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HEADER HYDROLASE 17-MAY-13 4KRY
TITLE STRUCTURE OF AES FROM E. COLI IN COVALENT COMPLEX WITH PMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: AES, ECE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: AES, B0476, JW0465, YBAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BRE 1162;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE31
KEYWDS ALPHA/BETA-HYDROLASE, HORMONE-SENSITIVE-LIPASE FAMILY, INHIBITION OF
KEYWDS 2 MALT, ACYL ESTERASE, PHENYLMETHYLSULFONYL-SERINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHIEFNER,K.GERBER,A.BROSIG,W.BOOS
REVDAT 1 21-AUG-13 4KRY 0
JRNL AUTH A.SCHIEFNER,K.GERBER,A.BROSIG,W.BOOS
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSES OF AES, AN INHIBITOR OF
JRNL TITL 2 MALT IN ESCHERICHIA COLI.
JRNL REF PROTEINS 2013
JRNL REFN ESSN 1097-0134
JRNL PMID 23934774
JRNL DOI 10.1002/PROT.24383
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 151348
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7572
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10608
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 566
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15320
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.34000
REMARK 3 B22 (A**2) : 1.34000
REMARK 3 B33 (A**2) : -2.67000
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): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.812
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15922 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14764 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21634 ; 1.447 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 33911 ; 0.804 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1927 ; 6.004 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 769 ;35.106 ;23.628
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2497 ;14.016 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 113 ;17.809 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2300 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18124 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3833 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
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 2 A 319
REMARK 3 ORIGIN FOR THE GROUP (A): 87.0869 4.1438 39.9422
REMARK 3 T TENSOR
REMARK 3 T11: 0.1618 T22: 0.3880
REMARK 3 T33: 0.3220 T12: -0.0034
REMARK 3 T13: -0.0010 T23: -0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 0.7521 L22: 0.0626
REMARK 3 L33: 0.8475 L12: -0.1661
REMARK 3 L13: -0.1998 L23: 0.0816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0774 S12: 0.1592 S13: -0.0266
REMARK 3 S21: 0.0576 S22: -0.0630 S23: -0.0381
REMARK 3 S31: -0.0481 S32: -0.1696 S33: 0.1404
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 2 B 319
REMARK 3 ORIGIN FOR THE GROUP (A): 86.5538 0.0674 -1.1747
REMARK 3 T TENSOR
REMARK 3 T11: 0.0914 T22: 0.4300
REMARK 3 T33: 0.3240 T12: 0.0043
REMARK 3 T13: 0.0094 T23: -0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 0.8828 L22: 0.0852
REMARK 3 L33: 0.8296 L12: 0.2122
REMARK 3 L13: 0.3357 L23: -0.0271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0490 S12: -0.0718 S13: 0.0520
REMARK 3 S21: -0.0306 S22: -0.0883 S23: -0.0173
REMARK 3 S31: 0.0309 S32: -0.0892 S33: 0.1373
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 319
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1685 -12.4349 -19.1438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0496 T22: 0.5921
REMARK 3 T33: 0.3128 T12: -0.0287
REMARK 3 T13: 0.0168 T23: -0.1707
REMARK 3 L TENSOR
REMARK 3 L11: 2.1295 L22: 0.1829
REMARK 3 L33: 0.1592 L12: -0.1689
REMARK 3 L13: -0.2330 L23: -0.1178
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: 0.4372 S13: -0.1664
REMARK 3 S21: 0.0813 S22: 0.0581 S23: 0.0146
REMARK 3 S31: -0.0468 S32: -0.0601 S33: 0.0146
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 319
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0458 -0.9951 -0.2619
REMARK 3 T TENSOR
REMARK 3 T11: 0.1902 T22: 0.3420
REMARK 3 T33: 0.3071 T12: -0.0325
REMARK 3 T13: -0.0029 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.2516 L22: 0.3769
REMARK 3 L33: 0.8566 L12: -0.1438
REMARK 3 L13: 0.0895 L23: 0.0714
REMARK 3 S TENSOR
REMARK 3 S11: -0.0197 S12: -0.0254 S13: 0.0021
REMARK 3 S21: -0.0099 S22: 0.0446 S23: 0.0012
REMARK 3 S31: 0.0126 S32: 0.0964 S33: -0.0249
