HEADER HYDROLASE/HYDROLASE INHIBITOR 17-OCT-13 4N88
TITLE CRYSTAL STRUCTURE OF TSE3-TSI3 COMPLEX WITH CALCIUM ION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 2-402;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: UNP RESIDUES 27-145;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PA3484;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 10 ORGANISM_TAXID: 208964;
SOURCE 11 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 12 GENE: PA3485;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LYSOZYME, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.SHANG
REVDAT 3 08-NOV-23 4N88 1 REMARK SEQADV LINK
REVDAT 2 18-JUN-14 4N88 1 JRNL
REVDAT 1 23-APR-14 4N88 0
JRNL AUTH D.LU,G.SHANG,H.ZHANG,Q.YU,X.CONG,J.YUAN,F.HE,C.ZHU,Y.ZHAO,
JRNL AUTH 2 K.YIN,Y.CHEN,J.HU,X.ZHANG,Z.YUAN,S.XU,W.HU,H.CANG,L.GU
JRNL TITL STRUCTURAL INSIGHTS INTO THE T6SS EFFECTOR PROTEIN TSE3 AND
JRNL TITL 2 THE TSE3-TSI3 COMPLEX FROM PSEUDOMONAS AERUGINOSA REVEAL A
JRNL TITL 3 CALCIUM-DEPENDENT MEMBRANE-BINDING MECHANISM
JRNL REF MOL.MICROBIOL. V. 92 1092 2014
JRNL REFN ISSN 0950-382X
JRNL PMID 24724564
JRNL DOI 10.1111/MMI.12616
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 33266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1681
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 41.3889 - 6.3988 0.99 2904 138 0.1634 0.2082
REMARK 3 2 6.3988 - 5.0819 1.00 2791 149 0.2034 0.2585
REMARK 3 3 5.0819 - 4.4404 0.99 2748 137 0.1741 0.2323
REMARK 3 4 4.4404 - 4.0347 0.99 2721 136 0.1658 0.2339
REMARK 3 5 4.0347 - 3.7458 0.98 2665 145 0.1873 0.2659
REMARK 3 6 3.7458 - 3.5250 0.99 2659 152 0.2193 0.2721
REMARK 3 7 3.5250 - 3.3486 0.97 2639 150 0.2337 0.2877
REMARK 3 8 3.3486 - 3.2029 0.97 2642 137 0.2435 0.3068
REMARK 3 9 3.2029 - 3.0796 0.96 2575 145 0.2517 0.3490
REMARK 3 10 3.0796 - 2.9734 0.94 2519 133 0.2523 0.3824
REMARK 3 11 2.9734 - 2.8804 0.92 2465 146 0.2573 0.3338
REMARK 3 12 2.8804 - 2.7980 0.83 2257 113 0.2625 0.3592
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 22.60
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.420
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) : -1.29560
REMARK 3 B22 (A**2) : 16.82880
REMARK 3 B33 (A**2) : -15.53320
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 8216
REMARK 3 ANGLE : 1.156 11186
REMARK 3 CHIRALITY : 0.074 1236
REMARK 3 PLANARITY : 0.005 1494
REMARK 3 DIHEDRAL : 15.880 3048
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 4N88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34326
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> 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: SOLVE
