HEADER HYDROLASE/ANTIBIOTIC 20-OCT-10 3PBN
TITLE CRYSTAL STRUCTURE OF APO PBP3 FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLIN-BINDING PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 50-579;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: FTSI, PA4418, PBPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PBP3, HYDROLASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN
REVDAT 3 21-FEB-24 3PBN 1 SEQADV
REVDAT 2 05-JAN-11 3PBN 1 JRNL
REVDAT 1 22-DEC-10 3PBN 0
JRNL AUTH S.HAN,R.P.ZANIEWSKI,E.S.MARR,B.M.LACEY,A.P.TOMARAS,
JRNL AUTH 2 A.EVDOKIMOV,J.R.MILLER,V.SHANMUGASUNDARAM
JRNL TITL STRUCTURAL BASIS FOR EFFECTIVENESS OF SIDEROPHORE-CONJUGATED
JRNL TITL 2 MONOCARBAMS AGAINST CLINICALLY RELEVANT STRAINS OF
JRNL TITL 3 PSEUDOMONAS AERUGINOSA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 22002 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 21135211
JRNL DOI 10.1073/PNAS.1013092107
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 29024
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1473
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.54
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2497
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2199
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2364
REMARK 3 BIN R VALUE (WORKING SET) : 0.2182
REMARK 3 BIN FREE R VALUE : 0.2489
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.33
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3333
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.06170
REMARK 3 B22 (A**2) : 7.21190
REMARK 3 B33 (A**2) : 8.84980
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) : 0.235
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.191
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.169
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.190
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.170
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3399 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 4613 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 1161 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 77 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 501 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 3399 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 443 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4012 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.27
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.99
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29054
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, 0.2M MGCL2, 0.1M TIS, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 30.08500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.66500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.08500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.66500
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 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 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 42
REMARK 465 GLY A 43
REMARK 465 HIS A 44
REMARK 465 HIS A 45
REMARK 465 HIS A 46
REMARK 465 HIS A 47
REMARK 465 HIS A 48
REMARK 465 HIS A 49
REMARK 465 ALA A 50
REMARK 465 ARG A 51
REMARK 465 SER A 52
REMARK 465 VAL A 53
REMARK 465 ARG A 54
REMARK 465 HIS A 55
REMARK 465 ILE A 56
REMARK 465 ALA A 57
REMARK 465 ILE A 58
REMARK 465 PRO A 59
REMARK 465 GLN A 116
REMARK 465 ASN A 117
REMARK 465 ALA A 118
REMARK 465 GLU A 119
REMARK 465 ARG A 120
REMARK 465 GLU A 121
REMARK 465 PHE A 122
REMARK 465 ILE A 123
REMARK 465 TYR A 124
REMARK 465 LEU A 125
REMARK 465 VAL A 126
REMARK 465 ARG A 127
