HEADER HYDROLASE 31-OCT-09 3KHX
TITLE CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE
TITLE 2 (SAPEP/DAPE) IN THE APO-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIPEPTIDASE SACOL1801;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: METALLOPEPTIDASE, DAPE;
COMPND 5 EC: 3.4.13.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 93062;
SOURCE 4 STRAIN: COL;
SOURCE 5 GENE: DIPEPTIDASE PEPV(SACOL1801);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DIPEPTIDASE, DAPE, METALLOPEPTIDASE, HYDROLASE, METAL-BINDING,
KEYWDS 2 METALLOPROTEASE, PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.GIRISH,B.GOPAL
REVDAT 3 01-NOV-23 3KHX 1 SEQADV
REVDAT 2 28-SEP-11 3KHX 1 JRNL VERSN
REVDAT 1 07-JUL-10 3KHX 0
JRNL AUTH T.S.GIRISH,B.GOPAL
JRNL TITL CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE
JRNL TITL 2 (SAPEP) REVEALS LARGE DOMAIN MOTIONS BETWEEN THE
JRNL TITL 3 MANGANESE-BOUND AND APO-STATES
JRNL REF J.BIOL.CHEM. V. 285 29406 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20610394
JRNL DOI 10.1074/JBC.M110.147579
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 48664
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2605
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) : 3598
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.77000
REMARK 3 B22 (A**2) : -3.24000
REMARK 3 B33 (A**2) : 2.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.320
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.242
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.494
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6668 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9048 ; 1.246 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 838 ; 6.211 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 324 ;35.166 ;25.309
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1059 ;17.707 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;19.486 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 999 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5152 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4193 ; 0.591 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6699 ; 1.094 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2475 ; 1.552 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2349 ; 2.483 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 6 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9340 4.0168 0.3684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0578 T22: 0.1143
REMARK 3 T33: 0.0186 T12: -0.0408
REMARK 3 T13: -0.0075 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 2.4669 L22: 2.3154
REMARK 3 L33: 3.2445 L12: 0.1905
REMARK 3 L13: 0.2503 L23: 0.2632
REMARK 3 S TENSOR
REMARK 3 S11: 0.1301 S12: -0.1978 S13: -0.0079
REMARK 3 S21: 0.2640 S22: -0.1727 S23: -0.1664
REMARK 3 S31: 0.1278 S32: 0.0743 S33: 0.0426
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 : A 390 A 465
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0711 4.4801 16.0846
REMARK 3 T TENSOR
REMARK 3 T11: 0.6096 T22: 0.8573
REMARK 3 T33: 0.3893 T12: -0.1584
REMARK 3 T13: -0.1538 T23: 0.1603
REMARK 3 L TENSOR
REMARK 3 L11: 1.8933 L22: 5.6898
REMARK 3 L33: 3.7564 L12: -2.6539