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E -9 E 319
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4057 -1.4861 39.6261
REMARK 3 T TENSOR
REMARK 3 T11: 0.2320 T22: 0.3303
REMARK 3 T33: 0.2950 T12: 0.0489
REMARK 3 T13: 0.0059 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.3669 L22: 0.1349
REMARK 3 L33: 0.6639 L12: 0.1551
REMARK 3 L13: 0.0081 L23: 0.0837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0419 S12: 0.0362 S13: 0.0244
REMARK 3 S21: 0.0283 S22: 0.0339 S23: 0.0363
REMARK 3 S31: 0.0617 S32: 0.1398 S33: 0.0081
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 319
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7465 7.0440 59.7359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.6739
REMARK 3 T33: 0.2428 T12: 0.0721
REMARK 3 T13: 0.0056 T23: -0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 1.9155 L22: 0.3480
REMARK 3 L33: 0.3018 L12: 0.2547
REMARK 3 L13: -0.2437 L23: -0.2769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0752 S12: -0.5711 S13: -0.0831
REMARK 3 S21: -0.1724 S22: -0.0326 S23: -0.0647
REMARK 3 S31: 0.0866 S32: 0.0061 S33: 0.1078
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4KRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8416
REMARK 200 MONOCHROMATOR : HORIZONTALLY FOCUSING SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151348
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4KRX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M TRIS/HCL,
REMARK 280 18% W/V PEG4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.09350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.54675
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 211.64025
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 A -13
REMARK 465 ARG A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 THR A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 ILE A 0
REMARK 465 MET A 1
REMARK 465 MET B -13
REMARK 465 ARG B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 THR B -3
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 ILE B 0
REMARK 465 MET B 1
REMARK 465 MET C -13
REMARK 465 ARG C -12
REMARK 465 GLY C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 THR C -3
REMARK 465 ASP C -2
REMARK 465 PRO C -1
REMARK 465 ILE C 0
REMARK 465 MET C 1
REMARK 465 MET D -13
REMARK 465 ARG D -12
REMARK 465 GLY D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 THR D -3
REMARK 465 ASP D -2
REMARK 465 PRO D -1
REMARK 465 ILE D 0
REMARK 465 MET D 1
REMARK 465 MET E -13
REMARK 465 ARG E -12
REMARK 465 GLY E -11
REMARK 465 SER E -10
REMARK 465 MET F -13
REMARK 465 ARG F -12
REMARK 465 GLY F -11
REMARK 465 SER F -10
REMARK 465 HIS F -9
REMARK 465 HIS F -8
REMARK 465 HIS F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 THR F -3
REMARK 465 ASP F -2
REMARK 465 PRO F -1
REMARK 465 ILE F 0
REMARK 465 MET F 1
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 E 41 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP E 101 CB - CG - OD1 ANGL. DEV. = 5.5 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 PRO A 29 -172.84 -61.49
REMARK 500 PHE A 95 -18.16 76.21
REMARK 500 ASN A 99 -174.01 -175.04
REMARK 500 SEB A 165 -118.72 54.46
REMARK 500 ASP A 202 158.90 179.14
REMARK 500 TYR A 240 -62.85 -120.70
REMARK 500 PHE A 261 42.47 -106.37
REMARK 500 ALA A 293 5.86 85.40
REMARK 500 PRO B 3 -39.35 -39.96
REMARK 500 LEU B 10 -19.07 -49.88
REMARK 500 PRO B 29 -172.52 -63.53
REMARK 500 THR B 34 66.60 -66.91
REMARK 500 ASP B 82 70.75 -103.26
REMARK 500 PHE B 95 -19.25 82.10
REMARK 500 ASN B 99 -170.08 -170.24
REMARK 500 SEB B 165 -118.46 55.41
REMARK 500 TYR B 240 -64.19 -121.23
REMARK 500 PHE B 261 41.05 -104.37
REMARK 500 THR C 36 155.12 -49.04
REMARK 500 PHE C 95 -15.17 72.45
REMARK 500 SEB C 165 -117.60 49.78
REMARK 500 TYR C 195 48.55 37.25
REMARK 500 TYR C 240 -65.17 -121.11
REMARK 500 PHE C 261 44.46 -109.48
REMARK 500 ASN D 5 39.51 -81.98
REMARK 500 ASP D 27 -47.86 -29.00
REMARK 500 PHE D 95 -18.51 81.73
REMARK 500 ASN D 99 -165.43 -168.38
REMARK 500 SEB D 165 -117.40 58.22
REMARK 500 TYR D 195 56.08 39.98
REMARK 500 PHE D 261 58.29 -106.93
REMARK 500 MET E 1 128.79 74.20
REMARK 500 PHE E 95 -14.35 70.26
REMARK 500 ASN E 99 -169.76 -165.17
REMARK 500 SEB E 165 -120.20 57.60
REMARK 500 TYR E 240 -64.54 -120.06
REMARK 500 PHE E 261 42.60 -105.86
REMARK 500 GLU F 4 -12.58 -161.73
REMARK 500 THR F 34 68.59 -115.26
REMARK 500 PHE F 95 -19.93 75.98
REMARK 500 SEB F 165 -109.94 54.06