REMARK 200 STARTING MODEL: 4N7S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.01M CALCIUM
REMARK 280 CHLORIDE,0.05M SODIUM CACODYLATE PH 6.5, 10% PEG4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 44.61800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.38100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.65850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.38100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.61800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.65850
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
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 SER B 23
REMARK 465 HIS B 24
REMARK 465 MET B 25
REMARK 465 SER D 23
REMARK 465 HIS D 24
REMARK 465 MET D 25
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 OH TYR A 236 OD2 ASP A 294 2.11
REMARK 500 O SER C 13 O HOH C 644 2.14
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 ASP A 17 17.23 52.40
REMARK 500 VAL A 38 61.49 -119.60
REMARK 500 THR A 77 -77.96 -135.71
REMARK 500 ASN A 93 31.93 85.11
REMARK 500 GLN A 99 44.00 -74.47
REMARK 500 ASP A 101 -126.14 58.43
REMARK 500 PHE A 127 35.27 -143.44
REMARK 500 THR A 133 39.63 -74.88
REMARK 500 SER A 180 -166.06 -102.73
REMARK 500 LEU A 238 -163.60 -107.96
REMARK 500 ASN A 273 54.50 -102.09
REMARK 500 PRO A 299 -73.67 -42.02
REMARK 500 TRP A 381 29.36 82.68
REMARK 500 ASN B 32 19.40 -64.62
REMARK 500 LEU B 65 -153.75 -77.61
REMARK 500 GLU B 66 124.14 155.88
REMARK 500 TRP B 107 118.31 -160.89
REMARK 500 ARG B 115 -163.63 -115.00
REMARK 500 GLU B 123 139.81 166.73
REMARK 500 ASP B 127 53.36 -107.47
REMARK 500 THR C 77 -89.90 -83.51
REMARK 500 ASN C 93 -74.77 83.08
REMARK 500 GLN C 99 47.84 -79.40
REMARK 500 ASP C 101 -127.95 61.16
REMARK 500 LYS C 171 21.82 80.47
REMARK 500 ASP C 172 101.09 -53.03
REMARK 500 THR C 177 -74.89 -57.33
REMARK 500 LYS C 178 -34.28 -27.54
REMARK 500 LEU C 238 -169.24 -114.95
REMARK 500 ASP C 253 48.79 -83.87
REMARK 500 ASN C 273 50.89 -101.92
REMARK 500 LEU C 401 -71.43 -71.47
REMARK 500 LYS D 58 74.61 -107.31
REMARK 500 GLU D 66 107.83 -164.39
REMARK 500 ASP D 77 109.65 63.04
REMARK 500 ALA D 79 140.66 -28.72
REMARK 500 ARG D 81 142.53 -175.62
REMARK 500 GLU D 123 150.76 169.62
REMARK 500 ASP D 127 45.22 -108.80
REMARK 500 GLU D 129 124.61 -38.16
REMARK 500
REMARK 500 REMARK: NULL
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 18 OD1
REMARK 620 2 ASP A 18 OD2 45.9
REMARK 620 3 GLN A 20 O 75.1 117.3
REMARK 620 4 GLU A 25 OE1 147.4 160.9 81.4
REMARK 620 5 GLU A 25 OE2 153.7 118.5 124.3 42.9
REMARK 620 6 HOH A 639 O 120.4 80.7 125.2 91.7 65.9
REMARK 620 7 HOH A 640 O 70.8 102.4 69.0 79.8 98.0 162.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 181 OD1
