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HEADER HYDROLASE 27-JUL-22 8AIS
TITLE CRYSTAL STRUCTURE OF CUTINASE PSCUT FROM PSEUDOMONAS SAUDIMASSILIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SAUDIMASSILIENSIS;
SOURCE 3 ORGANISM_TAXID: 1461581;
SOURCE 4 GENE: LIP1, BN1049_02053;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CUTINASE, ESTER BOND, CLEAVAGE, PET, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,M.D.ALLEN,A.R.PICKFORD,J.E.MCGEEHAN
REVDAT 1 08-MAR-23 8AIS 0
JRNL AUTH L.AVILAN,B.R.LICHTENSTEIN,G.KOENIG,M.ZAHN,M.D.ALLEN,
JRNL AUTH 2 L.OLIVEIRA,M.CLARK,V.BEMMER,R.GRAHAM,H.P.AUSTIN,G.DOMINICK,
JRNL AUTH 3 C.W.JOHNSON,G.T.BECKHAM,J.MCGEEHAN,A.R.PICKFORD
JRNL TITL CONCENTRATION-DEPENDENT INHIBITION OF MESOPHILIC PETASES ON
JRNL TITL 2 POLY(ETHYLENE TEREPHTHALATE) CAN BE ELIMINATED BY ENZYME
JRNL TITL 3 ENGINEERING
JRNL REF CHEMSUSCHEM 2023
JRNL DOI 10.1002/CSSC.202202277
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 112473
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.903
REMARK 3 FREE R VALUE TEST SET COUNT : 5514
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) : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7472
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.3960
REMARK 3 BIN FREE R VALUE SET COUNT : 366
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 684
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40800
REMARK 3 B22 (A**2) : 0.56800
REMARK 3 B33 (A**2) : -0.16300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.10300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6278 ; 0.009 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 5447 ; 0.002 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8548 ; 1.458 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12721 ; 0.528 ; 1.548
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 802 ; 6.824 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;12.458 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 930 ;12.615 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 912 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7396 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1308 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1225 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 153 ; 0.239 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3131 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 504 ; 0.219 ; 0.200
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): 3206 ; 1.266 ; 1.229
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3206 ; 1.263 ; 1.229
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4002 ; 2.017 ; 1.833
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4003 ; 2.017 ; 1.835
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3072 ; 1.670 ; 1.379
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3071 ; 1.664 ; 1.377
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4544 ; 2.573 ; 2.007
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4545 ; 2.573 ; 2.008
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 40 A 303 NULL
REMARK 3 1 A 40 A 303 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 2 A 40 A 303 NULL
REMARK 3 2 A 40 A 303 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 3 A 37 A 304 NULL
REMARK 3 3 A 37 A 304 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
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 40 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7682 -25.2766 107.6025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0298 T22: 0.0226
REMARK 3 T33: 0.0039 T12: -0.0207
REMARK 3 T13: -0.0031 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.3552 L22: 1.9870
REMARK 3 L33: 1.6223 L12: -0.1081
REMARK 3 L13: 0.0798 L23: -0.1256
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: 0.0779 S13: -0.0014
REMARK 3 S21: -0.1356 S22: 0.0473 S23: 0.0369
REMARK 3 S31: -0.0104 S32: -0.0138 S33: -0.0653
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7889 -25.9109 136.4125
REMARK 3 T TENSOR
REMARK 3 T11: 0.0051 T22: 0.1702
REMARK 3 T33: 0.0168 T12: -0.0157
REMARK 3 T13: 0.0075 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 1.7136 L22: 1.8513
REMARK 3 L33: 1.7193 L12: 0.3315
REMARK 3 L13: 0.2186 L23: 0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: 0.2509 S13: -0.0522
REMARK 3 S21: 0.0264 S22: 0.0946 S23: -0.0197
REMARK 3 S31: -0.0096 S32: 0.3377 S33: -0.0355
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4289 -52.9559 103.9966
REMARK 3 T TENSOR
REMARK 3 T11: 0.0208 T22: 0.0501
REMARK 3 T33: 0.0208 T12: -0.0075
REMARK 3 T13: 0.0162 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.7279 L22: 1.8998
REMARK 3 L33: 1.8321 L12: -0.2079
REMARK 3 L13: -0.4060 L23: 0.3306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: -0.0955 S13: -0.0493
REMARK 3 S21: -0.0352 S22: 0.0548 S23: -0.0442
REMARK 3 S31: -0.0198 S32: 0.0473 S33: -0.0520
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8AIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1292124337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113320
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 52.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.50700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: MOLREP
REMARK 200 STARTING MODEL: 4CG1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.6, 8% PEG
REMARK 280 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 79.39300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.40650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.39300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.40650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HOH C 633 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 635 LIES ON A SPECIAL POSITION.
