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HEADER HYDROLASE/HYDROLASE INHIBITOR 22-SEP-14 4RE6
TITLE ACYLAMINOACYL PEPTIDASE COMPLEXED WITH A CHLOROMETHYLKETONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-PEPTIDASE;
COMPND 5 EC: 3.4.19.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 272557;
SOURCE 4 STRAIN: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
SOURCE 5 GENE: APE_1547.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS BETA-PROPELLER, ALPHA-BETA-HYDROLASE FOLD, CHLOROMETHYL-KETONE
KEYWDS 2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.K.MENYHARD,Z.ORGOVAN,Z.SZELTNER,I.SZAMOSI,V.HARMAT
REVDAT 1 28-JAN-15 4RE6 0
JRNL AUTH D.K.MENYHARD,Z.ORGOVAN,Z.SZELTNER,I.SZAMOSI,V.HARMAT
JRNL TITL CATALYTICALLY DISTINCT STATES CAPTURED IN A CRYSTAL LATTICE:
JRNL TITL 2 THE SUBSTRATE-BOUND AND SCAVENGER STATES OF ACYLAMINOACYL
JRNL TITL 3 PEPTIDASE AND THEIR IMPLICATIONS FOR FUNCTIONALITY
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 2015
JRNL REFN ESSN 1399-0047
JRNL DOI 10.1107/S1399004714026819
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 64833
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, IMPORTED FROM
REMARK 3 ISOSTRUCTURAL DATA SET OF PDB
REMARK 3 ENTRY 3O4H.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3441
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2782
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17267
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 674
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -0.50000
REMARK 3 B12 (A**2) : 0.42000
REMARK 3 B13 (A**2) : 0.11000
REMARK 3 B23 (A**2) : 0.14000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.373
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.256
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.075
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.861
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17786 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 16844 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24181 ; 1.470 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 38682 ; 1.294 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2335 ; 5.844 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 725 ;32.251 ;22.510
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2787 ;15.060 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 163 ;17.548 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2704 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20342 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4003 ; 0.006 ; 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): 9270 ; 1.881 ; 2.390
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9270 ; 1.881 ; 2.390
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11584 ; 3.012 ; 3.582
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11609 ; 2.969 ; 3.544
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8516 ; 2.226 ; 2.563
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8587 ; 2.184 ; 2.534
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12674 ; 3.458 ; 3.721
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 19574 ; 5.192 ;18.969
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 19480 ; 5.151 ;18.918
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 579 B 6 579 31212 0.14 0.05
REMARK 3 2 A 5 581 C 5 581 35308 0.06 0.05
REMARK 3 3 A 5 581 D 5 581 31290 0.14 0.05
REMARK 3 4 B 6 579 C 6 579 31308 0.14 0.05
REMARK 3 5 B 6 579 D 6 579 33346 0.08 0.05
REMARK 3 6 C 5 581 D 5 581 31172 0.14 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 5 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2054 -20.2746 -1.2164
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: 0.0650
REMARK 3 T33: 0.0110 T12: 0.0087
REMARK 3 T13: -0.0045 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.5338 L22: 0.8416
REMARK 3 L33: 0.7022 L12: 0.1838
REMARK 3 L13: 0.2122 L23: 0.0664
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: -0.0353 S13: 0.0572
REMARK 3 S21: -0.0520 S22: -0.0064 S23: 0.0429
REMARK 3 S31: -0.0402 S32: -0.0882 S33: 0.0530
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 6 B 580
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2702 19.2386 12.2314
REMARK 3 T TENSOR
REMARK 3 T11: 0.0232 T22: 0.1044
REMARK 3 T33: 0.0612 T12: 0.0096
REMARK 3 T13: 0.0261 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3788 L22: 0.8701
REMARK 3 L33: 0.6759 L12: 0.3173
REMARK 3 L13: 0.3624 L23: 0.0609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.1309 S13: -0.0227
REMARK 3 S21: -0.0535 S22: 0.0627 S23: 0.0682
REMARK 3 S31: -0.0003 S32: 0.1382 S33: -0.0442
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 5 C 581
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9273 38.0016 -36.2516
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.0457
REMARK 3 T33: 0.0272 T12: -0.0049
REMARK 3 T13: 0.0041 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.7452 L22: 0.9372
REMARK 3 L33: 0.6743 L12: 0.1194
REMARK 3 L13: 0.0801 L23: -0.1843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0315 S12: 0.0708 S13: -0.0353
REMARK 3 S21: 0.0646 S22: -0.0323 S23: -0.1117
REMARK 3 S31: -0.0391 S32: 0.1302 S33: 0.0008
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 5 D 581
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5429 -0.9279 -49.0863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0612 T22: 0.0388
REMARK 3 T33: 0.0253 T12: 0.0147
REMARK 3 T13: 0.0324 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.8248 L22: 0.8258
REMARK 3 L33: 0.6143 L12: 0.3214
REMARK 3 L13: 0.2936 L23: 0.1536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: -0.0460 S13: -0.0218
REMARK 3 S21: 0.0338 S22: 0.0558 S23: -0.0201
REMARK 3 S31: 0.0465 S32: -0.0651 S33: -0.0302
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 4RE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-14.
