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HEADER HYDROLASE 11-MAR-19 6QZ4
TITLE STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_0224;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCJ136
KEYWDS MHETASE, PET DEGRADATION, STRUCTURAL GENOMICS, HYDROLASE, PLASTIC-
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 30-SEP-20 6QZ4 0
JRNL AUTH M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL STRUCTURE OF FROM MHETASE FROM IDEONELLA SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 122208
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 11726
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 46.2545 - 5.5900 0.97 7395 386 0.1635 0.1563
REMARK 3 2 5.5900 - 4.4381 0.99 7575 388 0.1479 0.1750
REMARK 3 3 4.4381 - 3.8774 0.99 7576 332 0.1487 0.1671
REMARK 3 4 3.8774 - 3.5230 0.98 7433 466 0.1643 0.1834
REMARK 3 5 3.5230 - 3.2706 0.98 7536 346 0.1721 0.1845
REMARK 3 6 3.2706 - 3.0778 0.99 7498 402 0.1782 0.2062
REMARK 3 7 3.0778 - 2.9237 0.99 7529 430 0.1751 0.2074
REMARK 3 8 2.9237 - 2.7964 0.99 7445 471 0.1874 0.1853
REMARK 3 9 2.7964 - 2.6888 0.98 7452 432 0.1829 0.2039
REMARK 3 10 2.6888 - 2.5960 0.99 7477 395 0.1905 0.2237
REMARK 3 11 2.5960 - 2.5148 0.98 7489 374 0.1828 0.1947
REMARK 3 12 2.5148 - 2.4430 0.99 7462 443 0.1879 0.2173
REMARK 3 13 2.4430 - 2.3786 0.98 7537 342 0.1880 0.2143
REMARK 3 14 2.3786 - 2.3206 0.98 7427 414 0.1946 0.2543
REMARK 3 15 2.3206 - 2.2679 0.98 7446 324 0.1942 0.2146
REMARK 3 16 2.2679 - 2.2196 0.98 7536 379 0.1953 0.2209
REMARK 3 17 2.2196 - 2.1752 0.98 7538 343 0.1938 0.2306
REMARK 3 18 2.1752 - 2.1342 0.98 7478 348 0.2000 0.2541
REMARK 3 19 2.1342 - 2.0960 0.98 7440 414 0.2038 0.2350
REMARK 3 20 2.0960 - 2.0605 0.98 7358 410 0.2046 0.2564
REMARK 3 21 2.0605 - 2.0273 0.97 7354 445 0.2149 0.2413
REMARK 3 22 2.0273 - 1.9961 0.97 7447 374 0.2174 0.2536
REMARK 3 23 1.9961 - 1.9667 0.98 7469 374 0.2211 0.2634
REMARK 3 24 1.9667 - 1.9390 0.98 7433 414 0.2244 0.2498
REMARK 3 25 1.9390 - 1.9128 0.97 7348 392 0.2355 0.2532
REMARK 3 26 1.9128 - 1.8880 0.97 7430 364 0.2386 0.2559
REMARK 3 27 1.8880 - 1.8644 0.97 7500 359 0.2415 0.2632
REMARK 3 28 1.8644 - 1.8419 0.97 7287 423 0.2451 0.2857
REMARK 3 29 1.8419 - 1.8205 0.98 7439 355 0.2559 0.2662
REMARK 3 30 1.8205 - 1.8000 0.94 7152 387 0.2734 0.2840
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440
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 : 0.003 8679
REMARK 3 ANGLE : 0.607 11851
REMARK 3 CHIRALITY : 0.042 1242
REMARK 3 PLANARITY : 0.004 1591
REMARK 3 DIHEDRAL : 3.782 6873
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 6QZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
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) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122377
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
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: 6QZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE (PH 4.5), 22.5% PEG
REMARK 280 10000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 45.10600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.99550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.40200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.99550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.10600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.40200
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/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 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 GLN A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 MET A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 CYS A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 LEU A 604
REMARK 465 GLU A 605
REMARK 465 HIS A 606
REMARK 465 HIS A 607
REMARK 465 HIS A 608
REMARK 465 HIS A 609
REMARK 465 HIS A 610
REMARK 465 HIS A 611
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 VAL B 5
REMARK 465 THR B 6
REMARK 465 THR B 7
REMARK 465 MET B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 ALA B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 ALA B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 CYS B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 GLN B 35
REMARK 465 LEU B 604
REMARK 465 GLU B 605
REMARK 465 HIS B 606
REMARK 465 HIS B 607
REMARK 465 HIS B 608
REMARK 465 HIS B 609
REMARK 465 HIS B 610
REMARK 465 HIS B 611
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 A 905 O HOH B 1127 1.85
REMARK 500 O HOH B 1413 O HOH B 1428 1.86
REMARK 500 O HOH A 1161 O HOH A 1482 1.87
REMARK 500 O HOH A 1453 O HOH A 1566 1.91
REMARK 500 O HOH A 986 O HOH A 1367 1.94
REMARK 500 O HOH A 1009 O HOH A 1562 1.95
REMARK 500 O HOH B 1192 O HOH B 1297 1.96
REMARK 500 O HOH B 1108 O HOH B 1380 1.97
