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HEADER HYDROLASE 26-APR-19 6JYM
TITLE CRYSTAL STRUCTURE OF PROLYL ENDOPEPTIDASE FROM HALIOTIS DISCUS HANNAI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.26;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALIOTIS DISCUS HANNAI;
SOURCE 3 ORGANISM_COMMON: JAPANESE ABALONE;
SOURCE 4 ORGANISM_TAXID: 42344;
SOURCE 5 GENE: PREP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS A SERINE PROTEASE SUBFAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LI,M.CAO,T.JIN
REVDAT 1 29-APR-20 6JYM 0
JRNL AUTH W.LI,M.CAO,T.JIN
JRNL TITL CRYSTAL STRUCTURE OF PROLYL ENDOPEPTIDASE FROM HALIOTIS
JRNL TITL 2 DISCUS HANNAI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 125368
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6269
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 46.1387 - 4.6591 0.99 4361 230 0.1795 0.1762
REMARK 3 2 4.6591 - 3.6986 1.00 4196 221 0.1460 0.1598
REMARK 3 3 3.6986 - 3.2312 1.00 4168 219 0.1499 0.1582
REMARK 3 4 3.2312 - 2.9358 1.00 4117 217 0.1609 0.1884
REMARK 3 5 2.9358 - 2.7254 0.99 4112 216 0.1791 0.1828
REMARK 3 6 2.7254 - 2.5647 0.99 4091 216 0.1820 0.1997
REMARK 3 7 2.5647 - 2.4363 0.99 4059 213 0.1795 0.1939
REMARK 3 8 2.4363 - 2.3303 0.99 4043 213 0.1803 0.1898
REMARK 3 9 2.3303 - 2.2406 0.99 4052 213 0.1785 0.1787
REMARK 3 10 2.2406 - 2.1632 0.99 4024 213 0.1768 0.1933
REMARK 3 11 2.1632 - 2.0956 0.99 4050 213 0.1769 0.1878
REMARK 3 12 2.0956 - 2.0357 0.98 3959 208 0.1717 0.2053
REMARK 3 13 2.0357 - 1.9821 0.98 3995 210 0.1825 0.1996
REMARK 3 14 1.9821 - 1.9337 0.98 4028 212 0.1802 0.2121
REMARK 3 15 1.9337 - 1.8898 0.98 3949 208 0.1844 0.1940
REMARK 3 16 1.8898 - 1.8496 0.98 3948 207 0.1943 0.2194
REMARK 3 17 1.8496 - 1.8126 0.97 3953 209 0.1964 0.2320
REMARK 3 18 1.8126 - 1.7784 0.97 3944 207 0.2039 0.2087
REMARK 3 19 1.7784 - 1.7466 0.97 3910 206 0.2062 0.2227
REMARK 3 20 1.7466 - 1.7170 0.97 3928 207 0.2016 0.2278
REMARK 3 21 1.7170 - 1.6893 0.97 3948 208 0.2086 0.2159
REMARK 3 22 1.6893 - 1.6633 0.96 3859 203 0.2014 0.2257
REMARK 3 23 1.6633 - 1.6388 0.96 3869 203 0.2040 0.2245
REMARK 3 24 1.6388 - 1.6158 0.95 3877 204 0.2095 0.2224
REMARK 3 25 1.6158 - 1.5939 0.95 3839 202 0.2102 0.2202
REMARK 3 26 1.5939 - 1.5732 0.94 3803 201 0.2124 0.2268
REMARK 3 27 1.5732 - 1.5536 0.94 3826 201 0.2246 0.2426
REMARK 3 28 1.5536 - 1.5348 0.94 3765 199 0.2247 0.2265
REMARK 3 29 1.5348 - 1.5170 0.93 3786 198 0.2345 0.2201
REMARK 3 30 1.5170 - 1.4999 0.91 3640 192 0.2467 0.2608
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.540
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 : 0.002 5884
REMARK 3 ANGLE : 0.457 7980
REMARK 3 CHIRALITY : 0.063 836
REMARK 3 PLANARITY : 0.003 1041
REMARK 3 DIHEDRAL : 15.443 3475
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 112.4328 7.1332 158.1781
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.1108
REMARK 3 T33: 0.1087 T12: -0.0040
REMARK 3 T13: 0.0073 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.2138 L22: 0.4172
REMARK 3 L33: 0.2773 L12: -0.0240
REMARK 3 L13: 0.0266 L23: 0.0120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0098 S13: 0.0331
REMARK 3 S21: -0.0184 S22: 0.0130 S23: -0.0276
REMARK 3 S31: 0.0025 S32: 0.0039 S33: -0.0164
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 6JYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300010842.
