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HEADER HYDROLASE 06-SEP-16 5T88
TITLE PROLYL OLIGOPEPTIDASE FROM PYROCOCCUS FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PROLYL OLIGOPEPTIDASE, HYPERTHERMOSTABLE, ALPHA/BETA HYDROLASE,
KEYWDS 2 PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ELLIS-GUARDIOLA,J.LEWIS,N.SUKUMAR
REVDAT 1 06-SEP-17 5T88 0
JRNL AUTH K.ELLIS-GUARDIOLA,N.SUKUMAR,J.LEWIS
JRNL TITL PROLYL OLIGOPEPTIDASE FROM PYROCOCCUS FURIOSUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 83441
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.1069 - 4.5824 1.00 5878 149 0.2195 0.2382
REMARK 3 2 4.5824 - 3.6376 1.00 5838 140 0.1646 0.2089
REMARK 3 3 3.6376 - 3.1779 1.00 5884 145 0.1764 0.2158
REMARK 3 4 3.1779 - 2.8874 1.00 5816 139 0.1943 0.2427
REMARK 3 5 2.8874 - 2.6805 1.00 5862 149 0.1949 0.3109
REMARK 3 6 2.6805 - 2.5224 1.00 5782 144 0.1953 0.2534
REMARK 3 7 2.5224 - 2.3961 1.00 5876 140 0.1879 0.2607
REMARK 3 8 2.3961 - 2.2918 1.00 5833 148 0.1832 0.2477
REMARK 3 9 2.2918 - 2.2036 1.00 5814 132 0.1850 0.2779
REMARK 3 10 2.2036 - 2.1275 1.00 5843 147 0.1859 0.2400
REMARK 3 11 2.1275 - 2.0610 1.00 5799 150 0.1936 0.2855
REMARK 3 12 2.0610 - 2.0021 1.00 5863 139 0.2099 0.2729
REMARK 3 13 2.0021 - 1.9494 1.00 5872 147 0.2300 0.3252
REMARK 3 14 1.9494 - 1.9018 0.94 5481 131 0.2565 0.3318
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 10377
REMARK 3 ANGLE : 1.435 14005
REMARK 3 CHIRALITY : 0.069 1466
REMARK 3 PLANARITY : 0.008 1780
REMARK 3 DIHEDRAL : 11.390 6184
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5T88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223835.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
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 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.17500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.3000
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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: 2BKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/W PEG 8000 100 MM TRIS PH 9.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 88.37850
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 MET A 593
REMARK 475 GLY A 594
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 GLU A 88 CG CD OE1 OE2
REMARK 480 ASP A 119 CG OD1 OD2
REMARK 480 ARG A 391 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 532 CG CD OE1 OE2
REMARK 480 GLU B 104 CG CD OE1 OE2
REMARK 480 ARG B 178 CD NE CZ NH1 NH2
REMARK 480 GLU B 241 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 OE1 GLN B 48 HE ARG B 361 1.46
REMARK 500 HG1 THR A 209 O HOH A 809 1.52