REMARK 500 OG1 THR B 328 O HOH B 901 1.98
REMARK 500 O HOH A 1710 O HOH A 1756 1.98
REMARK 500 O HOH B 1201 O HOH B 1286 1.98
REMARK 500 O HOH B 1200 O HOH B 1273 1.99
REMARK 500 O HOH A 1295 O HOH A 1472 1.99
REMARK 500 O HOH A 1416 O HOH A 1619 2.00
REMARK 500 O HOH B 1067 O HOH B 1388 2.00
REMARK 500 O HOH A 1632 O HOH B 1387 2.01
REMARK 500 O HOH B 1354 O HOH B 1363 2.04
REMARK 500 O HOH A 1329 O HOH A 1515 2.04
REMARK 500 O HOH A 1525 O HOH A 1599 2.05
REMARK 500 O HOH A 1217 O HOH A 1592 2.05
REMARK 500 O HOH A 936 O HOH A 1377 2.05
REMARK 500 N ASP B 60 O HOH B 902 2.06
REMARK 500 O ALA B 346 O HOH B 903 2.06
REMARK 500 O HOH A 1077 O HOH B 1282 2.06
REMARK 500 O HOH B 1430 O HOH B 1441 2.06
REMARK 500 O HOH A 1249 O HOH A 1695 2.07
REMARK 500 O HOH B 964 O HOH B 1085 2.08
REMARK 500 O HOH B 1323 O HOH B 1346 2.11
REMARK 500 OE1 GLU B 37 O HOH B 904 2.11
REMARK 500 O HOH A 1379 O HOH A 1432 2.12
REMARK 500 O HOH A 1748 O HOH A 1764 2.12
REMARK 500 O HOH B 1341 O HOH B 1403 2.13
REMARK 500 O HOH A 1650 O HOH A 1681 2.13
REMARK 500 O HOH A 1458 O HOH A 1551 2.13
REMARK 500 OG1 THR B 179 O HOH B 905 2.14
REMARK 500 O HOH A 1602 O HOH B 1311 2.14
REMARK 500 O HOH A 1716 O HOH A 1741 2.15
REMARK 500 O GLN B 297 O HOH B 906 2.15
REMARK 500 O HOH A 1361 O HOH A 1455 2.16
REMARK 500 O HOH B 1171 O HOH B 1297 2.18
REMARK 500 O HOH A 1278 O HOH A 1544 2.19
REMARK 500 O HOH A 1435 O HOH A 1490 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 1340 O HOH A 1442 3554 1.83
REMARK 500 O HOH B 1112 O HOH B 1241 3454 2.15
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 ALA A 67 33.10 -90.82
REMARK 500 ASN A 134 -145.71 58.85
REMARK 500 ASN A 171 44.74 -91.87
REMARK 500 TYR A 194 -32.17 -153.31
REMARK 500 SER A 225 -119.86 67.13
REMARK 500 ALA A 249 56.38 33.77
REMARK 500 TYR A 373 -91.90 -144.06
REMARK 500 SER A 383 -139.99 -135.59
REMARK 500 ASN A 408 10.11 -145.04
REMARK 500 ASN A 527 -146.55 -89.94
REMARK 500 CYS A 529 -17.93 68.99
REMARK 500 ALA B 67 32.09 -92.23
REMARK 500 ASN B 134 -149.16 60.38
REMARK 500 TYR B 194 -29.56 -155.87
REMARK 500 SER B 225 -120.53 65.23
REMARK 500 ALA B 249 54.41 36.19
REMARK 500 TYR B 373 -91.78 -148.81
REMARK 500 SER B 383 -140.09 -136.58
REMARK 500 VAL B 412 -64.43 -97.44
REMARK 500 GLU B 429A 73.18 -117.92
REMARK 500 SER B 491 32.77 -95.11
REMARK 500 ASN B 527 -147.10 -89.43
REMARK 500 CYS B 529 -19.99 69.57
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 A1758 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1759 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A1760 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A1761 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A1762 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A1763 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1764 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1765 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1766 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B1439 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1440 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B1441 DISTANCE = 6.35 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 69.7
REMARK 620 3 ASP A 307 OD1 71.6 136.5
REMARK 620 4 ASP A 307 OD2 74.8 132.2 50.5
REMARK 620 5 LEU A 309 O 84.2 81.4 75.7 125.9
REMARK 620 6 ASP A 311 OD1 145.1 77.4 132.2 138.9 79.7
REMARK 620 7 ILE A 313 O 100.2 79.4 126.8 76.4 157.4 84.4
REMARK 620 8 HOH A 916 O 142.4 147.7 72.2 74.7 96.2 70.6 93.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 68.0
REMARK 620 3 ASP B 307 OD1 75.0 140.2
REMARK 620 4 ASP B 307 OD2 77.6 130.8 49.3
REMARK 620 5 LEU B 309 O 76.3 85.4 71.8 119.8
REMARK 620 6 ASP B 311 OD1 142.5 77.4 131.3 138.9 87.0
REMARK 620 7 ILE B 313 O 102.0 77.6 125.4 76.5 162.1 83.8
REMARK 620 8 HOH B 912 O 142.5 149.4 68.3 72.9 98.9 72.6 93.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
DBREF1 6QZ4 A 1 603 UNP MHETH_IDESA
DBREF2 6QZ4 A A0A0K8P8E7 1 603
DBREF1 6QZ4 B 1 603 UNP MHETH_IDESA
DBREF2 6QZ4 B A0A0K8P8E7 1 603