REMARK 3 L13: 0.8490 L23: 0.9515
REMARK 3 S TENSOR
REMARK 3 S11: -0.2682 S12: -0.4726 S13: 0.2136
REMARK 3 S21: 0.9338 S22: 0.2602 S23: -0.7071
REMARK 3 S31: 0.3953 S32: 0.1222 S33: 0.0079
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 : B 190 B 384
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9231 17.9505 42.4685
REMARK 3 T TENSOR
REMARK 3 T11: 0.0450 T22: 0.1668
REMARK 3 T33: 0.1336 T12: 0.0060
REMARK 3 T13: 0.0698 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 1.5225 L22: 5.1724
REMARK 3 L33: 1.7508 L12: 0.0904
REMARK 3 L13: 0.4392 L23: -0.9682
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0295 S13: 0.1346
REMARK 3 S21: 0.2255 S22: 0.0287 S23: 0.1503
REMARK 3 S31: -0.1096 S32: 0.0157 S33: -0.0339
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 : A 185 A 384
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1176 56.4836 9.2140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0402 T22: 0.1230
REMARK 3 T33: 0.0561 T12: 0.0038
REMARK 3 T13: -0.0034 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 2.0079 L22: 5.5104
REMARK 3 L33: 1.9725 L12: -1.0427
REMARK 3 L13: -0.2713 L23: 1.2173
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: 0.0904 S13: -0.0589
REMARK 3 S21: -0.2500 S22: -0.0312 S23: -0.1264
REMARK 3 S31: 0.1452 S32: -0.0829 S33: -0.0555
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 : B 6 B 175
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9117 -32.9980 38.9504
REMARK 3 T TENSOR
REMARK 3 T11: 0.0303 T22: 0.0900
REMARK 3 T33: 0.1016 T12: -0.0070
REMARK 3 T13: 0.0280 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 2.5217 L22: 4.9389
REMARK 3 L33: 2.1071 L12: -0.5351
REMARK 3 L13: -0.2455 L23: 0.9548
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: 0.0329 S13: -0.1517
REMARK 3 S21: 0.2749 S22: -0.1421 S23: 0.1627
REMARK 3 S31: 0.1099 S32: -0.2939 S33: 0.0976
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 : B 390 B 465
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7191 -33.6828 38.3811
REMARK 3 T TENSOR
REMARK 3 T11: 0.2452 T22: 1.0324
REMARK 3 T33: 0.8122 T12: -0.2272
REMARK 3 T13: 0.2462 T23: -0.3599
REMARK 3 L TENSOR
REMARK 3 L11: 5.9190 L22: 5.2601
REMARK 3 L33: 1.1424 L12: -0.7966
REMARK 3 L13: 2.2724 L23: 0.4726
REMARK 3 S TENSOR
REMARK 3 S11: 0.1989 S12: -0.9867 S13: -0.4091
REMARK 3 S21: 0.4325 S22: -0.4126 S23: 1.5202
REMARK 3 S31: 0.2544 S32: -0.7952 S33: 0.2137
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51315
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 68.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
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) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : 0.41600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 1LFW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M BIS-TRIS,
REMARK 280 18.0% PEG 6000, PH 6.5, MICROBATCH METHOD UNDER OIL, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 67.08600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 GLY A -10
REMARK 465 LEU A -9
REMARK 465 VAL A -8
REMARK 465 PRO A -7
REMARK 465 ARG A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 GLY A 270
REMARK 465 MET A 271
REMARK 465 ASP A 272
