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HEADER HYDROLASE 17-AUG-07 2QZP
TITLE CRYSTAL STRUCTURE OF MUTATION OF AN ACYLPTIDE
TITLE 2 HYDROLASE/ESTERASE FROM AEROPYRUM PERNIX K1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 21-582;
COMPND 5 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-
COMPND 6 PEPTIDASE;
COMPND 7 EC: 3.4.19.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS CRYSTAL STRUCTURE, TRUNCATED, ACYLPEPTIDE HYDROLASE,
KEYWDS 2 AEROPYRUM PERNIX K1, CYTOPLASM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.F.ZHANG,B.S.ZHENG,Z.RAO
REVDAT 1 02-OCT-07 2QZP 0
JRNL AUTH H.F.ZHANG,B.S.ZHENG,Z.RAO
JRNL TITL EXPRESSION, PURIFICATION AND CRYSTAL STRUCTURE OF
JRNL TITL 2 A TRUNCATED ACYLPEPTIDE HYDROLASE FROM AEROPYRUM
JRNL TITL 3 PERNIX K1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 27467
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 SET) : 0.226
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1393
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3106
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 176
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8515
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 366
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.44000
REMARK 3 B22 (A**2) : -6.83000
REMARK 3 B33 (A**2) : 8.27000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 67.97
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QZP COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB044247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.17700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.77700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1VE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAAC, PEG3000, PH 4.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 31.55850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.79700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.09150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.79700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.55850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.09150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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: MONOMER
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ALA A 21
REMARK 465 ARG A 582
REMARK 465 ARG B 582
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
REMARK 500 OG1 THR A 130 OD1 ASP A 132 2.10
REMARK 500 O ARG A 511 O HOH A 630 2.10
REMARK 500 O ARG B 327 O HOH B 720 2.11
REMARK 500 N SER A 116 O HOH A 677 2.13
REMARK 500 O GLU A 562 N ALA A 564 2.17
REMARK 500 OD2 ASP A 563 O HOH A 585 2.18