REMARK 100 THE RCSB ID CODE IS RCSB087234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : SAGITALLY FOCUSING GE(220) AND A
REMARK 200 MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68281
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 200 DATA REDUNDANCY : 2.180
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 11.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 20.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 39.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3O4H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 78 MM SODIUM ACETATE BUFFER, 2.2% W/V
REMARK 280 PEG MW4000, 5.2 MM DITHIOTHREITOL, 0.34 MM EDTA. PROTEIN CRYSTALS
REMARK 280 WERE SOAKED IN THE INHIBITOR SOLUTION., PH 5.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 17.33062
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -95.74414
REMARK 350 BIOMT3 2 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 1
REMARK 465 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 ARG A 582
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 ASP B 482
REMARK 465 ARG B 581
REMARK 465 ARG B 582
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 ILE C 3
REMARK 465 ILE C 4
REMARK 465 ARG C 582
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 ILE D 3
REMARK 465 ILE D 4
REMARK 465 ARG D 582
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 5 CG SD CE
REMARK 470 LYS A 110 CD CE NZ
REMARK 470 ARG A 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 ARG A 244 CD NE CZ NH1 NH2
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 ARG A 327 NE CZ NH1 NH2
REMARK 470 GLU A 352 CG CD OE1 OE2
REMARK 470 GLU A 479 CD OE1 OE2
REMARK 470 LYS A 513 CD CE NZ
REMARK 470 ASP B 52 CG OD1 OD2
REMARK 470 VAL B 83 CG1 CG2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 GLN B 89 CG CD OE1 NE2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 ARG B 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 149 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 174 CZ NH1 NH2
REMARK 470 GLU B 234 OE1 OE2
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 ARG B 345 CZ NH1 NH2
REMARK 470 LYS B 410 CE NZ
REMARK 470 ARG B 431 CZ NH1 NH2
REMARK 470 LEU B 480 CG CD1 CD2
REMARK 470 ASN B 487 CG OD1 ND2
REMARK 470 GLU B 490 CG CD OE1 OE2
REMARK 470 GLN B 491 CG CD OE1 NE2
REMARK 470 ARG B 497 CD NE CZ NH1 NH2
REMARK 470 ILE B 499 CG1 CG2 CD1
REMARK 470 ARG B 501 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 513 CD CE NZ
REMARK 470 ARG B 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 530 CD CE NZ
REMARK 470 ARG B 542 CZ NH1 NH2
REMARK 470 HIS B 556 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ASP C 32 CG OD1 OD2
REMARK 470 LYS C 35 NZ
REMARK 470 GLU C 43 CG CD OE1 OE2
REMARK 470 ARG C 61 CZ NH1 NH2
REMARK 470 GLN C 89 CG CD OE1 NE2
REMARK 470 ARG C 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 122 CD OE1 OE2
REMARK 470 GLU C 131 CG CD OE1 OE2
REMARK 470 GLU C 217 CG CD OE1 OE2
REMARK 470 ILE C 330 CD1
REMARK 470 ARG C 501 NE CZ NH1 NH2
REMARK 470 ILE C 558 CD1
REMARK 470 LYS D 35 CE NZ
REMARK 470 PHE D 41 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 ILE D 78 CD1
REMARK 470 VAL D 83 CG1 CG2
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLU D 88 CG CD OE1 OE2
REMARK 470 GLN D 89 CG CD OE1 NE2
REMARK 470 ARG D 99 CZ NH1 NH2
REMARK 470 GLU D 102 CG CD OE1 OE2
