| content |
HEADER HYDROLASE,LYASE 04-MAR-16 5IKY
TITLE APO STRUCTURE OF OBC1, A BIFUNCTIONAL ENZYME FOR QUORUM SENSING-
TITLE 2 DEPENDENT OXALOGENESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXALATE BIOSYNTHETIC COMPONENT 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA THAILANDENSIS (STRAIN E264 / ATCC
SOURCE 3 700388 / DSM 13276 / CIP 106301);
SOURCE 4 ORGANISM_TAXID: 271848;
SOURCE 5 STRAIN: E264 / ATCC 700388 / DSM 13276 / CIP 106301;
SOURCE 6 GENE: DR63_4704;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ALPHA / BETA HYDROLASE, HYDROLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OH,S.RHEE
REVDAT 1 01-JUN-16 5IKY 0
JRNL AUTH J.OH,I.HWANG,S.RHEE
JRNL TITL STRUCTURAL INSIGHTS INTO AN OXALATE-PRODUCING SERINE
JRNL TITL 2 HYDROLASE WITH AN UNUSUAL OXYANION HOLE AND ADDITIONAL LYASE
JRNL TITL 3 ACTIVITY
JRNL REF J.BIOL.CHEM. 2016
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M116.727180
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 88922
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 38.7717 - 6.0184 0.96 6162 142 0.1844 0.2035
REMARK 3 2 6.0184 - 4.7798 1.00 6286 144 0.1731 0.2100
REMARK 3 3 4.7798 - 4.1764 1.00 6252 143 0.1513 0.1693
REMARK 3 4 4.1764 - 3.7949 1.00 6230 143 0.1723 0.2226
REMARK 3 5 3.7949 - 3.5231 1.00 6221 143 0.1933 0.2165
REMARK 3 6 3.5231 - 3.3155 1.00 6228 144 0.2035 0.2574
REMARK 3 7 3.3155 - 3.1495 1.00 6194 142 0.2219 0.2477
REMARK 3 8 3.1495 - 3.0125 1.00 6226 143 0.2384 0.2442
REMARK 3 9 3.0125 - 2.8966 1.00 6202 144 0.2360 0.2743
REMARK 3 10 2.8966 - 2.7966 1.00 6179 141 0.2472 0.2645
REMARK 3 11 2.7966 - 2.7092 1.00 6220 143 0.2613 0.2959
REMARK 3 12 2.7092 - 2.6318 1.00 6160 142 0.2759 0.3421
REMARK 3 13 2.6318 - 2.5625 1.00 6193 142 0.2932 0.2760
REMARK 3 14 2.5625 - 2.5000 1.00 6171 142 0.3101 0.3474
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 8011
REMARK 3 ANGLE : 0.722 10954
REMARK 3 CHIRALITY : 0.024 1272
REMARK 3 PLANARITY : 0.004 1438
REMARK 3 DIHEDRAL : 12.790 2807
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): 14.0477 -36.6277 27.1305
REMARK 3 T TENSOR
REMARK 3 T11: 0.5766 T22: 0.4724
REMARK 3 T33: 0.4624 T12: 0.0252
REMARK 3 T13: -0.1198 T23: 0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 0.8682 L22: 1.2365
REMARK 3 L33: 0.6250 L12: 0.1816
REMARK 3 L13: -0.1017 L23: -0.1863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: -0.1417 S13: -0.1190
REMARK 3 S21: 0.0970 S22: 0.0832 S23: -0.2121
REMARK 3 S31: 0.1380 S32: 0.2567 S33: 0.0027
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SF FILE CONTAINS FRIEDEL PAIRS UNDER
REMARK 3 I/F_MINUS AND I/F_PLUS COLUMNS.