REMARK 500 N GLY A 417 OE2 GLU A 419 2.18
REMARK 500 O THR B 451 O HOH B 615 2.18
REMARK 500 O LYS B 463 O HOH B 689 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 32 18.14 45.66
REMARK 500 SER A 42 171.81 -48.65
REMARK 500 GLU A 43 79.34 4.09
REMARK 500 ARG A 61 -72.77 -90.75
REMARK 500 ILE A 64 -157.55 -87.52
REMARK 500 ASN A 65 -39.35 -132.19
REMARK 500 TYR A 72 131.60 -13.45
REMARK 500 ARG A 76 155.53 176.66
REMARK 500 LYS A 85 79.23 66.24
REMARK 500 ALA A 87 -9.09 -56.09
REMARK 500 GLU A 88 6.77 81.35
REMARK 500 ARG A 99 73.74 -112.01
REMARK 500 LEU A 106 82.62 -57.19
REMARK 500 ALA A 108 37.27 -82.15
REMARK 500 MET A 112 -158.34 -157.05
REMARK 500 SER A 116 158.36 166.25
REMARK 500 PHE A 126 161.27 173.83
REMARK 500 ARG A 133 162.70 177.49
REMARK 500 PHE A 153 119.81 -33.69
REMARK 500 LEU A 187 138.63 -177.23
REMARK 500 SER A 199 155.11 171.46
REMARK 500 SER A 201 131.78 -171.39
REMARK 500 ARG A 216 -102.17 -76.90
REMARK 500 GLU A 217 -130.40 -121.60
REMARK 500 THR A 222 72.68 -118.28
REMARK 500 ALA A 247 114.10 -161.71
REMARK 500 ARG A 264 157.59 179.45
REMARK 500 GLU A 276 99.56 -56.94
REMARK 500 ARG A 287 126.40 -31.63
REMARK 500 THR A 297 -169.63 -127.99
REMARK 500 THR A 300 135.27 -173.98
REMARK 500 PRO A 306 132.74 -38.43
REMARK 500 PRO A 323 171.02 -58.37
REMARK 500 ASP A 342 20.92 -74.16
REMARK 500 PRO A 347 101.17 -58.09
REMARK 500 SER A 353 76.23 -103.11
REMARK 500 ARG A 355 22.47 -75.13
REMARK 500 PHE A 371 52.46 -62.31
REMARK 500 ALA A 372 -154.12 -128.05
REMARK 500 GLU A 373 161.66 176.86
REMARK 500 ASN A 396 70.88 -104.54
REMARK 500 TRP A 429 -70.86 -33.84
REMARK 500 ALA A 430 -68.43 -26.60
REMARK 500 SER A 445 -121.25 67.27
REMARK 500 PRO A 459 63.23 -61.55
REMARK 500 GLU A 479 5.83 -69.23
REMARK 500 LEU A 492 -3.08 -58.56
REMARK 500 GLU A 498 -5.99 -44.30
REMARK 500 ARG A 501 -61.84 -97.45
REMARK 500 PRO A 515 179.34 -55.41
REMARK 500 LEU A 516 126.41 -172.18
REMARK 500 ARG A 526 -61.67 -98.89
REMARK 500 ARG A 542 28.13 -79.55
REMARK 500 ASP A 553 40.78 37.71
REMARK 500 GLU A 562 -73.81 -56.93
REMARK 500 ASP A 563 8.49 -44.12
REMARK 500 ILE A 567 62.66 -104.79
REMARK 500 LEU A 568 6.09 -179.40
REMARK 500 ARG A 579 -61.16 -23.47
REMARK 500 GLU A 580 41.92 -74.62
REMARK 500 ASP B 34 82.06 -150.23
REMARK 500 LYS B 35 109.35 -160.38
REMARK 500 PHE B 41 79.95 -107.13
REMARK 500 SER B 42 -154.72 -167.67
REMARK 500 SER B 45 -140.77 -177.41
REMARK 500 ASN B 60 -144.13 -69.47
REMARK 500 ARG B 61 -87.76 -159.24
REMARK 500 LEU B 68 176.02 -57.51
REMARK 500 TYR B 72 122.07 -25.47
REMARK 500 VAL B 74 145.47 -33.67
REMARK 500 GLU B 88 11.95 83.78
REMARK 500 THR B 97 -37.94 -37.06