REMARK 465 PRO A 273
REMARK 465 SER A 274
REMARK 465 ILE A 275
REMARK 465 PHE A 320
REMARK 465 HIS A 321
REMARK 465 THR A 322
REMARK 465 ASP A 323
REMARK 465 VAL A 324
REMARK 465 MET A 325
REMARK 465 GLY A 326
REMARK 465 ASP A 406
REMARK 465 MET A 407
REMARK 465 THR A 408
REMARK 465 GLU A 409
REMARK 465 PRO A 410
REMARK 465 TYR A 411
REMARK 465 THR A 412
REMARK 465 ILE A 413
REMARK 465 GLY A 414
REMARK 465 GLY A 415
REMARK 465 GLY A 416
REMARK 465 THR A 417
REMARK 465 TYR A 418
REMARK 465 ALA A 419
REMARK 465 ARG A 420
REMARK 465 ASN A 421
REMARK 465 LEU A 422
REMARK 465 ASP A 423
REMARK 465 LYS A 424
REMARK 465 GLY A 425
REMARK 465 VAL A 426
REMARK 465 ALA A 427
REMARK 465 PHE A 428
REMARK 465 GLY A 429
REMARK 465 ALA A 430
REMARK 465 MET A 431
REMARK 465 PHE A 432
REMARK 465 SER A 433
REMARK 465 ASP A 434
REMARK 465 SER A 435
REMARK 465 GLU A 436
REMARK 465 ASP A 437
REMARK 465 LEU A 438
REMARK 465 MET A 439
REMARK 465 HIS A 440
REMARK 465 MET B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 GLY B -10
REMARK 465 LEU B -9
REMARK 465 VAL B -8
REMARK 465 PRO B -7
REMARK 465 ARG B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 SER B 0
REMARK 465 ALA B 90
REMARK 465 GLY B 91
REMARK 465 ASP B 92
REMARK 465 GLY B 93
REMARK 465 TRP B 94
REMARK 465 ASP B 95
REMARK 465 THR B 196
REMARK 465 GLU B 197
REMARK 465 ASN B 405
REMARK 465 ASP B 406
REMARK 465 MET B 407
REMARK 465 THR B 408
REMARK 465 GLU B 409
REMARK 465 PRO B 410
REMARK 465 TYR B 411
REMARK 465 THR B 412
REMARK 465 ILE B 413
REMARK 465 GLY B 414
REMARK 465 GLY B 415
REMARK 465 GLY B 416
REMARK 465 THR B 417
REMARK 465 TYR B 418
REMARK 465 ALA B 419
REMARK 465 ARG B 420
REMARK 465 ASN B 421
REMARK 465 LEU B 422
REMARK 465 ASP B 423
REMARK 465 LYS B 424
REMARK 465 GLY B 425
REMARK 465 VAL B 426
REMARK 465 ALA B 427
REMARK 465 PHE B 428
REMARK 465 GLY B 429
REMARK 465 ALA B 430
REMARK 465 MET B 431
REMARK 465 PHE B 432
REMARK 465 SER B 433
REMARK 465 ASP B 434
REMARK 465 SER B 435
REMARK 465 GLU B 436
REMARK 465 ASP B 437
REMARK 465 LEU B 438
REMARK 465 MET B 439
REMARK 465 HIS B 440
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 GLN A 7 CG CD OE1 NE2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 ASP A 152 CG OD1 OD2
REMARK 470 THR A 196 OG1 CG2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 ASP A 200 CG OD1 OD2
REMARK 470 GLU A 213 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLN A 249 CG CD OE1 NE2
REMARK 470 LYS A 266 CB CG CD CE NZ
REMARK 470 VAL A 268 CB CG1 CG2
REMARK 470 HIS A 269 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 319 CB CG CD CE NZ
REMARK 470 ASP A 327 CG OD1 OD2
REMARK 470 PHE A 355 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 358 CG CD OE1 OE2
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 ARG A 363 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 366 CG OD1 ND2
REMARK 470 GLN A 369 CG CD OE1 NE2
REMARK 470 LYS A 379 CG CD CE NZ
REMARK 470 VAL A 397 CG1 CG2
REMARK 470 TYR A 400 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 401 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 405 CG OD1 ND2
REMARK 470 GLN A 441 CG CD OE1 NE2
REMARK 470 LYS A 442 CG CD CE NZ
