| content |
HEADER HYDROLASE 05-OCT-23 8UGM
TITLE FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES E, BORONIC ACID-BASED COMPOUND Z27 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE E;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-0114;
SOURCE 3 ORGANISM_TAXID: 1385527;
SOURCE 4 GENE: SAUSA300_2518;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FPHE, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, BORONIC ACID, COVALENT, BORON-SERINE,
KEYWDS 3 BORON-HISTIDINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 16-OCT-24 8UGM 0
JRNL AUTH M.FELLNER
JRNL TITL FPHE, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES E, BORONIC ACID-BASED COMPOUND Z27 BOUND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 59652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3011
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 39.8200 - 4.6100 1.00 2634 166 0.1551 0.1761
REMARK 3 2 4.6100 - 3.6600 1.00 2618 142 0.1171 0.1525
REMARK 3 3 3.6600 - 3.2000 1.00 2676 99 0.1399 0.2020
REMARK 3 4 3.2000 - 2.9100 1.00 2578 140 0.1553 0.1716
REMARK 3 5 2.9100 - 2.7000 1.00 2617 148 0.1538 0.2087
REMARK 3 6 2.7000 - 2.5400 1.00 2599 131 0.1492 0.1989
REMARK 3 7 2.5400 - 2.4100 1.00 2609 136 0.1423 0.1668
REMARK 3 8 2.4100 - 2.3100 1.00 2585 132 0.1359 0.1805
REMARK 3 9 2.3100 - 2.2200 1.00 2579 148 0.1437 0.1849
REMARK 3 10 2.2200 - 2.1400 1.00 2577 149 0.1479 0.1975
REMARK 3 11 2.1400 - 2.0800 1.00 2624 132 0.1517 0.2001
REMARK 3 12 2.0800 - 2.0200 1.00 2598 120 0.1569 0.2123
REMARK 3 13 2.0200 - 1.9600 1.00 2563 157 0.1557 0.1997
REMARK 3 14 1.9600 - 1.9200 1.00 2595 149 0.1552 0.2068
REMARK 3 15 1.9100 - 1.8700 1.00 2557 149 0.1613 0.2066
REMARK 3 16 1.8700 - 1.8300 1.00 2632 107 0.1632 0.2178
REMARK 3 17 1.8300 - 1.8000 1.00 2549 142 0.1800 0.2350
REMARK 3 18 1.8000 - 1.7600 1.00 2628 141 0.1800 0.2333
REMARK 3 19 1.7600 - 1.7300 1.00 2527 165 0.1783 0.2029
REMARK 3 20 1.7300 - 1.7000 1.00 2634 122 0.1917 0.2458
REMARK 3 21 1.7000 - 1.6700 0.96 2492 120 0.2022 0.2492
REMARK 3 22 1.6700 - 1.6500 0.84 2170 116 0.2317 0.3019
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.430
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 : 0.010 4609
REMARK 3 ANGLE : 1.128 6271
REMARK 3 CHIRALITY : 0.059 675
REMARK 3 PLANARITY : 0.012 827
REMARK 3 DIHEDRAL : 6.426 611
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3377 -6.7123 9.6660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.0992
REMARK 3 T33: 0.1327 T12: 0.0094
REMARK 3 T13: 0.0169 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.9113 L22: 1.0519
REMARK 3 L33: 1.4142 L12: 0.1264
REMARK 3 L13: -0.0963 L23: -0.1166
REMARK 3 S TENSOR
REMARK 3 S11: 0.0662 S12: 0.0264 S13: 0.0997
REMARK 3 S21: -0.0226 S22: -0.0169 S23: -0.0214
REMARK 3 S31: -0.2083 S32: -0.0024 S33: -0.0481
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5992 -26.7166 -6.3223
REMARK 3 T TENSOR
REMARK 3 T11: 0.2578 T22: 0.1730
REMARK 3 T33: 0.2341 T12: -0.0033
REMARK 3 T13: -0.0130 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.3941 L22: 0.1726