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) : 190
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97894
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SILICON CRYSTAL (111)
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 125459
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
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: 1QFS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.2 M AMMONIUM
REMARK 280 CITRATE (DIBASIC), PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K
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 27.66250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.86950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.47750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.86950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.66250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.47750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 SER A -25
REMARK 465 SER A -24
REMARK 465 GLY A -23
REMARK 465 LEU A -22
REMARK 465 VAL A -21
REMARK 465 PRO A -20
REMARK 465 ARG A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 MET A -15
REMARK 465 ALA A -14
REMARK 465 SER A -13
REMARK 465 MET A -12
REMARK 465 THR A -11
REMARK 465 GLY A -10
REMARK 465 GLY A -9
REMARK 465 GLN A -8
REMARK 465 GLN A -7
REMARK 465 MET A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 CYS A 707
REMARK 465 GLY A 708
REMARK 465 ARG A 709
REMARK 465 THR A 710
REMARK 465 ARG A 711
REMARK 465 ALA A 712
REMARK 465 PRO A 713
REMARK 465 PRO A 714
REMARK 465 PRO A 715
REMARK 465 PRO A 716
REMARK 465 PRO A 717
REMARK 465 LEU A 718
REMARK 465 ARG A 719
REMARK 465 SER A 720
REMARK 465 GLY A 721
REMARK 465 CYS A 722
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 130 119.63 -161.53
REMARK 500 MET A 175 76.80 -156.57
REMARK 500 ARG A 273 -9.45 -144.93
REMARK 500 ASP A 283 50.84 -109.05
REMARK 500 ILE A 292 -61.68 -102.69
REMARK 500 ALA A 307 86.40 -152.64
REMARK 500 TYR A 310 153.42 75.19
REMARK 500 LYS A 334 -41.86 -133.20
REMARK 500 LYS A 345 -54.08 71.83
REMARK 500 TYR A 472 -77.79 -129.85
REMARK 500 CYS A 519 -123.16 55.47
REMARK 500 SER A 553 -111.89 58.38
REMARK 500 VAL A 577 45.63 38.24
REMARK 500 THR A 589 -112.91 38.53
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 A1812 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A1813 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A1814 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A1815 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A1816 DISTANCE = 6.88 ANGSTROMS
DBREF1 6JYM A 1 706 UNP A0A1X9T5X9_HALDH
DBREF2 6JYM A A0A1X9T5X9 1 706
SEQADV 6JYM MET A -35 UNP A0A1X9T5X INITIATING METHIONINE
SEQADV 6JYM GLY A -34 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -33 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -32 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -31 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -30 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -29 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -28 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -27 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -26 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -25 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -24 