REMARK 470 LYS D 110 CG CD CE NZ
REMARK 470 GLU D 131 CG CD OE1 OE2
REMARK 470 ARG D 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 149 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 164 CD1
REMARK 470 ARG D 174 NE CZ NH1 NH2
REMARK 470 ASP D 191 CG OD1 OD2
REMARK 470 ARG D 216 NE CZ NH1 NH2
REMARK 470 ARG D 431 CZ NH1 NH2
REMARK 470 ASP D 482 CG OD1 OD2
REMARK 470 ILE D 489 CD1
REMARK 470 GLN D 491 CG CD OE1 NE2
REMARK 470 ARG D 501 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 511 CD NE CZ NH1 NH2
REMARK 470 LYS D 513 CG CD CE NZ
REMARK 470 ARG D 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 530 CE NZ
REMARK 470 HIS D 556 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 580 CD OE1 OE2
REMARK 470 ARG D 581 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 NH1 ARG C 174 O HOH C 839 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 327 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG D 327 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 32 -134.64 55.66
REMARK 500 ARG A 61 -82.09 -103.19
REMARK 500 PRO A 151 40.21 -82.51
REMARK 500 THR A 214 -167.14 -106.02
REMARK 500 SER A 445 -126.03 58.21
REMARK 500 GLU A 580 43.13 -94.94
REMARK 500 ARG B 61 -81.94 -102.57
REMARK 500 THR B 130 -169.39 -124.33
REMARK 500 PRO B 151 40.61 -78.59
REMARK 500 THR B 214 -162.96 -108.96
REMARK 500 ARG B 216 -83.74 -123.03
REMARK 500 ASP B 414 49.06 -142.40
REMARK 500 SER B 445 -123.53 54.90
REMARK 500 ASN B 523 30.86 -143.69
REMARK 500 HIS B 556 13.89 -67.96
REMARK 500 ASP C 32 -132.60 54.61
REMARK 500 ARG C 61 -81.05 -103.96
REMARK 500 PRO C 151 39.42 -82.48
REMARK 500 THR C 214 -168.37 -107.77
REMARK 500 ARG C 216 24.57 -141.21
REMARK 500 ASP C 227 -0.04 -145.77
REMARK 500 ARG C 292 50.43 38.77
REMARK 500 ASP C 414 49.09 -140.54
REMARK 500 SER C 445 -126.13 57.35
REMARK 500 GLU C 580 42.16 -95.65
REMARK 500 ASP D 52 -67.64 -124.07
REMARK 500 ARG D 61 -82.06 -102.33
REMARK 500 PRO D 151 40.68 -81.52
REMARK 500 THR D 214 -165.51 -108.56
REMARK 500 ARG D 216 -84.89 -121.68
REMARK 500 ASP D 414 48.98 -142.23
REMARK 500 SER D 445 -121.97 55.32
REMARK 500 ASN D 523 31.33 -143.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 708 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH D 737 DISTANCE = 5.39 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 Y3A A 601
REMARK 610 Y3A C 601
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR
REMARK 630 MOLECULE NAME: N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-
REMARK 630 3-HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 Y3A A 601
REMARK 630 Y3A C 601
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: PHQ GLY GLY HPH 0QE
REMARK 630 DETAILS: THE CHLORORMETHYL KETONE INHIBITOR LINKED TO THE PROTEIN
REMARK 630 THROUGH TWO COVALENT BONDS WITH THE ACTIVE SITE SERINE AND
REMARK 630 HISTIDINE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y3A A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y3A C 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RE5 RELATED DB: PDB
