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HEADER HYDROLASE 11-APR-22 7ZJO
TITLE PHOSPHORYLATED THALASSOSPIRA SP. ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THALASSOSPIRA SP.;
SOURCE 3 ORGANISM_TAXID: 1912094;
SOURCE 4 GENE: CMO05_03125;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NICO21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-26B(+)
KEYWDS ESTERASE, LIPASE, INHIBITOR, COMPLEX, PHOSPHORYLATED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.LUND
REVDAT 1 29-OCT-25 7ZJO 0
JRNL AUTH B.A.LUND
JRNL TITL PHOSPHORYLATED THALASSOSPIRA SP. ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 113103
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.470
REMARK 3 FREE R VALUE TEST SET COUNT : 1658
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 64.1000 - 4.4600 0.97 9483 138 0.1747 0.1823
REMARK 3 2 4.4600 - 3.5400 0.97 9361 138 0.1499 0.1596
REMARK 3 3 3.5400 - 3.1000 0.97 9315 141 0.1600 0.2070
REMARK 3 4 3.1000 - 2.8100 0.97 9349 143 0.1532 0.1919
REMARK 3 5 2.8100 - 2.6100 0.97 9333 137 0.1535 0.1849
REMARK 3 6 2.6100 - 2.4600 0.97 9291 131 0.1553 0.2181
REMARK 3 7 2.4600 - 2.3300 0.97 9267 140 0.1619 0.2090
REMARK 3 8 2.3300 - 2.2300 0.97 9305 138 0.1710 0.2396
REMARK 3 9 2.2300 - 2.1500 0.96 9202 140 0.1841 0.2227
REMARK 3 10 2.1500 - 2.0700 0.96 9161 140 0.2021 0.2520
REMARK 3 11 2.0700 - 2.0100 0.96 9184 136 0.2179 0.2596
REMARK 3 12 2.0100 - 1.9500 0.96 9194 136 0.2445 0.2645
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.187
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.534
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.87
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 : 0.009 9958
REMARK 3 ANGLE : 0.921 13613
REMARK 3 CHIRALITY : 0.056 1546
REMARK 3 PLANARITY : 0.010 1795
REMARK 3 DIHEDRAL : 8.651 1428
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): 54.2926 0.6483 64.4392
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.2028
REMARK 3 T33: 0.1904 T12: -0.0088
REMARK 3 T13: 0.0107 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.1488 L22: 0.2063
REMARK 3 L33: 0.1756 L12: 0.0684
REMARK 3 L13: 0.0560 L23: 0.0305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0192 S12: -0.0414 S13: -0.0226
REMARK 3 S21: -0.0208 S22: -0.0090 S23: 0.0192
REMARK 3 S31: 0.0290 S32: -0.0491 S33: 0.0317
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 7ZJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1292122282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : POINTLESS 1.11.21, AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113113
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 64.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.07344
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36820
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: 4V2I
REMARK 200
REMARK 200 REMARK: PLATE-LIKE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 HEPES 7.5, 2 % V/V PEG 400 (STRUCTURE HT C6), PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.60500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.88400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.60500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 57.88400
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: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 80.51484
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 57.88400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 87.55395
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 ASP A 1
REMARK 465 LYS A 317
REMARK 465 ASP B 1
REMARK 465 PRO B 2
REMARK 465 LYS B 317
REMARK 465 ASP C 1
REMARK 465 PRO C 2
REMARK 465 LYS C 317
REMARK 465 LYS D 317