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -23 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM LEU A -22 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM VAL A -21 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A -20 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ARG A -19 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -18 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -17 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM HIS A -16 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM MET A -15 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ALA A -14 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -13 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM MET A -12 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM THR A -11 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -10 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -9 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLN A -8 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLN A -7 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM MET A -6 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -5 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ARG A -4 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A -3 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A -2 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLU A -1 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PHE A 0 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM CYS A 707 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A 708 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ARG A 709 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM THR A 710 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ARG A 711 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ALA A 712 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A 713 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A 714 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A 715 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A 716 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM PRO A 717 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM LEU A 718 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM ARG A 719 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM SER A 720 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM GLY A 721 UNP A0A1X9T5X EXPRESSION TAG
SEQADV 6JYM CYS A 722 UNP A0A1X9T5X EXPRESSION TAG
SEQRES 1 A 758 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 758 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 758 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET GLY LYS
SEQRES 4 A 758 PHE THR TYR PRO ASN ALA ARG ARG ASP GLU LEU VAL GLU
SEQRES 5 A 758 ASP TYR HIS GLY THR LYS VAL THR GLU TYR TYR ARG TRP
SEQRES 6 A 758 LEU GLU ASP PRO ASP SER GLU GLU THR LYS ALA PHE VAL
SEQRES 7 A 758 GLU ALA GLN ASN GLU LEU SER LYS PRO PHE LEU ASP ALA
SEQRES 8 A 758 CYS PRO ILE ARG GLU LYS LEU SER SER ARG ILE THR GLU
SEQRES 9 A 758 VAL TRP ASP TYR PRO LYS TYR SER CYS PRO GLY ARG HIS
SEQRES 10 A 758 GLY GLU TYR PHE TYR TYR TYR HIS ASN THR GLY LEU GLN
SEQRES 11 A 758 ASN GLN SER VAL LEU TYR ALA GLN LYS GLY LEU GLY ALA
SEQRES 12 A 758 ASP PRO SER VAL PHE LEU ASP PRO ASN SER LEU SER GLU