DBREF 4RE6 A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 4RE6 B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 4RE6 C 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 4RE6 D 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 C 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 C 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 C 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 C 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 C 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 C 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 C 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 C 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 C 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 C 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 C 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 C 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 C 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 C 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 C 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 C 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 C 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 C 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 C 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 C 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 C 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 C 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 C 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 C 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 C 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 C 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 C 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 C 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 C 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 C 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 C 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 C 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 C 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 C 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 C 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 C 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 C 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 C 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 C 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 C 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 C 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 C 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 C 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 C 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 C 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 D 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 D 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 D 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 D 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 D 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 D 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 D 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 D 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 D 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 D 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 D 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 D 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 D 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 D 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 D 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 D 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 D 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 D 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 D 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 D 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 D 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 D 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 D 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 D 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 D 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 D 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 D 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 D 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 D 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 D 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 D 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 D 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 D 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 D 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 D 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 D 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 D 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 D 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 D 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 D 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 D 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 D 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 D 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 D 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 D 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET Y3A A 601 23
HET CL A 602 1
HET CL A 603 1
HET CL B 601 1
HET CL B 602 1
HET Y3A C 601 20
HET CL C 602 1
HET CL C 603 1
HETNAM Y3A N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-3-
HETNAM 2 Y3A HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE
HETNAM CL CHLORIDE ION
HETSYN Y3A Z-GLY-GLY-PHE-CHLOROMETHYL KETONE (BOUND FORM)
FORMUL 5 Y3A 2(C22 H26 CL N3 O5)
FORMUL 6 CL 6(CL 1-)
FORMUL 13 HOH *674(H2 O)
HELIX 1 1 GLU A 8 VAL A 22 1 15
HELIX 2 2 LYS A 238 ARG A 244 1 7
HELIX 3 3 PRO A 323 SER A 329 1 7
HELIX 4 4 ASP A 379 ALA A 388 1 10
HELIX 5 5 GLY A 404 LYS A 410 1 7
HELIX 6 6 GLY A 417 SER A 433 1 17
HELIX 7 7 SER A 445 LYS A 458 1 14
HELIX 8 8 ASP A 473 SER A 481 1 9
HELIX 9 9 ASP A 482 THR A 493 1 12
HELIX 10 10 SER A 496 ARG A 503 1 8
HELIX 11 11 SER A 504 ILE A 512 5 9
HELIX 12 12 LEU A 529 ARG A 542 1 14
HELIX 13 13 THR A 560 GLU A 580 1 21
HELIX 14 14 GLU B 8 VAL B 22 1 15
HELIX 15 15 LYS B 238 ARG B 244 1 7
HELIX 16 16 PRO B 323 SER B 329 1 7
HELIX 17 17 ASP B 379 GLY B 389 1 11
HELIX 18 18 GLY B 404 LYS B 410 1 7
HELIX 19 19 GLY B 417 SER B 433 1 17
HELIX 20 20 SER B 445 LYS B 458 1 14
HELIX 21 21 ASP B 473 SER B 481 1 9
HELIX 22 22 ALA B 484 THR B 493 1 10
HELIX 23 23 SER B 496 ARG B 503 1 8
HELIX 24 24 SER B 504 ILE B 512 5 9
HELIX 25 25 LEU B 529 ARG B 542 1 14
HELIX 26 26 THR B 560 LEU B 568 1 9
HELIX 27 27 LEU B 568 ARG B 579 1 12
HELIX 28 28 GLU C 8 VAL C 22 1 15
HELIX 29 29 LYS C 238 ARG C 244 1 7
HELIX 30 30 PRO C 323 SER C 329 1 7
HELIX 31 31 ASP C 379 GLY C 389 1 11
HELIX 32 32 GLY C 404 LYS C 410 1 7
HELIX 33 33 GLY C 417 SER C 433 1 17
HELIX 34 34 SER C 445 LYS C 458 1 14
HELIX 35 35 ASP C 473 SER C 481 1 9
HELIX 36 36 ASP C 482 THR C 493 1 12
HELIX 37 37 SER C 496 ARG C 503 1 8
HELIX 38 38 SER C 504 ILE C 512 5 9
HELIX 39 39 LEU C 529 ARG C 542 1 14