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 A 1
REMARK 465 ILE A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 SER A 7
REMARK 465 GLN A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 MET A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 GLY A 17
REMARK 465 ALA A 18
REMARK 465 LEU A 19
REMARK 465 MET A 20
REMARK 465 PHE A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 SER A 24
REMARK 465 VAL A 25
REMARK 465 PHE A 26
REMARK 465 ALA A 27
REMARK 465 THR A 28
REMARK 465 ASN A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 THR A 32
REMARK 465 ASP A 33
REMARK 465 GLU A 34
REMARK 465 PRO A 35
REMARK 465 THR A 36
REMARK 465 ASN A 37
REMARK 465 PRO A 38
REMARK 465 GLY A 39
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 ASN B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 SER B 7
REMARK 465 GLN B 8
REMARK 465 THR B 9
REMARK 465 LEU B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 MET B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 GLY B 17
REMARK 465 ALA B 18
REMARK 465 LEU B 19
REMARK 465 MET B 20
REMARK 465 PHE B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 SER B 24
REMARK 465 VAL B 25
REMARK 465 PHE B 26
REMARK 465 ALA B 27
REMARK 465 THR B 28
REMARK 465 ASN B 29
REMARK 465 PRO B 30
REMARK 465 PRO B 31
REMARK 465 THR B 32
REMARK 465 ASP B 33
REMARK 465 GLU B 34
REMARK 465 PRO B 35
REMARK 465 THR B 36
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 ASN C 3
REMARK 465 LYS C 4
REMARK 465 LYS C 5
REMARK 465 LEU C 6
REMARK 465 SER C 7
REMARK 465 GLN C 8
REMARK 465 THR C 9
REMARK 465 LEU C 10
REMARK 465 LEU C 11
REMARK 465 SER C 12
REMARK 465 MET C 13
REMARK 465 ALA C 14
REMARK 465 ALA C 15
REMARK 465 ALA C 16
REMARK 465 GLY C 17
REMARK 465 ALA C 18
REMARK 465 LEU C 19
REMARK 465 MET C 20
REMARK 465 PHE C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 SER C 24
REMARK 465 VAL C 25
REMARK 465 PHE C 26
REMARK 465 ALA C 27
REMARK 465 THR C 28
REMARK 465 ASN C 29
REMARK 465 PRO C 30
REMARK 465 PRO C 31
REMARK 465 THR C 32
REMARK 465 ASP C 33
REMARK 465 GLU C 34
REMARK 465 PRO C 35
REMARK 465 THR C 36
REMARK 465 HIS C 305
REMARK 465 HIS C 306
REMARK 465 HIS C 307
REMARK 465 HIS C 308
REMARK 465 HIS C 309
REMARK 465 HIS C 310
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 HOH C 588 O HOH C 624 2.01
REMARK 500 O HOH C 410 O HOH C 461 2.12
REMARK 500 O LEU B 231 O HOH B 401 2.15
REMARK 500 O HOH B 493 O HOH C 495 2.16
REMARK 500 OG SER B 103 O HOH B 402 2.17
REMARK 500 O LEU C 303 O HOH C 401 2.18
REMARK 500 O HOH A 609 O HOH A 744 2.19
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 B 508 O HOH B 525 4648 2.19
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 129 -83.67 -151.39
REMARK 500 SER A 171 -125.72 68.55
REMARK 500 THR A 198 -168.65 -109.18
REMARK 500 HIS A 223 -93.43 -123.31
REMARK 500 ASN A 244 17.57 59.03
REMARK 500 LEU B 70 33.06 -87.47
REMARK 500 SER B 72 164.76 83.75
REMARK 500 PHE B 74 -8.06 -141.35
REMARK 500 ASP B 129 -84.68 -151.26
REMARK 500 SER B 171 -123.81 68.03
REMARK 500 THR B 198 -167.68 -109.06
REMARK 500 HIS B 223 -92.73 -121.41
REMARK 500 ASN B 244 18.97 59.18
REMARK 500 ASP C 129 -85.58 -149.45
REMARK 500 SER C 171 -124.03 69.01
REMARK 500 THR C 198 -167.09 -112.27
REMARK 500 HIS C 223 -91.70 -122.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 152 0.12 SIDE CHAIN
REMARK 500 ARG A 221 0.11 SIDE CHAIN