REMARK 4
REMARK 4 5IKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 49.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 1.65400
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: PHENIX
REMARK 200 STARTING MODEL: 4NNA
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 1M SODIUM CITRATE
REMARK 280 TRIBASIC, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 115.40500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.62911
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 84.57733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 115.40500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 66.62911
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 84.57733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 115.40500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 66.62911
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 84.57733
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 115.40500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 66.62911
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 84.57733
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 115.40500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 66.62911
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 84.57733
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 115.40500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 66.62911
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 84.57733
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 133.25822
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 169.15467
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 133.25822
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 169.15467
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 133.25822
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 169.15467
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 133.25822
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 169.15467
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 133.25822
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 169.15467
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 133.25822
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 169.15467
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1382 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1443 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1487 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 76
REMARK 465 GLY A 77
REMARK 465 ALA A 78
REMARK 465 PRO A 79
REMARK 465 GLU A 583
REMARK 465 SER A 584
REMARK 465 LEU A 585
REMARK 465 ALA A 659
REMARK 465 ARG A 660
REMARK 465 PRO A 661
REMARK 465 GLY A 662
REMARK 465 LYS A 663
REMARK 465 THR A 664
REMARK 465 VAL A 665
REMARK 465 THR A 666
REMARK 465 ARG A 667
REMARK 465 GLU A 668
REMARK 465 HIS A 669
REMARK 465 ALA A 670
REMARK 465 PRO A 754
REMARK 465 ALA A 755
REMARK 465 ASP A 756
REMARK 465 ALA A 757
REMARK 465 SER A 758
REMARK 465 GLU A 759
REMARK 465 PRO A 760
REMARK 465 PRO A 761
REMARK 465 THR A 817
REMARK 465 LEU A 818
REMARK 465 ARG A 819
REMARK 465 PRO A 820
REMARK 465 SER A 821
REMARK 465 ARG A 822
REMARK 465 GLN A 823
REMARK 465 THR A 824
REMARK 465 ARG A 825
REMARK 465 ARG A 826
REMARK 465 ASP A 827
REMARK 465 THR A 828
REMARK 465 VAL A 899
REMARK 465 ARG A 900
REMARK 465 ARG A 901
REMARK 465 ASP A 902
REMARK 465 ALA A 903
REMARK 465 ALA A 904
REMARK 465 GLY A 905
REMARK 465 PHE A 906
REMARK 465 PRO A 907
REMARK 465 LEU A 908
REMARK 465 TYR A 909
REMARK 465 GLN A 910
REMARK 465 ASP A 911
REMARK 465 GLY A 912
REMARK 465 ALA A 913
REMARK 465 ARG A 914
REMARK 465 ALA A 915
REMARK 465 ARG A 916
REMARK 465 SER A 1107
REMARK 465 SER A 1108
REMARK 465 MET A 1109
REMARK 465 THR A 1110
REMARK 465 ASP A 1111
REMARK 465 TYR A 1112
REMARK 465 ARG A 1113
REMARK 465 SER A 1114
REMARK 465 SER A 1115
REMARK 465 ALA A 1116
REMARK 465 ASN A 1117
REMARK 465 GLN A 1118
REMARK 465 THR A 1119
REMARK 465 THR A 1120
REMARK 465 ARG A 1121
REMARK 465 ARG A 1122
REMARK 465 ALA A 1123
REMARK 465 LEU A 1124
REMARK 465 ALA A 1125
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 38 CG OD1 OD2
REMARK 470 GLU A 41 CG CD OE1 OE2
REMARK 470 SER A 81 OG
REMARK 470 THR A 83 OG1 CG2
REMARK 470 VAL A 84 CG1 CG2
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 ARG A 262 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 287 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 LYS A 423 CG CD CE NZ
REMARK 470 GLU A 426 CG CD OE1 OE2
REMARK 470 SER A 581 OG
REMARK 470 ASP A 588 CG OD1 OD2
REMARK 470 GLU A 594 CG CD OE1 OE2
REMARK 470 ARG A 608 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 611 CG1 CG2
REMARK 470 GLU A 621 CG CD OE1 OE2
REMARK 470 TYR A 622 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 623 CG CD1 CD2
REMARK 470 VAL A 624 CG1 CG2
REMARK 470 TYR A 627 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 628 CG1 CG2 CD1
REMARK 470 GLN A 629 CG CD OE1 NE2
REMARK 470 ILE A 630 CG1 CG2 CD1
REMARK 470 GLU A 649 CG CD OE1 OE2
REMARK 470 ARG A 653 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 655 CG CD1 CD2
REMARK 470 GLU A 656 CG CD OE1 OE2
REMARK 470 ASP A 657 CG OD1 OD2
REMARK 470 TYR A 658 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 675 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 741 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 752 CG CD OE1 OE2
REMARK 470 VAL A 762 CG1 CG2
REMARK 470 ARG A 763 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 764 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 765 CG OD1 OD2