REMARK 500 TYR F 195 55.23 37.96
REMARK 500 ASP F 202 161.67 178.98
REMARK 500 TYR F 240 -70.02 -117.17
REMARK 500 TYR F 297 36.19 -97.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE F 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KRX RELATED DB: PDB
DBREF 4KRY A 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRY B 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRY C 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRY D 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRY E 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRY F 1 319 UNP P23872 AES_ECOLI 1 319
SEQADV 4KRY MET A -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG A -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY A -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER A -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS A -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR A -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP A -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO A -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE A 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRY MET B -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG B -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY B -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER B -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS B -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR B -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP B -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO B -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE B 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRY MET C -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG C -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY C -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER C -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS C -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR C -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP C -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO C -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE C 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRY MET D -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG D -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY D -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER D -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS D -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR D -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP D -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO D -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE D 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRY MET E -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG E -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY E -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER E -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS E -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR E -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP E -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO E -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE E 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRY MET F -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ARG F -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRY GLY F -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRY SER F -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRY HIS F -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRY THR F -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ASP F -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRY PRO F -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRY ILE F 0 UNP P23872 EXPRESSION TAG
SEQRES 1 A 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 A 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 A 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 A 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 A 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 A 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 A 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 A 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 A 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 A 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 A 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 A 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 A 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 A 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 A 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 A 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 A 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 A 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 A 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 A 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 A 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 A 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 A 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 A 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 A 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 A 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 B 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 B 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 B 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 B 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 B 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 B 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 B 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 B 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 B 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 B 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 B 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 B 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 B 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 B 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 B 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 B 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 B 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 B 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 B 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 B 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 B 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 B 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 B 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 B 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 B 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 B 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 C 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 C 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 C 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 C 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 C 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 C 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 C 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 C 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 C 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 C 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 C 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 C 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 C 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 C 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 C 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 C 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 C 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 C 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 C 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 C 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 C 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 C 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 C 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 C 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 C 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 C 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 D 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 D 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 D 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 D 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 D 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 D 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 D 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 D 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 D 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 D 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 D 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 D 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 