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 HE ARG D 76 O HOH D 505 1.54
REMARK 500 HH22 ARG A 69 O ASP A 75 1.57
REMARK 500 OE1 GLU D 222 O HOH D 501 1.99
REMARK 500 OG SER A 238 O HOH A 501 2.01
REMARK 500 O HOH C 737 O HOH C 788 2.03
REMARK 500 O HOH A 640 O HOH A 653 2.03
REMARK 500 O HOH C 772 O HOH C 809 2.03
REMARK 500 OD1 ASP D 178 O HOH D 502 2.06
REMARK 500 O HOH B 688 O HOH B 701 2.07
REMARK 500 O GLU A 239 O HOH A 502 2.08
REMARK 500 O HOH D 506 O HOH D 596 2.10
REMARK 500 O HOH C 729 O HOH C 737 2.10
REMARK 500 O HOH C 667 O HOH C 787 2.10
REMARK 500 O HOH C 697 O HOH C 797 2.11
REMARK 500 O HOH B 558 O HOH B 687 2.13
REMARK 500 O HOH A 690 O HOH B 697 2.14
REMARK 500 O HOH D 578 O HOH D 670 2.14
REMARK 500 O HOH B 680 O HOH C 694 2.15
REMARK 500 O GLY A 316 O HOH A 503 2.15
REMARK 500 O4 SO4 C 503 O HOH C 601 2.15
REMARK 500 O4 SO4 B 405 O HOH B 501 2.16
REMARK 500 O HOH C 729 O HOH C 788 2.16
REMARK 500 OE1 GLN A 144 O HOH A 504 2.18
REMARK 500 O HOH C 776 O HOH C 793 2.18
REMARK 500 O HOH C 733 O HOH C 746 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 556 O HOH B 683 2656 2.03
REMARK 500 O HOH A 600 O HOH C 817 4546 2.17
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 86 41.44 112.88
REMARK 500 TRP A 88 -29.57 71.59
REMARK 500 SEP A 158 -113.12 56.56
REMARK 500 TYR A 186 64.44 30.66
REMARK 500 TRP A 206 -62.99 72.08
REMARK 500 ASN A 254 78.06 -115.60
REMARK 500 SER B 40 29.25 -77.61
REMARK 500 ALA B 44 99.03 -16.60
REMARK 500 ALA B 86 43.09 105.08
REMARK 500 TRP B 88 -26.51 72.52
REMARK 500 SEP B 158 -114.60 59.73
REMARK 500 TYR B 186 68.51 27.40
REMARK 500 TRP B 206 -67.78 70.86
REMARK 500 ALA C 86 43.21 107.53
REMARK 500 TRP C 88 -25.04 73.47
REMARK 500 SEP C 158 -116.56 61.49
REMARK 500 TYR C 186 66.97 26.34
REMARK 500 TRP C 206 -65.97 70.28
REMARK 500 ASN C 254 78.95 -111.85
REMARK 500 ALA D 86 44.93 107.48
REMARK 500 TRP D 88 -29.17 71.99
REMARK 500 SEP D 158 -115.96 59.44
REMARK 500 TYR D 186 61.90 31.96
REMARK 500 TRP D 206 -57.42 70.66
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 D 673 DISTANCE = 5.90 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4V2I RELATED DB: PDB
REMARK 900 4V2I CONTAINS THE SAME PROTEIN WITHOUT PHOSPHORYLATION OF THE
REMARK 900 ACTIVE SITE SERINE
DBREF1 7ZJO A 1 317 UNP A0A2E9W914_9PROT
DBREF2 7ZJO A A0A2E9W914 27 343
DBREF1 7ZJO B 1 317 UNP A0A2E9W914_9PROT
DBREF2 7ZJO B A0A2E9W914 27 343
DBREF1 7ZJO C 1 317 UNP A0A2E9W914_9PROT
DBREF2 7ZJO C A0A2E9W914 27 343
DBREF1 7ZJO D 1 317 UNP A0A2E9W914_9PROT
DBREF2 7ZJO D A0A2E9W914 27 343
SEQRES 1 A 317 ASP PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 A 317 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 A 317 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 A 317 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 A 317 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 A 317 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 A 317 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 A 317 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 A 317 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 A 317 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 A 317 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 A 317 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 A 317 ASP SEP VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 A 317 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 A 317 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 A 317 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 A 317 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 A 317 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 A 317 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 A 317 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 A 317 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 A 317 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 A 317 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 A 317 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 A 317 ALA LEU HIS GLY LYS