REMARK 470 VAL A 766 CG1 CG2
REMARK 470 ASP A 769 CG OD1 OD2
REMARK 470 GLU A 770 CG CD OE1 OE2
REMARK 470 LEU A 771 CG CD1 CD2
REMARK 470 LYS A 796 CG CD CE NZ
REMARK 470 GLN A 811 CG CD OE1 NE2
REMARK 470 ASP A 815 CG OD1 OD2
REMARK 470 LEU A 830 CG CD1 CD2
REMARK 470 ARG A 831 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 842 CG OD1 OD2
REMARK 470 GLU A 870 CG CD OE1 OE2
REMARK 470 ARG A 878 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 885 CG1 CG2
REMARK 470 ASP A 886 CG OD1 OD2
REMARK 470 LYS A 887 CG CD CE NZ
REMARK 470 LYS A 890 CG CD CE NZ
REMARK 470 LEU A 891 CG CD1 CD2
REMARK 470 TYR A 893 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 894 OG1 CG2
REMARK 470 GLU A 895 CG CD OE1 OE2
REMARK 470 ARG A 896 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 897 CG CD OE1 NE2
REMARK 470 LEU A 898 CG CD1 CD2
REMARK 470 ARG A 917 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 919 CG OD1 ND2
REMARK 470 GLU A 921 CG CD OE1 OE2
REMARK 470 GLN A 922 CG CD OE1 NE2
REMARK 470 GLU A 924 CG CD OE1 OE2
REMARK 470 ARG A 925 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 950 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 953 CG CD OE1 OE2
REMARK 470 ARG A 954 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 955 CG CD1 CD2
REMARK 470 LEU A 957 CG CD1 CD2
REMARK 470 THR A 958 OG1 CG2
REMARK 470 ASP A 960 CG OD1 OD2
REMARK 470 GLU A 961 CG CD OE1 OE2
REMARK 470 HIS A1026 CG ND1 CD2 CE1 NE2
REMARK 470 THR A1027 OG1 CG2
REMARK 470 GLN A1028 CG CD OE1 NE2
REMARK 470 ARG A1072 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1088 CG CD NE CZ NH1 NH2
REMARK 470 THR A1096 OG1 CG2
REMARK 470 HIS A1099 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A1102 CG CD1 CD2
REMARK 470 ARG A1103 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1104 CG CD OE1 OE2
REMARK 470 GLN A1106 CG CD OE1 NE2
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 ALA A 174 N ASP A 177 2.18
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 96 71.27 -154.34
REMARK 500 HIS A 157 71.56 -157.99
REMARK 500 ALA A 174 -101.60 -68.02
REMARK 500 VAL A 175 -48.67 0.59
REMARK 500 ASP A 285 72.97 -157.11
REMARK 500 ARG A 294 2.01 -68.54
REMARK 500 THR A 362 -85.77 -116.20
REMARK 500 PRO A 589 -162.77 -72.79
REMARK 500 ALA A 590 32.31 -79.56
REMARK 500 ASP A 619 57.05 -97.40
REMARK 500 ALA A 625 -8.00 68.97
REMARK 500 TYR A 627 53.88 -110.09
REMARK 500 GLU A 656 39.67 -85.76
REMARK 500 ASN A 738 44.48 -93.73
REMARK 500 GLU A 770 64.48 -156.85
REMARK 500 ALA A 814 67.60 -102.84
REMARK 500 ALA A 889 -169.89 -112.46
REMARK 500 ILE A 918 -72.84 -55.86
REMARK 500 SER A 935 -113.81 57.11
REMARK 500 ARG A1064 -158.77 -98.84
REMARK 500 ALA A1094 96.97 -58.26