REMARK 620 2 ASP A 253 O 82.2
REMARK 620 3 GLN A 254 OE1 151.9 89.1
REMARK 620 4 GLU A 258 OE1 83.2 88.2 69.7
REMARK 620 5 GLU A 258 OE2 88.3 135.7 79.2 47.6
REMARK 620 6 GLN A 280 OE1 134.1 140.4 65.2 108.3 71.2
REMARK 620 7 HOH A 601 O 111.9 66.1 88.5 146.9 153.9 82.8
REMARK 620 8 HOH B 202 O 73.8 128.8 130.3 131.3 88.7 65.3 81.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 258 OE2
REMARK 620 2 ASP A 262 OD1 84.6
REMARK 620 3 ASP A 262 OD2 80.6 48.5
REMARK 620 4 SER A 275 O 143.8 79.6 64.5
REMARK 620 5 SER A 275 OG 135.7 132.8 139.6 75.9
REMARK 620 6 GLN A 280 OE1 84.4 136.5 88.2 85.1 80.6
REMARK 620 7 GLU B 126 OE2 85.6 111.5 156.5 130.6 61.2 109.3
REMARK 620 8 GLU B 126 OE1 95.5 62.4 110.9 105.4 86.2 160.7 51.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 375 OE2
REMARK 620 2 GLU A 375 OE1 46.5
REMARK 620 3 SER A 378 OG 71.9 114.5
REMARK 620 4 ARG A 379 O 85.4 71.0 86.5
REMARK 620 5 ASP A 382 OD1 120.5 75.8 166.4 88.7
REMARK 620 6 ASN A 384 O 82.1 84.4 110.3 154.5 78.7
REMARK 620 7 HOH B 201 O 132.7 163.0 74.9 125.1 97.6 78.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 18 OD1
REMARK 620 2 ASP C 18 OD2 49.4
REMARK 620 3 GLN C 20 O 121.9 73.6
REMARK 620 4 GLU C 25 OE1 144.2 136.1 83.6
REMARK 620 5 GLU C 25 OE2 96.7 124.6 128.6 48.9
REMARK 620 6 HOH C 608 O 84.8 60.4 75.0 77.9 76.5
REMARK 620 7 HOH C 644 O 75.8 85.5 91.3 132.8 133.2 145.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 181 OD1
REMARK 620 2 ASP C 253 O 71.4
REMARK 620 3 GLN C 254 OE1 143.0 85.1
REMARK 620 4 GLU C 258 OE1 81.3 78.2 65.9
REMARK 620 5 GLU C 258 OE2 89.4 123.8 80.3 46.3
REMARK 620 6 GLN C 280 OE1 140.5 146.0 71.6 112.2 77.2
REMARK 620 7 HOH C 602 O 104.5 64.4 89.5 137.0 165.9 90.4
REMARK 620 8 HOH C 645 O 79.5 126.8 137.0 139.9 98.6 66.4 82.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 258 OE2
REMARK 620 2 ASP C 262 OD1 84.5
REMARK 620 3 ASP C 262 OD2 83.6 46.6
REMARK 620 4 SER C 275 O 148.2 75.3 64.7
REMARK 620 5 SER C 275 OG 144.1 127.1 129.4 66.0
REMARK 620 6 GLN C 280 OE1 94.3 137.0 90.4 84.7 74.4
REMARK 620 7 GLU D 126 OE1 84.2 95.6 141.2 121.4 76.7 127.2
REMARK 620 8 GLU D 126 OE2 116.8 63.5 104.8 75.5 72.7 146.3 50.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 375 OE2
REMARK 620 2 GLU C 375 OE1 47.1
REMARK 620 3 SER C 378 OG 80.8 124.5
REMARK 620 4 ARG C 379 O 89.4 65.3 102.6
REMARK 620 5 ASP C 382 OD1 113.4 67.6 164.4 72.3
REMARK 620 6 ASN C 384 O 86.5 87.4 110.5 145.4 78.0
REMARK 620 7 HOH D 211 O 153.7 152.9 82.6 114.2 86.1 80.3
REMARK 620 N 1 2 3 4 5 6
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M5E RELATED DB: PDB
REMARK 900 ITS COMPLEX
REMARK 900 RELATED ID: 4N80 RELATED DB: PDB