REMARK 500 HZ1 LYS B 108 O HOH B 825 1.53
REMARK 500 OE1 GLU B 305 HH TYR B 307 1.54
REMARK 500 HG SER A 477 OXT PRO A 709 1.56
REMARK 500 O GLU A 94 H GLY A 116 1.56
REMARK 500 HG1 THR B 209 O HOH B 824 1.58
REMARK 500 H GLU B 390 O HOH B 812 1.59
REMARK 500 O HOH A 970 O HOH A 1009 2.09
REMARK 500 O HOH B 858 O HOH B 1162 2.10
REMARK 500 O HOH A 909 O HOH A 919 2.13
REMARK 500 O HOH A 999 O HOH A 1121 2.14
REMARK 500 O HOH A 935 O HOH A 1005 2.14
REMARK 500 O HOH A 1043 O HOH A 1063 2.15
REMARK 500 O HOH B 936 O HOH B 1159 2.15
REMARK 500 O HOH A 908 O HOH A 1064 2.16
REMARK 500 O HOH A 1077 O HOH A 1099 2.17
REMARK 500 O HOH A 921 O HOH A 1126 2.17
REMARK 500 O HOH A 1044 O HOH A 1169 2.18
REMARK 500 O HOH A 1073 O HOH B 1098 2.19
REMARK 500 O HOH B 1024 O HOH B 1249 2.19
REMARK 500 O HOH A 835 O HOH A 1002 2.19
REMARK 500 O HOH A 981 O HOH A 1007 2.19
REMARK 500 O HOH A 1009 O HOH A 1081 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1091 O HOH B 847 11410 2.08
REMARK 500 O HOH A 1247 O HOH B 1265 21149 2.09
REMARK 500 O HOH A 911 O HOH A 988 1554 2.18
REMARK 500 O HOH A 1068 O HOH B 1009 1655 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 LYS A 68 -126.51 57.79
REMARK 500 LYS A 148 -122.02 57.87
REMARK 500 ARG A 289 -125.69 56.74
REMARK 500 ASP A 331 -158.83 -129.81
REMARK 500 LYS A 352 -77.44 -117.60
REMARK 500 TYR A 401 -79.63 -135.11
REMARK 500 ALA A 444 0.48 -68.58
REMARK 500 ARG A 447 -121.48 52.07
REMARK 500 SER A 477 -126.71 52.12
REMARK 500 TYR A 501 58.92 33.69
REMARK 500 ILE A 504 -49.42 -138.10
REMARK 500 TYR A 513 -124.73 54.77
REMARK 500 HIS A 592 -131.21 -112.93
REMARK 500 LYS B 68 -131.46 65.18
REMARK 500 ARG B 289 -123.99 58.24
REMARK 500 ASP B 331 -160.91 -129.97
REMARK 500 LYS B 352 -81.25 -117.81
REMARK 500 TYR B 401 -79.29 -139.19
REMARK 500 ARG B 447 -121.06 51.91
REMARK 500 SER B 477 -124.48 57.36
REMARK 500 TYR B 501 62.29 30.35
REMARK 500 ILE B 504 -48.44 -140.31
REMARK 500 TYR B 513 -125.09 54.35
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 A1251 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1252 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1253 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A1254 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A1255 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A1256 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A1257 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A1258 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A1259 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH A1260 DISTANCE = 10.42 ANGSTROMS