SEQADV 6QZ4 LEU A 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 GLU A 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS A 611 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 LEU B 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 GLU B 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ4 HIS B 611 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 A 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 A 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 A 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 A 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 A 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 A 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 A 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 A 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 A 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 A 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 A 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 A 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 A 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 A 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 A 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 A 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 A 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 A 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 A 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 A 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 A 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 A 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 A 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 A 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 A 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 A 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 A 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 A 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 A 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 A 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 A 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 A 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 A 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 A 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 A 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 A 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 A 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 A 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 A 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 A 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 A 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 A 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 A 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 A 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 A 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 A 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 611 MET GLN THR THR VAL THR THR MET LEU LEU ALA SER VAL
SEQRES 2 B 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 B 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 B 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 B 611 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 6 B 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 B 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 B 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 B 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 10 B 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 11 B 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 B 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 B 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 B 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 B 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 16 B 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 B 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 B 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 19 B 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 B 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 B 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 B 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 B 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 B 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 B 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 B 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 B 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 B 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 29 B 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 B 611 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 31 B 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 B 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 B 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 B 611 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 35 B 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 B 611 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 37 B 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 B 611 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 39 B 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 B 611 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 B 611 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 42 B 611 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 43 B 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 B 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 B 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 B 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 B 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
HET CA A 801 1
HET SO4 A 802 5
HET CA B 801 1
HET SO4 B 802 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *1407(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 SER A 286 5 5
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 TRP A 394 LEU A 399 1 6
HELIX 17 AB8 GLY A 414 PHE A 424 1 11
HELIX 18 AB9 PRO A 432 THR A 434 5 3
HELIX 19 AC1 GLN A 435 PHE A 443 1 9
HELIX 20 AC2 ILE A 447 TRP A 453 5 7
HELIX 21 AC3 SER A 462 GLY A 468 1 7
HELIX 22 AC4 LEU A 474 ARG A 480 1 7
HELIX 23 AC5 SER A 496 MET A 511 1 16
HELIX 24 AC6 GLY A 513 GLY A 516 5 4
HELIX 25 AC7 MET A 540 GLY A 551 1 12
HELIX 26 AC8 THR A 563 GLY A 568 5 6
HELIX 27 AC9 THR A 593 ALA A 595 5 3
HELIX 28 AD1 SER B 47 ALA B 53 1 7
HELIX 29 AD2 ALA B 152 ASN B 156 5 5
HELIX 30 AD3 LEU B 177 LEU B 184 5 8
HELIX 31 AD4 ASP B 185 TYR B 194 1 10
HELIX 32 AD5 TYR B 194 GLY B 213 1 20
HELIX 33 AD6 SER B 225 PHE B 238 1 14
HELIX 34 AD7 GLN B 253 PRO B 255 5 3
HELIX 35 AD8 LYS B 256 ALA B 269 1 14
HELIX 36 AD9 PRO B 270 ALA B 272 5 3
HELIX 37 AE1 LEU B 282 SER B 286 5 5
HELIX 38 AE2 SER B 288 ASP B 304 1 17
HELIX 39 AE3 ALA B 305 GLY B 308 5 4
HELIX 40 AE4 ASN B 316 PHE B 324 1 9
HELIX 41 AE5 SER B 350 GLY B 363 1 14
HELIX 42 AE6 ASP B 379 SER B 383 5 5
HELIX 43 AE7 TRP B 394 LEU B 399 1 6
HELIX 44 AE8 GLY B 414 PHE B 424 1 11
HELIX 45 AE9 PRO B 432 THR B 434 5 3
HELIX 46 AF1 GLN B 435 LYS B 442 1 8
HELIX 47 AF2 ILE B 447 TRP B 453 5 7
HELIX 48 AF3 SER B 462 GLY B 468 1 7
HELIX 49 AF4 LEU B 474 ARG B 480 1 7
HELIX 50 AF5 SER B 496 MET B 511 1 16
HELIX 51 AF6 GLY B 513 GLY B 516 5 4
HELIX 52 AF7 MET B 540 GLY B 551 1 12
HELIX 53 AF8 THR B 563 GLY B 568 5 6
HELIX 54 AF9 THR B 593 ALA B 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O HIS A 91 N ARG A 76
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O ARG A 519 N LEU A 486
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 600 N ILE A 582
SHEET 1 AA5 9 THR B 68 ARG B 76 0
SHEET 2 AA5 9 HIS B 91 THR B 102 -1 O HIS B 91 N ARG B 76
SHEET 3 AA5 9 PRO B 108 PRO B 118 -1 O LEU B 115 N VAL B 94
SHEET 4 AA5 9 ALA B 158 THR B 162 -1 O THR B 159 N ARG B 116
SHEET 5 AA5 9 ARG B 124 GLU B 128 1 N PHE B 126 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O ARG B 519 N LEU B 486
SHEET 1 AA6 2 LEU B 385 SER B 386 0
SHEET 2 AA6 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA7 2 ILE B 557 TRP B 560 0
SHEET 2 AA7 2 THR B 573 LEU B 576 -1 O LEU B 576 N ILE B 557
SHEET 1 AA8 2 ILE B 582 TYR B 585 0
SHEET 2 AA8 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.06
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.04
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.04
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.04
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.04
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.05
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.03
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.04
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.03
LINK O ASP A 304 CA CA A 801 1555 1555 2.55
LINK OD1 ASP A 304 CA CA A 801 1555 1555 2.44
LINK OD1 ASP A 307 CA CA A 801 1555 1555 2.61
LINK OD2 ASP A 307 CA CA A 801 1555 1555 2.54
LINK O LEU A 309 CA CA A 801 1555 1555 2.33
LINK OD1 ASP A 311 CA CA A 801 1555 1555 2.48
LINK O ILE A 313 CA CA A 801 1555 1555 2.37
LINK CA CA A 801 O HOH A 916 1555 1555 2.53
LINK O ASP B 304 CA CA B 801 1555 1555 2.56
LINK OD1 ASP B 304 CA CA B 801 1555 1555 2.47
LINK OD1 ASP B 307 CA CA B 801 1555 1555 2.68
LINK OD2 ASP B 307 CA CA B 801 1555 1555 2.57
LINK O LEU B 309 CA CA B 801 1555 1555 2.34
LINK OD1 ASP B 311 CA CA B 801 1555 1555 2.55
LINK O ILE B 313 CA CA B 801 1555 1555 2.32
LINK CA CA B 801 O HOH B 912 1555 1555 2.60
CISPEP 1 THR A 426 PRO A 427 0 0.19
CISPEP 2 TYR A 579 PRO A 580 0 4.36
CISPEP 3 THR B 426 PRO B 427 0 -0.26
CISPEP 4 TYR B 579 PRO B 580 0 4.42
SITE 1 AC1 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC1 6 ILE A 313 HOH A 916
SITE 1 AC2 7 SER A 131 GLY A 132 SER A 225 TRP A 397
SITE 2 AC2 7 HIS A 528 HOH A 915 HOH A1121
SITE 1 AC3 6 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AC3 6 ILE B 313 HOH B 912
SITE 1 AC4 5 SER B 131 GLY B 132 SER B 225 TRP B 397
SITE 2 AC4 5 HIS B 528
CRYST1 90.212 92.804 159.991 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 0.011085 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006250 0.00000
TER 4218 PRO A 603
TER 8428 PRO B 603
MASTER 498 0 4 54 30 0 8 6 9805 2 50 94
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