REMARK 500 ARG B 99 83.03 -150.21
REMARK 500 GLU B 107 -22.96 -35.06
REMARK 500 MET B 112 -154.10 -136.12
REMARK 500 SER B 116 -161.89 -168.70
REMARK 500 THR B 120 -83.45 -83.69
REMARK 500 GLU B 122 -17.59 -165.66
REMARK 500 VAL B 124 79.50 -111.43
REMARK 500 ARG B 133 145.53 -173.89
REMARK 500 ASP B 140 -168.96 -163.01
REMARK 500 ARG B 160 103.43 -165.05
REMARK 500 SER B 180 -177.92 179.88
REMARK 500 LEU B 187 119.30 169.35
REMARK 500 SER B 201 121.36 -172.08
REMARK 500 MET B 206 47.66 101.61
REMARK 500 ALA B 210 94.22 174.72
REMARK 500 ASP B 232 169.91 -40.86
REMARK 500 LYS B 238 64.61 -109.67
REMARK 500 ARG B 244 60.73 25.58
REMARK 500 THR B 249 -72.46 -68.02
REMARK 500 ASP B 256 -2.52 -46.12
REMARK 500 ARG B 292 49.54 77.67
REMARK 500 SER B 301 159.32 168.82
REMARK 500 LEU B 302 -35.73 -39.85
REMARK 500 THR B 304 120.26 179.68
REMARK 500 PRO B 306 104.91 -49.76
REMARK 500 PRO B 323 163.93 -39.63
REMARK 500 PRO B 361 108.42 -52.66
REMARK 500 HIS B 367 -164.59 -69.39
REMARK 500 PHE B 371 72.79 -47.07
REMARK 500 SER B 375 -151.00 -131.28
REMARK 500 ASP B 376 48.23 -97.61
REMARK 500 THR B 380 -75.00 -39.10
REMARK 500 PHE B 381 -38.09 -37.95
REMARK 500 ASN B 396 58.24 -108.63
REMARK 500 CYS B 416 68.82 69.97
REMARK 500 ALA B 427 -70.94 -53.88
REMARK 500 TRP B 429 -72.35 -35.40
REMARK 500 ALA B 430 -27.10 -39.41
REMARK 500 SER B 445 -124.47 53.33
REMARK 500 VAL B 472 -73.86 -67.51
REMARK 500 LEU B 480 41.94 -106.63
REMARK 500 SER B 496 125.77 -5.72
REMARK 500 GLU B 498 -44.18 -27.79
REMARK 500 PRO B 505 -10.30 -40.21
REMARK 500 ASP B 510 1.85 -64.96
REMARK 500 PRO B 521 106.93 -57.58
REMARK 500 LYS B 530 -72.78 -58.31
REMARK 500 PRO B 531 -37.35 -39.94
REMARK 500 LYS B 544 110.90 -16.54
REMARK 500 PHE B 546 131.89 -172.87
REMARK 500 THR B 560 160.46 167.03
REMARK 500 GLU B 562 33.79 -68.71
REMARK 500 ASP B 563 15.51 -154.54
REMARK 500 LYS B 566 0.99 -58.55
REMARK 500 GLU B 580 14.46 -59.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2QZP A 21 582 UNP Q9YBQ2 APEH_AERPE 21 582
DBREF 2QZP B 21 582 UNP Q9YBQ2 APEH_AERPE 21 582
SEQRES 1 A 562 ALA VAL GLU LYS TYR SER LEU GLN GLY VAL VAL ASP GLY
SEQRES 2 A 562 ASP LYS LEU LEU VAL VAL GLY PHE SER GLU GLY SER VAL
SEQRES 3 A 562 ASN ALA TYR LEU TYR ASP GLY GLY GLU THR VAL LYS LEU
SEQRES 4 A 562 ASN ARG GLU PRO ILE ASN SER VAL LEU ASP PRO HIS TYR
SEQRES 5 A 562 GLY VAL GLY ARG VAL ILE LEU VAL ARG ASP VAL SER LYS
SEQRES 6 A 562 GLY ALA GLU GLN HIS ALA LEU PHE LYS VAL ASN THR SER
SEQRES 7 A 562 ARG PRO GLY GLU GLU GLN ARG LEU GLU ALA VAL LYS PRO
SEQRES 8 A 562 MET ARG ILE LEU SER GLY VAL ASP THR GLY GLU ALA VAL
