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HEADER HYDROLASE 10-FEB-17 5N4D
TITLE PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 25MER
TITLE 2 MACROCYCLIZATION SUBSTRATE - D661A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 3 ORGANISM_TAXID: 109633;
SOURCE 4 GENE: POPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 11 ORGANISM_TAXID: 109633
KEYWDS AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH
REVDAT 1 01-NOV-17 5N4D 0
JRNL AUTH C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES
JRNL TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-00862-4
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11RC3_2553: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 203908
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 10067
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 46.8943 - 5.0317 0.99 6795 389 0.1990 0.2076
REMARK 3 2 5.0317 - 3.9945 1.00 6612 343 0.1521 0.1782
REMARK 3 3 3.9945 - 3.4898 1.00 6590 332 0.1649 0.1949
REMARK 3 4 3.4898 - 3.1708 1.00 6539 338 0.1796 0.2205
REMARK 3 5 3.1708 - 2.9435 1.00 6499 342 0.1909 0.2314
REMARK 3 6 2.9435 - 2.7700 1.00 6481 355 0.1932 0.2260
REMARK 3 7 2.7700 - 2.6313 1.00 6542 304 0.1945 0.2179
REMARK 3 8 2.6313 - 2.5168 1.00 6478 324 0.1968 0.2414
REMARK 3 9 2.5168 - 2.4199 1.00 6474 329 0.1863 0.2355
REMARK 3 10 2.4199 - 2.3364 1.00 6435 353 0.1828 0.2357
REMARK 3 11 2.3364 - 2.2633 1.00 6479 324 0.1870 0.2476
REMARK 3 12 2.2633 - 2.1986 1.00 6436 340 0.1872 0.2274
REMARK 3 13 2.1986 - 2.1408 1.00 6401 377 0.1871 0.2348
REMARK 3 14 2.1408 - 2.0885 1.00 6438 346 0.1912 0.2387
REMARK 3 15 2.0885 - 2.0410 1.00 6443 338 0.1903 0.2287
REMARK 3 16 2.0410 - 1.9976 1.00 6430 315 0.1933 0.2312
REMARK 3 17 1.9976 - 1.9577 1.00 6441 311 0.2011 0.2453
REMARK 3 18 1.9577 - 1.9207 1.00 6437 321 0.2125 0.2543
REMARK 3 19 1.9207 - 1.8864 1.00 6419 342 0.2296 0.2598
REMARK 3 20 1.8864 - 1.8544 1.00 6443 315 0.2425 0.2844
REMARK 3 21 1.8544 - 1.8245 1.00 6435 317 0.2344 0.2846
REMARK 3 22 1.8245 - 1.7964 1.00 6427 329 0.2459 0.2975
REMARK 3 23 1.7964 - 1.7700 1.00 6383 346 0.2530 0.2880
REMARK 3 24 1.7700 - 1.7451 1.00 6396 336 0.2574 0.2822
REMARK 3 25 1.7451 - 1.7215 1.00 6418 325 0.2700 0.3044
REMARK 3 26 1.7215 - 1.6991 1.00 6435 306 0.2827 0.3096
REMARK 3 27 1.6991 - 1.6779 1.00 6412 332 0.3049 0.3350
REMARK 3 28 1.6779 - 1.6577 1.00 6385 344 0.3057 0.3354
REMARK 3 29 1.6577 - 1.6384 1.00 6375 359 0.3197 0.3719
REMARK 3 30 1.6384 - 1.6200 1.00 6363 335 0.3390 0.3388
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160
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 : 0.016 12202
REMARK 3 ANGLE : 1.400 16608
REMARK 3 CHIRALITY : 0.090 1753
REMARK 3 PLANARITY : 0.010 2162
REMARK 3 DIHEDRAL : 5.619 9813
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 5N4D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 204059
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 49.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9300
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 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000, 100 MM TRIS PH 8.3, 90 MM
REMARK 280 SODIUM/POTASSIUM PHOSPHATE, 12.5MM HEXAMMINE COBALT CHLORIDE.