D 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 D 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 D 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 D 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 D 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 D 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 D 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 D 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 D 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 D 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 D 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 D 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 D 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 D 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 E 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 E 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 E 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 E 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 E 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 E 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 E 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 E 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 E 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 E 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 E 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 E 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 E 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 E 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 E 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 E 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 E 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 E 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 E 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 E 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 E 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 E 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 E 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 E 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 E 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 E 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 F 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 F 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 F 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 F 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 F 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 F 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 F 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 F 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 F 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 F 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 F 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 F 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 F 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 F 333 MET SER ARG ILE GLY PHE ALA GLY ASP SEB ALA GLY ALA
SEQRES 15 F 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 F 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 F 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 F 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 F 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 F 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 F 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 F 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 F 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 F 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 F 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 F 333 ALA GLN PHE PHE THR ALA GLN LEU
MODRES 4KRY SEB A 165 SER O-BENZYLSULFONYL-SERINE
MODRES 4KRY SEB B 165 SER O-BENZYLSULFONYL-SERINE
MODRES 4KRY SEB C 165 SER O-BENZYLSULFONYL-SERINE
MODRES 4KRY SEB D 165 SER O-BENZYLSULFONYL-SERINE
MODRES 4KRY SEB E 165 SER O-BENZYLSULFONYL-SERINE
MODRES 4KRY SEB F 165 SER O-BENZYLSULFONYL-SERINE
HET SEB A 165 16
HET SEB B 165 16
HET SEB C 165 16
HET SEB D 165 16
HET SEB E 165 16
HET SEB F 165 16
HET PGE A 401 10
HET PGE A 402 10
HET IMD A 403 5
HET PGE B 401 10
HET IMD B 402 5
HET PGE C 401 10
HET PGE D 401 10
HET PGE D 402 10
HET 1PE D 403 16
HET IMD D 404 5
HET IMD D 405 5
HET PGE E 401 10
HET 1PE E 402 16
HET PGE F 401 10