REMARK 500 ARG A 286 0.12 SIDE CHAIN
REMARK 500 ARG A 291 0.08 SIDE CHAIN
REMARK 500 ARG A 297 0.08 SIDE CHAIN
REMARK 500 ARG B 152 0.16 SIDE CHAIN
REMARK 500 ARG B 199 0.10 SIDE CHAIN
REMARK 500 ARG B 221 0.10 SIDE CHAIN
REMARK 500 ARG C 152 0.11 SIDE CHAIN
REMARK 500 ARG C 221 0.11 SIDE CHAIN
REMARK 500 ARG C 297 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8AIS A 1 302 UNP A0A078MGG8_9PSED
DBREF2 8AIS A A0A078MGG8 1 302
DBREF1 8AIS B 1 302 UNP A0A078MGG8_9PSED
DBREF2 8AIS B A0A078MGG8 1 302
DBREF1 8AIS C 1 302 UNP A0A078MGG8_9PSED
DBREF2 8AIS C A0A078MGG8 1 302
SEQADV 8AIS LEU A 303 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS GLU A 304 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 305 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 306 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 307 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 308 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 309 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS A 310 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS LEU B 303 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS GLU B 304 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 305 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 306 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 307 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 308 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 309 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS B 310 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS LEU C 303 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS GLU C 304 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 305 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 306 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 307 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 308 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 309 UNP A0A078MGG EXPRESSION TAG
SEQADV 8AIS HIS C 310 UNP A0A078MGG EXPRESSION TAG
SEQRES 1 A 310 MET ILE ASN LYS LYS LEU SER GLN THR LEU LEU SER MET
SEQRES 2 A 310 ALA ALA ALA GLY ALA LEU MET PHE SER ALA SER VAL PHE
SEQRES 3 A 310 ALA THR ASN PRO PRO THR ASP GLU PRO THR ASN PRO GLY
SEQRES 4 A 310 GLN SER TYR GLU ARG GLY PRO ASP PRO THR VAL ALA PHE
SEQRES 5 A 310 LEU GLU ALA SER SER GLY PRO TYR SER VAL ARG THR SER
SEQRES 6 A 310 ARG VAL SER GLY LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 A 310 ILE HIS TYR PRO THR GLY THR THR GLY THR MET ALA ALA
SEQRES 8 A 310 ILE VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 A 310 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER HIS GLY PHE
SEQRES 10 A 310 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 A 310 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 A 310 TYR LEU VAL ASP GLN ASN SER SER ARG THR SER PRO VAL
SEQRES 13 A 310 ASN GLY MET ILE ASP THR GLU ARG LEU GLY VAL ILE GLY
SEQRES 14 A 310 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 A 310 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 A 310 ASP THR THR ARG PHE SER GLY VAL GLN ALA PRO THR LEU
SEQRES 17 A 310 ILE PHE ALA CYS GLU SER ASP LEU ILE ALA PRO VAL ARG
SEQRES 18 A 310 SER HIS ALA SER PRO PHE TYR ASN GLN LEU PRO ASN ASP
SEQRES 19 A 310 ILE ASP LYS ALA TYR VAL GLU ILE ASN ASN GLY SER HIS
SEQRES 20 A 310 TYR CYS ALA ASN GLY GLY GLY LEU ASN ASN ASP VAL LEU
SEQRES 21 A 310 SER ARG PHE GLY VAL SER TRP MET LYS ARG PHE LEU ASP