SEQRES 9 A 562 VAL PHE THR GLY ALA THR GLU ASP ARG VAL ALA LEU TYR
SEQRES 10 A 562 ALA LEU ASP GLY GLY GLY LEU ARG GLU LEU ALA ARG LEU
SEQRES 11 A 562 PRO GLY PHE GLY PHE VAL SER ASP ILE ARG GLY ASP LEU
SEQRES 12 A 562 ILE ALA GLY LEU GLY PHE PHE GLY GLY GLY ARG VAL SER
SEQRES 13 A 562 LEU PHE THR SER ASN LEU SER SER GLY GLY LEU ARG VAL
SEQRES 14 A 562 PHE ASP SER GLY GLU GLY SER PHE SER SER ALA SER ILE
SEQRES 15 A 562 SER PRO GLY MET LYS VAL THR ALA GLY LEU GLU THR ALA
SEQRES 16 A 562 ARG GLU ALA ARG LEU VAL THR VAL ASP PRO ARG ASP GLY
SEQRES 17 A 562 SER VAL GLU ASP LEU GLU LEU PRO SER LYS ASP PHE SER
SEQRES 18 A 562 SER TYR ARG PRO THR ALA ILE THR TRP LEU GLY TYR LEU
SEQRES 19 A 562 PRO ASP GLY ARG LEU ALA VAL VAL ALA ARG ARG GLU GLY
SEQRES 20 A 562 ARG SER ALA VAL PHE ILE ASP GLY GLU ARG VAL GLU ALA
SEQRES 21 A 562 PRO GLN GLY ASN HIS GLY ARG VAL VAL LEU TRP ARG GLY
SEQRES 22 A 562 LYS LEU VAL THR SER HIS THR SER LEU SER THR PRO PRO
SEQRES 23 A 562 ARG ILE VAL SER LEU PRO SER GLY GLU PRO LEU LEU GLU
SEQRES 24 A 562 GLY GLY LEU PRO GLU ASP LEU ARG ARG SER ILE ALA GLY
SEQRES 25 A 562 SER ARG LEU VAL TRP VAL GLU SER PHE ASP GLY SER ARG
SEQRES 26 A 562 VAL PRO THR TYR VAL LEU GLU SER GLY ARG ALA PRO THR
SEQRES 27 A 562 PRO GLY PRO THR VAL VAL LEU VAL HIS GLY GLY PRO PHE
SEQRES 28 A 562 ALA GLU ASP SER ASP SER TRP ASP THR PHE ALA ALA SER
SEQRES 29 A 562 LEU ALA ALA ALA GLY PHE HIS VAL VAL MET PRO ASN TYR
SEQRES 30 A 562 ARG GLY SER THR GLY TYR GLY GLU GLU TRP ARG LEU LYS
SEQRES 31 A 562 ILE ILE GLY ASP PRO CYS GLY GLY GLU LEU GLU ASP VAL
SEQRES 32 A 562 SER ALA ALA ALA ARG TRP ALA ARG GLU SER GLY LEU ALA
SEQRES 33 A 562 SER GLU LEU TYR ILE MET GLY TYR SER TYR GLY GLY TYR
SEQRES 34 A 562 MET THR LEU CYS ALA LEU THR MET LYS PRO GLY LEU PHE
SEQRES 35 A 562 LYS ALA GLY VAL ALA GLY ALA SER VAL VAL ASP TRP GLU
SEQRES 36 A 562 GLU MET TYR GLU LEU SER ASP ALA ALA PHE ARG ASN PHE
SEQRES 37 A 562 ILE GLU GLN LEU THR GLY GLY SER ARG GLU ILE MET ARG
SEQRES 38 A 562 SER ARG SER PRO ILE ASN HIS VAL ASP ARG ILE LYS GLU
SEQRES 39 A 562 PRO LEU ALA LEU ILE HIS PRO GLN ASN ASP SER ARG THR
SEQRES 40 A 562 PRO LEU LYS PRO LEU LEU ARG LEU MET GLY GLU LEU LEU
SEQRES 41 A 562 ALA ARG GLY LYS THR PHE GLU ALA HIS ILE ILE PRO ASP
SEQRES 42 A 562 ALA GLY HIS ALA ILE ASN THR MET GLU ASP ALA VAL LYS
SEQRES 43 A 562 ILE LEU LEU PRO ALA VAL PHE PHE LEU ALA THR GLN ARG
SEQRES 44 A 562 GLU ARG ARG
SEQRES 1 B 562 ALA VAL GLU LYS TYR SER LEU GLN GLY VAL VAL ASP GLY
SEQRES 2 B 562 ASP LYS LEU LEU VAL VAL GLY PHE SER GLU GLY SER VAL
SEQRES 3 B 562 ASN ALA TYR LEU TYR ASP GLY GLY GLU THR VAL LYS LEU