REMARK 465 GLY A 128
REMARK 465 LEU A 129
REMARK 465 THR A 130
REMARK 465 PRO A 131
REMARK 465 GLU A 132
REMARK 465 GLN A 133
REMARK 465 GLY A 134
REMARK 465 GLU A 135
REMARK 465 GLY A 136
REMARK 465 VAL A 137
REMARK 465 ILE A 138
REMARK 465 ALA A 139
REMARK 465 LEU A 140
REMARK 465 GLY A 188
REMARK 465 VAL A 189
REMARK 465 PRO A 190
REMARK 465 GLY A 191
REMARK 465 LYS A 192
REMARK 465 ARG A 193
REMARK 465 GLN A 194
REMARK 465 VAL A 195
REMARK 465 LEU A 196
REMARK 465 LYS A 197
REMARK 465 ASP A 198
REMARK 465 ARG A 199
REMARK 465 ARG A 200
REMARK 465 GLY A 201
REMARK 465 ARG A 202
REMARK 465 VAL A 203
REMARK 465 ILE A 204
REMARK 465 LYS A 205
REMARK 465 ASP A 206
REMARK 465 VAL A 207
REMARK 465 GLN A 208
REMARK 465 VAL A 209
REMARK 465 THR A 210
REMARK 465 LYS A 211
REMARK 465 ASN A 212
REMARK 465 ALA A 213
REMARK 465 LYS A 214
REMARK 465 PRO A 215
REMARK 465 GLY A 216
REMARK 465 VAL A 491
REMARK 465 SER A 492
REMARK 465 VAL A 493
REMARK 465 GLY A 494
REMARK 465 THR A 495
REMARK 465 LYS A 496
REMARK 465 GLY A 497
REMARK 465 TYR A 498
REMARK 465 ARG A 499
REMARK 465 GLU A 500
REMARK 465 THR A 562
REMARK 465 ALA A 563
REMARK 465 THR A 564
REMARK 465 GLU A 565
REMARK 465 GLN A 566
REMARK 465 GLN A 567
REMARK 465 GLN A 568
REMARK 465 VAL A 569
REMARK 465 ASN A 570
REMARK 465 ALA A 571
REMARK 465 ALA A 572
REMARK 465 PRO A 573
REMARK 465 ALA A 574
REMARK 465 LYS A 575
REMARK 465 GLY A 576
REMARK 465 GLY A 577
REMARK 465 ARG A 578
REMARK 465 GLY A 579
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 ALA A 84 138.65 -171.52
REMARK 500 PRO A 86 48.50 -75.56
REMARK 500 LYS A 87 -34.26 -149.56
REMARK 500 PRO A 320 30.47 -93.85
REMARK 500 ARG A 338 -85.55 -121.45
REMARK 500 GLU A 386 124.35 -36.26
REMARK 500 ASN A 427 41.13 -86.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PBO RELATED DB: PDB
REMARK 900 CEFTAZIDIME
REMARK 900 RELATED ID: 3PBQ RELATED DB: PDB
REMARK 900 IMIPENEM
REMARK 900 RELATED ID: 3PBR RELATED DB: PDB
REMARK 900 MEROPENEM
REMARK 900 RELATED ID: 3PBS RELATED DB: PDB
REMARK 900 AZTREONAM
REMARK 900 RELATED ID: 3PBT RELATED DB: PDB
REMARK 900 MC-1
DBREF 3PBN A 50 579 UNP Q51504 Q51504_PSEAE 50 579
SEQADV 3PBN MET A 42 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN GLY A 43 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 44 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 45 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 46 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 47 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 48 UNP Q51504 EXPRESSION TAG
SEQADV 3PBN HIS A 49 UNP Q51504 EXPRESSION TAG
SEQRES 1 A 538 MET GLY HIS HIS HIS HIS HIS HIS ALA ARG SER VAL ARG
SEQRES 2 A 538 HIS ILE ALA ILE PRO ALA HIS ARG GLY LEU ILE THR ASP
SEQRES 3 A 538 ARG ASN GLY GLU PRO LEU ALA VAL SER THR PRO VAL THR
SEQRES 4 A 538 THR LEU TRP ALA ASN PRO LYS GLU LEU MET THR ALA LYS
SEQRES 5 A 538 GLU ARG TRP PRO GLN LEU ALA ALA ALA LEU GLY GLN ASP
SEQRES 6 A 538 THR LYS LEU PHE ALA ASP ARG ILE GLU GLN ASN ALA GLU
SEQRES 7 A 538 ARG GLU PHE ILE TYR LEU VAL ARG GLY LEU THR PRO GLU
SEQRES 8 A 538 GLN GLY GLU GLY VAL ILE ALA LEU LYS VAL PRO GLY VAL
SEQRES 9 A 538 TYR SER ILE GLU GLU PHE ARG ARG PHE TYR PRO ALA GLY
SEQRES 10 A 538 GLU VAL VAL ALA HIS ALA VAL GLY PHE THR ASP VAL ASP
SEQRES 11 A 538 ASP ARG GLY ARG GLU GLY ILE GLU LEU ALA PHE ASP GLU
SEQRES 12 A 538 TRP LEU ALA GLY VAL PRO GLY LYS ARG GLN VAL LEU LYS
SEQRES 13 A 538 ASP ARG ARG GLY ARG VAL ILE LYS ASP VAL GLN VAL THR
SEQRES 14 A 538 LYS ASN ALA LYS PRO GLY LYS THR LEU ALA LEU SER ILE
SEQRES 15 A 538 ASP LEU ARG LEU GLN TYR LEU ALA HIS ARG GLU LEU ARG
