 THR B 21 -1 N TYR B 20 O CYS B 152
SHEET 1 E 4 PRO C 84 PRO C 86 0
SHEET 2 E 4 LYS B 201 SER B 210 -1 O GLY B 209 N VAL C 85
SHEET 3 E 4 GLY B 219 LYS B 223 -1 O VAL B 220 N TRP B 208
SHEET 4 E 4 MET B 175 ALA B 178 -1 N PHE B 176 O TYR B 221
SHEET 1 F 2 GLU C 99 THR C 100 0
SHEET 2 F 2 SER C 105 PHE C 106 -1 O PHE C 106 N GLU C 99
SHEET 1 G 2 VAL C 151 VAL C 156 0
SHEET 2 G 2 ARG C 159 ILE C 164 -1 O LEU C 161 N PHE C 154
SHEET 1 H 7 TYR A 20 THR A 21 0
SHEET 2 H 7 LYS A 151 PRO A 156 -1 O CYS A 152 N TYR A 20
SHEET 3 H 7 GLN A 130 GLY A 135 -1 N ILE A 133 O LEU A 153
SHEET 4 H 7 PRO A 195 CYS A 198 -1 O VAL A 197 N LEU A 132
SHEET 5 H 7 LYS A 201 TRP A 208 -1 O LYS A 201 N CYS A 198
SHEET 6 H 7 GLY A 219 LYS A 223 -1 O VAL A 220 N TRP A 208
SHEET 7 H 7 MET A 175 ALA A 178 -1 N PHE A 176 O TYR A 221
SHEET 1 I 7 GLN A 30 ASN A 34 0
SHEET 2 I 7 HIS A 38 ASN A 46 -1 O CYS A 40 N LEU A 33
SHEET 3 I 7 TRP A 49 SER A 52 -1 O VAL A 51 N SER A 43
SHEET 4 I 7 MET A 101 LEU A 105 -1 O ILE A 103 N VAL A 50
SHEET 5 I 7 GLN A 78 VAL A 87 -1 N ILE A 86 O LEU A 102
SHEET 6 I 7 GLN A 62 LEU A 65 -1 N VAL A 63 O ILE A 80
SHEET 7 I 7 GLN A 30 ASN A 34 -1 N ASN A 34 O GLN A 62
SHEET 1 J 7 GLN B 30 ASN B 34 0
SHEET 2 J 7 HIS B 38 ASN B 46 -1 O CYS B 40 N LEU B 33
SHEET 3 J 7 TRP B 49 SER B 52 -1 O VAL B 51 N SER B 43
SHEET 4 J 7 MET B 101 LEU B 105 -1 O ILE B 103 N VAL B 50
SHEET 5 J 7 GLN B 78 VAL B 87 -1 N SER B 83 O LYS B 104
SHEET 6 J 7 GLN B 62 LEU B 65 -1 N LEU B 65 O GLN B 78
SHEET 7 J 7 GLN B 30 ASN B 34 -1 N ASN B 34 O GLN B 62
SSBOND 1 CYS C 43 CYS C 89 1555 1555 1.83
SSBOND 2 CYS C 139 CYS C 148 1555 1555 2.02
SSBOND 3 CYS C 141 CYS C 144 1555 1555 2.04
SSBOND 4 CYS A 22 CYS A 152 1555 1555 2.03
SSBOND 5 CYS A 40 CYS A 56 1555 1555 2.02
SSBOND 6 CYS A 124 CYS A 225 1555 1555 2.01
SSBOND 7 CYS A 131 CYS A 198 1555 1555 2.04
SSBOND 8 CYS A 163 CYS A 177 1555 1555 2.05
SSBOND 9 CYS A 188 CYS A 212 1555 1555 2.04
SSBOND 10 CYS B 22 CYS B 152 1555 1555 2.03
SSBOND 11 CYS B 40 CYS B 56 1555 1555 2.04
SSBOND 12 CYS B 124 CYS B 225 1555 1555 2.03
SSBOND 13 CYS B 131 CYS B 198 1555 1555 2.04
SSBOND 14 CYS B 163 CYS B 177 1555 1555 2.04