REMARK 470 TYR A 445 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 449 CG CD CE NZ
REMARK 470 GLU A 469 CG CD OE1 OE2
REMARK 470 LYS B 3 CG CD CE NZ
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 GLN B 7 CG CD OE1 NE2
REMARK 470 GLN B 8 CG CD OE1 NE2
REMARK 470 GLU B 34 CG CD OE1 OE2
REMARK 470 ILE B 109 CG1 CG2 CD1
REMARK 470 LYS B 128 CG CD CE NZ
REMARK 470 LYS B 138 CG CD CE NZ
REMARK 470 LEU B 195 CG CD1 CD2
REMARK 470 ASP B 200 CG OD1 OD2
REMARK 470 ASP B 255 CG OD1 OD2
REMARK 470 THR B 322 OG1 CG2
REMARK 470 VAL B 324 CG1 CG2
REMARK 470 MET B 325 CG SD CE
REMARK 470 GLU B 340 CG CD OE1 OE2
REMARK 470 ASN B 341 CG OD1 ND2
REMARK 470 GLN B 369 CG CD OE1 NE2
REMARK 470 GLN B 441 CG CD OE1 NE2
REMARK 470 LYS B 442 CG CD CE NZ
REMARK 470 TYR B 445 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 449 CG CD CE NZ
REMARK 470 GLU B 468 CG CD OE1 OE2
REMARK 470 GLU B 469 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 449 C
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 GLU A 230 -66.97 -135.46
REMARK 500 ALA A 267 -159.95 -104.45
REMARK 500 VAL A 268 -163.70 112.92
REMARK 500 ALA A 342 34.92 72.43
REMARK 500 GLN A 403 -33.65 -134.67
REMARK 500 ALA B 110 166.31 161.52
REMARK 500 GLU B 230 -164.97 -111.01
REMARK 500 VAL B 324 -133.07 61.29
REMARK 500 GLN B 403 57.00 -92.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KHZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF R350A MUTANT OF STAPHYLOCOCCUS AUREUS
REMARK 900 METALLOPEPTIDASE (SAPEP/DAPE) IN THE APO-FORM
REMARK 900 RELATED ID: 3KI9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS METALLOPEPTIDASE (SAPEP/
REMARK 900 DAPE) IN THE MN2+ BOUND FORM
DBREF 3KHX A 1 469 UNP Q5HF23 PEPVL_STAAC 1 469
DBREF 3KHX B 1 469 UNP Q5HF23 PEPVL_STAAC 1 469
SEQADV 3KHX MET A -22 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY A -21 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A -20 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A -19 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -18 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -17 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -16 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -15 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -14 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -13 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A -12 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A -11 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY A -10 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX LEU A -9 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX VAL A -8 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX PRO A -7 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX ARG A -6 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY A -5 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A -4 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS A -3 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX MET A -2 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX ALA A -1 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER A 0 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX MET B -22 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY B -21 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B -20 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B -19 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -18 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -17 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -16 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -15 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -14 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -13 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B -12 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B -11 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY B -10 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX LEU B -9 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX VAL B -8 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX PRO B -7 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX ARG B -6 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX GLY B -5 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B -4 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX HIS B -3 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX MET B -2 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX ALA B -1 UNP Q5HF23 EXPRESSION TAG
SEQADV 3KHX SER B 0 UNP Q5HF23 EXPRESSION TAG
SEQRES 1 A 492 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 492 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET TRP LYS
SEQRES 3 A 492 GLU LYS VAL GLN GLN TYR GLU ASP GLN ILE ILE ASN ASP
SEQRES 4 A 492 LEU LYS GLY LEU LEU ALA ILE GLU SER VAL ARG ASP ASP
SEQRES 5 A 492 ALA LYS ALA SER GLU ASP ALA PRO VAL GLY PRO GLY PRO
SEQRES 6 A 492 ARG LYS ALA LEU ASP TYR MET TYR GLU ILE ALA HIS ARG
SEQRES 7 A 492 ASP GLY PHE THR THR HIS ASP VAL ASP HIS ILE ALA GLY
SEQRES 8 A 492 ARG ILE GLU ALA GLY LYS GLY ASN ASP VAL LEU GLY ILE
SEQRES 9 A 492 LEU CYS HIS VAL ASP VAL VAL PRO ALA GLY ASP GLY TRP
SEQRES 10 A 492 ASP SER ASN PRO PHE GLU PRO VAL VAL THR GLU ASP ALA
SEQRES 11 A 492 ILE ILE ALA ARG GLY THR LEU ASP ASP LYS GLY PRO THR
SEQRES 12 A 492 ILE ALA ALA TYR TYR ALA ILE LYS ILE LEU GLU ASP MET
SEQRES 13 A 492 ASN VAL ASP TRP LYS LYS ARG ILE HIS MET ILE ILE GLY
SEQRES 14 A 492 THR ASP GLU GLU SER ASP TRP LYS CYS THR ASP ARG TYR
SEQRES 15 A 492 PHE LYS THR GLU GLU MET PRO THR LEU GLY PHE ALA PRO
SEQRES 16 A 492 ASP ALA GLU PHE PRO CYS ILE HIS GLY GLU LYS GLY ILE
SEQRES 17 A 492 THR THR PHE ASP LEU VAL GLN ASN LYS LEU THR GLU ASP
SEQRES 18 A 492 GLN ASP GLU PRO ASP TYR GLU LEU ILE THR PHE LYS SER
SEQRES 19 A 492 GLY GLU ARG TYR ASN MET VAL PRO ASP HIS ALA GLU ALA
SEQRES 20 A 492 ARG VAL LEU VAL LYS GLU ASN MET THR ASP VAL ILE GLN
SEQRES 21 A 492 ASP PHE GLU TYR PHE LEU GLU GLN ASN HIS LEU GLN GLY
SEQRES 22 A 492 ASP SER THR VAL ASP SER GLY ILE LEU VAL LEU THR VAL
SEQRES 23 A 492 GLU GLY LYS ALA VAL HIS GLY MET ASP PRO SER ILE GLY
SEQRES 24 A 492 VAL ASN ALA GLY LEU TYR LEU LEU LYS PHE LEU ALA SER
SEQRES 25 A 492 LEU ASN LEU ASP ASN ASN ALA GLN ALA PHE VAL ALA PHE
SEQRES 26 A 492 SER ASN ARG TYR LEU PHE ASN SER ASP PHE GLY GLU LYS
SEQRES 27 A 492 MET GLY MET LYS PHE HIS THR ASP VAL MET GLY ASP VAL
SEQRES 28 A 492 THR THR ASN ILE GLY VAL ILE THR TYR ASP ASN GLU ASN