SEQRES 16 A 538 ASN ALA LEU LEU GLU ASN GLY ALA LYS ALA GLY SER LEU
SEQRES 17 A 538 VAL ILE MET ASP VAL LYS THR GLY GLU ILE LEU ALA MET
SEQRES 18 A 538 THR ASN GLN PRO THR TYR ASN PRO ASN ASN ARG ARG ASN
SEQRES 19 A 538 LEU GLN PRO ALA ALA MET ARG ASN ARG ALA MET ILE ASP
SEQRES 20 A 538 VAL PHE GLU PRO GLY SER THR VAL LYS PRO PHE SER MET
SEQRES 21 A 538 SER ALA ALA LEU ALA SER GLY ARG TRP LYS PRO SER ASP
SEQRES 22 A 538 ILE VAL ASP VAL TYR PRO GLY THR LEU GLN ILE GLY ARG
SEQRES 23 A 538 TYR THR ILE ARG ASP VAL SER ARG ASN SER ARG GLN LEU
SEQRES 24 A 538 ASP LEU THR GLY ILE LEU ILE LYS SER SER ASN VAL GLY
SEQRES 25 A 538 ILE SER LYS ILE ALA PHE ASP ILE GLY ALA GLU SER ILE
SEQRES 26 A 538 TYR SER VAL MET GLN GLN VAL GLY LEU GLY GLN ASP THR
SEQRES 27 A 538 GLY LEU GLY PHE PRO GLY GLU ARG VAL GLY ASN LEU PRO
SEQRES 28 A 538 ASN HIS ARG LYS TRP PRO LYS ALA GLU THR ALA THR LEU
SEQRES 29 A 538 ALA TYR GLY TYR GLY LEU SER VAL THR ALA ILE GLN LEU
SEQRES 30 A 538 ALA HIS ALA TYR ALA ALA LEU ALA ASN ASP GLY LYS SER
SEQRES 31 A 538 VAL PRO LEU SER MET THR ARG VAL ASP ARG VAL PRO ASP
SEQRES 32 A 538 GLY VAL GLN VAL ILE SER PRO GLU VAL ALA SER THR VAL
SEQRES 33 A 538 GLN GLY MET LEU GLN GLN VAL VAL GLU ALA GLN GLY GLY
SEQRES 34 A 538 VAL PHE ARG ALA GLN VAL PRO GLY TYR HIS ALA ALA GLY
SEQRES 35 A 538 LYS SER GLY THR ALA ARG LYS VAL SER VAL GLY THR LYS
SEQRES 36 A 538 GLY TYR ARG GLU ASN ALA TYR ARG SER LEU PHE ALA GLY
SEQRES 37 A 538 PHE ALA PRO ALA THR ASP PRO ARG ILE ALA MET VAL VAL
SEQRES 38 A 538 VAL ILE ASP GLU PRO SER LYS ALA GLY TYR PHE GLY GLY
SEQRES 39 A 538 LEU VAL SER ALA PRO VAL PHE SER LYS VAL MET ALA GLY
SEQRES 40 A 538 ALA LEU ARG LEU MET ASN VAL PRO PRO ASP ASN LEU PRO
SEQRES 41 A 538 THR ALA THR GLU GLN GLN GLN VAL ASN ALA ALA PRO ALA
SEQRES 42 A 538 LYS GLY GLY ARG GLY
FORMUL 2 HOH *117(H2 O)
HELIX 1 1 GLU A 88 GLU A 94 5 7
HELIX 2 2 ARG A 95 GLY A 104 1 10
HELIX 3 3 ASP A 106 GLU A 115 1 10
HELIX 4 4 ALA A 157 VAL A 160 5 4
HELIX 5 5 VAL A 161 GLY A 166 1 6
HELIX 6 6 GLU A 176 PHE A 182 1 7
HELIX 7 7 PHE A 182 ALA A 187 1 6
HELIX 8 8 ASP A 224 GLY A 243 1 20
HELIX 9 9 GLN A 277 ARG A 282 5 6
HELIX 10 10 ASN A 283 ASP A 288 1 6
HELIX 11 11 PRO A 292 THR A 295 5 4
HELIX 12 12 VAL A 296 SER A 307 1 12
HELIX 13 13 LEU A 342 LYS A 348 1 7
HELIX 14 14 SER A 350 GLY A 362 1 13
HELIX 15 15 GLY A 362 VAL A 373 1 12
HELIX 16 16 PRO A 398 TYR A 407 1 10
HELIX 17 17 THR A 414 ASN A 427 1 14
HELIX 18 18 SER A 450 ALA A 467 1 18
HELIX 19 19 VAL A 471 GLN A 475 5 5
HELIX 20 20 PHE A 533 VAL A 537 5 5
HELIX 21 21 SER A 538 MET A 553 1 16
SHEET 1 A 4 GLU A 149 PHE A 154 0
SHEET 2 A 4 PRO A 72 THR A 80 -1 N THR A 77 O ARG A 152
SHEET 3 A 4 ILE A 65 THR A 66 -1 N ILE A 65 O LEU A 73
SHEET 4 A 4 LEU A 219 ALA A 220 1 O LEU A 219 N THR A 66
SHEET 1 B 5 ILE A 259 GLN A 265 0
SHEET 2 B 5 ALA A 246 ASP A 253 -1 N LEU A 249 O THR A 263
SHEET 3 B 5 ILE A 518 ASP A 525 -1 O ALA A 519 N MET A 252
SHEET 4 B 5 TYR A 503 ALA A 511 -1 N SER A 505 O ILE A 524
SHEET 5 B 5 ALA A 482 ARG A 489 -1 N GLY A 486 O LEU A 506
SHEET 1 C 2 ILE A 315 ASP A 317 0
SHEET 2 C 2 GLN A 339 ASP A 341 -1 O LEU A 340 N VAL A 316
SHEET 1 D 2 THR A 322 ILE A 325 0
SHEET 2 D 2 TYR A 328 ARG A 331 -1 O TYR A 328 N ILE A 325
SHEET 1 E 2 LYS A 430 SER A 431 0
SHEET 2 E 2 VAL A 446 GLN A 447 -1 O VAL A 446 N SER A 431
CISPEP 1 GLN A 265 PRO A 266 0 -3.40
CISPEP 2 TYR A 319 PRO A 320 0 3.21
CISPEP 3 ALA A 511 PRO A 512 0 -13.96
CRYST1 60.170 79.330 90.030 90.00 90.00 90.00 P 21 21 21 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 0.016620 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
