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HEADER HYDROLASE/HYDROLASE INHIBITOR 22-SEP-14 4RE5
TITLE ACYLAMINOACYL PEPTIDASE COMPLEXED WITH A CHLOROMETHYLKETONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B;
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 4RE5 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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 85520
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 2HU5
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4499
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6271
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 315
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8591
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 662
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : -1.37000
REMARK 3 B33 (A**2) : 1.68000
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): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.984
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8968 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8525 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12208 ; 1.720 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19581 ; 1.140 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1186 ; 6.303 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;32.581 ;22.568
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1410 ;13.426 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 81 ;18.933 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1363 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10270 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2029 ; 0.005 ; 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): 4649 ; 1.876 ; 1.645
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4648 ; 1.876 ; 1.644
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5813 ; 2.735 ; 2.453
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5814 ; 2.735 ; 2.453
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4319 ; 2.680 ; 1.891
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4320 ; 2.679 ; 1.891
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6377 ; 3.994 ; 2.740
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10400 ; 7.089 ;14.382
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10401 ; 7.089 ;14.383
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 : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 8 581 B 8 581 34440 0.08 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 23 A 320
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3025 40.6544 -19.5604
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1374
REMARK 3 T33: 0.0829 T12: -0.0056
REMARK 3 T13: -0.0433 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.2618 L22: 0.8170
REMARK 3 L33: 0.1332 L12: -0.1119
REMARK 3 L13: 0.0848 L23: 0.0909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: 0.0473 S13: 0.0405
REMARK 3 S21: 0.0061 S22: -0.0831 S23: 0.1041
REMARK 3 S31: -0.0914 S32: 0.0530 S33: 0.0850
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 23 B 320
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0158 -31.2765 -22.2622
REMARK 3 T TENSOR
REMARK 3 T11: 0.2882 T22: 0.1156
REMARK 3 T33: 0.3182 T12: -0.0077
REMARK 3 T13: -0.0824 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.5075 L22: 2.8145
REMARK 3 L33: 0.1121 L12: -0.8548
REMARK 3 L13: 0.2222 L23: -0.4334
REMARK 3 S TENSOR
REMARK 3 S11: 0.2357 S12: 0.0141 S13: -0.2795
REMARK 3 S21: 0.0954 S22: -0.0883 S23: 0.7170
REMARK 3 S31: 0.0830 S32: 0.0463 S33: -0.1473
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 22
REMARK 3 RESIDUE RANGE : A 321 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1670 13.6125 -17.1942
REMARK 3 T TENSOR
REMARK 3 T11: 0.1235 T22: 0.1658
REMARK 3 T33: 0.1073 T12: 0.0076
REMARK 3 T13: -0.0364 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.1684 L22: 0.6508
REMARK 3 L33: 0.1617 L12: 0.0340
REMARK 3 L13: 0.1445 L23: 0.0829
REMARK 3 S TENSOR
REMARK 3 S11: 0.0789 S12: 0.0743 S13: -0.0519
REMARK 3 S21: 0.0626 S22: -0.0557 S23: 0.0120
REMARK 3 S31: 0.0205 S32: 0.0570 S33: -0.0233
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 22
REMARK 3 RESIDUE RANGE : B 321 B 581
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7643 -4.7001 -30.5172
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.1673
REMARK 3 T33: 0.3667 T12: 0.0486
REMARK 3 T13: -0.1143 T23: -0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 0.0754 L22: 2.6692
REMARK 3 L33: 0.0178 L12: 0.3689
REMARK 3 L13: 0.0126 L23: 0.0138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0170 S13: 0.0898
REMARK 3 S21: -0.1342 S22: -0.0337 S23: 0.7942
REMARK 3 S31: 0.0158 S32: 0.0521 S33: -0.0008
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 4RE5 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 RCSB087233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : RIGAKU CONFOCAL BLUE OPTICS
REMARK 200 OPTICS : MIRRORS (BLUE)
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90022
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.930
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.81
REMARK 200 R MERGE FOR SHELL (I) : 68.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.270
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 2HU5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 78 MM SODIUM ACETATE BUFFER, 2.4% W/V
REMARK 280 PEG MW4000, 6.7MM DITHIOTHREITOL AND 0.44 MM EDTA. THE PROTEIN
REMARK 280 WAS CO-CRYSTALLIZED WITH THE INHIBITOR., PH 4.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.90650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.04000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.04000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.90650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.21500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS DIMER CONSISTING OF CHAINS A AND
REMARK 300 B OF THE ASYMMETRIC UNIT.