SEQRES 13 A 758 ASP GLY THR VAL SER LEU ARG GLY THR ALA PHE SER GLU
SEQRES 14 A 758 ASN ASP GLN PHE PHE ALA TYR GLY LEU SER LYS SER GLY
SEQRES 15 A 758 SER ASP TRP VAL THR ILE LYS PHE LYS LYS ALA PRO SER
SEQRES 16 A 758 GLY GLU ASP LEU PRO ASP THR LEU GLU ARG VAL LYS PHE
SEQRES 17 A 758 SER SER MET ALA TRP THR HIS ASP HIS LYS GLY LEU PHE
SEQRES 18 A 758 TYR ASN ARG TYR LEU GLU GLN GLN GLY LYS SER ASP GLY
SEQRES 19 A 758 THR GLU THR THR MET ASN VAL ASP GLN LYS LEU PHE TYR
SEQRES 20 A 758 HIS ARG LEU GLY THR ASP GLN SER GLU ASP VAL LEU VAL
SEQRES 21 A 758 ALA GLU PHE PRO GLU HIS PRO ARG TRP MET ILE GLY ALA
SEQRES 22 A 758 GLU VAL SER ASP CYS GLY ARG TYR LEU VAL MET THR ILE
SEQRES 23 A 758 HIS GLU GLY CYS ASP PRO VAL ASN ARG LEU TYR TYR VAL
SEQRES 24 A 758 ASP LEU LYS SER MET GLN ASN GLU ILE ARG GLY VAL LEU
SEQRES 25 A 758 SER TYR VAL LYS ILE VAL ASP ASN PHE ASP ALA GLU TYR
SEQRES 26 A 758 GLU TYR ILE THR ASN ASP GLY SER LYS PHE THR PHE LYS
SEQRES 27 A 758 THR ASN LEU ASN ALA SER ARG TYR LYS LEU ILE ASN ILE
SEQRES 28 A 758 ASP PHE ALA ASP PRO ASP GLN SER ASN TRP GLN THR LEU
SEQRES 29 A 758 VAL ASP GLU ASP GLU LYS SER VAL LEU GLU TRP ALA ALA
SEQRES 30 A 758 CYS VAL ASN LYS ASP LYS LEU ILE LEU CYS TYR LEU LYS
SEQRES 31 A 758 ASP VAL LYS ASN GLU LEU TYR VAL HIS GLY LEU SER SER
SEQRES 32 A 758 GLY SER ARG MET SER GLN LEU PRO LEU GLU VAL GLY SER
SEQRES 33 A 758 VAL VAL GLY TYR SER GLY LYS LYS LYS TYR ASP GLU ILE
SEQRES 34 A 758 PHE TYR GLN PHE THR SER PHE LEU THR PRO GLY ILE ILE
SEQRES 35 A 758 TYR ARG CYS ASP MET THR THR ASP THR TYR THR PRO LYS
SEQRES 36 A 758 THR PHE ARG GLU ILE LYS VAL LYS ASP PHE ASP THR SER
SEQRES 37 A 758 GLN PHE GLU THR GLU GLN VAL PHE PHE PRO SER LYS ASP
SEQRES 38 A 758 GLY THR LYS ILE PRO MET PHE ILE VAL HIS ARG LYS GLY
SEQRES 39 A 758 LEU VAL HIS ASP GLY SER HIS PRO VAL MET LEU TYR GLY
SEQRES 40 A 758 TYR GLY GLY PHE ASN ILE SER ILE THR PRO SER PHE SER
SEQRES 41 A 758 PRO SER ARG LEU VAL PHE LEU GLN HIS LEU GLY GLY VAL
SEQRES 42 A 758 TYR ALA ILE ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY
SEQRES 43 A 758 GLU SER TRP HIS LYS ALA GLY ASN CYS ALA ASN LYS GLN
SEQRES 44 A 758 ASN VAL PHE ASP ASP PHE GLN SER ALA ALA GLN TYR LEU
SEQRES 45 A 758 ILE GLU ASN LYS TRP THR SER ALA LYS ARG ILE THR ILE
SEQRES 46 A 758 ASN GLY GLY SER ASN GLY GLY LEU LEU VAL GLY ALA CYS
SEQRES 47 A 758 ILE ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA VAL ALA
SEQRES 48 A 758 GLN VAL GLY VAL LEU ASP MET LEU ARG PHE HIS LYS PHE
SEQRES 49 A 758 THR ILE GLY HIS ALA TRP THR THR ASP TYR GLY SER SER
SEQRES 50 A 758 ASP SER THR ASP ASP PHE LYS VAL LEU ILE LYS TYR SER
SEQRES 51 A 758 PRO LEU HIS ASN ILE ARG GLU GLN LYS ASP GLN TYR PRO
SEQRES 52 A 758 ALA LEU LEU LEU LEU THR GLY ASP HIS ASP ASP ARG VAL
SEQRES 53 A 758 VAL PRO LEU HIS SER LEU LYS PHE LEU ALA GLN ILE GLN
SEQRES 54 A 758 TYR THR PHE LYS ASP SER ASP SER GLN THR ASN PRO LEU
SEQRES 55 A 758 MET GLY ARG ILE ASP THR LYS SER GLY HIS GLY PHE GLY
SEQRES 56 A 758 LYS PRO THR ALA LYS VAL ILE GLU GLU LEU THR ASP ILE
SEQRES 57 A 758 TYR SER PHE MET HIS GLN THR VAL GLY LEU LYS TRP SER
SEQRES 58 A 758 ASP CYS GLY ARG THR ARG ALA PRO PRO PRO PRO PRO LEU
SEQRES 59 A 758 ARG SER GLY CYS
FORMUL 2 HOH *1016(H2 O)
HELIX 1 AA1 TYR A 27 ASP A 32 5 6
HELIX 2 AA2 SER A 35 ALA A 55 1 21