REMARK 280 CRYSTALS WERE CRYOPROTECTED WITH 12% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.15K
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 49.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.44000
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, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 THR A 228
REMARK 465 ARG A 229
REMARK 465 THR A 728
REMARK 465 VAL A 729
REMARK 465 GLU A 730
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 THR B 728
REMARK 465 VAL B 729
REMARK 465 GLU B 730
REMARK 465 ILE C 1
REMARK 465 TRP C 2
REMARK 465 GLY C 3
REMARK 465 ILE C 4
REMARK 465 GLY C 5
REMARK 465 CYS C 6
REMARK 465 ASN C 7
REMARK 465 ILE D 1
REMARK 465 TRP D 2
REMARK 465 GLY D 3
REMARK 465 ILE D 4
REMARK 465 GLY D 5
REMARK 465 CYS D 6
REMARK 465 ASN D 7
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 LYS A 727 CG CD CE NZ
REMARK 470 LYS B 727 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 972 O HOH B 1461 2.02
REMARK 500 O CYS D 25 O1 GOL D 101 2.09
REMARK 500 O HOH A 1360 O HOH A 1494 2.12
REMARK 500 O HOH A 983 O HOH A 1547 2.13
REMARK 500 NH1 ARG B 222 O THR B 228 2.15
REMARK 500 O HOH A 1443 O HOH A 1592 2.17
REMARK 500 O HOH A 1418 O HOH A 1567 2.17
REMARK 500 OD2 ASP A 295 O HOH A 901 2.18
REMARK 500 NZ LYS B 564 O HOH B 901 2.18
REMARK 500 O HOH A 1454 O HOH A 1568 2.19
REMARK 500 NH1 ARG A 663 OE2 GLU C 12 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 B 1454 O HOH B 1487 3557 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 155 CB - CG - CD ANGL. DEV. = -17.0 DEGREES
REMARK 500 LYS A 155 CD - CE - NZ ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG B 101 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 124 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 542 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 542 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 10 50.22 -98.93
REMARK 500 ASP A 280 -167.93 -161.89
REMARK 500 ALA A 311 -29.47 -145.42
REMARK 500 ALA A 332 78.03 -161.18
REMARK 500 TYR A 335 165.96 68.40
REMARK 500 GLU A 369 -41.29 70.19
REMARK 500 GLU A 452 -56.61 72.85
REMARK 500 TYR A 496 -68.40 -125.97
REMARK 500 ARG A 543 -118.63 52.62
REMARK 500 SER A 577 -114.10 58.54
REMARK 500 ALA A 605 -25.34 -141.91
REMARK 500 THR A 614 -105.45 16.24
REMARK 500 ASN B 10 54.75 -93.27
REMARK 500 ARG B 229 70.13 -65.81
REMARK 500 ASP B 280 -167.98 -163.46
REMARK 500 ALA B 311 -30.20 -143.90
REMARK 500 ALA B 332 77.86 -159.85
REMARK 500 TYR B 335 163.87 68.77
REMARK 500 GLU B 369 -39.39 72.28
REMARK 500 GLU B 452 -56.44 72.90
REMARK 500 TYR B 496 -70.44 -123.57
REMARK 500 ARG B 543 -118.73 50.09
REMARK 500 SER B 577 -115.92 58.89
REMARK 500 ALA B 605 -24.28 -144.02
REMARK 500 THR B 614 -93.11 1.18
REMARK 500 ASP D 23 58.04 -141.62
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 B1621 DISTANCE = 5.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 101
DBREF 5N4D A 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4D B 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4D C 1 25 UNP H2E7Q5 H2E7Q5_9AGAR 11 35
DBREF 5N4D D 1 25 UNP H2E7Q5 H2E7Q5_9AGAR 11 35
SEQADV 5N4D ALA A 661 UNP H2E7Q8 ASP 661 ENGINEERED MUTATION
SEQADV 5N4D ALA B 661 UNP H2E7Q8 ASP 661 ENGINEERED MUTATION
SEQRES 1 A 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 A 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 A 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 A 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 A 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 A 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 A 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 A 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 A 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 A 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 A 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 A 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 A 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 A 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 A 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 A 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 A 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 A 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 