SEQRES 4 B 562 ASN ARG GLU PRO ILE ASN SER VAL LEU ASP PRO HIS TYR
SEQRES 5 B 562 GLY VAL GLY ARG VAL ILE LEU VAL ARG ASP VAL SER LYS
SEQRES 6 B 562 GLY ALA GLU GLN HIS ALA LEU PHE LYS VAL ASN THR SER
SEQRES 7 B 562 ARG PRO GLY GLU GLU GLN ARG LEU GLU ALA VAL LYS PRO
SEQRES 8 B 562 MET ARG ILE LEU SER GLY VAL ASP THR GLY GLU ALA VAL
SEQRES 9 B 562 VAL PHE THR GLY ALA THR GLU ASP ARG VAL ALA LEU TYR
SEQRES 10 B 562 ALA LEU ASP GLY GLY GLY LEU ARG GLU LEU ALA ARG LEU
SEQRES 11 B 562 PRO GLY PHE GLY PHE VAL SER ASP ILE ARG GLY ASP LEU
SEQRES 12 B 562 ILE ALA GLY LEU GLY PHE PHE GLY GLY GLY ARG VAL SER
SEQRES 13 B 562 LEU PHE THR SER ASN LEU SER SER GLY GLY LEU ARG VAL
SEQRES 14 B 562 PHE ASP SER GLY GLU GLY SER PHE SER SER ALA SER ILE
SEQRES 15 B 562 SER PRO GLY MET LYS VAL THR ALA GLY LEU GLU THR ALA
SEQRES 16 B 562 ARG GLU ALA ARG LEU VAL THR VAL ASP PRO ARG ASP GLY
SEQRES 17 B 562 SER VAL GLU ASP LEU GLU LEU PRO SER LYS ASP PHE SER
SEQRES 18 B 562 SER TYR ARG PRO THR ALA ILE THR TRP LEU GLY TYR LEU
SEQRES 19 B 562 PRO ASP GLY ARG LEU ALA VAL VAL ALA ARG ARG GLU GLY
SEQRES 20 B 562 ARG SER ALA VAL PHE ILE ASP GLY GLU ARG VAL GLU ALA
SEQRES 21 B 562 PRO GLN GLY ASN HIS GLY ARG VAL VAL LEU TRP ARG GLY
SEQRES 22 B 562 LYS LEU VAL THR SER HIS THR SER LEU SER THR PRO PRO
SEQRES 23 B 562 ARG ILE VAL SER LEU PRO SER GLY GLU PRO LEU LEU GLU
SEQRES 24 B 562 GLY GLY LEU PRO GLU ASP LEU ARG ARG SER ILE ALA GLY
SEQRES 25 B 562 SER ARG LEU VAL TRP VAL GLU SER PHE ASP GLY SER ARG
SEQRES 26 B 562 VAL PRO THR TYR VAL LEU GLU SER GLY ARG ALA PRO THR
SEQRES 27 B 562 PRO GLY PRO THR VAL VAL LEU VAL HIS GLY GLY PRO PHE
SEQRES 28 B 562 ALA GLU ASP SER ASP SER TRP ASP THR PHE ALA ALA SER
SEQRES 29 B 562 LEU ALA ALA ALA GLY PHE HIS VAL VAL MET PRO ASN TYR
SEQRES 30 B 562 ARG GLY SER THR GLY TYR GLY GLU GLU TRP ARG LEU LYS
SEQRES 31 B 562 ILE ILE GLY ASP PRO CYS GLY GLY GLU LEU GLU ASP VAL
SEQRES 32 B 562 SER ALA ALA ALA ARG TRP ALA ARG GLU SER GLY LEU ALA
SEQRES 33 B 562 SER GLU LEU TYR ILE MET GLY TYR SER TYR GLY GLY TYR
SEQRES 34 B 562 MET THR LEU CYS ALA LEU THR MET LYS PRO GLY LEU PHE
SEQRES 35 B 562 LYS ALA GLY VAL ALA GLY ALA SER VAL VAL ASP TRP GLU
SEQRES 36 B 562 GLU MET TYR GLU LEU SER ASP ALA ALA PHE ARG ASN PHE
SEQRES 37 B 562 ILE GLU GLN LEU THR GLY GLY SER ARG GLU ILE MET ARG
SEQRES 38 B 562 SER ARG SER PRO ILE ASN HIS VAL ASP ARG ILE LYS GLU
SEQRES 39 B 562 PRO LEU ALA LEU ILE HIS PRO GLN ASN ASP SER ARG THR
SEQRES 40 B 562 PRO LEU LYS PRO LEU LEU ARG LEU MET GLY GLU LEU LEU
SEQRES 41 B 562 ALA ARG GLY LYS THR PHE GLU ALA HIS ILE ILE PRO ASP
SEQRES 42 B 562 ALA GLY HIS ALA ILE ASN THR MET GLU ASP ALA VAL LYS