REMARK 500 LEU A1105 37.58 -95.47
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 MG A1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 477 OE2
REMARK 620 2 HOH A1321 O 153.8
REMARK 620 3 HOH A1430 O 101.7 52.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IKZ RELATED DB: PDB
DBREF1 5IKY A 1 1125 UNP A0A096YSN3_BURTA
DBREF2 5IKY A A0A096YSN3 1 1125
SEQRES 1 A 1125 MET VAL LYS THR PHE TYR ILE THR ALA ALA PRO VAL GLY
SEQRES 2 A 1125 ALA VAL PRO LYS PHE LEU ASP PRO LEU GLU PRO LYS PHE
SEQRES 3 A 1125 ILE PRO HIS ALA LEU LEU GLU LEU LEU PRO ALA ASP ARG
SEQRES 4 A 1125 ARG GLU ALA THR ILE LYS ALA LEU GLU ALA ASN GLY TRP
SEQRES 5 A 1125 GLU ALA VAL PRO ALA GLY GLY ILE VAL ARG GLU TYR GLY
SEQRES 6 A 1125 TYR ASP ALA PRO ILE ASP LEU THR ASP TYR ASP GLY ALA
SEQRES 7 A 1125 PRO ALA SER ALA THR VAL HIS ASP ALA LEU ARG ASN ASN
SEQRES 8 A 1125 GLY TRP THR PRO SER GLY SER VAL TRP HIS ARG THR GLN
SEQRES 9 A 1125 THR SER PRO SER LEU ALA GLN PRO PRO LEU ILE THR ARG
SEQRES 10 A 1125 ASN THR LEU GLU ARG LEU SER SER VAL ASP LEU VAL ARG
SEQRES 11 A 1125 GLN ILE VAL LEU GLN LEU THR THR PHE GLY TRP THR ALA
SEQRES 12 A 1125 THR GLU ASP GLY SER LEU THR TRP ALA HIS ASP ARG ILE
SEQRES 13 A 1125 HIS THR TYR LEU SER PRO ASP PHE VAL GLU ARG MET ARG
SEQRES 14 A 1125 ALA ASP ASN ALA ALA VAL LEU ASP SER LEU PHE GLU ASN
SEQRES 15 A 1125 GLY TRP ARG MET CYS GLY ALA GLY HIS TRP GLN PRO GLY
SEQRES 16 A 1125 LYS ALA ARG SER PRO TYR LEU PRO ILE THR ALA ASN GLY
SEQRES 17 A 1125 ILE VAL ASP ALA SER ARG GLU ALA LEU ARG GLU GLY ALA
SEQRES 18 A 1125 ALA VAL VAL HIS LEU HIS THR ARG ALA THR ASP ASP GLN
SEQRES 19 A 1125 ALA THR LEU ALA ILE PRO GLY LEU ASN THR PRO ILE GLY
SEQRES 20 A 1125 ILE GLY SER GLN ARG ASN HIS ILE VAL LEU ASP ASP TYR
SEQRES 21 A 1125 ASP ARG ILE MET PRO THR LEU LEU ASP LEU GLU PRO SER
SEQRES 22 A 1125 ALA ILE LEU ASN LEU SER THR SER ALA ARG GLY ASP ARG
SEQRES 23 A 1125 ARG ALA SER GLN SER PRO LEU ARG ARG ALA HIS LEU LYS
SEQRES 24 A 1125 ARG TYR GLY HIS ALA GLN LEU ALA PRO ASP VAL ALA SER
SEQRES 25 A 1125 PHE SER PRO GLY PRO VAL VAL PHE GLN ALA GLY GLY GLY
SEQRES 26 A 1125 TYR ASP ASN PRO ASN ALA PHE LEU ALA ASP GLN LEU ALA
SEQRES 27 A 1125 HIS PHE ALA GLU VAL GLY VAL ARG PRO GLU ILE GLU VAL
SEQRES 28 A 1125 PHE ASN HIS THR ILE VAL GLU ASN SER VAL THR LEU TYR
SEQRES 29 A 1125 GLN SER PRO LEU VAL LYS ALA GLY VAL PRO VAL LEU PHE
SEQRES 30 A 1125 MET LEU VAL ALA ALA VAL ASP GLN TYR HIS ARG ASP PRO
SEQRES 31 A 1125 VAL SER GLY ASP THR SER ASP ASP SER LEU ILE ASP VAL
SEQRES 32 A 1125 PRO THR ARG LYS ALA ILE ALA LYS LEU LEU GLN ALA GLY
SEQRES 33 A 1125 THR ASP ASP ALA HIS GLU LYS ALA VAL GLU LEU ALA ALA
SEQRES 34 A 1125 THR GLN LEU ARG PRO THR VAL GLU LYS LEU ARG ASP ASN
SEQRES 35 A 1125 PHE PRO SER CYS LYS ILE SER LEU LEU LEU PRO GLY PRO