A 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 A 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 A 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 A 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 A 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 A 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 A 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 A 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 A 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 A 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 A 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 A 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 A 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 A 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 A 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 A 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 A 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 A 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 A 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 A 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 A 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 A 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 A 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 A 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 A 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 A 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 A 730 ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 A 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 A 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 A 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 A 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 A 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 A 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ALA GLY ARG
SEQRES 52 A 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 A 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 A 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 A 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 A 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 A 730 VAL GLU
SEQRES 1 B 730 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 B 730 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 B 730 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 B 730 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 B 730 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 B 730 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 B 730 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 B 730 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 B 730 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 B 730 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 B 730 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 B 730 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 B 730 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 B 730 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 B 730 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 B 730 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 B 730 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 B 730 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 B 730 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 B 730 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 B 730 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 B 730 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 B 730 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 B 730 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 B 730 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 B 730 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 B 730 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 B 730 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 B 730 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 B 730 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 B 730 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 B 730 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 B 730 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 B 730 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 B 730 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 B 730 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 B 730 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 B 730 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 B 730 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 B 730 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 B 730 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 B 730 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 B 730 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 B 730 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 B 730 ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 B 730 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 B 730 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 B 730 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 B 730 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 B 730 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 B 730 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ALA GLY ARG
SEQRES 52 B 730 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 B 730 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 B 730 LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY LYS
SEQRES 55 B 730 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 B 730 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 B 730 VAL GLU
SEQRES 1 C 25 ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS
SEQRES 2 C 25 VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 D 25 ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS
SEQRES 2 D 25 VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
HET GOL A 801 6
HET GOL A 802 6
HET GOL B 801 6
HET GOL D 101 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *1492(H2 O)
HELIX 1 AA1 TYR A 37 GLU A 42 5 6
HELIX 2 AA2 THR A 44 GLN A 64 1 21
HELIX 3 AA3 ALA A 66 ASN A 80 1 15
HELIX 4 AA4 ASP A 119 LYS A 122 5 4
HELIX 5 AA5 GLY A 123 VAL A 127 1 5
HELIX 6 AA6 ASP A 133 LEU A 137 5 5
HELIX 7 AA7 SER A 181 GLY A 188 1 8
HELIX 8 AA8 THR A 244 ASP A 248 5 5
HELIX 9 AA9 ASP A 454 ASP A 456 5 3
HELIX 10 AB1 SER A 508 GLY A 519 1 12
HELIX 11 AB2 GLY A 534 GLY A 540 1 7
HELIX 12 AB3 GLY A 541 THR A 545 5 5
HELIX 13 AB4 LYS A 546 ASN A 563 1 18
HELIX 14 AB5 SER A 577 ALA A 590 1 14
HELIX 15 AB6 LYS A 609 PHE A 613 5 5
HELIX 16 AB7 GLY A 616 ALA A 618 5 3
HELIX 17 AB8 TRP A 619 GLY A 624 1 6
HELIX 18 AB9 ILE A 628 TYR A 636 1 9
HELIX 19 AC1 PRO A 637 ASN A 643 5 7
HELIX 20 AC2 PRO A 666 VAL A 680 1 15
HELIX 21 AC3 PRO A 703 LEU A 722 1 20
HELIX 22 AC4 TYR B 37 GLU B 42 5 6
HELIX 23 AC5 THR B 44 GLN B 64 1 21
HELIX 24 AC6 ALA B 66 ASN B 80 1 15
HELIX 25 AC7 ASP B 119 LYS B 122 5 4
HELIX 26 AC8 GLY B 123 VAL B 127 1 5
HELIX 27 AC9 ASP B 133 LEU B 137 5 5
HELIX 28 AD1 SER B 181 GLY B 188 1 8
HELIX 29 AD2 THR B 244 ASP B 248 5 5
HELIX 30 AD3 ASP B 454 ASP B 456 5 3
HELIX 31 AD4 SER B 508 GLY B 519 1 12
HELIX 32 AD5 GLY B 534 GLY B 540 1 7
HELIX 33 AD6 GLY B 541 THR B 545 5 5
HELIX 34 AD7 LYS B 546 ASN B 563 1 18
HELIX 35 AD8 SER B 577 ALA B 590 1 14
HELIX 36 AD9 LYS B 609 ALA B 618 5 10
HELIX 37 AE1 TRP B 619 GLY B 624 1 6
HELIX 38 AE2 ILE B 628 TYR B 636 1 9
HELIX 39 AE3 PRO B 637 ASN B 643 5 7
HELIX 40 AE4 PRO B 666 VAL B 680 1 15
HELIX 41 AE5 PRO B 703 LEU B 722 1 20
SHEET 1 AA1 2 VAL A 20 SER A 25 0
SHEET 2 AA1 2 GLY A 29 PRO A 34 -1 O VAL A 31 N TYR A 23
SHEET 1 AA2 3 LYS A 83 PHE A 84 0
SHEET 2 AA2 3 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA2 3 THR A 88 LEU A 89 -1 N THR A 88 O TYR A 96
SHEET 1 AA3 4 LYS A 83 PHE A 84 0
SHEET 2 AA3 4 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA3 4 VAL A 108 SER A 112 -1 O TYR A 110 N TRP A 97
SHEET 4 AA3 4 GLY A 128 PHE A 132 -1 O PHE A 132 N LEU A 109
SHEET 1 AA4 4 ALA A 143 PHE A 150 0
SHEET 2 AA4 4 PHE A 156 HIS A 163 -1 O ALA A 160 N LEU A 147
SHEET 3 AA4 4 SER A 169 SER A 175 -1 O THR A 170 N VAL A 161
SHEET 4 AA4 4 VAL A 197 PHE A 200 -1 O VAL A 197 N ILE A 171
SHEET 1 AA5 4 ILE A 206 TRP A 207 0
SHEET 2 AA5 4 GLY A 213 ARG A 218 -1 O LEU A 215 N ILE A 206
SHEET 3 AA5 4 MET A 235 LYS A 240 -1 O HIS A 239 N PHE A 214
SHEET 4 AA5 4 ILE A 249 TYR A 252 -1 O TYR A 252 N MET A 236
SHEET 1 AA6 4 ILE A 261 THR A 266 0
SHEET 2 AA6 4 TYR A 272 PHE A 278 -1 O TYR A 274 N ASP A 265