REMARK 3 L33: 3.3686 L12: -0.8184
REMARK 3 L13: 3.4285 L23: -0.8232
REMARK 3 S TENSOR
REMARK 3 S11: 0.1619 S12: 0.1344 S13: 0.0435
REMARK 3 S21: -0.0365 S22: -0.1009 S23: -0.0249
REMARK 3 S31: 0.1465 S32: 0.1254 S33: -0.1136
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5633 -13.3852 -24.3035
REMARK 3 T TENSOR
REMARK 3 T11: 0.0891 T22: 0.0986
REMARK 3 T33: 0.1308 T12: 0.0026
REMARK 3 T13: 0.0115 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.1312 L22: 1.3609
REMARK 3 L33: 2.3295 L12: 0.1796
REMARK 3 L13: 0.1657 L23: 0.6943
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0154 S13: -0.0168
REMARK 3 S21: -0.0230 S22: 0.0325 S23: -0.0400
REMARK 3 S31: 0.0747 S32: 0.0928 S33: 0.0078
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1245 -7.0405 -23.8243
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.1512
REMARK 3 T33: 0.1383 T12: -0.0196
REMARK 3 T13: -0.0041 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.6387 L22: 1.0564
REMARK 3 L33: 1.7829 L12: 0.0698
REMARK 3 L13: -0.0730 L23: 0.2654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: 0.0187 S13: 0.0802
REMARK 3 S21: -0.0128 S22: 0.0865 S23: -0.1169
REMARK 3 S31: -0.0865 S32: 0.3426 S33: -0.0252
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2407 -16.0591 16.2666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.1216
REMARK 3 T33: 0.1327 T12: -0.0080
REMARK 3 T13: 0.0090 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.9374 L22: 1.3764
REMARK 3 L33: 2.1667 L12: 0.0836
REMARK 3 L13: 0.3560 L23: -0.0096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0958 S12: -0.0847 S13: 0.0209
REMARK 3 S21: 0.0675 S22: -0.0300 S23: 0.0950
REMARK 3 S31: 0.0268 S32: -0.2611 S33: -0.0682
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 8UGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1000278047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-22
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220220
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59687
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 46.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.94400
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 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20UL 25.0 MG/ML FPHE (10MM HEPES PH
REMARK 280 7.5, 100MM NACL) WERE MIXED WITH 3UL Z27 (50MM IN DMSO) AND
REMARK 280 INCUBATED AT 4C OVERNIGHT. 0.3 UL FPHE-Z27 SOLUTION WAS MIXED
REMARK 280 WITH 0.15 UL OF RESERVOIR SOLUTION. SITTING DROP RESERVOIR
REMARK 280 CONTAINED 25 UL OF 180MM CALCIUM ACETATE, 100MM MES PH 6.5, 22.5%
REMARK 280 PEG 2000 MME. CRYSTAL APPEARED WITHIN 2.5 DAYS AT 16C AND GREW
REMARK 280 UNTIL 14.5 DAYS WHEN IT WAS FROZEN IN A SOLUTION OF ~25%
REMARK 280 GLYCEROL, 75% RESERVOIR., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 36.98550
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 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 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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 574 O HOH B 590 1.88