HELIX 40 40 THR C 560 GLU C 580 1 21
HELIX 41 41 GLU D 8 VAL D 22 1 15
HELIX 42 42 LYS D 238 ARG D 244 1 7
HELIX 43 43 PRO D 323 SER D 329 1 7
HELIX 44 44 ASP D 379 GLY D 389 1 11
HELIX 45 45 GLY D 404 LYS D 410 1 7
HELIX 46 46 GLY D 417 SER D 433 1 17
HELIX 47 47 SER D 445 LYS D 458 1 14
HELIX 48 48 ASP D 473 SER D 481 1 9
HELIX 49 49 ASP D 482 THR D 493 1 12
HELIX 50 50 SER D 496 ARG D 503 1 8
HELIX 51 51 SER D 504 ILE D 512 5 9
HELIX 52 52 LEU D 529 ARG D 542 1 14
HELIX 53 53 THR D 560 LEU D 568 1 9
HELIX 54 54 LEU D 568 ARG D 579 1 12
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 SER A 42 -1 O LEU A 37 N GLY A 29
SHEET 3 A 4 SER A 45 ASP A 52 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 GLU A 55 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 4 SER A 66 VAL A 67 0
SHEET 2 B 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 4 HIS A 90 ASN A 96 -1 O PHE A 93 N LEU A 79
SHEET 4 B 4 GLN A 104 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 C 5 ASP A 69 PRO A 70 0
SHEET 2 C 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 C 5 VAL A 124 ALA A 129 -1 O VAL A 125 N VAL A 118
SHEET 4 C 5 VAL A 134 ASP A 140 -1 O TYR A 137 N PHE A 126
SHEET 5 C 5 GLY A 143 LEU A 150 -1 O LEU A 150 N VAL A 134
SHEET 1 D 4 GLY A 154 ARG A 160 0
SHEET 2 D 4 LEU A 163 GLY A 171 -1 O LEU A 167 N PHE A 155
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O PHE A 178 N GLY A 166
SHEET 4 D 4 GLY A 185 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 4 GLY A 195 ILE A 202 0
SHEET 2 E 4 VAL A 208 THR A 214 -1 O GLU A 213 N SER A 196
SHEET 3 E 4 ALA A 218 VAL A 223 -1 O ARG A 219 N LEU A 212
SHEET 4 E 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 F 4 ALA A 247 TYR A 253 0
SHEET 2 F 4 LEU A 259 ARG A 265 -1 O ALA A 260 N GLY A 252
SHEET 3 F 4 ARG A 268 ILE A 273 -1 O PHE A 272 N VAL A 261
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O GLU A 276 N ILE A 273
SHEET 1 G 4 ASN A 284 TRP A 291 0
SHEET 2 G 4 LYS A 294 SER A 301 -1 O LYS A 294 N TRP A 291
SHEET 3 G 4 THR A 304 LEU A 311 -1 O ARG A 307 N HIS A 299
SHEET 4 G 4 PRO A 316 LEU A 318 -1 O LEU A 317 N ILE A 308
SHEET 1 H16 ILE A 330 GLU A 339 0
SHEET 2 H16 ARG A 345 SER A 353 -1 O VAL A 346 N VAL A 338
SHEET 3 H16 HIS A 391 PRO A 395 -1 O MET A 394 N TYR A 349
SHEET 4 H16 GLY A 360 VAL A 366 1 N VAL A 363 O HIS A 391
SHEET 5 H16 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 H16 ALA A 464 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 H16 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 H16 PHE A 546 ILE A 551 1 O GLU A 547 N LEU A 518
SHEET 9 H16 PHE B 546 ILE B 551 -1 O ALA B 548 N ILE A 550
SHEET 10 H16 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 H16 ALA B 464 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 H16 ALA B 436 TYR B 444 1 N GLY B 443 O GLY B 468
SHEET 13 H16 GLY B 360 VAL B 366 1 N VAL B 364 O TYR B 440
SHEET 14 H16 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 H16 ARG B 345 SER B 353 -1 N TYR B 349 O MET B 394
SHEET 16 H16 ILE B 330 GLU B 339 -1 N VAL B 338 O VAL B 346
SHEET 1 I 4 LYS B 24 VAL B 31 0
SHEET 2 I 4 LYS B 35 SER B 42 -1 O LEU B 37 N GLN B 28
SHEET 3 I 4 SER B 45 ASP B 52 -1 O SER B 45 N SER B 42
SHEET 4 I 4 GLU B 55 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 J 4 SER B 66 VAL B 67 0