REMARK 525 HOH B1271 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1272 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1273 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B1274 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B1275 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B1276 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH B1277 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B1278 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B1279 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B1280 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B1281 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH B1282 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH B1283 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH B1284 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH B1285 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH B1286 DISTANCE = 7.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO A 708 and PRO A
REMARK 800 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO B 709 and PRO B
REMARK 800 710
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS HAVE CONFIRMED THE IDENTITY OF RESIDUE 464 BY HR-ESI-MS,
REMARK 999 AND CRYSTALLOGRAPHY
DBREF 5T88 A 1 616 UNP Q51714 Q51714_9EURY 1 616
DBREF 5T88 B 1 616 UNP Q51714 Q51714_9EURY 1 616
SEQADV 5T88 LEU A 464 UNP Q51714 ARG 464 VARIANT
SEQADV 5T88 LEU B 464 UNP Q51714 ARG 464 VARIANT
SEQRES 1 A 616 MET GLU ASP PRO TYR ILE TRP MET GLU ASN LEU GLU ASP
SEQRES 2 A 616 GLU ARG VAL LEU LYS ILE ILE GLU GLU GLU ASN LYS ARG
SEQRES 3 A 616 PHE ARG GLU PHE ILE GLY GLU LEU SER ASP LYS LEU PHE
SEQRES 4 A 616 PRO GLU VAL TRP GLU GLN PHE SER GLN PRO THR ILE GLY
SEQRES 5 A 616 MET ALA ARG ILE THR LYS LYS GLY ILE ILE ALA SER TYR
SEQRES 6 A 616 SER GLU LYS ASP ARG VAL VAL ILE LYS TRP PHE ASN GLY
SEQRES 7 A 616 ASP VAL ILE VAL ASP SER LYS GLU LEU GLU ARG GLU VAL
SEQRES 8 A 616 GLY ASP GLU VAL LEU LEU GLN GLY PHE THR THR ASP GLU
SEQRES 9 A 616 GLU GLY GLU LYS LEU ALA TYR SER PHE SER ILE GLY GLY
SEQRES 10 A 616 ALA ASP GLU GLY ILE THR ARG ILE ILE ASP LEU LYS THR
SEQRES 11 A 616 GLY GLU VAL ILE GLU GLU ILE LYS PRO SER ILE TRP ASN
SEQRES 12 A 616 ILE THR PHE LEU LYS ASP GLY TYR TYR PHE THR ARG PHE
SEQRES 13 A 616 TYR ARG LYS GLU LYS THR PRO ASP GLY VAL ASN PRO PRO
SEQRES 14 A 616 ALA ALA ARG MET PHE TRP LYS ASP ARG GLU GLY GLU ARG
SEQRES 15 A 616 MET VAL PHE GLY GLU GLY LEU THR SER GLY TYR PHE MET
SEQRES 16 A 616 SER ILE ARG LYS SER SER ASP GLY LYS PHE ALA ILE VAL
SEQRES 17 A 616 THR LEU THR TYR GLY TRP ASN GLN GLY GLU VAL TYR ILE
SEQRES 18 A 616 GLY PRO ILE ASP ASN PRO GLN GLU TRP LYS LYS VAL TYR