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: 3530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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 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 MET A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
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 PRO B 6
REMARK 465 VAL B 7
REMARK 465 ARG B 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 GLU A 8 CG CD OE1 OE2
REMARK 470 PHE A 9 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 11 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 LYS A 94 CE NZ
REMARK 470 ARG A 497 CD NE CZ NH1 NH2
REMARK 470 GLU A 498 CD OE1 OE2
REMARK 470 GLU B 8 CG CD OE1 OE2
REMARK 470 PHE B 9 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 11 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 32 CG OD1 OD2
REMARK 470 LYS B 35 NZ
REMARK 470 GLU B 43 CG CD OE1 OE2
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 ARG B 61 NE CZ NH1 NH2
REMARK 470 LYS B 94 CE NZ
REMARK 470 ARG B 99 CZ NH1 NH2
REMARK 470 LYS B 207 CG CD CE NZ
REMARK 470 ARG B 216 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 226 NE CZ NH1 NH2
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 470 LYS B 238 CD CE NZ
REMARK 470 SER B 241 OG
REMARK 470 ARG B 244 CZ NH1 NH2
REMARK 470 LEU B 290 CG CD1 CD2
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 GLU B 315 CG CD OE1 OE2
REMARK 470 LEU B 317 CG CD1 CD2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 ARG B 327 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 328 CG CD NE CZ NH1 NH2
REMARK 470 SER B 329 OG
REMARK 470 ILE B 330 CG1 CG2 CD1
REMARK 470 ARG B 334 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 345 CD NE CZ NH1 NH2
REMARK 470 GLU B 352 CG CD OE1 OE2
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 ARG B 511 NE CZ NH1 NH2
REMARK 470 GLU B 580 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 965 O HOH A 1028 2.18
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 B 149 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 149 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 497 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 497 NE - CZ - NH2 ANGL. DEV. = -6.0 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 -128.38 46.73
REMARK 500 ASP A 52 40.48 -142.66
REMARK 500 ARG A 61 -80.59 -99.86
REMARK 500 THR A 130 -167.58 -118.16
REMARK 500 PRO A 151 3.95 -66.15
REMARK 500 ASP A 414 43.36 -143.03
REMARK 500 SER A 445 -123.37 67.79
REMARK 500 ALA A 469 49.46 39.04
REMARK 500 ASP B 32 -126.60 45.10
REMARK 500 ASP B 52 -54.86 -140.18
REMARK 500 ARG B 61 -81.00 -98.60
REMARK 500 THR B 130 -169.81 -119.78
REMARK 500 PRO B 151 1.75 -69.06
REMARK 500 SER B 445 -124.67 67.83
REMARK 500 ALA B 469 52.91 38.73
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 A 899 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A1053 DISTANCE = 5.12 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 B 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 B 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 ACT A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y3A B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RE6 RELATED DB: PDB
DBREF 4RE5 A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 4RE5 B 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
HET Y3A A 601 20
HET ACT A 602 4
HET MPD A 603 8
HET CL A 604 1
HET Y3A B 601 20
HET MPD B 602 8
HET MPD B 603 8
HETNAM Y3A N-[(BENZYLOXY)CARBONYL]GLYCYL-N-[(2S,3R)-4-CHLORO-3-
HETNAM 2 Y3A HYDROXY-1-PHENYLBUTAN-2-YL]GLYCINAMIDE
HETNAM ACT ACETATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CL CHLORIDE ION
HETSYN Y3A Z-GLY-GLY-PHE-CHLOROMETHYL KETONE (BOUND FORM)