SHEET 2 J 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 J 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 J 4 GLN B 104 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 K 5 ASP B 69 PRO B 70 0
SHEET 2 K 5 ARG B 113 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 K 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 K 5 VAL B 134 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 K 5 GLY B 143 LEU B 150 -1 O LEU B 150 N VAL B 134
SHEET 1 L 4 GLY B 154 ARG B 160 0
SHEET 2 L 4 LEU B 163 PHE B 169 -1 O LEU B 167 N PHE B 155
SHEET 3 L 4 VAL B 175 ASN B 181 -1 O PHE B 178 N GLY B 166
SHEET 4 L 4 GLY B 185 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 M 4 SER B 196 ILE B 202 0
SHEET 2 M 4 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 M 4 ARG B 219 VAL B 223 -1 O ARG B 219 N LEU B 212
SHEET 4 M 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 N 4 ALA B 247 TYR B 253 0
SHEET 2 N 4 LEU B 259 ARG B 265 -1 O ALA B 260 N GLY B 252
SHEET 3 N 4 ARG B 268 ILE B 273 -1 O PHE B 272 N VAL B 261
SHEET 4 N 4 GLU B 276 VAL B 278 -1 O GLU B 276 N ILE B 273
SHEET 1 O 4 ASN B 284 TRP B 291 0
SHEET 2 O 4 LYS B 294 SER B 301 -1 O LYS B 294 N TRP B 291
SHEET 3 O 4 THR B 304 LEU B 311 -1 O ARG B 307 N HIS B 299
SHEET 4 O 4 PRO B 316 LEU B 318 -1 O LEU B 317 N ILE B 308
SHEET 1 P 4 LYS C 24 VAL C 31 0
SHEET 2 P 4 LYS C 35 SER C 42 -1 O LEU C 37 N GLY C 29
SHEET 3 P 4 SER C 45 ASP C 52 -1 O TYR C 49 N VAL C 38
SHEET 4 P 4 GLU C 55 LYS C 58 -1 O VAL C 57 N LEU C 50
SHEET 1 Q 4 SER C 66 VAL C 67 0
SHEET 2 Q 4 ARG C 76 ASP C 82 -1 O VAL C 80 N SER C 66
SHEET 3 Q 4 HIS C 90 ASN C 96 -1 O PHE C 93 N LEU C 79
SHEET 4 Q 4 GLN C 104 ARG C 105 -1 O GLN C 104 N LYS C 94
SHEET 1 R 5 ASP C 69 PRO C 70 0
SHEET 2 R 5 ARG C 113 ASP C 119 1 O ASP C 119 N ASP C 69
SHEET 3 R 5 VAL C 124 ALA C 129 -1 O VAL C 125 N VAL C 118
SHEET 4 R 5 VAL C 134 ASP C 140 -1 O TYR C 137 N PHE C 126
SHEET 5 R 5 GLY C 143 LEU C 150 -1 O LEU C 150 N VAL C 134
SHEET 1 S 4 GLY C 154 ARG C 160 0
SHEET 2 S 4 LEU C 163 GLY C 171 -1 O LEU C 167 N PHE C 155
SHEET 3 S 4 ARG C 174 ASN C 181 -1 O PHE C 178 N GLY C 166
SHEET 4 S 4 GLY C 185 PHE C 190 -1 O PHE C 190 N LEU C 177
SHEET 1 T 4 SER C 196 ILE C 202 0
SHEET 2 T 4 VAL C 208 GLU C 213 -1 O GLU C 213 N SER C 196
SHEET 3 T 4 ALA C 218 VAL C 223 -1 O ARG C 219 N LEU C 212
SHEET 4 T 4 VAL C 230 ASP C 232 -1 O GLU C 231 N THR C 222
SHEET 1 U 4 ALA C 247 TYR C 253 0
SHEET 2 U 4 LEU C 259 ARG C 265 -1 O ALA C 260 N GLY C 252
SHEET 3 U 4 ARG C 268 ILE C 273 -1 O PHE C 272 N VAL C 261
SHEET 4 U 4 GLU C 276 VAL C 278 -1 O GLU C 276 N ILE C 273
SHEET 1 V 4 ASN C 284 TRP C 291 0
SHEET 2 V 4 LYS C 294 SER C 301 -1 O LYS C 294 N TRP C 291
SHEET 3 V 4 THR C 304 LEU C 311 -1 O ARG C 307 N HIS C 299
SHEET 4 V 4 PRO C 316 LEU C 318 -1 O LEU C 317 N ILE C 308
SHEET 1 W16 ILE C 330 GLU C 339 0
SHEET 2 W16 ARG C 345 SER C 353 -1 O VAL C 346 N VAL C 338
SHEET 3 W16 HIS C 391 PRO C 395 -1 O MET C 394 N TYR C 349
SHEET 4 W16 GLY C 360 VAL C 366 1 N VAL C 363 O HIS C 391
SHEET 5 W16 ALA C 436 TYR C 444 1 O TYR C 440 N VAL C 364
SHEET 6 W16 ALA C 464 GLY C 468 1 O GLY C 468 N GLY C 443
SHEET 7 W16 LEU C 516 PRO C 521 1 O ALA C 517 N ALA C 467
SHEET 8 W16 PHE C 546 ILE C 551 1 O GLU C 547 N LEU C 518
SHEET 9 W16 PHE D 546 ILE D 551 -1 O ALA D 548 N ILE C 550
SHEET 10 W16 LEU D 516 PRO D 521 1 N LEU D 518 O GLU D 547
SHEET 11 W16 ALA D 464 GLY D 468 1 N ALA D 467 O ALA D 517