SEQRES 19 A 616 SER ALA SER VAL PRO VAL GLU ALA ILE ASP VAL VAL ASN
SEQRES 20 A 616 GLY LYS LEU TYR ILE LEU THR LYS GLU GLY LYS GLY LEU
SEQRES 21 A 616 GLY LYS ILE ILE ALA ILE LYS ASN GLY LYS ILE ASP GLU
SEQRES 22 A 616 VAL ILE PRO GLU GLY GLU PHE PRO LEU GLU TRP ALA VAL
SEQRES 23 A 616 ILE VAL ARG ASP LYS ILE LEU ALA GLY ARG LEU VAL HIS
SEQRES 24 A 616 ALA SER TYR LYS LEU GLU VAL TYR THR LEU ASN GLY GLU
SEQRES 25 A 616 LYS ILE LYS GLU ILE THR PHE ASP VAL PRO GLY SER LEU
SEQRES 26 A 616 TYR PRO LEU ASP LYS ASP GLU GLU ARG VAL LEU LEU ARG
SEQRES 27 A 616 TYR THR SER PHE THR ILE PRO TYR ARG LEU TYR GLU PHE
SEQRES 28 A 616 LYS ASP ASP LEU ARG LEU ILE GLU GLU ARG LYS VAL GLU
SEQRES 29 A 616 GLY GLU PHE ARG VAL GLU GLU ASP PHE ALA THR SER LYS
SEQRES 30 A 616 ASP GLY THR LYS VAL HIS TYR PHE ILE VAL LYS GLY GLU
SEQRES 31 A 616 ARG ASP GLU LYS ARG ALA TRP VAL PHE GLY TYR GLY GLY
SEQRES 32 A 616 PHE ASN ILE ALA LEU THR PRO MET PHE PHE PRO GLN VAL
SEQRES 33 A 616 ILE PRO PHE LEU LYS ARG GLY GLY THR PHE ILE MET ALA
SEQRES 34 A 616 ASN LEU ARG GLY GLY SER GLU TYR GLY GLU GLU TRP HIS
SEQRES 35 A 616 ARG ALA GLY MET ARG GLU ASN LYS GLN ASN VAL PHE ASP
SEQRES 36 A 616 ASP PHE ILE ALA VAL LEU GLU LYS LEU LYS LYS GLU GLY
SEQRES 37 A 616 TYR LYS VAL ALA ALA TRP GLY ARG SER ASN GLY GLY LEU
SEQRES 38 A 616 LEU VAL SER ALA THR LEU THR GLN ARG PRO ASP VAL MET
SEQRES 39 A 616 ASP SER ALA LEU ILE GLY TYR PRO VAL ILE ASP MET LEU
SEQRES 40 A 616 ARG PHE HIS LYS LEU TYR ILE GLY SER VAL TRP ILE PRO
SEQRES 41 A 616 GLU TYR GLY ASN PRO GLU ASP PRO LYS ASP ARG GLU PHE
SEQRES 42 A 616 LEU LEU LYS TYR SER PRO TYR HIS ASN VAL ASP PRO LYS
SEQRES 43 A 616 LYS LYS TYR PRO PRO THR LEU ILE TYR THR GLY LEU HIS
SEQRES 44 A 616 ASP ASP ARG VAL HIS PRO ALA HIS ALA LEU LYS PHE PHE
SEQRES 45 A 616 MET LYS LEU LYS GLU ILE GLY ALA PRO VAL TYR LEU ARG
SEQRES 46 A 616 VAL GLU THR LYS SER GLY HIS MET GLY ALA SER PRO GLU
SEQRES 47 A 616 THR ARG ALA ARG GLU LEU THR ASP LEU LEU ALA PHE VAL
SEQRES 48 A 616 LEU LYS THR LEU SER
SEQRES 1 B 616 MET GLU ASP PRO TYR ILE TRP MET GLU ASN LEU GLU ASP
SEQRES 2 B 616 GLU ARG VAL LEU LYS ILE ILE GLU GLU GLU ASN LYS ARG
SEQRES 3 B 616 PHE ARG GLU PHE ILE GLY GLU LEU SER ASP LYS LEU PHE
SEQRES 4 B 616 PRO GLU VAL TRP GLU GLN PHE SER GLN PRO THR ILE GLY
SEQRES 5 B 616 MET ALA ARG ILE THR LYS LYS GLY ILE ILE ALA SER TYR
SEQRES 6 B 616 SER GLU LYS ASP ARG VAL VAL ILE LYS TRP PHE ASN GLY
SEQRES 7 B 616 ASP VAL ILE VAL ASP SER LYS GLU LEU GLU ARG GLU VAL
SEQRES 8 B 616 GLY ASP GLU VAL LEU LEU GLN GLY PHE THR THR ASP GLU
SEQRES 9 B 616 GLU GLY GLU LYS LEU ALA TYR SER PHE SER ILE GLY GLY