SSBOND 15 CYS B 188 CYS B 212 1555 1555 2.03
LINK NA NA A 1 OG1 THR A 122 1555 1555 3.19
LINK NA NA A 1 O HOH A 293 1555 1555 3.20
LINK NA NA A 3 OE1 GLN A 170 1555 1555 2.90
LINK NA NA A 3 OG ASER A 210 1555 1555 3.01
LINK NA NA A 3 O HOH A 250 1555 1555 3.01
LINK NA NA A 3 O HOH A 289 1555 1555 2.92
LINK CA CA A 5 O CYS A 40 1555 1555 3.13
LINK CA CA A 5 O HOH A 253 1555 1555 3.09
LINK NA NA A 7 O HIS A 38 1555 1555 2.74
SITE 1 AC1 5 GLN C 12 LEU C 21 TYR C 22 LYS C 175
SITE 2 AC1 5 PHE C 176
SITE 1 AC2 5 PRO C 2 VAL C 4 LEU C 73 THR C 131
SITE 2 AC2 5 TYR C 134
SITE 1 AC3 2 TYR A 37 HOH C 218
SITE 1 AC4 4 GOL A 2 VAL A 73 SER C 64 ALA C 65
SITE 1 AC5 6 SER A 110 LEU C 13 LEU C 15 GLY C 16
SITE 2 AC5 6 ASN C 18 PRO C 20
SITE 1 AC6 3 GLY B 143 LYS C 78 TRP C 122
SITE 1 AC7 3 THR A 122 SER A 123 LYS A 201
SITE 1 AC8 4 GLN A 170 SER A 210 HOH A 250 HOH A 289
SITE 1 AC9 4 HIS A 38 CYS A 40 GLY A 190 HOH A 253
SITE 1 BC1 2 ACT A 6 HIS A 38
SITE 1 BC2 2 GLY A 60 LYS A 215
SITE 1 BC3 1 LYS A 232
SITE 1 BC4 9 ASN A 94 THR A 95 LEU A 96 GLN A 170
SITE 2 BC4 9 TRP A 208 HOH A 268 HOH A 299 PHE C 143
SITE 3 BC4 9 ACT C 181
SITE 1 BC5 6 SER A 35 TYR A 37 PHE A 39 LYS A 58
SITE 2 BC5 6 HOH A 297 PRO C 149
SITE 1 BC6 6 GLN A 130 CYS A 131 VAL A 197 CYS A 198
SITE 2 BC6 6 SER A 199 GLY A 200
SITE 1 BC7 4 SER A 81 LYS A 106 GLN A 214 LYS A 215
SITE 1 BC8 5 NA A 7 TYR A 37 HIS A 38 HOH A 315
SITE 2 BC8 5 ARG C 126
SITE 1 BC9 2 LYS B 140 SER B 142
SITE 1 CC1 1 GLY B 60
SITE 1 CC2 5 ASN B 94 THR B 95 GLN B 170 TRP B 208
SITE 2 CC2 5 PRO C 84
SITE 1 CC3 5 GLN B 189 GLY B 211 CYS B 212 HOH B 271
SITE 2 CC3 5 THR C 91
SITE 1 CC4 3 SER B 85 ILE B 86 VAL B 87
SITE 1 CC5 8 EDO B 8 CYS B 124 ALA B 125 ASP B 160
SITE 2 CC5 8 GLN B 203 LYS B 223 CYS B 225 HOH B 279
SITE 1 CC6 6 EDO B 7 ASP B 160 THR B 172 SER B 173
SITE 2 CC6 6 MET B 175 LYS B 223
SITE 1 CC7 4 ASN B 97 ASN B 98 SER B 173 ASN B 174
SITE 1 CC8 2 HIS B 55 TYR C 114
CRYST1 76.634 110.863 152.991 90.00 90.00 90.00 C 2 2 21 16
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 0.013049 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006536 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