FORMUL 3 Y3A 2(C22 H26 CL N3 O5)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 MPD 3(C6 H14 O2)
FORMUL 6 CL CL 1-
FORMUL 10 HOH *662(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 GLY A 494 1 13
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 ARG A 581 1 22
HELIX 14 14 PHE B 9 VAL B 22 1 14
HELIX 15 15 LYS B 238 ARG B 244 1 7
HELIX 16 16 PRO B 323 ARG B 328 1 6
HELIX 17 17 ASP B 379 ALA B 388 1 10
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 LEU B 480 1 8
HELIX 22 22 ASP B 482 GLY B 494 1 13
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 PRO B 528 ARG B 542 1 15
HELIX 26 26 THR B 560 GLU B 580 1 21
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 SER A 42 -1 O LYS A 35 N VAL A 31
SHEET 3 A 4 SER A 45 TYR A 51 -1 O ASN A 47 N GLY A 40
SHEET 4 A 4 VAL A 57 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 GLU A 103 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 GLY A 117 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 ALA A 165 N SER A 157
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O SER A 176 N GLY A 168
SHEET 4 D 4 ARG A 188 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 VAL A 223 N VAL A 208
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 VAL A 262 N TRP A 250
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 VAL A 278 N VAL A 271
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 THR A 348 N VAL A 336
SHEET 3 H16 HIS A 391 PRO A 395 -1 O VAL A 392 N LEU A 351
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 GLY A 465 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 GLY B 465 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 LEU B 351 O VAL B 392
SHEET 16 H16 ILE B 330 GLU B 339 -1 N VAL B 336 O THR B 348
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 GLY B 29
SHEET 3 I 4 SER B 45 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 I 4 THR B 56 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 GLU B 103 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 GLY B 171 -1 O ALA B 165 N ASP B 158
SHEET 3 L 4 ARG B 174 ASN B 181 -1 O SER B 176 N GLY B 168
SHEET 4 L 4 ARG B 188 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 M 4 GLY B 195 ILE B 202 0
SHEET 2 M 4 VAL B 208 THR B 214 -1 O GLU B 213 N SER B 196
SHEET 3 M 4 ALA B 218 VAL B 223 -1 O VAL B 223 N VAL B 208
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 VAL B 262 N TRP B 250
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 VAL B 278 N VAL B 271
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 VAL B 309 N THR B 297
SHEET 4 O 4 PRO B 316 LEU B 318 -1 O LEU B 317 N ILE B 308
LINK OG SER A 445 C4 Y3A A 601 1555 1555 1.38
LINK OG SER B 445 C4 Y3A B 601 1555 1555 1.39
LINK NE2 HIS A 556 C15 Y3A A 601 1555 1555 1.49
LINK NE2 HIS B 556 C15 Y3A B 601 1555 1555 1.49
CISPEP 1 LEU A 311 PRO A 312 0 6.87
CISPEP 2 THR A 358 PRO A 359 0 2.76
CISPEP 3 GLY A 369 PRO A 370 0 6.24
CISPEP 4 LEU B 311 PRO B 312 0 0.93
CISPEP 5 THR B 358 PRO B 359 0 6.06
CISPEP 6 GLY B 369 PRO B 370 0 10.04
SITE 1 AC1 9 GLY A 368 GLY A 369 SER A 445 TYR A 446
SITE 2 AC1 9 PHE A 485 PHE A 488 ARG A 526 HIS A 556
SITE 3 AC1 9 HOH A1130
SITE 1 AC2 3 ARG A 277 HOH A 837 HOH A 848
SITE 1 AC3 5 TRP A 337 ARG A 345 TYR A 403 TRP A 407
SITE 2 AC3 5 HOH A 807
SITE 1 AC4 7 GLY B 368 GLY B 369 SER B 445 TYR B 446
SITE 2 AC4 7 PHE B 485 ARG B 526 HIS B 556
SITE 1 AC5 4 ASN B 65 SER B 66 ILE B 114 HOH B 708
SITE 1 AC6 6 HIS A 549 LEU A 569 PHE A 573 HIS B 549
SITE 2 AC6 6 PRO B 570 HOH B 748
CRYST1 63.813 104.430 170.080 90.00 90.00 90.00 P 21 21 21 8
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 0.015671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005880 0.00000
TER 4423 ARG A 581
TER 8699 ARG B 581
MASTER 520 0 7 26 74 0 11 6 9322 2 72 90
END |