REMARK 500 O HOH B 405 O HOH B 487 1.89
REMARK 500 O HOH A 491 O HOH A 527 1.89
REMARK 500 O HOH A 417 O HOH A 611 1.93
REMARK 500 O HOH B 413 O HOH B 535 1.98
REMARK 500 O HOH A 407 O HOH B 424 2.03
REMARK 500 OG SER A 103 O1 WKK A 301 2.18
REMARK 500 OE2 GLU B 154 O HOH B 401 2.18
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 408 O HOH A 526 2455 1.98
REMARK 500 O HOH A 551 O HOH A 601 2445 2.04
REMARK 500 O HOH A 556 O HOH B 484 1655 2.12
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 SER A 103 -123.96 52.67
REMARK 500 SER B 103 -125.76 59.06
REMARK 500 GLU B 201 -50.83 -124.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 80 0.08 SIDE CHAIN
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 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 15 O
REMARK 620 2 ASN A 168 OD1 88.4
REMARK 620 3 HOH A 476 O 157.6 80.8
REMARK 620 4 HOH A 533 O 79.7 23.1 82.8
REMARK 620 5 HOH A 537 O 92.4 52.7 96.4 74.8
REMARK 620 6 HOH A 551 O 85.6 152.9 95.2 130.0 153.8
REMARK 620 7 HOH A 601 O 87.1 103.0 76.5 81.2 155.7 50.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 83 OE1
REMARK 620 2 TYR A 116 OH 72.1
REMARK 620 3 HOH A 494 O 71.1 133.3
REMARK 620 4 HOH A 498 O 114.4 83.0 86.9
REMARK 620 5 HOH B 411 O 133.3 151.5 74.4 94.0
REMARK 620 6 HOH B 457 O 142.7 76.0 146.1 79.8 75.5
REMARK 620 7 HOH B 485 O 78.8 95.1 104.8 165.0 80.6 85.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 114 O
REMARK 620 2 HOH A 587 O 80.7
REMARK 620 3 HOH A 603 O 85.4 57.5
REMARK 620 4 HOH A 614 O 100.5 127.8 172.5
REMARK 620 5 HOH B 418 O 140.5 127.0 88.3 84.1
REMARK 620 6 HOH B 488 O 68.2 145.9 104.8 73.5 75.9
REMARK 620 7 HOH B 582 O 140.9 61.7 83.3 94.7 76.4 150.8
REMARK 620 N 1 2 3 4 5 6
DBREF 8UGM A 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
DBREF 8UGM B 1 276 UNP Q2FDS6 Y2518_STAA3 1 276
SEQADV 8UGM GLY A -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8UGM PRO A -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8UGM GLY A 0 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8UGM GLY B -2 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8UGM PRO B -1 UNP Q2FDS6 EXPRESSION TAG
SEQADV 8UGM GLY B 0 UNP Q2FDS6 EXPRESSION TAG
SEQRES 1 A 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 A 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 A 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 A 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 A 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 A 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 A 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 A 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 A 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 A 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 A 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 A 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 A 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 A 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 A 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 A 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 A 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 A 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 A 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 A 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 A 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 A 279 LEU LEU ASN MET TRP GLY