SHEET 12 W16 ALA D 436 TYR D 444 1 N GLY D 443 O GLY D 468
SHEET 13 W16 GLY D 360 VAL D 366 1 N VAL D 364 O TYR D 440
SHEET 14 W16 HIS D 391 PRO D 395 1 O HIS D 391 N VAL D 363
SHEET 15 W16 ARG D 345 SER D 353 -1 N TYR D 349 O MET D 394
SHEET 16 W16 ILE D 330 GLU D 339 -1 N VAL D 338 O VAL D 346
SHEET 1 X 4 LYS D 24 VAL D 31 0
SHEET 2 X 4 LYS D 35 SER D 42 -1 O LEU D 37 N GLY D 29
SHEET 3 X 4 SER D 45 TYR D 51 -1 O TYR D 49 N VAL D 38
SHEET 4 X 4 VAL D 57 LYS D 58 -1 O VAL D 57 N LEU D 50
SHEET 1 Y 4 SER D 66 VAL D 67 0
SHEET 2 Y 4 ARG D 76 ASP D 82 -1 O VAL D 80 N SER D 66
SHEET 3 Y 4 HIS D 90 ASN D 96 -1 O PHE D 93 N LEU D 79
SHEET 4 Y 4 GLN D 104 ARG D 105 -1 O GLN D 104 N LYS D 94
SHEET 1 Z 5 ASP D 69 PRO D 70 0
SHEET 2 Z 5 ARG D 113 ASP D 119 1 O ASP D 119 N ASP D 69
SHEET 3 Z 5 VAL D 124 ALA D 129 -1 O VAL D 125 N VAL D 118
SHEET 4 Z 5 VAL D 134 ASP D 140 -1 O TYR D 137 N PHE D 126
SHEET 5 Z 5 GLY D 143 LEU D 150 -1 O LEU D 150 N VAL D 134
SHEET 1 AA 4 GLY D 154 ARG D 160 0
SHEET 2 AA 4 LEU D 163 PHE D 169 -1 O LEU D 167 N PHE D 155
SHEET 3 AA 4 VAL D 175 ASN D 181 -1 O PHE D 178 N GLY D 166
SHEET 4 AA 4 GLY D 185 PHE D 190 -1 O PHE D 190 N LEU D 177
SHEET 1 AB 4 SER D 196 ILE D 202 0
SHEET 2 AB 4 VAL D 208 GLU D 213 -1 O GLU D 213 N SER D 196
SHEET 3 AB 4 ARG D 219 VAL D 223 -1 O ARG D 219 N LEU D 212
SHEET 4 AB 4 VAL D 230 ASP D 232 -1 O GLU D 231 N THR D 222
SHEET 1 AC 4 ALA D 247 TYR D 253 0
SHEET 2 AC 4 LEU D 259 ARG D 265 -1 O ALA D 260 N GLY D 252
SHEET 3 AC 4 ARG D 268 ILE D 273 -1 O PHE D 272 N VAL D 261
SHEET 4 AC 4 GLU D 276 VAL D 278 -1 O GLU D 276 N ILE D 273
SHEET 1 AD 4 ASN D 284 TRP D 291 0
SHEET 2 AD 4 LYS D 294 SER D 301 -1 O LYS D 294 N TRP D 291
SHEET 3 AD 4 THR D 304 LEU D 311 -1 O ARG D 307 N HIS D 299
SHEET 4 AD 4 PRO D 316 LEU D 318 -1 O LEU D 317 N ILE D 308
SSBOND 1 CYS A 416 CYS A 453 1555 1555 2.04
SSBOND 2 CYS B 416 CYS B 453 1555 1555 2.02
SSBOND 3 CYS C 416 CYS C 453 1555 1555 2.03
SSBOND 4 CYS D 416 CYS D 453 1555 1555 2.04
LINK OG SER A 445 C4 Y3A A 601 1555 1555 1.40
LINK OG SER C 445 C4 Y3A C 601 1555 1555 1.41
LINK NE2 HIS A 556 C15 Y3A A 601 1555 1555 1.44
LINK NE2 HIS C 556 C15 Y3A C 601 1555 1555 1.44
CISPEP 1 LEU A 311 PRO A 312 0 1.88
CISPEP 2 THR A 358 PRO A 359 0 0.82
CISPEP 3 GLY A 369 PRO A 370 0 9.06
CISPEP 4 LEU B 311 PRO B 312 0 11.59
CISPEP 5 THR B 358 PRO B 359 0 -0.31
CISPEP 6 GLY B 369 PRO B 370 0 10.71
CISPEP 7 LEU C 311 PRO C 312 0 2.08
CISPEP 8 THR C 358 PRO C 359 0 -2.50
CISPEP 9 GLY C 369 PRO C 370 0 7.79
CISPEP 10 LEU D 311 PRO D 312 0 8.22
CISPEP 11 THR D 358 PRO D 359 0 -0.05
CISPEP 12 GLY D 369 PRO D 370 0 7.10
SITE 1 AC1 8 GLY A 369 SER A 445 TYR A 446 PHE A 485
SITE 2 AC1 8 PHE A 488 ARG A 526 HIS A 556 HOH A 752
SITE 1 AC2 1 ARG A 345
SITE 1 AC3 1 ALA B 388
SITE 1 AC4 3 GLN B 282 SER B 301 THR B 304
SITE 1 AC5 10 PHE C 153 GLY C 368 GLY C 369 SER C 445
SITE 2 AC5 10 PHE C 485 PHE C 488 ARG C 526 HIS C 556
SITE 3 AC5 10 HOH C 711 HOH C 738
CRYST1 71.580 97.300 99.160 105.15 103.96 100.26 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013970 0.002529 0.004514 0.00000
SCALE2 0.000000 0.010445 0.003511 0.00000
SCALE3 0.000000 0.000000 0.010963 0.00000
TER 4384 ARG A 581
TER 8662 GLU B 580
TER 13039 ARG C 581
TER 17355 ARG D 581
MASTER 595 0 8 54 148 0 8 617990 4 55 180
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