SEQRES 1 B 317 ASP PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 B 317 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 B 317 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 B 317 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 B 317 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 B 317 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 B 317 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 B 317 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 B 317 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 B 317 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 B 317 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 B 317 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 B 317 ASP SEP VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 B 317 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 B 317 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 B 317 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 B 317 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 B 317 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 B 317 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 B 317 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 B 317 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 B 317 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 B 317 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 B 317 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 B 317 ALA LEU HIS GLY LYS
SEQRES 1 C 317 ASP PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 C 317 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 C 317 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 C 317 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 C 317 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 C 317 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 C 317 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 C 317 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 C 317 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 C 317 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 C 317 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 C 317 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 C 317 ASP SEP VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 C 317 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 C 317 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 C 317 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 C 317 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 C 317 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 C 317 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 C 317 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 C 317 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 C 317 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 C 317 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 C 317 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 C 317 ALA LEU HIS GLY LYS
SEQRES 1 D 317 ASP PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 D 317 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 D 317 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 D 317 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 D 317 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 D 317 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 D 317 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 D 317 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 D 317 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 D 317 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 D 317 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 D 317 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 D 317 ASP SEP VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 D 317 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 D 317 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 D 317 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 D 317 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 D 317 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 D 317 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 D 317 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 D 317 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 D 317 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 D 317 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 D 317 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 D 317 ALA LEU HIS GLY LYS
MODRES 7ZJO SEP A 158 SER MODIFIED RESIDUE
MODRES 7ZJO SEP B 158 SER MODIFIED RESIDUE
MODRES 7ZJO SEP C 158 SER MODIFIED RESIDUE
MODRES 7ZJO SEP D 158 SER MODIFIED RESIDUE
HET SEP A 158 13
HET SEP B 158 13
HET SEP C 158 13
HET SEP D 158 13
HET EDO A 401 10
HET NPO B 401 15
HET EDO B 402 10
HET SO4 B 403 5
HET 1PE B 404 38
HET SO4 B 405 5
HET EDO B 406 20
HET EDO B 407 10
HET NPO C 501 15
HET 1PE C 502 38
HET SO4 C 503 5
HET EDO C 504 10
HET EDO C 505 10
HET EDO C 506 10
HET EDO C 507 10
HET NPO D 401 15
HET EDO D 402 20
HETNAM SEP PHOSPHOSERINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NPO P-NITROPHENOL
HETNAM SO4 SULFATE ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN SEP PHOSPHONOSERINE
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 1 SEP 4(C3 H8 N O6 P)
FORMUL 5 EDO 9(C2 H6 O2)
FORMUL 6 NPO 3(C6 H5 N O3)
FORMUL 8 SO4 3(O4 S 2-)
FORMUL 9 1PE 2(C10 H22 O6)
FORMUL 22 HOH *784(H2 O)
HELIX 1 AA1 GLU A 5 GLY A 19 1 15
HELIX 2 AA2 ALA A 22 LEU A 26 5 5
HELIX 3 AA3 THR A 27 GLN A 39 1 13
HELIX 4 AA4 HIS A 96 ASN A 108 1 13
HELIX 5 AA5 PRO A 125 HIS A 141 1 17
HELIX 6 AA6 HIS A 141 ASN A 146 1 6
HELIX 7 AA7 SEP A 158 GLY A 175 1 18
HELIX 8 AA8 ASN A 195 PHE A 201 1 7
HELIX 9 AA9 THR A 208 LEU A 220 1 13
HELIX 10 AB1 THR A 232 ALA A 236 5 5
HELIX 11 AB2 THR A 237 SER A 242 1 6
HELIX 12 AB3 LEU A 257 ALA A 271 1 15
HELIX 13 AB4 LEU A 290 ALA A 294 5 5
HELIX 14 AB5 THR A 296 GLY A 316 1 21
HELIX 15 AB6 GLU B 5 LEU B 15 1 11
HELIX 16 AB7 ALA B 22 LEU B 26 5 5
HELIX 17 AB8 THR B 27 GLN B 39 1 13
HELIX 18 AB9 HIS B 96 ASN B 108 1 13
HELIX 19 AC1 PRO B 125 HIS B 141 1 17
HELIX 20 AC2 HIS B 141 ASN B 146 1 6
HELIX 21 AC3 SEP B 158 GLY B 175 1 18
HELIX 22 AC4 ASN B 195 PHE B 201 1 7
HELIX 23 AC5 THR B 208 LEU B 220 1 13
HELIX 24 AC6 THR B 232 ALA B 236 5 5
HELIX 25 AC7 THR B 237 SER B 242 1 6
HELIX 26 AC8 LEU B 257 ALA B 271 1 15
HELIX 27 AC9 LEU B 290 ALA B 294 5 5
HELIX 28 AD1 THR B 296 GLY B 316 1 21
HELIX 29 AD2 GLU C 5 LEU C 15 1 11
HELIX 30 AD3 ALA C 22 LEU C 26 5 5
HELIX 31 AD4 THR C 27 GLN C 39 1 13
HELIX 32 AD5 HIS C 96 ASN C 108 1 13
HELIX 33 AD6 PRO C 125 HIS C 141 1 17
HELIX 34 AD7 HIS C 141 ASN C 146 1 6
HELIX 35 AD8 SEP C 158 GLY C 175 1 18
HELIX 36 AD9 ASN C 195 PHE C 201 1 7
HELIX 37 AE1 THR C 208 LEU C 220 1 13
HELIX 38 AE2 THR C 232 ALA C 236 5 5
HELIX 39 AE3 THR C 237 SER C 242 1 6
HELIX 40 AE4 LEU C 257 ALA C 271 1 15
HELIX 41 AE5 LEU C 290 ALA C 294 5 5
HELIX 42 AE6 THR C 296 GLY C 316 1 21
HELIX 43 AE7 GLU D 5 GLY D 19 1 15
HELIX 44 AE8 ALA D 22 LEU D 26 5 5