SEQRES 29 A 492 ALA GLY LEU PHE GLY ILE ASN LEU ARG TYR PRO GLU GLY
SEQRES 30 A 492 PHE GLU PHE GLU LYS ALA MET ASP ARG PHE ALA ASN GLU
SEQRES 31 A 492 ILE GLN GLN TYR GLY PHE GLU VAL LYS LEU GLY LYS VAL
SEQRES 32 A 492 GLN PRO PRO HIS TYR VAL ASP LYS ASN ASP PRO PHE VAL
SEQRES 33 A 492 GLN LYS LEU VAL THR ALA TYR ARG ASN GLN THR ASN ASP
SEQRES 34 A 492 MET THR GLU PRO TYR THR ILE GLY GLY GLY THR TYR ALA
SEQRES 35 A 492 ARG ASN LEU ASP LYS GLY VAL ALA PHE GLY ALA MET PHE
SEQRES 36 A 492 SER ASP SER GLU ASP LEU MET HIS GLN LYS ASN GLU TYR
SEQRES 37 A 492 ILE THR LYS LYS GLN LEU PHE ASN ALA THR SER ILE TYR
SEQRES 38 A 492 LEU GLU ALA ILE TYR SER LEU CYS VAL GLU GLU
SEQRES 1 B 492 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 492 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET TRP LYS
SEQRES 3 B 492 GLU LYS VAL GLN GLN TYR GLU ASP GLN ILE ILE ASN ASP
SEQRES 4 B 492 LEU LYS GLY LEU LEU ALA ILE GLU SER VAL ARG ASP ASP
SEQRES 5 B 492 ALA LYS ALA SER GLU ASP ALA PRO VAL GLY PRO GLY PRO
SEQRES 6 B 492 ARG LYS ALA LEU ASP TYR MET TYR GLU ILE ALA HIS ARG
SEQRES 7 B 492 ASP GLY PHE THR THR HIS ASP VAL ASP HIS ILE ALA GLY
SEQRES 8 B 492 ARG ILE GLU ALA GLY LYS GLY ASN ASP VAL LEU GLY ILE
SEQRES 9 B 492 LEU CYS HIS VAL ASP VAL VAL PRO ALA GLY ASP GLY TRP
SEQRES 10 B 492 ASP SER ASN PRO PHE GLU PRO VAL VAL THR GLU ASP ALA
SEQRES 11 B 492 ILE ILE ALA ARG GLY THR LEU ASP ASP LYS GLY PRO THR
SEQRES 12 B 492 ILE ALA ALA TYR TYR ALA ILE LYS ILE LEU GLU ASP MET
SEQRES 13 B 492 ASN VAL ASP TRP LYS LYS ARG ILE HIS MET ILE ILE GLY
SEQRES 14 B 492 THR ASP GLU GLU SER ASP TRP LYS CYS THR ASP ARG TYR
SEQRES 15 B 492 PHE LYS THR GLU GLU MET PRO THR LEU GLY PHE ALA PRO
SEQRES 16 B 492 ASP ALA GLU PHE PRO CYS ILE HIS GLY GLU LYS GLY ILE
SEQRES 17 B 492 THR THR PHE ASP LEU VAL GLN ASN LYS LEU THR GLU ASP
SEQRES 18 B 492 GLN ASP GLU PRO ASP TYR GLU LEU ILE THR PHE LYS SER
SEQRES 19 B 492 GLY GLU ARG TYR ASN MET VAL PRO ASP HIS ALA GLU ALA
SEQRES 20 B 492 ARG VAL LEU VAL LYS GLU ASN MET THR ASP VAL ILE GLN
SEQRES 21 B 492 ASP PHE GLU TYR PHE LEU GLU GLN ASN HIS LEU GLN GLY
SEQRES 22 B 492 ASP SER THR VAL ASP SER GLY ILE LEU VAL LEU THR VAL
SEQRES 23 B 492 GLU GLY LYS ALA VAL HIS GLY MET ASP PRO SER ILE GLY
SEQRES 24 B 492 VAL ASN ALA GLY LEU TYR LEU LEU LYS PHE LEU ALA SER
SEQRES 25 B 492 LEU ASN LEU ASP ASN ASN ALA GLN ALA PHE VAL ALA PHE
SEQRES 26 B 492 SER ASN ARG TYR LEU PHE ASN SER ASP PHE GLY GLU LYS
SEQRES 27 B 492 MET GLY MET LYS PHE HIS THR ASP VAL MET GLY ASP VAL
SEQRES 28 B 492 THR THR ASN ILE GLY VAL ILE THR TYR ASP ASN GLU ASN
SEQRES 29 B 492 ALA GLY LEU PHE GLY ILE ASN LEU ARG TYR PRO GLU GLY
SEQRES 30 B 492 PHE GLU PHE GLU LYS ALA MET ASP ARG PHE ALA ASN GLU
SEQRES 31 B 492 ILE GLN GLN TYR GLY PHE GLU VAL LYS LEU GLY LYS VAL
SEQRES 32 B 492 GLN PRO PRO HIS TYR VAL ASP LYS ASN ASP PRO PHE VAL
SEQRES 33 B 492 GLN LYS LEU VAL THR ALA TYR ARG ASN GLN THR ASN ASP
SEQRES 34 B 492 MET THR GLU PRO TYR THR ILE GLY GLY GLY THR TYR ALA
SEQRES 35 B 492 ARG ASN LEU ASP LYS GLY VAL ALA PHE GLY ALA MET PHE
SEQRES 36 B 492 SER ASP SER GLU ASP LEU MET HIS GLN LYS ASN GLU TYR
SEQRES 37 B 492 ILE THR LYS LYS GLN LEU PHE ASN ALA THR SER ILE TYR