SHEET 3 AA6 4 LEU A 286 GLU A 291 -1 O ALA A 290 N LEU A 273
SHEET 4 AA6 4 ARG A 304 VAL A 307 -1 O ARG A 304 N VAL A 289
SHEET 1 AA7 4 TYR A 314 HIS A 320 0
SHEET 2 AA7 4 LEU A 323 THR A 328 -1 O TYR A 325 N THR A 318
SHEET 3 AA7 4 LYS A 336 ASP A 341 -1 O ILE A 338 N ILE A 326
SHEET 4 AA7 4 GLU A 348 ILE A 353 -1 O PHE A 352 N VAL A 337
SHEET 1 AA8 4 LYS A 360 ALA A 367 0
SHEET 2 AA8 4 TYR A 371 ARG A 378 -1 O VAL A 373 N ASN A 365
SHEET 3 AA8 4 LYS A 381 TYR A 387 -1 O TYR A 385 N ALA A 374
SHEET 4 AA8 4 GLN A 393 LEU A 397 -1 O LEU A 394 N LEU A 386
SHEET 1 AA9 4 ALA A 404 ALA A 408 0
SHEET 2 AA9 4 HIS A 415 GLY A 422 -1 O SER A 421 N ALA A 404
SHEET 3 AA9 4 THR A 425 ASP A 433 -1 O THR A 428 N LEU A 420
SHEET 4 AA9 4 PHE A 442 THR A 447 -1 O SER A 443 N ARG A 431
SHEET 1 AB1 8 PHE A 458 GLU A 466 0
SHEET 2 AB1 8 LYS A 472 HIS A 480 -1 O ILE A 473 N TYR A 465
SHEET 3 AB1 8 ILE A 521 PRO A 525 -1 O PHE A 522 N VAL A 478
SHEET 4 AB1 8 ALA A 491 TYR A 494 1 N ILE A 492 O ALA A 523
SHEET 5 AB1 8 VAL A 571 ALA A 576 1 O ALA A 572 N GLN A 493
SHEET 6 AB1 8 ALA A 597 GLU A 601 1 O GLU A 601 N GLY A 575
SHEET 7 AB1 8 ALA A 652 GLY A 660 1 O ALA A 652 N ALA A 598
SHEET 8 AB1 8 LEU A 687 LEU A 696 1 O LEU A 688 N THR A 653
SHEET 1 AB2 2 VAL B 20 SER B 25 0
SHEET 2 AB2 2 GLY B 29 PRO B 34 -1 O VAL B 33 N ASP B 21
SHEET 1 AB3 3 LYS B 83 PHE B 84 0
SHEET 2 AB3 3 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB3 3 THR B 88 LEU B 89 -1 N THR B 88 O TYR B 96
SHEET 1 AB4 4 LYS B 83 PHE B 84 0
SHEET 2 AB4 4 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB4 4 VAL B 108 SER B 112 -1 O TYR B 110 N TRP B 97
SHEET 4 AB4 4 GLY B 128 PHE B 132 -1 O PHE B 131 N LEU B 109
SHEET 1 AB5 4 ALA B 143 PHE B 150 0
SHEET 2 AB5 4 PHE B 156 HIS B 163 -1 O ALA B 160 N LEU B 147
SHEET 3 AB5 4 SER B 169 SER B 175 -1 O THR B 170 N VAL B 161
SHEET 4 AB5 4 VAL B 197 PHE B 200 -1 O VAL B 197 N ILE B 171
SHEET 1 AB6 4 ILE B 206 TRP B 207 0
SHEET 2 AB6 4 GLY B 213 ARG B 218 -1 O LEU B 215 N ILE B 206
SHEET 3 AB6 4 MET B 235 LYS B 240 -1 O MET B 235 N ARG B 218
SHEET 4 AB6 4 ILE B 249 TYR B 252 -1 O TYR B 252 N MET B 236
SHEET 1 AB7 4 ILE B 261 THR B 266 0
SHEET 2 AB7 4 TYR B 272 PHE B 278 -1 O TYR B 274 N ASP B 265
SHEET 3 AB7 4 LEU B 286 GLU B 291 -1 O ALA B 290 N LEU B 273
SHEET 4 AB7 4 ARG B 304 VAL B 307 -1 O ARG B 304 N VAL B 289
SHEET 1 AB8 4 TYR B 314 HIS B 320 0
SHEET 2 AB8 4 LEU B 323 THR B 328 -1 O TYR B 325 N THR B 318
SHEET 3 AB8 4 LYS B 336 ASP B 341 -1 O ILE B 338 N ILE B 326
SHEET 4 AB8 4 GLU B 348 ILE B 353 -1 O PHE B 352 N VAL B 337
SHEET 1 AB9 4 LYS B 360 ALA B 367 0
SHEET 2 AB9 4 TYR B 371 ARG B 378 -1 O ILE B 375 N GLN B 363
SHEET 3 AB9 4 LYS B 381 TYR B 387 -1 O TYR B 387 N PHE B 372
SHEET 4 AB9 4 GLN B 393 LEU B 397 -1 O LEU B 394 N LEU B 386
SHEET 1 AC1 4 ALA B 404 ALA B 408 0
SHEET 2 AC1 4 HIS B 415 GLY B 422 -1 O SER B 421 N ALA B 404
SHEET 3 AC1 4 THR B 425 ASP B 433 -1 O THR B 428 N LEU B 420
SHEET 4 AC1 4 PHE B 442 THR B 447 -1 O SER B 443 N ARG B 431
SHEET 1 AC2 8 PHE B 458 GLU B 466 0
SHEET 2 AC2 8 LYS B 472 HIS B 480 -1 O ILE B 473 N TYR B 465
SHEET 3 AC2 8 ILE B 521 PRO B 525 -1 O PHE B 522 N VAL B 478
SHEET 4 AC2 8 ALA B 491 TYR B 494 1 N ILE B 492 O ALA B 523
SHEET 5 AC2 8 VAL B 571 ALA B 576 1 O ALA B 572 N GLN B 493
SHEET 6 AC2 8 ALA B 597 GLU B 601 1 O VAL B 599 N ILE B 573
SHEET 7 AC2 8 ALA B 652 GLY B 660 1 O THR B 656 N PRO B 600
SHEET 8 AC2 8 LEU B 687 LEU B 696 1 O LEU B 688 N THR B 653
SITE 1 AC1 11 GLN A 59 LEU A 62 ASP A 63 ILE A 68
SITE 2 AC1 11 GLN A 69 LYS A 709 ASP A 713 HOH A1082
SITE 3 AC1 11 HOH A1215 HOH A1466 LYS B 389
SITE 1 AC2 9 SER A 421 PRO A 426 PHE A 506 PHE A 507
SITE 2 AC2 9 HOH A 943 HOH A1073 HOH A1103 HOH A1136
SITE 3 AC2 9 ASP C 15
SITE 1 AC3 8 SER B 421 PRO B 426 PHE B 506 PHE B 507
SITE 2 AC3 8 HOH B1105 HOH B1107 ASP D 15 HOH D 208
SITE 1 AC4 8 ASN B 409 ARG B 410 GLN B 411 HOH B1256
SITE 2 AC4 8 HOH B1321 CYS D 25 HOH D 203 HOH D 205
CRYST1 99.040 114.880 141.310 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 0.010097 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007077 0.00000
TER 5763 LYS A 727
TER 11559 LYS B 727
TER 11697 CYS C 25
TER 11835 CYS D 25
MASTER 422 0 4 41 82 0 10 613224 4 24 118
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