SEQRES 43 B 562 ILE LEU LEU PRO ALA VAL PHE PHE LEU ALA THR GLN ARG
SEQRES 44 B 562 GLU ARG ARG
FORMUL 3 HOH *366(H2 O)
HELIX 1 1 ASP A 239 ARG A 244 1 6
HELIX 2 2 ASP A 379 ALA A 388 1 10
HELIX 3 3 GLY A 404 LEU A 409 1 6
HELIX 4 4 GLY A 417 SER A 433 1 17
HELIX 5 5 SER A 445 MET A 457 1 13
HELIX 6 6 ASP A 473 LEU A 480 1 8
HELIX 7 7 ASP A 482 THR A 493 1 12
HELIX 8 8 SER A 496 ARG A 503 1 8
HELIX 9 9 SER A 504 VAL A 509 5 6
HELIX 10 10 LEU A 529 ARG A 542 1 14
HELIX 11 11 MET A 561 LEU A 568 5 8
HELIX 12 12 LEU A 569 GLU A 580 1 12
HELIX 13 13 GLU B 324 SER B 329 1 6
HELIX 14 14 ASP B 379 ALA B 388 1 10
HELIX 15 15 GLY B 404 LEU B 409 1 6
HELIX 16 16 GLY B 417 SER B 433 1 17
HELIX 17 17 SER B 445 LYS B 458 1 14
HELIX 18 18 TRP B 474 LEU B 480 1 7
HELIX 19 19 ASP B 482 THR B 493 1 12
HELIX 20 20 SER B 496 ARG B 503 1 8
HELIX 21 21 SER B 504 ILE B 512 5 9
HELIX 22 22 PRO B 528 ARG B 542 1 15
HELIX 23 23 LEU B 568 GLU B 580 1 13
SHEET 1 A 4 TYR A 25 VAL A 31 0
SHEET 2 A 4 LYS A 35 GLY A 40 -1 O LEU A 37 N GLY A 29
SHEET 3 A 4 ASN A 47 TYR A 51 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 VAL A 57 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 3 SER A 66 VAL A 67 0
SHEET 2 B 3 VAL A 77 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 3 HIS A 90 VAL A 95 -1 O VAL A 95 N VAL A 77
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 THR A 127 N SER A 116
SHEET 4 C 5 VAL A 134 ASP A 140 -1 O LEU A 139 N VAL A 124
SHEET 5 C 5 GLY A 143 LEU A 150 -1 O LEU A 147 N LEU A 136
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 ASP A 158
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 SER A 201 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 TRP A 250 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 ARG A 268 N ARG A 265
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O VAL A 278 N VAL A 271
SHEET 1 G 4 VAL A 289 TRP A 291 0
SHEET 2 G 4 LYS A 294 THR A 297 -1 O LYS A 294 N TRP A 291
SHEET 3 G 4 ILE A 308 SER A 310 -1 O VAL A 309 N THR A 297
SHEET 4 G 4 PRO A 316 LEU A 318 -1 O LEU A 318 N ILE A 308
SHEET 1 H12 ARG A 334 GLU A 339 0
SHEET 2 H12 ARG A 345 LEU A 351 -1 O VAL A 350 N ARG A 334
SHEET 3 H12 HIS A 391 PRO A 395 -1 O MET A 394 N TYR A 349
SHEET 4 H12 GLY A 360 VAL A 366 1 N VAL A 363 O HIS A 391
SHEET 5 H12 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 H12 ALA A 464 GLY A 468 1 O ALA A 464 N ILE A 441
SHEET 7 H12 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 H12 GLU A 547 ILE A 551 1 O HIS A 549 N HIS A 520
SHEET 9 H12 PHE B 546 ILE B 551 -1 O ALA B 548 N ILE A 550
SHEET 10 H12 LEU B 516 PRO B 521 1 N HIS B 520 O HIS B 549