SEQRES 38 B 492 LEU GLU ALA ILE TYR SER LEU CYS VAL GLU GLU
FORMUL 3 HOH *182(H2 O)
HELIX 1 1 TRP A 2 GLN A 8 1 7
HELIX 2 2 TYR A 9 ALA A 22 1 14
HELIX 3 3 GLY A 39 ASP A 56 1 18
HELIX 4 4 ASP A 116 MET A 133 1 18
HELIX 5 5 ASP A 157 GLU A 163 1 7
HELIX 6 6 ASN A 231 ASN A 246 1 16
HELIX 7 7 ASN A 278 ALA A 288 1 11
HELIX 8 8 ASP A 293 LEU A 307 1 15
HELIX 9 9 GLY A 313 GLY A 317 5 5
HELIX 10 10 GLU A 356 GLN A 369 1 14
HELIX 11 11 VAL A 386 ASN A 389 5 4
HELIX 12 12 ASP A 390 ASN A 402 1 13
HELIX 13 13 LYS A 448 VAL A 467 1 20
HELIX 14 14 MET B 1 GLN B 8 1 8
HELIX 15 15 TYR B 9 ALA B 22 1 14
HELIX 16 16 ASP B 28 ALA B 32 5 5
HELIX 17 17 GLY B 39 ASP B 56 1 18
HELIX 18 18 ASP B 116 MET B 133 1 18
HELIX 19 19 ASP B 157 GLU B 163 1 7
HELIX 20 20 MET B 232 ASN B 246 1 15
HELIX 21 21 ASP B 272 GLY B 276 5 5
HELIX 22 22 ASN B 278 ALA B 288 1 11
HELIX 23 23 ASP B 293 LEU B 307 1 15
HELIX 24 24 GLU B 356 GLN B 370 1 15
HELIX 25 25 VAL B 386 ASN B 389 5 4
HELIX 26 26 ASP B 390 GLN B 403 1 14
HELIX 27 27 LYS B 448 VAL B 467 1 20
SHEET 1 A 5 THR A 59 VAL A 63 0
SHEET 2 A 5 ALA A 67 GLY A 73 -1 O ALA A 67 N VAL A 63
SHEET 3 A 5 ARG A 140 GLY A 146 -1 O ILE A 145 N GLY A 68
SHEET 4 A 5 VAL A 78 HIS A 84 1 N CYS A 83 O GLY A 146
SHEET 5 A 5 LEU A 168 PHE A 170 1 O LEU A 168 N GLY A 80
SHEET 1 B 3 VAL A 102 VAL A 103 0
SHEET 2 B 3 ALA A 107 ILE A 109 -1 O ILE A 109 N VAL A 102
SHEET 3 B 3 TYR A 445 THR A 447 -1 O ILE A 446 N ILE A 108
SHEET 1 C 8 GLN A 249 ASP A 255 0
SHEET 2 C 8 ILE A 258 GLU A 264 -1 O VAL A 260 N THR A 253
SHEET 3 C 8 HIS A 221 VAL A 228 -1 N VAL A 226 O LEU A 259
SHEET 4 C 8 TYR A 204 SER A 211 -1 N GLU A 205 O LEU A 227
SHEET 5 C 8 THR A 329 ASP A 338 -1 O TYR A 337 N PHE A 209
SHEET 6 C 8 LEU A 344 TYR A 351 -1 O ARG A 350 N THR A 329
SHEET 7 C 8 GLY A 184 GLN A 192 -1 N PHE A 188 O ILE A 347
SHEET 8 C 8 PHE A 373 GLN A 381 -1 O GLN A 381 N ILE A 185
SHEET 1 D 5 THR B 59 VAL B 63 0
SHEET 2 D 5 ALA B 67 GLY B 73 -1 O ALA B 67 N VAL B 63
SHEET 3 D 5 ARG B 140 GLY B 146 -1 O ILE B 145 N GLY B 68
SHEET 4 D 5 VAL B 78 HIS B 84 1 N LEU B 79 O HIS B 142
SHEET 5 D 5 LEU B 168 PHE B 170 1 O PHE B 170 N GLY B 80
SHEET 1 E 3 VAL B 102 VAL B 103 0
SHEET 2 E 3 ALA B 107 ILE B 109 -1 O ILE B 109 N VAL B 102
SHEET 3 E 3 TYR B 445 THR B 447 -1 O ILE B 446 N ILE B 108
SHEET 1 F 8 GLN B 249 ASP B 255 0
SHEET 2 F 8 ILE B 258 GLU B 264 -1 O VAL B 260 N THR B 253
SHEET 3 F 8 HIS B 221 VAL B 228 -1 N VAL B 226 O LEU B 259
SHEET 4 F 8 TYR B 204 SER B 211 -1 N GLU B 205 O LEU B 227
SHEET 5 F 8 THR B 329 ASP B 338 -1 O TYR B 337 N PHE B 209
SHEET 6 F 8 LEU B 344 TYR B 351 -1 O GLY B 346 N VAL B 334
SHEET 7 F 8 GLY B 184 GLN B 192 -1 N PHE B 188 O ILE B 347
SHEET 8 F 8 PHE B 373 GLN B 381 -1 O GLU B 374 N VAL B 191
SSBOND 1 CYS A 155 CYS A 178 1555 1555 2.03
SSBOND 2 CYS B 155 CYS B 178 1555 1555 2.04
CISPEP 1 ASP A 115 ASP A 116 0 9.47
CISPEP 2 ASP B 115 ASP B 116 0 2.97
CISPEP 3 ASP B 323 VAL B 324 0 0.78
CISPEP 4 ASN B 341 ALA B 342 0 -8.28
CRYST1 64.823 134.172 68.282 90.00 94.52 90.00 P 1 21 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 0.015427 0.000000 0.001220 0.00000
SCALE2 0.000000 0.007453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END