SEQRES 1 B 279 GLY PRO GLY MET GLU THR LEU GLU LEU GLN GLY ALA LYS
SEQRES 2 B 279 LEU ARG TYR HIS GLN VAL GLY GLN GLY PRO VAL LEU ILE
SEQRES 3 B 279 PHE ILE PRO GLY ALA ASN GLY THR GLY ASP ILE PHE LEU
SEQRES 4 B 279 PRO LEU ALA GLU GLN LEU LYS ASP HIS PHE THR VAL VAL
SEQRES 5 B 279 ALA VAL ASP ARG ARG ASP TYR GLY GLU SER GLU LEU THR
SEQRES 6 B 279 GLU PRO LEU PRO ASP SER ALA SER ASN PRO ASP SER ASP
SEQRES 7 B 279 TYR ARG VAL LYS ARG ASP ALA GLN ASP ILE ALA GLU LEU
SEQRES 8 B 279 ALA LYS SER LEU SER ASP GLU PRO VAL TYR ILE LEU GLY
SEQRES 9 B 279 SER SER SER GLY SER ILE VAL ALA MET HIS VAL LEU LYS
SEQRES 10 B 279 ASP TYR PRO GLU VAL VAL LYS LYS ILE ALA PHE HIS GLU
SEQRES 11 B 279 PRO PRO ILE ASN THR PHE LEU PRO ASP SER THR TYR TRP
SEQRES 12 B 279 LYS ASP LYS ASN ASP ASP ILE VAL HIS GLN ILE LEU THR
SEQRES 13 B 279 GLU GLY LEU GLU LYS GLY MET LYS THR PHE GLY GLU THR
SEQRES 14 B 279 LEU ASN ILE ALA PRO ILE ASP ALA LYS MET MET SER GLN
SEQRES 15 B 279 PRO ALA ASP THR GLU GLU GLY ARG ILE GLU GLN TYR LYS
SEQRES 16 B 279 ARG THR MET PHE TRP LEU GLU PHE GLU ILE ARG GLN TYR
SEQRES 17 B 279 THR HIS SER ASN ILE THR LEU ASP ASP PHE THR LYS TYR
SEQRES 18 B 279 SER ASP LYS ILE THR LEU LEU ASN GLY THR ASP SER ARG
SEQRES 19 B 279 GLY SER PHE PRO GLN ASP VAL ASN PHE TYR ILE ASN LYS
SEQRES 20 B 279 GLU THR GLY ILE PRO ILE VAL ASP ILE PRO GLY GLY HIS
SEQRES 21 B 279 LEU GLY TYR ILE GLN LYS PRO GLU GLY PHE ALA ASP VAL
SEQRES 22 B 279 LEU LEU ASN MET TRP GLY
HET WKK A 301 17
HET WKK A 302 19
HET CA A 303 1
HET CA A 304 1
HET CA A 305 1
HET WKK B 301 19
HET WKK B 302 17
HETNAM WKK 1-BENZOTHIOPHEN-3-YLBORONIC ACID
HETNAM CA CALCIUM ION
FORMUL 3 WKK 4(C8 H7 B O2 S)
FORMUL 5 CA 3(CA 2+)
FORMUL 10 HOH *483(H2 O)
HELIX 1 AA1 THR A 31 ILE A 34 5 4
HELIX 2 AA2 PHE A 35 LYS A 43 1 9
HELIX 3 AA3 PRO A 66 ASN A 71 5 6
HELIX 4 AA4 ASP A 75 SER A 93 1 19
HELIX 5 AA5 SER A 103 TYR A 116 1 14
HELIX 6 AA6 ASP A 136 THR A 153 1 18
HELIX 7 AA7 THR A 153 LEU A 167 1 15
HELIX 8 AA8 ALA A 170 GLN A 179 1 10
HELIX 9 AA9 THR A 183 GLU A 201 1 19
HELIX 10 AB1 GLU A 201 HIS A 207 1 7
HELIX 11 AB2 THR A 211 TYR A 218 1 8
HELIX 12 AB3 SER A 233 GLY A 247 1 15
HELIX 13 AB4 LEU A 258 LYS A 263 1 6
HELIX 14 AB5 LYS A 263 GLY A 276 1 14
HELIX 15 AB6 THR B 31 ILE B 34 5 4
HELIX 16 AB7 PHE B 35 LYS B 43 1 9
HELIX 17 AB8 PRO B 66 ASN B 71 5 6
HELIX 18 AB9 ASP B 75 SER B 93 1 19
HELIX 19 AC1 SER B 103 TYR B 116 1 14
HELIX 20 AC2 ASP B 136 THR B 153 1 18
HELIX 21 AC3 THR B 153 LEU B 167 1 15
HELIX 22 AC4 ALA B 170 GLN B 179 1 10
HELIX 23 AC5 THR B 183 GLU B 201 1 19
HELIX 24 AC6 GLU B 201 HIS B 207 1 7
HELIX 25 AC7 THR B 211 LYS B 217 1 7