REMARK 900 RELATED ID: 4N7S RELATED DB: PDB
REMARK 900 RELATED ID: 4M5F RELATED DB: PDB
DBREF 4N88 A 2 402 UNP Q9HYC5 Q9HYC5_PSEAE 2 402
DBREF 4N88 B 27 145 UNP Q9HYC4 Q9HYC4_PSEAE 27 145
DBREF 4N88 C 2 402 UNP Q9HYC5 Q9HYC5_PSEAE 2 402
DBREF 4N88 D 27 145 UNP Q9HYC4 Q9HYC4_PSEAE 27 145
SEQADV 4N88 SER B 23 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 HIS B 24 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 MET B 25 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 MET B 26 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 SER D 23 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 HIS D 24 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 MET D 25 UNP Q9HYC4 EXPRESSION TAG
SEQADV 4N88 MET D 26 UNP Q9HYC4 EXPRESSION TAG
SEQRES 1 A 401 THR ALA THR SER ASP LEU ILE GLU SER LEU ILE SER TYR
SEQRES 2 A 401 SER TRP ASP ASP TRP GLN VAL THR ARG GLN GLU ALA ARG
SEQRES 3 A 401 ARG VAL ILE ALA ALA ILE ARG ASN ASP ASN VAL PRO ASP
SEQRES 4 A 401 ALA THR ILE ALA ALA LEU ASP LYS SER GLY SER LEU ILE
SEQRES 5 A 401 LYS LEU PHE GLN ARG VAL GLY PRO PRO GLU LEU ALA ARG
SEQRES 6 A 401 SER LEU ILE ALA SER ILE ALA GLY ARG THR THR MET GLN
SEQRES 7 A 401 ARG TYR GLN ALA ARG ASN ALA LEU ILE ARG SER LEU ILE
SEQRES 8 A 401 ASN ASN PRO LEU GLY THR GLN THR ASP ASN TRP ILE TYR
SEQRES 9 A 401 PHE PRO THR ILE THR PHE PHE ASP ILE CYS ALA ASP LEU
SEQRES 10 A 401 ALA ASP ALA ALA GLY ARG LEU GLY PHE ALA ALA ALA GLY
SEQRES 11 A 401 ALA THR GLY VAL ALA SER GLN ALA ILE GLN GLY PRO PHE
SEQRES 12 A 401 SER GLY VAL GLY ALA THR GLY VAL ASN PRO THR ASP LEU
SEQRES 13 A 401 PRO SER ILE ALA PHE GLY ASP GLN LEU LYS LEU LEU ASN
SEQRES 14 A 401 LYS ASP PRO ALA THR VAL THR LYS TYR SER ASN PRO LEU
SEQRES 15 A 401 GLY ASP LEU GLY ALA TYR LEU SER GLN LEU SER PRO GLN
SEQRES 16 A 401 ASP LYS LEU ASN GLN ALA GLN THR LEU VAL GLY GLN PRO
SEQRES 17 A 401 ILE SER THR LEU PHE PRO ASP ALA TYR PRO GLY ASN PRO
SEQRES 18 A 401 PRO SER ARG ALA LYS VAL MET SER ALA ALA ALA ARG LYS
SEQRES 19 A 401 TYR ASP LEU THR PRO GLN LEU ILE GLY ALA ILE ILE LEU
SEQRES 20 A 401 ALA GLU GLN ARG ASP GLN THR ARG ASP GLU ASP ALA LYS
SEQRES 21 A 401 ASP TYR GLN ALA ALA VAL SER ILE LYS SER ALA ASN THR
SEQRES 22 A 401 SER ILE GLY LEU GLY GLN VAL VAL VAL SER THR ALA ILE
SEQRES 23 A 401 LYS TYR GLU LEU PHE THR ASP LEU LEU GLY GLN PRO VAL
SEQRES 24 A 401 ARG ARG GLY LEU SER ARG LYS ALA VAL ALA THR LEU LEU
SEQRES 25 A 401 ALA SER ASP GLU PHE ASN ILE PHE ALA THR ALA ARG TYR
SEQRES 26 A 401 ILE ARG TYR VAL ALA ASN LEU ALA SER GLN GLN ASP LEU
SEQRES 27 A 401 ARG LYS LEU PRO LYS THR ARG GLY ALA PHE PRO SER ILE
SEQRES 28 A 401 ASP LEU ARG ALA TYR ALA GLY ASN PRO ARG ASN TRP PRO