SEQRES 22 A 310 ASN ASP THR ARG TYR SER GLN PHE LEU CYS GLY PRO ARG
SEQRES 23 A 310 HIS GLU SER ASP ARG LYS ILE SER GLU TYR ARG GLY ASN
SEQRES 24 A 310 CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 310 MET ILE ASN LYS LYS LEU SER GLN THR LEU LEU SER MET
SEQRES 2 B 310 ALA ALA ALA GLY ALA LEU MET PHE SER ALA SER VAL PHE
SEQRES 3 B 310 ALA THR ASN PRO PRO THR ASP GLU PRO THR ASN PRO GLY
SEQRES 4 B 310 GLN SER TYR GLU ARG GLY PRO ASP PRO THR VAL ALA PHE
SEQRES 5 B 310 LEU GLU ALA SER SER GLY PRO TYR SER VAL ARG THR SER
SEQRES 6 B 310 ARG VAL SER GLY LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 B 310 ILE HIS TYR PRO THR GLY THR THR GLY THR MET ALA ALA
SEQRES 8 B 310 ILE VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 B 310 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER HIS GLY PHE
SEQRES 10 B 310 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 B 310 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 B 310 TYR LEU VAL ASP GLN ASN SER SER ARG THR SER PRO VAL
SEQRES 13 B 310 ASN GLY MET ILE ASP THR GLU ARG LEU GLY VAL ILE GLY
SEQRES 14 B 310 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 B 310 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 B 310 ASP THR THR ARG PHE SER GLY VAL GLN ALA PRO THR LEU
SEQRES 17 B 310 ILE PHE ALA CYS GLU SER ASP LEU ILE ALA PRO VAL ARG
SEQRES 18 B 310 SER HIS ALA SER PRO PHE TYR ASN GLN LEU PRO ASN ASP
SEQRES 19 B 310 ILE ASP LYS ALA TYR VAL GLU ILE ASN ASN GLY SER HIS
SEQRES 20 B 310 TYR CYS ALA ASN GLY GLY GLY LEU ASN ASN ASP VAL LEU
SEQRES 21 B 310 SER ARG PHE GLY VAL SER TRP MET LYS ARG PHE LEU ASP
SEQRES 22 B 310 ASN ASP THR ARG TYR SER GLN PHE LEU CYS GLY PRO ARG
SEQRES 23 B 310 HIS GLU SER ASP ARG LYS ILE SER GLU TYR ARG GLY ASN
SEQRES 24 B 310 CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 310 MET ILE ASN LYS LYS LEU SER GLN THR LEU LEU SER MET
SEQRES 2 C 310 ALA ALA ALA GLY ALA LEU MET PHE SER ALA SER VAL PHE
SEQRES 3 C 310 ALA THR ASN PRO PRO THR ASP GLU PRO THR ASN PRO GLY
SEQRES 4 C 310 GLN SER TYR GLU ARG GLY PRO ASP PRO THR VAL ALA PHE
SEQRES 5 C 310 LEU GLU ALA SER SER GLY PRO TYR SER VAL ARG THR SER
SEQRES 6 C 310 ARG VAL SER GLY LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 C 310 ILE HIS TYR PRO THR GLY THR THR GLY THR MET ALA ALA
SEQRES 8 C 310 ILE VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 C 310 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER HIS GLY PHE
SEQRES 10 C 310 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 C 310 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 C 310 TYR LEU VAL ASP GLN ASN SER SER ARG THR SER PRO VAL
SEQRES 13 C 310 ASN GLY MET ILE ASP THR GLU ARG LEU GLY VAL ILE GLY
SEQRES 14 C 310 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 C 310 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 C 310 ASP THR THR ARG PHE SER GLY VAL GLN ALA PRO THR LEU
SEQRES 17 C 310 ILE PHE ALA CYS GLU SER ASP LEU ILE ALA PRO VAL ARG
SEQRES 18 C 310 SER HIS ALA SER PRO PHE TYR ASN GLN LEU PRO ASN ASP
SEQRES 19 C 310 ILE ASP LYS ALA TYR VAL GLU ILE ASN ASN GLY SER HIS
SEQRES 20 C 310 TYR CYS ALA ASN GLY GLY GLY LEU ASN ASN ASP VAL LEU
SEQRES 21 C 310 SER ARG PHE GLY VAL SER TRP MET LYS ARG PHE LEU ASP
SEQRES 22 C 310 ASN ASP THR ARG TYR SER GLN PHE LEU CYS GLY PRO ARG
SEQRES 23 C 310 HIS GLU SER ASP ARG LYS ILE SER GLU TYR ARG GLY ASN