SEQRES 36 A 1125 PHE GLN ALA LEU LEU VAL ASP VAL ALA ILE ALA LEU ASP
SEQRES 37 A 1125 LEU ASP GLY ILE ARG VAL GLY LEU GLU ASP ALA LEU ASN
SEQRES 38 A 1125 VAL PHE ASP ALA ARG VAL PRO GLY GLY VAL ARG LYS ALA
SEQRES 39 A 1125 CYS GLY THR GLY ASP GLN VAL ARG TRP LEU ARG ARG GLU
SEQRES 40 A 1125 LEU GLU ARG ARG GLY ILE GLY ILE VAL ASP ALA GLU THR
SEQRES 41 A 1125 LEU ARG ASP GLU LEU GLY MET SER ARG PRO ASP VAL ALA
SEQRES 42 A 1125 LEU PHE ARG GLN ALA GLU ALA ALA LEU ALA HIS TYR PRO
SEQRES 43 A 1125 ALA ASP GLU ARG LEU VAL SER ALA ASP THR ILE LEU ASP
SEQRES 44 A 1125 ALA LEU HIS PRO ILE VAL ASP THR TYR ARG LYS ILE GLU
SEQRES 45 A 1125 ASP ARG LEU ALA ALA HIS LEU ALA SER ALA GLU SER LEU
SEQRES 46 A 1125 PRO ALA ASP PRO ALA ALA LEU ALA GLU HIS VAL LEU THR
SEQRES 47 A 1125 ALA ALA ARG SER PHE GLY ILE THR ILE ARG SER PHE VAL
SEQRES 48 A 1125 GLU GLU LEU ASP ARG TYR GLU ASP HIS GLU TYR LEU VAL
SEQRES 49 A 1125 ALA ARG TYR ILE GLN ILE PRO GLN ALA LEU ASN PHE ALA
SEQRES 50 A 1125 ARG GLU LEU LEU VAL PRO ARG GLY TYR SER ILE GLU ALA
SEQRES 51 A 1125 TYR ASP ARG ALA LEU GLU ASP TYR ALA ARG PRO GLY LYS
SEQRES 52 A 1125 THR VAL THR ARG GLU HIS ALA SER TYR SER VAL ARG VAL
SEQRES 53 A 1125 ASP GLN PHE LYS PRO LEU PRO LEU ARG CYS LEU GLU TYR
SEQRES 54 A 1125 LEU VAL GLY ILE PRO CYS ARG TYR ASN SER ASP TYR SER
SEQRES 55 A 1125 ASN VAL VAL ASN LEU GLY LEU ARG GLN SER PRO ARG TYR
SEQRES 56 A 1125 SER ALA THR MET ALA LEU LEU TYR HIS ALA LEU ARG GLU
SEQRES 57 A 1125 LEU THR LEU GLU LEU ARG ASP ARG SER ASN ALA SER ARG
SEQRES 58 A 1125 LYS ALA CYS GLY PRO LEU TRP THR VAL LEU GLU THR PRO
SEQRES 59 A 1125 ALA ASP ALA SER GLU PRO PRO VAL ARG ARG ASP VAL ALA
SEQRES 60 A 1125 PRO ASP GLU LEU ALA ALA ALA ILE ALA SER VAL ASP TRP
SEQRES 61 A 1125 VAL VAL LEU PRO SER THR PRO THR THR ASN TYR PRO LEU
SEQRES 62 A 1125 GLY ILE LYS LEU SER ASN GLY MET ALA GLN LEU PHE HIS
SEQRES 63 A 1125 GLY PHE VAL ALA GLN ILE ALA ALA ASP PRO THR LEU ARG
SEQRES 64 A 1125 PRO SER ARG GLN THR ARG ARG ASP THR PRO LEU ARG LEU
SEQRES 65 A 1125 LEU ALA ILE THR HIS SER GLY ARG ARG ASP ASP GLY GLU
SEQRES 66 A 1125 THR VAL ILE GLU ALA SER MET LEU HIS ASN ARG PHE ALA
SEQRES 67 A 1125 LEU ASN ALA ASP PRO SER GLY ILE TYR PHE SER GLU GLU
SEQRES 68 A 1125 SER GLN LEU ILE TYR GLU ARG LEU ILE LEU PRO ARG LEU
SEQRES 69 A 1125 VAL ASP LYS PRO ALA LYS LEU ALA TYR THR GLU ARG GLN
SEQRES 70 A 1125 LEU VAL ARG ARG ASP ALA ALA GLY PHE PRO LEU TYR GLN
SEQRES 71 A 1125 ASP GLY ALA ARG ALA ARG ARG ILE ASN ALA GLU GLN ILE
SEQRES 72 A 1125 GLU ARG LEU PRO LEU LEU LYS CYS PHE ALA HIS SER SER
SEQRES 73 A 1125 GLY ILE ALA THR ALA GLN GLN LEU ASP VAL GLN ALA CYS
SEQRES 74 A 1125 ARG ASP GLY GLU ARG LEU GLY LEU THR GLY ASP GLU LEU
SEQRES 75 A 1125 ARG ALA PHE PHE ASP ARG ALA LEU LEU VAL SER PHE GLY