SEQRES 29 A 401 ARG ASP ASN VAL ARG ALA LEU ALA SER GLU TYR THR SER
SEQRES 30 A 401 ARG PRO TRP ASP ASP ASN LEU SER PRO GLY TRP PRO MET
SEQRES 31 A 401 PHE VAL ASP ASP ALA TYR ALA THR PHE LEU ASP
SEQRES 1 B 123 SER HIS MET MET THR LEU THR HIS PRO ASN GLY LEU VAL
SEQRES 2 B 123 VAL GLU ARG PRO VAL GLY PHE ASP ALA ARG ARG SER ALA
SEQRES 3 B 123 GLU GLY PHE ARG PHE ASP GLU GLY GLY LYS LEU ARG ASN
SEQRES 4 B 123 PRO ARG GLN LEU GLU VAL GLN ARG GLN ASP ALA PRO PRO
SEQRES 5 B 123 PRO PRO ASP LEU ALA SER ARG ARG LEU GLY ASP GLY GLU
SEQRES 6 B 123 ALA ARG TYR LYS VAL GLU GLU ASP ASP GLY GLY SER ALA
SEQRES 7 B 123 GLY SER GLU TYR ARG LEU TRP ALA ALA LYS PRO ALA GLY
SEQRES 8 B 123 ALA ARG TRP ILE VAL VAL SER ALA SER GLU GLN SER GLU
SEQRES 9 B 123 ASP GLY GLU PRO THR PHE ALA LEU ALA TRP ALA LEU LEU
SEQRES 10 B 123 GLU ARG ALA ARG LEU GLN
SEQRES 1 C 401 THR ALA THR SER ASP LEU ILE GLU SER LEU ILE SER TYR
SEQRES 2 C 401 SER TRP ASP ASP TRP GLN VAL THR ARG GLN GLU ALA ARG
SEQRES 3 C 401 ARG VAL ILE ALA ALA ILE ARG ASN ASP ASN VAL PRO ASP
SEQRES 4 C 401 ALA THR ILE ALA ALA LEU ASP LYS SER GLY SER LEU ILE
SEQRES 5 C 401 LYS LEU PHE GLN ARG VAL GLY PRO PRO GLU LEU ALA ARG
SEQRES 6 C 401 SER LEU ILE ALA SER ILE ALA GLY ARG THR THR MET GLN
SEQRES 7 C 401 ARG TYR GLN ALA ARG ASN ALA LEU ILE ARG SER LEU ILE
SEQRES 8 C 401 ASN ASN PRO LEU GLY THR GLN THR ASP ASN TRP ILE TYR
SEQRES 9 C 401 PHE PRO THR ILE THR PHE PHE ASP ILE CYS ALA ASP LEU
SEQRES 10 C 401 ALA ASP ALA ALA GLY ARG LEU GLY PHE ALA ALA ALA GLY
SEQRES 11 C 401 ALA THR GLY VAL ALA SER GLN ALA ILE GLN GLY PRO PHE
SEQRES 12 C 401 SER GLY VAL GLY ALA THR GLY VAL ASN PRO THR ASP LEU
SEQRES 13 C 401 PRO SER ILE ALA PHE GLY ASP GLN LEU LYS LEU LEU ASN
SEQRES 14 C 401 LYS ASP PRO ALA THR VAL THR LYS TYR SER ASN PRO LEU
SEQRES 15 C 401 GLY ASP LEU GLY ALA TYR LEU SER GLN LEU SER PRO GLN
SEQRES 16 C 401 ASP LYS LEU ASN GLN ALA GLN THR LEU VAL GLY GLN PRO
SEQRES 17 C 401 ILE SER THR LEU PHE PRO ASP ALA TYR PRO GLY ASN PRO
SEQRES 18 C 401 PRO SER ARG ALA LYS VAL MET SER ALA ALA ALA ARG LYS
SEQRES 19 C 401 TYR ASP LEU THR PRO GLN LEU ILE GLY ALA ILE ILE LEU
SEQRES 20 C 401 ALA GLU GLN ARG ASP GLN THR ARG ASP GLU ASP ALA LYS
SEQRES 21 C 401 ASP TYR GLN ALA ALA VAL SER ILE LYS SER ALA ASN THR
SEQRES 22 C 401 SER ILE GLY LEU GLY GLN VAL VAL VAL SER THR ALA ILE
SEQRES 23 C 401 LYS TYR GLU LEU PHE THR ASP LEU LEU GLY GLN PRO VAL
SEQRES 24 C 401 ARG ARG GLY LEU SER ARG LYS ALA VAL ALA THR LEU LEU
SEQRES 25 C 401 ALA SER ASP GLU PHE ASN ILE PHE ALA THR ALA ARG TYR
SEQRES 26 C 401 ILE ARG TYR VAL ALA ASN LEU ALA SER GLN GLN ASP LEU
SEQRES 27 C 401 ARG LYS LEU PRO LYS THR ARG GLY ALA PHE PRO SER ILE
SEQRES 28 C 401 ASP LEU ARG ALA TYR ALA GLY ASN PRO ARG ASN TRP PRO