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM IMD IMIDAZOLE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 1 SEB 6(C10 H13 N O5 S)
FORMUL 7 PGE 8(C6 H14 O4)
FORMUL 9 IMD 4(C3 H5 N2 1+)
FORMUL 15 1PE 2(C10 H22 O6)
FORMUL 21 HOH *449(H2 O)
HELIX 1 1 PRO A 8 ILE A 13 1 6
HELIX 2 2 SER A 14 ASN A 22 1 9
HELIX 3 3 THR A 36 ASN A 52 1 17
HELIX 4 4 HIS A 103 GLN A 115 1 13
HELIX 5 5 PRO A 132 GLN A 148 1 17
HELIX 6 6 GLN A 148 GLN A 153 1 6
HELIX 7 7 SEB A 165 GLN A 182 1 18
HELIX 8 8 SER A 203 LEU A 209 1 7
HELIX 9 9 THR A 217 LEU A 229 1 13
HELIX 10 10 ASN A 231 SER A 237 5 7
HELIX 11 11 CYS A 241 ASN A 245 5 5
HELIX 12 12 LEU A 264 HIS A 278 1 15
HELIX 13 13 ALA A 293 SER A 298 5 6
HELIX 14 14 MET A 301 GLN A 318 1 18
HELIX 15 15 LEU A 319 LEU A 319 5 1
HELIX 16 16 LYS B 2 LYS B 6 5 5
HELIX 17 17 PRO B 8 ILE B 13 1 6
HELIX 18 18 SER B 14 ASN B 22 1 9
HELIX 19 19 THR B 36 ALA B 53 1 18
HELIX 20 20 HIS B 103 GLN B 115 1 13
HELIX 21 21 PRO B 132 GLN B 148 1 17
HELIX 22 22 GLN B 148 GLN B 153 1 6
HELIX 23 23 SEB B 165 LYS B 181 1 17
HELIX 24 24 SER B 203 LEU B 209 1 7
HELIX 25 25 THR B 217 LEU B 229 1 13
HELIX 26 26 ASN B 231 SER B 237 5 7
HELIX 27 27 CYS B 241 ASN B 245 5 5
HELIX 28 28 LEU B 264 HIS B 278 1 15
HELIX 29 29 ALA B 293 SER B 298 5 6
HELIX 30 30 MET B 301 ALA B 317 1 17
HELIX 31 31 GLN B 318 LEU B 319 5 2
HELIX 32 32 LYS C 2 LYS C 6 5 5
HELIX 33 33 SER C 14 ASN C 22 1 9
HELIX 34 34 THR C 36 PHE C 50 1 15
HELIX 35 35 TRP C 51 ALA C 53 5 3
HELIX 36 36 HIS C 103 GLN C 115 1 13
HELIX 37 37 PRO C 132 GLN C 148 1 17
HELIX 38 38 GLN C 148 GLN C 153 1 6
HELIX 39 39 SEB C 165 LYS C 181 1 17
HELIX 40 40 SER C 203 LEU C 209 1 7
HELIX 41 41 THR C 217 LEU C 229 1 13
HELIX 42 42 ASN C 231 SER C 237 5 7
HELIX 43 43 CYS C 241 ASN C 245 5 5
HELIX 44 44 LEU C 264 HIS C 278 1 15
HELIX 45 45 ALA C 293 SER C 298 5 6
HELIX 46 46 MET C 301 ALA C 317 1 17
HELIX 47 47 PRO D 8 LEU D 12 5 5
HELIX 48 48 SER D 14 ASN D 22 1 9
HELIX 49 49 THR D 36 ALA D 53 1 18
HELIX 50 50 HIS D 103 GLN D 115 1 13
HELIX 51 51 PRO D 132 GLN D 148 1 17
HELIX 52 52 GLN D 148 GLN D 153 1 6
HELIX 53 53 SEB D 165 LYS D 181 1 17
HELIX 54 54 SER D 203 LEU D 209 1 7
HELIX 55 55 THR D 217 LEU D 229 1 13
HELIX 56 56 ASP D 232 SER D 237 5 6
HELIX 57 57 CYS D 241 ASN D 245 5 5
HELIX 58 58 LEU D 264 HIS D 278 1 15
HELIX 59 59 ALA D 293 SER D 298 5 6
HELIX 60 60 MET D 301 GLN D 318 1 18
HELIX 61 61 LYS E 2 LYS E 6 5 5
HELIX 62 62 PRO E 8 ILE E 13 1 6
HELIX 63 63 SER E 14 ASN E 22 1 9
HELIX 64 64 THR E 36 ALA E 53 1 18
HELIX 65 65 HIS E 103 GLN E 115 1 13
HELIX 66 66 PRO E 132 GLN E 148 1 17
HELIX 67 67 GLN E 148 GLN E 153 1 6
HELIX 68 68 SEB E 165 GLN E 182 1 18
HELIX 69 69 SER E 203 LEU E 209 1 7
HELIX 70 70 THR E 217 LEU E 229 1 13
HELIX 71 71 ASN E 231 SER E 237 5 7
HELIX 72 72 CYS E 241 ASN E 245 5 5
HELIX 73 73 LEU E 264 HIS E 278 1 15
HELIX 74 74 ALA E 293 SER E 298 5 6
HELIX 75 75 MET E 301 ALA E 317 1 17
HELIX 76 76 PRO F 8 ILE F 13 1 6
HELIX 77 77 GLU F 16 ASN F 22 1 7
HELIX 78 78 THR F 36 PHE F 50 1 15
HELIX 79 79 TRP F 51 ALA F 53 5 3
HELIX 80 80 HIS F 103 GLN F 115 1 13
HELIX 81 81 PRO F 132 GLN F 148 1 17
HELIX 82 82 GLN F 148 GLN F 153 1 6
HELIX 83 83 SEB F 165 GLN F 182 1 18
HELIX 84 84 SER F 203 GLY F 210 1 8
HELIX 85 85 THR F 217 LEU F 229 1 13
HELIX 86 86 ASN F 231 SER F 237 5 7
HELIX 87 87 CYS F 241 ASN F 245 5 5
HELIX 88 88 LEU F 264 HIS F 278 1 15
HELIX 89 89 ALA F 293 TYR F 297 5 5
HELIX 90 90 MET F 301 GLN F 318 1 18
SHEET 1 A 8 ALA A 59 VAL A 65 0
SHEET 2 A 8 VAL A 72 CYS A 78 -1 O VAL A 72 N VAL A 65
SHEET 3 A 8 THR A 117 ILE A 121 -1 O VAL A 118 N PHE A 77
SHEET 4 A 8 THR A 86 LEU A 90 1 N LEU A 87 O THR A 117
SHEET 5 A 8 ARG A 158 ASP A 164 1 O ALA A 162 N LEU A 90
SHEET 6 A 8 LYS A 187 TRP A 194 1 O LYS A 187 N ILE A 159
SHEET 7 A 8 CYS A 254 ALA A 259 1 O PHE A 255 N VAL A 191
SHEET 8 A 8 CYS A 282 TYR A 287 1 O GLU A 283 N ILE A 256
SHEET 1 B 8 ALA B 59 VAL B 65 0
SHEET 2 B 8 VAL B 72 CYS B 78 -1 O LEU B 76 N ARG B 61
SHEET 3 B 8 THR B 117 ILE B 121 -1 O VAL B 118 N PHE B 77
SHEET 4 B 8 THR B 86 LEU B 90 1 N LEU B 87 O ILE B 119
SHEET 5 B 8 ARG B 158 ASP B 164 1 O GLY B 160 N PHE B 88
SHEET 6 B 8 LYS B 187 TRP B 194 1 O LEU B 192 N PHE B 161
SHEET 7 B 8 CYS B 254 ALA B 259 1 O PHE B 255 N VAL B 191
SHEET 8 B 8 CYS B 282 TYR B 287 1 O GLU B 283 N ILE B 256
SHEET 1 C 8 ALA C 59 THR C 67 0
SHEET 2 C 8 GLY C 70 CYS C 78 -1 O CYS C 78 N ALA C 59
SHEET 3 C 8 THR C 117 ILE C 121 -1 O VAL C 118 N PHE C 77