SEQRES 10 B 616 ALA ASP GLU GLY ILE THR ARG ILE ILE ASP LEU LYS THR
SEQRES 11 B 616 GLY GLU VAL ILE GLU GLU ILE LYS PRO SER ILE TRP ASN
SEQRES 12 B 616 ILE THR PHE LEU LYS ASP GLY TYR TYR PHE THR ARG PHE
SEQRES 13 B 616 TYR ARG LYS GLU LYS THR PRO ASP GLY VAL ASN PRO PRO
SEQRES 14 B 616 ALA ALA ARG MET PHE TRP LYS ASP ARG GLU GLY GLU ARG
SEQRES 15 B 616 MET VAL PHE GLY GLU GLY LEU THR SER GLY TYR PHE MET
SEQRES 16 B 616 SER ILE ARG LYS SER SER ASP GLY LYS PHE ALA ILE VAL
SEQRES 17 B 616 THR LEU THR TYR GLY TRP ASN GLN GLY GLU VAL TYR ILE
SEQRES 18 B 616 GLY PRO ILE ASP ASN PRO GLN GLU TRP LYS LYS VAL TYR
SEQRES 19 B 616 SER ALA SER VAL PRO VAL GLU ALA ILE ASP VAL VAL ASN
SEQRES 20 B 616 GLY LYS LEU TYR ILE LEU THR LYS GLU GLY LYS GLY LEU
SEQRES 21 B 616 GLY LYS ILE ILE ALA ILE LYS ASN GLY LYS ILE ASP GLU
SEQRES 22 B 616 VAL ILE PRO GLU GLY GLU PHE PRO LEU GLU TRP ALA VAL
SEQRES 23 B 616 ILE VAL ARG ASP LYS ILE LEU ALA GLY ARG LEU VAL HIS
SEQRES 24 B 616 ALA SER TYR LYS LEU GLU VAL TYR THR LEU ASN GLY GLU
SEQRES 25 B 616 LYS ILE LYS GLU ILE THR PHE ASP VAL PRO GLY SER LEU
SEQRES 26 B 616 TYR PRO LEU ASP LYS ASP GLU GLU ARG VAL LEU LEU ARG
SEQRES 27 B 616 TYR THR SER PHE THR ILE PRO TYR ARG LEU TYR GLU PHE
SEQRES 28 B 616 LYS ASP ASP LEU ARG LEU ILE GLU GLU ARG LYS VAL GLU
SEQRES 29 B 616 GLY GLU PHE ARG VAL GLU GLU ASP PHE ALA THR SER LYS
SEQRES 30 B 616 ASP GLY THR LYS VAL HIS TYR PHE ILE VAL LYS GLY GLU
SEQRES 31 B 616 ARG ASP GLU LYS ARG ALA TRP VAL PHE GLY TYR GLY GLY
SEQRES 32 B 616 PHE ASN ILE ALA LEU THR PRO MET PHE PHE PRO GLN VAL
SEQRES 33 B 616 ILE PRO PHE LEU LYS ARG GLY GLY THR PHE ILE MET ALA
SEQRES 34 B 616 ASN LEU ARG GLY GLY SER GLU TYR GLY GLU GLU TRP HIS
SEQRES 35 B 616 ARG ALA GLY MET ARG GLU ASN LYS GLN ASN VAL PHE ASP
SEQRES 36 B 616 ASP PHE ILE ALA VAL LEU GLU LYS LEU LYS LYS GLU GLY
SEQRES 37 B 616 TYR LYS VAL ALA ALA TRP GLY ARG SER ASN GLY GLY LEU
SEQRES 38 B 616 LEU VAL SER ALA THR LEU THR GLN ARG PRO ASP VAL MET
SEQRES 39 B 616 ASP SER ALA LEU ILE GLY TYR PRO VAL ILE ASP MET LEU
SEQRES 40 B 616 ARG PHE HIS LYS LEU TYR ILE GLY SER VAL TRP ILE PRO
SEQRES 41 B 616 GLU TYR GLY ASN PRO GLU ASP PRO LYS ASP ARG GLU PHE
SEQRES 42 B 616 LEU LEU LYS TYR SER PRO TYR HIS ASN VAL ASP PRO LYS
SEQRES 43 B 616 LYS LYS TYR PRO PRO THR LEU ILE TYR THR GLY LEU HIS
SEQRES 44 B 616 ASP ASP ARG VAL HIS PRO ALA HIS ALA LEU LYS PHE PHE
SEQRES 45 B 616 MET LYS LEU LYS GLU ILE GLY ALA PRO VAL TYR LEU ARG
SEQRES 46 B 616 VAL GLU THR LYS SER GLY HIS MET GLY ALA SER PRO GLU
SEQRES 47 B 616 THR ARG ALA ARG GLU LEU THR ASP LEU LEU ALA PHE VAL
SEQRES 48 B 616 LEU LYS THR LEU SER
HET CL A 701 1