SEQRES 29 C 401 ARG ASP ASN VAL ARG ALA LEU ALA SER GLU TYR THR SER
SEQRES 30 C 401 ARG PRO TRP ASP ASP ASN LEU SER PRO GLY TRP PRO MET
SEQRES 31 C 401 PHE VAL ASP ASP ALA TYR ALA THR PHE LEU ASP
SEQRES 1 D 123 SER HIS MET MET THR LEU THR HIS PRO ASN GLY LEU VAL
SEQRES 2 D 123 VAL GLU ARG PRO VAL GLY PHE ASP ALA ARG ARG SER ALA
SEQRES 3 D 123 GLU GLY PHE ARG PHE ASP GLU GLY GLY LYS LEU ARG ASN
SEQRES 4 D 123 PRO ARG GLN LEU GLU VAL GLN ARG GLN ASP ALA PRO PRO
SEQRES 5 D 123 PRO PRO ASP LEU ALA SER ARG ARG LEU GLY ASP GLY GLU
SEQRES 6 D 123 ALA ARG TYR LYS VAL GLU GLU ASP ASP GLY GLY SER ALA
SEQRES 7 D 123 GLY SER GLU TYR ARG LEU TRP ALA ALA LYS PRO ALA GLY
SEQRES 8 D 123 ALA ARG TRP ILE VAL VAL SER ALA SER GLU GLN SER GLU
SEQRES 9 D 123 ASP GLY GLU PRO THR PHE ALA LEU ALA TRP ALA LEU LEU
SEQRES 10 D 123 GLU ARG ALA ARG LEU GLN
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET CA C 501 1
HET CA C 502 1
HET CA C 503 1
HET CA C 504 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 8(CA 2+)
FORMUL 13 HOH *99(H2 O)
HELIX 1 1 THR A 2 SER A 13 1 12
HELIX 2 2 THR A 22 ASN A 35 1 14
HELIX 3 3 VAL A 38 LYS A 48 1 11
HELIX 4 4 GLY A 50 VAL A 59 1 10
HELIX 5 5 PRO A 61 GLY A 74 1 14
HELIX 6 6 GLN A 79 LEU A 91 1 13
HELIX 7 7 THR A 100 ILE A 104 5 5
HELIX 8 8 PRO A 107 LEU A 125 1 19
HELIX 9 9 GLY A 146 GLY A 151 1 6
HELIX 10 10 ASN A 153 LEU A 157 5 5
HELIX 11 11 ALA A 161 ASN A 170 1 10
HELIX 12 12 ASP A 172 SER A 180 1 9
HELIX 13 13 ASP A 185 GLN A 192 1 8
HELIX 14 14 SER A 194 GLN A 208 1 15
HELIX 15 15 PHE A 214 TYR A 218 5 5
HELIX 16 16 SER A 224 ASP A 237 1 14
HELIX 17 17 THR A 239 ASP A 253 1 15
HELIX 18 18 THR A 255 ALA A 265 1 11
HELIX 19 19 VAL A 283 TYR A 289 1 7
HELIX 20 20 GLY A 297 LEU A 304 1 8
HELIX 21 21 SER A 305 LEU A 313 1 9
HELIX 22 22 SER A 315 GLN A 336 1 22
HELIX 23 23 ASP A 338 LYS A 341 5 4
HELIX 24 24 LEU A 342 PHE A 349 1 8
HELIX 25 25 LEU A 354 GLY A 359 5 6
HELIX 26 26 ASN A 360 TRP A 364 5 5
HELIX 27 27 PRO A 365 SER A 378 1 14
HELIX 28 28 GLY A 388 ASP A 402 1 15
HELIX 29 29 PHE B 132 ARG B 141 1 10
HELIX 30 30 ALA C 3 SER C 13 1 11
HELIX 31 31 THR C 22 ASN C 35 1 14
HELIX 32 32 VAL C 38 SER C 49 1 12
HELIX 33 33 GLY C 50 VAL C 59 1 10
HELIX 34 34 PRO C 61 THR C 76 1 16
HELIX 35 35 GLN C 79 SER C 90 1 12
HELIX 36 36 THR C 100 ILE C 104 5 5
HELIX 37 37 PRO C 107 LEU C 125 1 19
HELIX 38 38 GLY C 146 GLY C 151 1 6
HELIX 39 39 ASN C 153 LEU C 157 5 5
HELIX 40 40 ALA C 161 LYS C 171 1 11
HELIX 41 41 ASP C 172 SER C 180 1 9
HELIX 42 42 ASP C 185 LEU C 193 1 9
HELIX 43 43 SER C 194 GLN C 208 1 15
HELIX 44 44 PHE C 214 TYR C 218 5 5
HELIX 45 45 SER C 224 ASP C 237 1 14