HELIX 3 AA3 ILE A 58 ASP A 71 1 14
HELIX 4 AA4 ASP A 114 SER A 119 5 6
HELIX 5 AA5 ASP A 217 ASP A 221 5 5
HELIX 6 AA6 ASP A 321 TRP A 325 5 5
HELIX 7 AA7 ASP A 430 SER A 432 5 3
HELIX 8 AA8 SER A 484 LEU A 494 1 11
HELIX 9 AA9 GLY A 510 ALA A 516 1 7
HELIX 10 AB1 GLY A 517 ALA A 520 5 4
HELIX 11 AB2 ASN A 521 ASN A 539 1 19
HELIX 12 AB3 SER A 543 LYS A 545 5 3
HELIX 13 AB4 SER A 553 ARG A 566 1 14
HELIX 14 AB5 PRO A 567 PHE A 570 5 4
HELIX 15 AB6 ARG A 584 PHE A 588 5 5
HELIX 16 AB7 ILE A 590 ALA A 593 5 4
HELIX 17 AB8 TRP A 594 GLY A 599 1 6
HELIX 18 AB9 SER A 603 SER A 614 1 12
HELIX 19 AC1 PRO A 615 ASN A 618 5 4
HELIX 20 AC2 PRO A 642 PHE A 656 1 15
HELIX 21 AC3 PRO A 681 VAL A 700 1 20
SHEET 1 AA1 2 LEU A 14 TYR A 18 0
SHEET 2 AA1 2 THR A 21 GLU A 25 -1 O THR A 21 N TYR A 18
SHEET 1 AA2 3 LYS A 74 TYR A 75 0
SHEET 2 AA2 3 TYR A 84 ASN A 90 -1 O ASN A 90 N LYS A 74
SHEET 3 AA2 3 GLY A 79 HIS A 81 -1 N HIS A 81 O TYR A 84
SHEET 1 AA3 4 LYS A 74 TYR A 75 0
SHEET 2 AA3 4 TYR A 84 ASN A 90 -1 O ASN A 90 N LYS A 74
SHEET 3 AA3 4 VAL A 98 GLN A 102 -1 O TYR A 100 N TYR A 87
SHEET 4 AA3 4 SER A 110 LEU A 113 -1 O SER A 110 N ALA A 101
SHEET 1 AA4 7 VAL A 124 PHE A 131 0
SHEET 2 AA4 7 PHE A 137 LYS A 144 -1 O ALA A 139 N ALA A 130
SHEET 3 AA4 7 VAL A 150 LYS A 156 -1 O LYS A 153 N TYR A 140
SHEET 4 AA4 7 ASP A 162 TRP A 177 -1 O VAL A 170 N VAL A 150
SHEET 5 AA4 7 GLY A 183 ARG A 188 -1 O PHE A 185 N ALA A 176
SHEET 6 AA4 7 LYS A 208 ARG A 213 -1 O PHE A 210 N TYR A 186
SHEET 7 AA4 7 VAL A 222 ALA A 225 -1 O ALA A 225 N LEU A 209
SHEET 1 AA5 4 MET A 234 VAL A 239 0
SHEET 2 AA5 4 TYR A 245 HIS A 251 -1 O VAL A 247 N GLU A 238
SHEET 3 AA5 4 ARG A 259 ASP A 264 -1 O VAL A 263 N LEU A 246
SHEET 4 AA5 4 VAL A 279 VAL A 282 -1 O ILE A 281 N LEU A 260
SHEET 1 AA6 4 GLU A 290 ASP A 295 0
SHEET 2 AA6 4 LYS A 298 THR A 303 -1 O THR A 300 N THR A 293
SHEET 3 AA6 4 LYS A 311 ASP A 316 -1 O ILE A 315 N PHE A 299
SHEET 4 AA6 4 GLN A 326 VAL A 329 -1 O GLN A 326 N ASN A 314
SHEET 1 AA7 4 VAL A 336 VAL A 343 0
SHEET 2 AA7 4 LYS A 347 LEU A 353 -1 O ILE A 349 N ALA A 341
SHEET 3 AA7 4 ASN A 358 GLY A 364 -1 O HIS A 363 N LEU A 348
SHEET 4 AA7 4 ARG A 370 LEU A 374 -1 O MET A 371 N VAL A 362
SHEET 1 AA8 4 SER A 380 SER A 385 0
SHEET 2 AA8 4 GLU A 392 SER A 399 -1 O PHE A 394 N SER A 385
SHEET 3 AA8 4 THR A 402 ASP A 410 -1 O TYR A 407 N TYR A 395
SHEET 4 AA8 4 LYS A 419 ILE A 424 -1 O LYS A 419 N ARG A 408
SHEET 1 AA9 8 PHE A 434 PRO A 442 0
SHEET 2 AA9 8 LYS A 448 ARG A 456 -1 O ILE A 449 N PHE A 441
SHEET 3 AA9 8 VAL A 497 ALA A 501 -1 O TYR A 498 N VAL A 454
SHEET 4 AA9 8 VAL A 467 TYR A 470 1 N TYR A 470 O ALA A 499
SHEET 5 AA9 8 ILE A 547 GLY A 552 1 O THR A 548 N LEU A 469
SHEET 6 AA9 8 CYS A 572 GLN A 576 1 O VAL A 574 N ILE A 549
SHEET 7 AA9 8 ALA A 628 GLY A 634 1 O ALA A 628 N ALA A 573
SHEET 8 AA9 8 LEU A 666 ASP A 671 1 O MET A 667 N LEU A 629
CISPEP 1 ALA A 157 PRO A 158 0 4.12
CRYST1 55.325 104.955 137.739 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018075 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009528 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007260 0.00000
TER 5728 ASP A 706
MASTER 342 0 0 21 40 0 0 6 6673 1 0 59
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