SHEET 11 H12 ALA B 464 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 H12 TYR B 440 TYR B 444 1 N ILE B 441 O VAL B 466
SHEET 1 I 3 LYS B 24 TYR B 25 0
SHEET 2 I 3 LEU B 36 PHE B 41 -1 O PHE B 41 N LYS B 24
SHEET 3 I 3 ASN B 47 TYR B 51 -1 O ASN B 47 N GLY B 40
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 4 ASP B 69 PRO B 70 0
SHEET 2 K 4 VAL B 118 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 K 4 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 K 4 ARG B 113 ILE B 114 -1 N ARG B 113 O ALA B 129
SHEET 1 L 5 ASP B 69 PRO B 70 0
SHEET 2 L 5 VAL B 118 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 L 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 L 5 VAL B 134 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 L 5 GLY B 143 LEU B 150 -1 O GLY B 143 N ASP B 140
SHEET 1 M 4 PHE B 153 ARG B 160 0
SHEET 2 M 4 LEU B 163 GLY B 171 -1 O ALA B 165 N ASP B 158
SHEET 3 M 4 ARG B 174 PHE B 178 -1 O SER B 176 N GLY B 168
SHEET 4 M 4 VAL B 189 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 N 3 GLY B 195 PHE B 197 0
SHEET 2 N 3 LEU B 212 THR B 214 -1 O GLU B 213 N SER B 196
SHEET 3 N 3 ALA B 218 ARG B 219 -1 O ARG B 219 N LEU B 212
SHEET 1 O 2 SER B 201 ILE B 202 0
SHEET 2 O 2 VAL B 208 THR B 209 -1 O THR B 209 N SER B 201
SHEET 1 P 4 ILE B 248 TYR B 253 0
SHEET 2 P 4 LEU B 259 ARG B 265 -1 O VAL B 262 N TRP B 250
SHEET 3 P 4 ARG B 268 ILE B 273 -1 O PHE B 272 N VAL B 261
SHEET 4 P 4 GLU B 276 ARG B 277 -1 O GLU B 276 N ILE B 273
SHEET 1 Q 4 VAL B 289 LEU B 290 0
SHEET 2 Q 4 LEU B 295 SER B 301 -1 O VAL B 296 N VAL B 289
SHEET 3 Q 4 THR B 304 SER B 310 -1 O THR B 304 N SER B 301
SHEET 4 Q 4 GLU B 315 LEU B 318 -1 O GLU B 315 N SER B 310
SHEET 1 R 5 ARG B 334 VAL B 338 0
SHEET 2 R 5 VAL B 346 LEU B 351 -1 O VAL B 346 N VAL B 338
SHEET 3 R 5 HIS B 391 PRO B 395 -1 O VAL B 392 N LEU B 351
SHEET 4 R 5 GLY B 360 VAL B 364 1 N VAL B 363 O VAL B 393
SHEET 5 R 5 ALA B 436 GLU B 438 1 O GLU B 438 N THR B 362
SSBOND 1 CYS A 416 CYS A 453 1555 1555 2.03
SSBOND 2 CYS B 416 CYS B 453 1555 1555 2.04
CISPEP 1 LEU A 311 PRO A 312 0 -0.50
CISPEP 2 THR A 358 PRO A 359 0 -0.05
CISPEP 3 GLY A 369 PRO A 370 0 0.42
CISPEP 4 LEU B 311 PRO B 312 0 -0.18
CISPEP 5 THR B 358 PRO B 359 0 0.36
CISPEP 6 GLY B 369 PRO B 370 0 -0.23
CRYST1 63.117 102.183 163.594 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 0.015844 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009786 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006113 0.00000
TER 4256 ARG A 581
TER 8517 ARG B 581
MASTER 392 0 0 23 78 0 0 6 8881 2 4 88
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