HELIX 46 46 THR C 239 ASP C 253 1 15
HELIX 47 47 THR C 255 SER C 268 1 14
HELIX 48 48 VAL C 283 TYR C 289 1 7
HELIX 49 49 GLY C 297 LEU C 304 1 8
HELIX 50 50 SER C 305 LEU C 313 1 9
HELIX 51 51 SER C 315 GLN C 336 1 22
HELIX 52 52 ASP C 338 LYS C 341 5 4
HELIX 53 53 LEU C 342 PHE C 349 1 8
HELIX 54 54 ARG C 355 GLY C 359 5 5
HELIX 55 55 ASN C 360 TRP C 364 5 5
HELIX 56 56 PRO C 365 SER C 378 1 14
HELIX 57 57 GLY C 388 ASP C 402 1 15
HELIX 58 58 PHE D 132 ARG D 141 1 10
SHEET 1 A 2 SER A 275 ILE A 276 0
SHEET 2 A 2 VAL A 281 VAL A 282 -1 O VAL A 281 N ILE A 276
SHEET 1 B 2 LEU B 34 VAL B 35 0
SHEET 2 B 2 ARG B 143 LEU B 144 -1 O ARG B 143 N VAL B 35
SHEET 1 C 7 PHE B 42 SER B 47 0
SHEET 2 C 7 GLY B 50 GLU B 55 -1 O ASP B 54 N ASP B 43
SHEET 3 C 7 VAL B 67 GLN B 70 -1 O VAL B 67 N PHE B 51
SHEET 4 C 7 ARG B 115 ALA B 121 -1 O TRP B 116 N GLN B 70
SHEET 5 C 7 GLY B 101 ALA B 112 -1 N LEU B 106 O ALA B 121
SHEET 6 C 7 ALA B 88 GLY B 98 -1 N LYS B 91 O TRP B 107
SHEET 7 C 7 ALA B 79 ARG B 81 -1 N ALA B 79 O TYR B 90
SHEET 1 D 6 PHE B 42 SER B 47 0
SHEET 2 D 6 GLY B 50 GLU B 55 -1 O ASP B 54 N ASP B 43
SHEET 3 D 6 VAL B 67 GLN B 70 -1 O VAL B 67 N PHE B 51
SHEET 4 D 6 ARG B 115 ALA B 121 -1 O TRP B 116 N GLN B 70
SHEET 5 D 6 GLY B 101 ALA B 112 -1 N LEU B 106 O ALA B 121
SHEET 6 D 6 GLN B 124 SER B 125 -1 O SER B 125 N SER B 102
SHEET 1 E 2 SER C 275 ILE C 276 0
SHEET 2 E 2 VAL C 281 VAL C 282 -1 O VAL C 281 N ILE C 276
SHEET 1 F 2 LEU D 28 THR D 29 0
SHEET 2 F 2 VAL D 35 VAL D 36 -1 O VAL D 36 N LEU D 28
SHEET 1 G 6 PHE D 42 ARG D 46 0
SHEET 2 G 6 PHE D 51 GLU D 55 -1 O ASP D 54 N ASP D 43
SHEET 3 G 6 GLN D 64 GLN D 70 -1 O VAL D 67 N PHE D 51
SHEET 4 G 6 ARG D 115 SER D 125 -1 O VAL D 118 N GLN D 68
SHEET 5 G 6 GLY D 101 ALA D 112 -1 N ALA D 108 O VAL D 119
SHEET 6 G 6 ARG D 89 GLY D 98 -1 N ARG D 89 O ALA D 109
LINK OD1 ASP A 18 CA CA A 501 1555 1555 2.78
LINK OD2 ASP A 18 CA CA A 501 1555 1555 2.88
LINK O GLN A 20 CA CA A 501 1555 1555 2.60
LINK OE1 GLU A 25 CA CA A 501 1555 1555 2.81
LINK OE2 GLU A 25 CA CA A 501 1555 1555 3.15
LINK OD1 ASN A 181 CA CA A 504 1555 1555 2.38
LINK O ASP A 253 CA CA A 504 1555 1555 2.51
LINK OE1 GLN A 254 CA CA A 504 1555 1555 2.36
LINK OE2 GLU A 258 CA CA A 503 1555 1555 2.53
LINK OE1 GLU A 258 CA CA A 504 1555 1555 2.60
LINK OE2 GLU A 258 CA CA A 504 1555 1555 2.86
LINK OD1 ASP A 262 CA CA A 503 1555 1555 2.60
LINK OD2 ASP A 262 CA CA A 503 1555 1555 2.72
LINK O SER A 275 CA CA A 503 1555 1555 2.56
LINK OG SER A 275 CA CA A 503 1555 1555 2.87
LINK OE1 GLN A 280 CA CA A 503 1555 1555 2.55
LINK OE1 GLN A 280 CA CA A 504 1555 1555 2.99
LINK OE2 GLU A 375 CA CA A 502 1555 1555 2.61