HET CL A 702 1
HET TRS A 703 20
HET TRS A 704 20
HET TRS A 705 20
HET TRS A 706 20
HET TRS A 707 20
HET PRO A 708 14
HET PRO A 709 15
HET CL B 701 1
HET CL B 702 1
HET TRS B 703 20
HET TRS B 704 20
HET TRS B 705 20
HET TRS B 706 20
HET TRS B 707 20
HET TRS B 708 20
HET PRO B 709 14
HET PRO B 710 15
HETNAM CL CHLORIDE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM PRO PROLINE
HETSYN TRS TRIS BUFFER
FORMUL 3 CL 4(CL 1-)
FORMUL 5 TRS 11(C4 H12 N O3 1+)
FORMUL 10 PRO 4(C5 H9 N O2)
FORMUL 22 HOH *946(H2 O)
HELIX 1 AA1 TYR A 5 ASN A 10 5 6
HELIX 2 AA2 ASP A 13 SER A 47 1 35
HELIX 3 AA3 SER A 84 GLY A 92 1 9
HELIX 4 AA4 ASN A 226 TRP A 230 5 5
HELIX 5 AA5 PHE A 413 GLN A 415 5 3
HELIX 6 AA6 VAL A 416 ARG A 422 1 7
HELIX 7 AA7 GLY A 438 ALA A 444 1 7
HELIX 8 AA8 GLY A 445 GLU A 448 5 4
HELIX 9 AA9 ASN A 449 GLU A 467 1 19
HELIX 10 AB1 SER A 477 ARG A 490 1 14
HELIX 11 AB2 PRO A 491 MET A 494 5 4
HELIX 12 AB3 ARG A 508 LEU A 512 5 5
HELIX 13 AB4 ILE A 514 VAL A 517 5 4
HELIX 14 AB5 TRP A 518 GLY A 523 1 6
HELIX 15 AB6 ASP A 527 SER A 538 1 12
HELIX 16 AB7 PRO A 539 ASN A 542 5 4
HELIX 17 AB8 PRO A 565 ILE A 578 1 14
HELIX 18 AB9 SER A 596 LEU A 615 1 20
HELIX 19 AC1 TYR B 5 ASN B 10 5 6
HELIX 20 AC2 ASP B 13 SER B 47 1 35
HELIX 21 AC3 SER B 84 GLY B 92 1 9
HELIX 22 AC4 ASN B 226 TRP B 230 5 5
HELIX 23 AC5 LYS B 255 GLY B 259 5 5
HELIX 24 AC6 GLN B 415 ARG B 422 1 8
HELIX 25 AC7 GLY B 438 ALA B 444 1 7
HELIX 26 AC8 GLY B 445 GLU B 448 5 4
HELIX 27 AC9 ASN B 449 GLU B 467 1 19
HELIX 28 AD1 SER B 477 ARG B 490 1 14
HELIX 29 AD2 PRO B 491 MET B 494 5 4
HELIX 30 AD3 ARG B 508 LEU B 512 5 5
HELIX 31 AD4 ILE B 514 VAL B 517 5 4
HELIX 32 AD5 TRP B 518 GLY B 523 1 6
HELIX 33 AD6 ASP B 527 SER B 538 1 12
HELIX 34 AD7 PRO B 539 ASN B 542 5 4
HELIX 35 AD8 PRO B 565 GLU B 577 1 13
HELIX 36 AD9 HIS B 592 ALA B 595 5 4
HELIX 37 AE1 SER B 596 LEU B 615 1 20
SHEET 1 AA1 4 THR A 50 THR A 57 0
SHEET 2 AA1 4 GLY A 60 GLU A 67 -1 O ILE A 62 N ARG A 55
SHEET 3 AA1 4 ARG A 70 TRP A 75 -1 O LYS A 74 N ALA A 63
SHEET 4 AA1 4 VAL A 80 ASP A 83 -1 O ILE A 81 N ILE A 73
SHEET 1 AA2 4 VAL A 95 THR A 102 0
SHEET 2 AA2 4 LYS A 108 ILE A 115 -1 O ALA A 110 N THR A 101
SHEET 3 AA2 4 ILE A 122 ASP A 127 -1 O ILE A 122 N PHE A 113
SHEET 4 AA2 4 VAL A 133 ILE A 137 -1 O ILE A 137 N THR A 123
SHEET 1 AA3 4 TRP A 142 LEU A 147 0
SHEET 2 AA3 4 GLY A 150 TYR A 157 -1 O GLY A 150 N LEU A 147
SHEET 3 AA3 4 ALA A 170 ASP A 177 -1 O ALA A 170 N TYR A 157
SHEET 4 AA3 4 GLY A 180 PHE A 185 -1 O VAL A 184 N MET A 173
SHEET 1 AA4 4 TYR A 193 LYS A 199 0
SHEET 2 AA4 4 PHE A 205 TYR A 212 -1 O ILE A 207 N ARG A 198