SEQRES 76 A 1125 SER ALA ALA ASP ILE HIS LEU ASP TRP LEU GLY THR SER
SEQRES 77 A 1125 VAL VAL ASP VAL THR ALA PHE ASN ASP VAL ARG SER LEU
SEQRES 78 A 1125 ALA GLY THR THR SER ARG HIS TYR VAL ILE GLN PRO GLY
SEQRES 79 A 1125 GLU HIS ALA ASP VAL LEU GLN HIS CYS LEU VAL HIS THR
SEQRES 80 A 1125 GLN PRO ALA ASP TYR ARG TYR ASP HIS ALA THR PRO VAL
SEQRES 81 A 1125 TRP GLN ASP GLY ARG GLN GLY LYS ILE VAL ALA ARG LEU
SEQRES 82 A 1125 THR GLY VAL PHE LEU LEU ASP ASP HIS ALA ARG LEU ASP
SEQRES 83 A 1125 ASP GLY HIS SER ILE ARG ARG TYR LEU ALA ALA SER PRO
SEQRES 84 A 1125 LEU TRP LEU ARG GLN TRP ILE ALA ARG PHE HIS ASP ALA
SEQRES 85 A 1125 PRO ALA ASP THR GLY ALA HIS ALA ILE LEU ARG GLU LEU
SEQRES 86 A 1125 GLN SER SER MET THR ASP TYR ARG SER SER ALA ASN GLN
SEQRES 87 A 1125 THR THR ARG ARG ALA LEU ALA
HET MG A1201 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 HOH *200(H2 O)
HELIX 1 AA1 HIS A 29 LEU A 34 1 6
HELIX 2 AA2 PRO A 36 ASN A 50 1 15
HELIX 3 AA3 THR A 73 TYR A 75 5 3
HELIX 4 AA4 SER A 81 ASN A 91 1 11
HELIX 5 AA5 THR A 116 ARG A 122 1 7
HELIX 6 AA6 SER A 125 PHE A 139 1 15
HELIX 7 AA7 SER A 161 ALA A 173 1 13
HELIX 8 AA8 VAL A 175 ASN A 182 1 8
HELIX 9 AA9 THR A 205 GLU A 219 1 15
HELIX 10 AB1 VAL A 256 GLU A 271 1 16
HELIX 11 AB2 ASP A 285 SER A 289 5 5
HELIX 12 AB3 PRO A 292 HIS A 297 1 6
HELIX 13 AB4 PRO A 329 GLY A 344 1 16
HELIX 14 AB5 ASN A 353 VAL A 361 1 9
HELIX 15 AB6 TYR A 364 ALA A 371 1 8
HELIX 16 AB7 ASP A 402 GLY A 416 1 15
HELIX 17 AB8 THR A 417 PHE A 443 1 27
HELIX 18 AB9 PRO A 453 ALA A 458 5 6
HELIX 19 AC1 LEU A 459 LEU A 467 1 9
HELIX 20 AC2 GLY A 496 ARG A 511 1 16
HELIX 21 AC3 ASP A 517 LEU A 525 1 9
HELIX 22 AC4 ARG A 529 LEU A 542 1 14
HELIX 23 AC5 SER A 553 LEU A 561 1 9
HELIX 24 AC6 LEU A 561 ALA A 580 1 20
HELIX 25 AC7 ALA A 591 PHE A 603 1 13
HELIX 26 AC8 PHE A 610 TYR A 617 5 8
HELIX 27 AC9 ILE A 628 VAL A 642 1 15
HELIX 28 AD1 ASP A 652 ASP A 657 5 6
HELIX 29 AD2 ARG A 675 PHE A 679 5 5
HELIX 30 AD3 PRO A 681 VAL A 691 1 11
HELIX 31 AD4 LEU A 707 SER A 712 5 6
HELIX 32 AD5 ARG A 714 ASP A 735 1 22
HELIX 33 AD6 ALA A 772 VAL A 778 1 7
HELIX 34 AD7 TYR A 791 ALA A 814 1 24
HELIX 35 AD8 ILE A 848 ALA A 861 1 14
HELIX 36 AD9 SER A 869 ILE A 880 1 12
HELIX 37 AE1 LEU A 881 VAL A 885 5 5
HELIX 38 AE2 ASN A 919 ILE A 923 5 5
HELIX 39 AE3 SER A 936 GLY A 956 1 21
HELIX 40 AE4 THR A 958 ASP A 967 1 10
HELIX 41 AE5 ASP A 997 GLY A 1003 1 7
HELIX 42 AE6 SER A 1006 VAL A 1010 5 5
HELIX 43 AE7 GLY A 1014 HIS A 1026 1 13
HELIX 44 AE8 GLN A 1028 TYR A 1032 5 5
HELIX 45 AE9 SER A 1070 ALA A 1077 1 8
HELIX 46 AF1 PRO A 1079 ASP A 1091 1 13
HELIX 47 AF2 THR A 1096 GLU A 1104 1 9
SHEET 1 AA110 GLY A 514 ILE A 515 0
SHEET 2 AA110 THR A 4 ALA A 9 1 N PHE A 5 O GLY A 514