LINK OE1 GLU A 375 CA CA A 502 1555 1555 2.87
LINK OG SER A 378 CA CA A 502 1555 1555 2.65
LINK O ARG A 379 CA CA A 502 1555 1555 2.51
LINK OD1 ASP A 382 CA CA A 502 1555 1555 2.57
LINK O ASN A 384 CA CA A 502 1555 1555 2.49
LINK CA CA A 501 O HOH A 639 1555 1555 2.70
LINK CA CA A 501 O HOH A 640 1555 1555 2.94
LINK CA CA A 502 O HOH B 201 1555 1555 3.12
LINK CA CA A 503 OE2 GLU B 126 1555 1555 2.43
LINK CA CA A 503 OE1 GLU B 126 1555 1555 2.64
LINK CA CA A 504 O HOH A 601 1555 1555 2.72
LINK CA CA A 504 O HOH B 202 1555 1555 2.92
LINK OD1 ASP C 18 CA CA C 501 1555 1555 2.65
LINK OD2 ASP C 18 CA CA C 501 1555 1555 2.67
LINK O GLN C 20 CA CA C 501 1555 1555 2.75
LINK OE1 GLU C 25 CA CA C 501 1555 1555 2.65
LINK OE2 GLU C 25 CA CA C 501 1555 1555 2.69
LINK OD1 ASN C 181 CA CA C 504 1555 1555 2.37
LINK O ASP C 253 CA CA C 504 1555 1555 2.60
LINK OE1 GLN C 254 CA CA C 504 1555 1555 2.33
LINK OE2 GLU C 258 CA CA C 503 1555 1555 2.51
LINK OE1 GLU C 258 CA CA C 504 1555 1555 2.70
LINK OE2 GLU C 258 CA CA C 504 1555 1555 2.85
LINK OD1 ASP C 262 CA CA C 503 1555 1555 2.66
LINK OD2 ASP C 262 CA CA C 503 1555 1555 2.86
LINK O SER C 275 CA CA C 503 1555 1555 2.68
LINK OG SER C 275 CA CA C 503 1555 1555 2.77
LINK OE1 GLN C 280 CA CA C 503 1555 1555 2.44
LINK OE1 GLN C 280 CA CA C 504 1555 1555 2.97
LINK OE2 GLU C 375 CA CA C 502 1555 1555 2.65
LINK OE1 GLU C 375 CA CA C 502 1555 1555 2.80
LINK OG SER C 378 CA CA C 502 1555 1555 2.53
LINK O ARG C 379 CA CA C 502 1555 1555 2.54
LINK OD1 ASP C 382 CA CA C 502 1555 1555 2.59
LINK O ASN C 384 CA CA C 502 1555 1555 2.37
LINK CA CA C 501 O HOH C 608 1555 1555 2.73
LINK CA CA C 501 O HOH C 644 1555 1555 2.71
LINK CA CA C 502 O HOH D 211 1555 1555 3.06
LINK CA CA C 503 OE1 GLU D 126 1555 1555 2.58
LINK CA CA C 503 OE2 GLU D 126 1555 1555 2.64
LINK CA CA C 504 O HOH C 602 1555 1555 2.72
LINK CA CA C 504 O HOH C 645 1555 1555 2.63
SITE 1 AC1 5 ASP A 18 GLN A 20 GLU A 25 HOH A 639
SITE 2 AC1 5 HOH A 640
SITE 1 AC2 5 GLU A 375 SER A 378 ARG A 379 ASP A 382
SITE 2 AC2 5 ASN A 384
SITE 1 AC3 5 GLU A 258 ASP A 262 SER A 275 GLN A 280
SITE 2 AC3 5 GLU B 126
SITE 1 AC4 7 ASN A 181 ASP A 253 GLN A 254 GLU A 258
SITE 2 AC4 7 GLN A 280 HOH A 601 HOH B 202
SITE 1 AC5 5 ASP C 18 GLN C 20 GLU C 25 HOH C 608
SITE 2 AC5 5 HOH C 644
SITE 1 AC6 6 GLU C 375 SER C 378 ARG C 379 ASP C 382
SITE 2 AC6 6 ASN C 384 HOH D 211
SITE 1 AC7 5 GLU C 258 ASP C 262 SER C 275 GLN C 280
SITE 2 AC7 5 GLU D 126
SITE 1 AC8 7 ASN C 181 ASP C 253 GLN C 254 GLU C 258
SITE 2 AC8 7 GLN C 280 HOH C 602 HOH C 645
CRYST1 89.236 95.317 160.762 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 0.011206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