SHEET 4 C 8 THR C 86 LEU C 90 1 N LEU C 87 O ILE C 119
SHEET 5 C 8 ARG C 158 ASP C 164 1 O ALA C 162 N LEU C 90
SHEET 6 C 8 LYS C 187 TRP C 194 1 O LYS C 187 N ILE C 159
SHEET 7 C 8 CYS C 254 ALA C 259 1 O PHE C 255 N LEU C 193
SHEET 8 C 8 CYS C 282 TYR C 287 1 O GLU C 283 N ILE C 256
SHEET 1 D 8 ALA D 59 VAL D 65 0
SHEET 2 D 8 VAL D 72 CYS D 78 -1 O LEU D 76 N ARG D 61
SHEET 3 D 8 THR D 117 ILE D 121 -1 O VAL D 118 N PHE D 77
SHEET 4 D 8 THR D 86 LEU D 90 1 N LEU D 87 O THR D 117
SHEET 5 D 8 ARG D 158 ASP D 164 1 O GLY D 160 N PHE D 88
SHEET 6 D 8 LYS D 187 TRP D 194 1 O TRP D 194 N GLY D 163
SHEET 7 D 8 CYS D 254 ALA D 259 1 O PHE D 255 N LEU D 193
SHEET 8 D 8 CYS D 282 TYR D 287 1 O GLU D 283 N ILE D 256
SHEET 1 E 8 ALA E 59 VAL E 65 0
SHEET 2 E 8 VAL E 72 CYS E 78 -1 O LEU E 76 N ARG E 61
SHEET 3 E 8 THR E 117 ILE E 121 -1 O VAL E 118 N PHE E 77
SHEET 4 E 8 THR E 86 LEU E 90 1 N LEU E 87 O THR E 117
SHEET 5 E 8 ARG E 158 ASP E 164 1 O ALA E 162 N LEU E 90
SHEET 6 E 8 LYS E 187 TRP E 194 1 O LEU E 192 N PHE E 161
SHEET 7 E 8 CYS E 254 ALA E 259 1 O PHE E 255 N LEU E 193
SHEET 8 E 8 CYS E 282 TYR E 287 1 O GLU E 283 N ILE E 256
SHEET 1 F 8 ALA F 59 THR F 67 0
SHEET 2 F 8 GLY F 70 CYS F 78 -1 O LEU F 76 N ARG F 61
SHEET 3 F 8 THR F 117 ILE F 121 -1 O VAL F 118 N PHE F 77
SHEET 4 F 8 THR F 86 LEU F 90 1 N LEU F 87 O THR F 117
SHEET 5 F 8 ARG F 158 ASP F 164 1 O GLY F 160 N PHE F 88
SHEET 6 F 8 LYS F 187 TRP F 194 1 O LEU F 192 N PHE F 161
SHEET 7 F 8 CYS F 254 ALA F 259 1 O PHE F 255 N LEU F 193
SHEET 8 F 8 CYS F 282 TYR F 287 1 O TYR F 287 N GLY F 258
SSBOND 1 CYS A 143 CYS A 185 1555 1555 2.08
SSBOND 2 CYS B 143 CYS B 185 1555 1555 2.05
SSBOND 3 CYS C 143 CYS C 185 1555 1555 2.05
SSBOND 4 CYS D 143 CYS D 185 1555 1555 2.09
SSBOND 5 CYS E 143 CYS E 185 1555 1555 2.12
SSBOND 6 CYS F 143 CYS F 185 1555 1555 2.06
LINK C ASP A 164 N SEB A 165 1555 1555 1.34
LINK C SEB A 165 N ALA A 166 1555 1555 1.33
LINK C ASP B 164 N SEB B 165 1555 1555 1.34
LINK C SEB B 165 N ALA B 166 1555 1555 1.34
LINK C ASP C 164 N SEB C 165 1555 1555 1.33
LINK C SEB C 165 N ALA C 166 1555 1555 1.33
LINK C ASP D 164 N SEB D 165 1555 1555 1.34
LINK C SEB D 165 N ALA D 166 1555 1555 1.34
LINK C ASP E 164 N SEB E 165 1555 1555 1.34
LINK C SEB E 165 N ALA E 166 1555 1555 1.34
LINK C ASP F 164 N SEB F 165 1555 1555 1.33
LINK C SEB F 165 N ALA F 166 1555 1555 1.32
CISPEP 1 SER A 126 PRO A 127 0 2.54
CISPEP 2 PHE A 131 PRO A 132 0 -0.62
CISPEP 3 SER B 126 PRO B 127 0 7.69
CISPEP 4 PHE B 131 PRO B 132 0 2.29
CISPEP 5 SER C 126 PRO C 127 0 3.11
CISPEP 6 PHE C 131 PRO C 132 0 5.57
CISPEP 7 SER D 126 PRO D 127 0 3.32
CISPEP 8 PHE D 131 PRO D 132 0 2.44
CISPEP 9 SER E 126 PRO E 127 0 5.20
CISPEP 10 PHE E 131 PRO E 132 0 1.69
CISPEP 11 SER F 126 PRO F 127 0 7.01
CISPEP 12 PHE F 131 PRO F 132 0 6.57
SITE 1 AC1 7 GLY A 199 LEU A 200 ARG A 206 LEU A 221
SITE 2 AC1 7 GLN A 222 GLU A 225 TYR A 240
SITE 1 AC2 7 ALA A 62 MET A 64 GLU A 73 ALA D 140
SITE 2 AC2 7 CYS D 143 TYR D 144 GLN D 147
SITE 1 AC3 1 TYR A 239
SITE 1 AC4 6 LEU B 197 GLY B 199 LEU B 200 ARG B 206
SITE 2 AC4 6 GLU B 225 TYR B 240
SITE 1 AC5 5 LYS B 302 ASP B 305 GLU B 306 LYS C 302
SITE 2 AC5 5 ASP C 305
SITE 1 AC6 9 LEU C 197 GLY C 199 LEU C 200 ARG C 201
SITE 2 AC6 9 ARG C 206 LEU C 221 GLU C 225 TYR C 240
SITE 3 AC6 9 ASP C 267
SITE 1 AC7 8 LEU D 197 GLY D 199 LEU D 200 ARG D 201
SITE 2 AC7 8 ARG D 206 LEU D 221 GLU D 225 TYR D 240
SITE 1 AC8 6 ASP D 122 TYR D 123 THR D 124 LEU D 125
SITE 2 AC8 6 GLU D 128 HOH D 566
SITE 1 AC9 6 ASN A 99 ASP A 101 TRP D 177 LYS D 181
SITE 2 AC9 6 TYR D 239 HOH D 598
SITE 1 BC1 3 ASN D 99 ASP D 101 HOH D 526
SITE 1 BC2 5 LYS D 302 ASP D 305 LYS E 302 ASP E 305
SITE 2 BC2 5 GLU E 306
SITE 1 BC3 7 GLY E 199 LEU E 200 ARG E 206 LEU E 221
SITE 2 BC3 7 GLU E 225 TYR E 240 HOH E 534
SITE 1 BC4 8 ALA B 62 MET B 64 GLU B 73 ALA E 140
SITE 2 BC4 8 CYS E 143 TYR E 144 GLN E 147 ILE E 183
SITE 1 BC5 7 LEU F 197 GLY F 199 LEU F 200 ARG F 206
SITE 2 BC5 7 LEU F 221 TYR F 240 ASP F 267
CRYST1 111.401 111.401 282.187 90.00 90.00 90.00 P 41 24
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 0.008977 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003544 0.00000
TER 2538 LEU A 319
TER 5084 LEU B 319
TER 7639 LEU C 319
TER 10185 LEU D 319
TER 12846 LEU E 319
TER 15384 LEU F 319
MASTER 585 0 20 90 48 0 27 615901 6 252 156
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