SHEET 3 AA110 GLY A 471 VAL A 474 1 O VAL A 474 N THR A 8
SHEET 4 AA110 CYS A 446 LEU A 451 1 N LEU A 450 O ARG A 473
SHEET 5 AA110 VAL A 375 VAL A 380 1 N PHE A 377 O LYS A 447
SHEET 6 AA110 ARG A 346 VAL A 351 1 N VAL A 351 O MET A 378
SHEET 7 AA110 VAL A 310 PHE A 313 1 N ALA A 311 O GLU A 348
SHEET 8 AA110 ILE A 275 LEU A 278 1 N LEU A 278 O VAL A 310
SHEET 9 AA110 VAL A 223 LEU A 226 1 N LEU A 226 O ASN A 277
SHEET 10 AA110 THR A 4 ALA A 9 1 N ALA A 9 O HIS A 225
SHEET 1 AA2 2 LYS A 17 PHE A 18 0
SHEET 2 AA2 2 ARG A 198 SER A 199 1 O SER A 199 N LYS A 17
SHEET 1 AA3 3 PHE A 26 PRO A 28 0
SHEET 2 AA3 3 GLY A 190 TRP A 192 -1 O HIS A 191 N ILE A 27
SHEET 3 AA3 3 GLU A 53 VAL A 55 -1 N VAL A 55 O GLY A 190
SHEET 1 AA4 3 ILE A 156 LEU A 160 0
SHEET 2 AA4 3 ILE A 60 TYR A 64 -1 N ARG A 62 O THR A 158
SHEET 3 AA4 3 ARG A 185 MET A 186 -1 O ARG A 185 N VAL A 61
SHEET 1 AA5 3 ILE A 70 ASP A 71 0
SHEET 2 AA5 3 VAL A 99 ARG A 102 -1 O TRP A 100 N ILE A 70
SHEET 3 AA5 3 TRP A 93 SER A 96 -1 N THR A 94 O HIS A 101
SHEET 1 AA6 3 LEU A 114 ILE A 115 0
SHEET 2 AA6 3 LEU A 149 THR A 150 -1 O LEU A 149 N ILE A 115
SHEET 3 AA6 3 THR A 142 ALA A 143 -1 N THR A 142 O THR A 150
SHEET 1 AA7 2 ALA A 235 LEU A 237 0
SHEET 2 AA7 2 ILE A 246 ILE A 248 -1 O ILE A 246 N LEU A 237
SHEET 1 AA8 2 VAL A 318 VAL A 319 0
SHEET 2 AA8 2 GLY A 325 TYR A 326 -1 O TYR A 326 N VAL A 318
SHEET 1 AA9 2 TYR A 386 ARG A 388 0
SHEET 2 AA9 2 THR A 395 ASP A 397 -1 O SER A 396 N HIS A 387
SHEET 1 AB1 2 ASN A 481 PHE A 483 0
SHEET 2 AB1 2 VAL A 491 LYS A 493 -1 O ARG A 492 N VAL A 482
SHEET 1 AB2 2 ARG A 696 TYR A 697 0
SHEET 2 AB2 2 VAL A 704 VAL A 705 -1 O VAL A 705 N ARG A 696
SHEET 1 AB3 9 ARG A 764 VAL A 766 0
SHEET 2 AB3 9 LEU A 747 GLU A 752 -1 N GLU A 752 O ARG A 764
SHEET 3 AB3 9 LEU A 832 THR A 836 -1 O ALA A 834 N THR A 749
SHEET 4 AB3 9 TRP A 780 VAL A 782 1 N VAL A 782 O LEU A 833
SHEET 5 AB3 9 LEU A 929 SER A 935 1 O PHE A 932 N VAL A 781
SHEET 6 AB3 9 ALA A 969 SER A 976 1 O LEU A 970 N LEU A 929
SHEET 7 AB3 9 SER A 988 VAL A 992 1 O VAL A 992 N GLY A 975
SHEET 8 AB3 9 ILE A1049 THR A1054 1 O ALA A1051 N VAL A 989
SHEET 9 AB3 9 THR A1038 ASP A1043 -1 N VAL A1040 O ARG A1052
LINK OE2 GLU A 477 MG MG A1201 1555 1555 2.37
LINK MG MG A1201 O HOH A1321 1555 1555 2.58
LINK MG MG A1201 O HOH A1430 1555 1555 2.70
CISPEP 1 VAL A 373 PRO A 374 0 -1.64
SITE 1 AC1 6 HIS A 225 HIS A 227 GLU A 477 HOH A1321
SITE 2 AC1 6 HOH A1430 HOH A1459
CRYST1 230.810 230.810 253.732 90.00 90.00 120.00 H 3 2 18
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 0.004333 0.002501 0.000000 0.00000
SCALE2 0.000000 0.005003 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003941 0.00000
TER 7836 GLN A1106
MASTER 532 0 1 47 43 0 2 6 8036 1 4 87
END |