HELIX 26 AC8 TYR B 218 ASP B 220 5 3
HELIX 27 AC9 SER B 233 GLY B 247 1 15
HELIX 28 AD1 LEU B 258 LYS B 263 1 6
HELIX 29 AD2 LYS B 263 GLY B 276 1 14
SHEET 1 AA1 3 GLU A 2 LEU A 6 0
SHEET 2 AA1 3 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA1 3 GLU A 60 LEU A 61 -1 O GLU A 60 N LYS A 10
SHEET 1 AA2 8 GLU A 2 LEU A 6 0
SHEET 2 AA2 8 ALA A 9 GLY A 17 -1 O LEU A 11 N LEU A 4
SHEET 3 AA2 8 THR A 47 ASP A 52 -1 O ALA A 50 N HIS A 14
SHEET 4 AA2 8 VAL A 21 ILE A 25 1 N PHE A 24 O VAL A 49
SHEET 5 AA2 8 VAL A 97 SER A 102 1 O TYR A 98 N ILE A 23
SHEET 6 AA2 8 VAL A 120 HIS A 126 1 O LYS A 121 N VAL A 97
SHEET 7 AA2 8 ILE B 222 GLY B 227 1 O THR B 223 N PHE A 125
SHEET 8 AA2 8 ILE B 250 ILE B 253 1 O VAL B 251 N LEU B 224
SHEET 1 AA3 8 ILE A 250 ILE A 253 0
SHEET 2 AA3 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA3 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA3 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA3 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA3 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA3 8 ALA B 9 GLY B 17 -1 N HIS B 14 O ALA B 50
SHEET 8 AA3 8 GLU B 2 LEU B 6 -1 N GLU B 2 O TYR B 13
SHEET 1 AA4 8 ILE A 250 ILE A 253 0
SHEET 2 AA4 8 ILE A 222 GLY A 227 1 N LEU A 224 O VAL A 251
SHEET 3 AA4 8 VAL B 120 HIS B 126 1 O PHE B 125 N LEU A 225
SHEET 4 AA4 8 VAL B 97 SER B 102 1 N VAL B 97 O LYS B 121
SHEET 5 AA4 8 VAL B 21 ILE B 25 1 N ILE B 23 O TYR B 98
SHEET 6 AA4 8 THR B 47 ASP B 52 1 O VAL B 49 N PHE B 24
SHEET 7 AA4 8 ALA B 9 GLY B 17 -1 N HIS B 14 O ALA B 50
SHEET 8 AA4 8 GLU B 60 LEU B 61 -1 O GLU B 60 N LYS B 10
LINK OG SER A 103 B1 WKK A 301 1555 1555 1.41
LINK NE2 HIS A 257 B1 WKK B 302 1555 1555 1.46
LINK B1 WKK A 301 NE2 HIS B 257 1555 1555 1.45
LINK OG SER B 103 B1 WKK B 302 1555 1555 1.41
LINK O GLN A 15 CA CA A 303 1555 1555 2.23
LINK OE1 GLN A 83 CA CA A 304 1555 1555 2.35
LINK O LYS A 114 CA CA A 305 1555 1555 2.34
LINK OH TYR A 116 CA CA A 304 1555 1555 2.56
LINK OD1 ASN A 168 CA CA A 303 1555 2445 2.28
LINK CA CA A 303 O HOH A 476 1555 2455 2.39
LINK CA CA A 303 O HOH A 533 1555 2455 2.54
LINK CA CA A 303 O HOH A 537 1555 2455 2.35
LINK CA CA A 303 O HOH A 551 1555 2455 2.15
LINK CA CA A 303 O HOH A 601 1555 1555 2.56
LINK CA CA A 304 O HOH A 494 1555 1555 2.41
LINK CA CA A 304 O HOH A 498 1555 1555 2.41
LINK CA CA A 304 O HOH B 411 1555 1655 2.53
LINK CA CA A 304 O HOH B 457 1555 1655 2.39
LINK CA CA A 304 O HOH B 485 1555 1655 2.39
LINK CA CA A 305 O HOH A 587 1555 1555 2.36
LINK CA CA A 305 O HOH A 603 1555 1555 2.57
LINK CA CA A 305 O HOH A 614 1555 1555 2.24
LINK CA CA A 305 O HOH B 418 1555 1655 2.34
LINK CA CA A 305 O HOH B 488 1555 1555 2.57
LINK CA CA A 305 O HOH B 582 1555 1655 2.37
CRYST1 46.723 73.971 73.183 90.00 91.43 90.00 P 1 21 1 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 0.021403 0.000000 0.000534 0.00000
SCALE2 0.000000 0.013519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013669 0.00000
TER 4413 GLY A 276
TER 8773 GLY B 276
MASTER 412 0 7 29 27 0 0 6 4918 2 91 44
END |