SEQRES 24 C 310 CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
HET ACT A 401 4
HETNAM ACT ACETATE ION
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 HOH *684(H2 O)
HELIX 1 AA1 THR A 49 ALA A 55 1 7
HELIX 2 AA2 SER A 68 SER A 72 5 5
HELIX 3 AA3 TRP A 107 SER A 114 1 8
HELIX 4 AA4 GLN A 130 ASN A 149 1 20
HELIX 5 AA5 MET A 172 SER A 182 1 11
HELIX 6 AA6 HIS A 223 LEU A 231 1 9
HELIX 7 AA7 ASN A 256 ASP A 273 1 18
HELIX 8 AA8 ASP A 275 ARG A 277 5 3
HELIX 9 AA9 TYR A 278 CYS A 283 1 6
HELIX 10 AB1 ARG A 286 ASP A 290 5 5
HELIX 11 AB2 THR B 49 ALA B 55 1 7
HELIX 12 AB3 TRP B 107 SER B 114 1 8
HELIX 13 AB4 GLN B 130 ASN B 149 1 20
HELIX 14 AB5 MET B 172 SER B 182 1 11
HELIX 15 AB6 HIS B 223 LEU B 231 1 9
HELIX 16 AB7 ASN B 256 ASP B 273 1 18
HELIX 17 AB8 ASP B 275 ARG B 277 5 3
HELIX 18 AB9 TYR B 278 CYS B 283 1 6
HELIX 19 AC1 ARG B 286 ASP B 290 5 5
HELIX 20 AC2 THR C 49 ALA C 55 1 7
HELIX 21 AC3 TRP C 107 SER C 114 1 8
HELIX 22 AC4 GLN C 130 ASN C 149 1 20
HELIX 23 AC5 MET C 172 SER C 182 1 11
HELIX 24 AC6 HIS C 223 LEU C 231 1 9
HELIX 25 AC7 ASN C 256 ASP C 273 1 18
HELIX 26 AC8 ASP C 275 ARG C 277 5 3
HELIX 27 AC9 TYR C 278 CYS C 283 1 6
HELIX 28 AD1 ARG C 286 ASP C 290 5 5
SHEET 1 AA1 6 VAL A 62 VAL A 67 0
SHEET 2 AA1 6 GLY A 77 PRO A 82 -1 O GLY A 77 N VAL A 67
SHEET 3 AA1 6 VAL A 118 ILE A 122 -1 O VAL A 119 N HIS A 80
SHEET 4 AA1 6 MET A 89 GLY A 97 1 N ILE A 92 O MET A 120
SHEET 5 AA1 6 ILE A 160 SER A 171 1 O ILE A 168 N ILE A 95
SHEET 6 AA1 6 ALA A 188 LEU A 192 1 O LEU A 192 N GLY A 169
SHEET 1 AA2 3 THR A 207 CYS A 212 0
SHEET 2 AA2 3 LYS A 237 ILE A 242 1 O ILE A 242 N ALA A 211
SHEET 3 AA2 3 ILE A 293 GLY A 298 -1 O GLU A 295 N GLU A 241
SHEET 1 AA3 6 VAL B 62 VAL B 67 0
SHEET 2 AA3 6 GLY B 77 PRO B 82 -1 O ILE B 79 N SER B 65
SHEET 3 AA3 6 VAL B 118 ILE B 122 -1 O VAL B 119 N HIS B 80
SHEET 4 AA3 6 MET B 89 GLY B 97 1 N ILE B 92 O MET B 120
SHEET 5 AA3 6 ILE B 160 SER B 171 1 O ASP B 161 N MET B 89
SHEET 6 AA3 6 ALA B 188 LEU B 192 1 O LEU B 192 N GLY B 169
SHEET 1 AA4 3 THR B 207 CYS B 212 0
SHEET 2 AA4 3 LYS B 237 ILE B 242 1 O ILE B 242 N ALA B 211
SHEET 3 AA4 3 ILE B 293 GLY B 298 -1 O GLU B 295 N GLU B 241
SHEET 1 AA5 6 VAL C 62 VAL C 67 0
SHEET 2 AA5 6 GLY C 77 PRO C 82 -1 O GLY C 77 N VAL C 67
SHEET 3 AA5 6 VAL C 118 ILE C 122 -1 O VAL C 119 N HIS C 80
SHEET 4 AA5 6 MET C 89 GLY C 97 1 N ILE C 92 O MET C 120
SHEET 5 AA5 6 ILE C 160 SER C 171 1 O ASP C 161 N MET C 89
SHEET 6 AA5 6 ALA C 188 LEU C 192 1 O LEU C 192 N GLY C 169
SHEET 1 AA6 3 THR C 207 CYS C 212 0
SHEET 2 AA6 3 LYS C 237 ILE C 242 1 O ILE C 242 N ALA C 211
SHEET 3 AA6 3 ILE C 293 GLY C 298 -1 O GLU C 295 N GLU C 241
SSBOND 1 CYS A 212 CYS A 249 1555 1555 2.09
SSBOND 2 CYS A 283 CYS A 300 1555 1555 2.22
SSBOND 3 CYS B 212 CYS B 249 1555 1555 2.08
SSBOND 4 CYS B 283 CYS B 300 1555 1555 2.17
SSBOND 5 CYS C 212 CYS C 249 1555 1555 2.08
SSBOND 6 CYS C 283 CYS C 300 1555 1555 2.18
CISPEP 1 CYS A 300 PRO A 301 0 -2.10
CISPEP 2 CYS B 300 PRO B 301 0 -2.31
CISPEP 3 CYS C 300 PRO C 301 0 -2.24
CRYST1 158.786 56.813 105.796 90.00 121.63 90.00 C 1 2 1 12
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 0.006298 0.000000 0.003879 0.00000
SCALE2 0.000000 0.017602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011101 0.00000
TER 2031 GLU A 304
TER 4076 GLU B 304
TER 6118 GLU C 304
MASTER 564 0 1 28 27 0 0 6 6792 3 16 72
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