SHEET 3 AA4 4 GLN A 216 PRO A 223 -1 O TYR A 220 N VAL A 208
SHEET 4 AA4 4 LYS A 231 ALA A 236 -1 O ALA A 236 N GLY A 217
SHEET 1 AA5 4 GLU A 241 VAL A 246 0
SHEET 2 AA5 4 LYS A 249 THR A 254 -1 O TYR A 251 N ILE A 243
SHEET 3 AA5 4 LYS A 262 LYS A 267 -1 O ILE A 264 N ILE A 252
SHEET 4 AA5 4 LYS A 270 ILE A 275 -1 O VAL A 274 N ILE A 263
SHEET 1 AA6 4 LEU A 282 VAL A 288 0
SHEET 2 AA6 4 LYS A 291 VAL A 298 -1 O LEU A 293 N VAL A 286
SHEET 3 AA6 4 SER A 301 THR A 308 -1 O GLU A 305 N ALA A 294
SHEET 4 AA6 4 LYS A 313 ILE A 317 -1 O ILE A 317 N LEU A 304
SHEET 1 AA7 4 SER A 324 LYS A 330 0
SHEET 2 AA7 4 VAL A 335 SER A 341 -1 O LEU A 336 N LEU A 328
SHEET 3 AA7 4 ILE A 344 PHE A 351 -1 O PHE A 351 N VAL A 335
SHEET 4 AA7 4 LEU A 355 ARG A 361 -1 O ARG A 356 N GLU A 350
SHEET 1 AA8 8 ARG A 368 THR A 375 0
SHEET 2 AA8 8 LYS A 381 LYS A 388 -1 O VAL A 382 N ALA A 374
SHEET 3 AA8 8 GLY A 424 ALA A 429 -1 O MET A 428 N PHE A 385
SHEET 4 AA8 8 ARG A 395 PHE A 399 1 N PHE A 399 O ILE A 427
SHEET 5 AA8 8 LYS A 470 ARG A 476 1 O LYS A 470 N ALA A 396
SHEET 6 AA8 8 SER A 496 GLY A 500 1 O LEU A 498 N ALA A 473
SHEET 7 AA8 8 THR A 552 GLY A 557 1 O LEU A 553 N ILE A 499
SHEET 8 AA8 8 VAL A 582 GLU A 587 1 O TYR A 583 N THR A 552
SHEET 1 AA9 4 THR B 50 THR B 57 0
SHEET 2 AA9 4 GLY B 60 GLU B 67 -1 O ILE B 62 N ARG B 55
SHEET 3 AA9 4 ARG B 70 TRP B 75 -1 O VAL B 72 N TYR B 65
SHEET 4 AA9 4 VAL B 80 ASP B 83 -1 O ILE B 81 N ILE B 73
SHEET 1 AB1 4 VAL B 95 THR B 102 0
SHEET 2 AB1 4 LYS B 108 ILE B 115 -1 O SER B 112 N GLN B 98
SHEET 3 AB1 4 ILE B 122 ASP B 127 -1 O ILE B 126 N LEU B 109
SHEET 4 AB1 4 VAL B 133 ILE B 137 -1 O ILE B 137 N THR B 123
SHEET 1 AB2 4 TRP B 142 PHE B 146 0
SHEET 2 AB2 4 GLY B 150 TYR B 157 -1 O THR B 154 N TRP B 142
SHEET 3 AB2 4 ALA B 170 ASP B 177 -1 O PHE B 174 N PHE B 153
SHEET 4 AB2 4 GLY B 180 PHE B 185 -1 O VAL B 184 N MET B 173
SHEET 1 AB3 4 TYR B 193 LYS B 199 0
SHEET 2 AB3 4 PHE B 205 TYR B 212 -1 O ILE B 207 N ARG B 198
SHEET 3 AB3 4 GLN B 216 PRO B 223 -1 O TYR B 220 N VAL B 208
SHEET 4 AB3 4 LYS B 231 ALA B 236 -1 O LYS B 231 N ILE B 221
SHEET 1 AB4 4 GLU B 241 VAL B 246 0
SHEET 2 AB4 4 LYS B 249 THR B 254 -1 O TYR B 251 N ILE B 243
SHEET 3 AB4 4 LYS B 262 LYS B 267 -1 O LYS B 262 N THR B 254
SHEET 4 AB4 4 LYS B 270 ILE B 275 -1 O VAL B 274 N ILE B 263
SHEET 1 AB5 4 LEU B 282 VAL B 288 0
SHEET 2 AB5 4 LYS B 291 VAL B 298 -1 O LEU B 293 N VAL B 286
SHEET 3 AB5 4 SER B 301 THR B 308 -1 O TYR B 307 N ILE B 292
SHEET 4 AB5 4 LYS B 313 ILE B 317 -1 O ILE B 317 N LEU B 304
SHEET 1 AB6 4 SER B 324 LYS B 330 0
SHEET 2 AB6 4 VAL B 335 SER B 341 -1 O ARG B 338 N TYR B 326