HELIX 45 AE9 THR D 27 GLN D 39 1 13
HELIX 46 AF1 HIS D 96 ASN D 108 1 13
HELIX 47 AF2 PRO D 125 HIS D 141 1 17
HELIX 48 AF3 HIS D 141 ASN D 146 1 6
HELIX 49 AF4 SEP D 158 GLY D 175 1 18
HELIX 50 AF5 ASN D 195 PHE D 201 1 7
HELIX 51 AF6 THR D 208 LEU D 220 1 13
HELIX 52 AF7 THR D 232 ALA D 236 5 5
HELIX 53 AF8 THR D 237 SER D 242 1 6
HELIX 54 AF9 LEU D 257 ALA D 271 1 15
HELIX 55 AG1 LEU D 290 ALA D 294 5 5
HELIX 56 AG2 THR D 296 GLY D 316 1 21
SHEET 1 AA1 8 VAL A 48 PHE A 55 0
SHEET 2 AA1 8 THR A 63 PRO A 70 -1 O ILE A 67 N THR A 51
SHEET 3 AA1 8 ALA A 110 ASP A 115 -1 O PHE A 113 N ARG A 66
SHEET 4 AA1 8 LEU A 77 PHE A 83 1 N ILE A 80 O VAL A 112
SHEET 5 AA1 8 VAL A 147 ASP A 157 1 O ALA A 153 N VAL A 81
SHEET 6 AA1 8 ALA A 181 PHE A 185 1 O PHE A 185 N GLY A 156
SHEET 7 AA1 8 ALA A 247 ASN A 254 1 O LEU A 248 N LEU A 184
SHEET 8 AA1 8 VAL A 275 ILE A 284 1 O THR A 276 N ALA A 247
SHEET 1 AA216 VAL B 48 PHE B 55 0
SHEET 2 AA216 THR B 63 PRO B 70 -1 O ILE B 67 N THR B 51
SHEET 3 AA216 ALA B 110 ASP B 115 -1 O PHE B 113 N ARG B 66
SHEET 4 AA216 LEU B 77 PHE B 83 1 N ILE B 80 O VAL B 112
SHEET 5 AA216 VAL B 147 ASP B 157 1 O ALA B 153 N VAL B 81
SHEET 6 AA216 ALA B 181 PHE B 185 1 O PHE B 185 N GLY B 156
SHEET 7 AA216 ALA B 247 ASN B 254 1 O LEU B 248 N LEU B 184
SHEET 8 AA216 VAL B 275 ILE B 284 1 O THR B 276 N ALA B 247
SHEET 9 AA216 VAL D 275 ILE D 284 -1 O ARG D 279 N ARG B 279
SHEET 10 AA216 ALA D 247 ASN D 254 1 N VAL D 249 O THR D 276
SHEET 11 AA216 ALA D 181 PHE D 185 1 N LEU D 184 O LEU D 248
SHEET 12 AA216 VAL D 147 ASP D 157 1 N GLY D 156 O PHE D 185
SHEET 13 AA216 LEU D 77 PHE D 83 1 N VAL D 81 O ALA D 153
SHEET 14 AA216 ALA D 110 ASP D 115 1 O VAL D 112 N ILE D 80
SHEET 15 AA216 THR D 63 PRO D 70 -1 N ARG D 66 O PHE D 113
SHEET 16 AA216 VAL D 48 PHE D 55 -1 N THR D 51 O ILE D 67
SHEET 1 AA3 8 VAL C 48 PHE C 55 0
SHEET 2 AA3 8 THR C 63 PRO C 70 -1 O ILE C 67 N THR C 51
SHEET 3 AA3 8 ALA C 110 ASP C 115 -1 O PHE C 113 N ARG C 66
SHEET 4 AA3 8 LEU C 77 PHE C 83 1 N ILE C 80 O VAL C 112
SHEET 5 AA3 8 VAL C 147 ASP C 157 1 O ALA C 153 N VAL C 81
SHEET 6 AA3 8 ALA C 181 PHE C 185 1 O PHE C 185 N GLY C 156
SHEET 7 AA3 8 ALA C 247 ASN C 254 1 O LEU C 248 N LEU C 184
SHEET 8 AA3 8 VAL C 275 ILE C 284 1 O THR C 276 N ALA C 247
LINK C ASP A 157 N SEP A 158 1555 1555 1.34
LINK C SEP A 158 N VAL A 159 1555 1555 1.34
LINK C ASP B 157 N SEP B 158 1555 1555 1.34
LINK C SEP B 158 N VAL B 159 1555 1555 1.33
LINK C ASP C 157 N SEP C 158 1555 1555 1.33
LINK C SEP C 158 N VAL C 159 1555 1555 1.34
LINK C ASP D 157 N SEP D 158 1555 1555 1.34
LINK C SEP D 158 N VAL D 159 1555 1555 1.34
CISPEP 1 SER A 119 PRO A 120 0 1.78
CISPEP 2 TYR A 124 PRO A 125 0 1.16
CISPEP 3 GLY A 176 PRO A 177 0 1.12
CISPEP 4 GLY A 204 PRO A 205 0 6.94
CISPEP 5 GLY B 20 PRO B 21 0 -0.27
CISPEP 6 SER B 119 PRO B 120 0 0.79
CISPEP 7 TYR B 124 PRO B 125 0 3.39
CISPEP 8 GLY B 176 PRO B 177 0 -2.40
CISPEP 9 GLY B 204 PRO B 205 0 10.26
CISPEP 10 GLY C 20 PRO C 21 0 0.71
CISPEP 11 SER C 119 PRO C 120 0 1.95
CISPEP 12 TYR C 124 PRO C 125 0 1.11
CISPEP 13 GLY C 176 PRO C 177 0 -1.71
CISPEP 14 GLY C 204 PRO C 205 0 10.46
CISPEP 15 SER D 119 PRO D 120 0 3.33
CISPEP 16 TYR D 124 PRO D 125 0 2.02
CISPEP 17 GLY D 176 PRO D 177 0 2.80
CISPEP 18 GLY D 204 PRO D 205 0 7.55
CRYST1 161.210 115.768 87.554 90.00 90.06 90.00 C 1 2 1 16
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 0.006203 0.000000 0.000006 0.00000
SCALE2 0.000000 0.008638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011422 0.00000
TER 4748 GLY A 316
TER 9466 GLY B 316
TER 14200 GLY C 316
TER 18980 GLY D 316
MASTER 354 0 21 56 32 0 0 610463 4 306 100
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