SHEET 3 AB6 4 ILE B 344 PHE B 351 -1 O TYR B 349 N LEU B 337
SHEET 4 AB6 4 LEU B 355 ARG B 361 -1 O ARG B 356 N GLU B 350
SHEET 1 AB7 8 ARG B 368 THR B 375 0
SHEET 2 AB7 8 LYS B 381 LYS B 388 -1 O VAL B 382 N ALA B 374
SHEET 3 AB7 8 GLY B 424 ALA B 429 -1 O MET B 428 N PHE B 385
SHEET 4 AB7 8 ARG B 395 PHE B 399 1 N PHE B 399 O ILE B 427
SHEET 5 AB7 8 LYS B 470 ARG B 476 1 O ALA B 472 N VAL B 398
SHEET 6 AB7 8 SER B 496 GLY B 500 1 O GLY B 500 N GLY B 475
SHEET 7 AB7 8 THR B 552 GLY B 557 1 O LEU B 553 N ILE B 499
SHEET 8 AB7 8 VAL B 582 GLU B 587 1 O GLU B 587 N THR B 556
LINK C PRO A 708 N PRO A 709 1555 1555 1.48
LINK C PRO B 709 N PRO B 710 1555 1555 1.48
CISPEP 1 LYS A 138 PRO A 139 0 1.14
CISPEP 2 PRO A 168 PRO A 169 0 -0.23
CISPEP 3 LYS B 138 PRO B 139 0 2.77
CISPEP 4 PRO B 168 PRO B 169 0 0.14
SITE 1 AC1 3 ARG A 476 TYR A 555 ARG A 600
SITE 1 AC2 5 ARG A 476 TYR A 501 HIS A 592 ARG A 600
SITE 2 AC2 5 GLU A 603
SITE 1 AC3 12 THR A 488 GLN A 489 LYS A 536 ASN A 542
SITE 2 AC3 12 HOH A 867 HOH A 974 LYS B 161 ASN B 167
SITE 3 AC3 12 LYS B 377 ASP B 378 GLY B 379 HOH B 835
SITE 1 AC4 2 TYR B 437 TRP B 441
SITE 1 AC5 8 MET A 1 LEU A 507 ARG A 508 LYS A 511
SITE 2 AC5 8 GLU A 526 HOH A 803 HOH A 924 HOH A 951
SITE 1 AC6 8 GLY A 99 PHE A 100 THR A 101 SER A 112
SITE 2 AC6 8 ILE A 141 TRP A 142 ASN A 143 ILE A 144
SITE 1 AC7 7 GLY A 52 SER A 64 SER A 66 VAL A 71
SITE 2 AC7 7 LEU A 97 HOH A 810 HOH A 824
SITE 1 AC8 3 ARG B 476 TYR B 555 ARG B 600
SITE 1 AC9 5 ARG B 476 TYR B 501 ARG B 600 GLU B 603
SITE 2 AC9 5 HOH B1068
SITE 1 AD1 5 THR A 380 LYS A 381 TRP A 441 LYS B 529
SITE 2 AD1 5 GLU B 532
SITE 1 AD2 7 MET B 1 LEU B 507 ARG B 508 HIS B 510
SITE 2 AD2 7 LYS B 511 PRO B 525 GLU B 526
SITE 1 AD3 11 GLY B 99 ALA B 110 TYR B 111 SER B 112
SITE 2 AD3 11 THR B 123 ILE B 141 TRP B 142 ASN B 143
SITE 3 AD3 11 ILE B 144 HOH B 874 HOH B1016
SITE 1 AD4 7 GLY B 116 GLY B 117 ALA B 118 ASP B 119
SITE 2 AD4 7 LYS B 270 LYS B 394 GLU B 467
SITE 1 AD5 6 ASP B 36 PHE B 39 GLU B 312 LYS B 313
SITE 2 AD5 6 ARG B 602 HOH B1105
SITE 1 AD6 6 GLU B 160 THR B 375 ALA B 459 LYS B 463
SITE 2 AD6 6 LYS B 466 HOH B1022
SITE 1 AD7 6 TYR A 401 ILE A 406 SER A 477 ASN A 478
SITE 2 AD7 6 TRP A 518 ARG A 562
SITE 1 AD8 7 TYR B 401 PHE B 404 SER B 477 ASN B 478
SITE 2 AD8 7 TRP B 518 ARG B 562 HOH B 809
CRYST1 55.535 176.757 57.901 90.00 106.03 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 0.018007 0.000000 0.005172 0.00000
SCALE2 0.000000 0.005657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017969 0.00000
TER 10004 SER A 616
TER 20010 SER B 616
MASTER 434 0 19 37 72 0 33 611086 2 224 96
END |