HEADER METAL TRANSPORT 29-SEP-15 5E1J
TITLE STRUCTURE OF VOLTAGE-GATED TWO-PORE CHANNEL TPC1 FROM ARABIDOPSIS
TITLE 2 THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TWO PORE CALCIUM CHANNEL PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALCIUM CHANNEL PROTEIN 1,ATCCH1,FATTY ACID OXYGENATION UP-
COMPND 5 REGULATED PROTEIN 2,VOLTAGE-DEPENDENT CALCIUM CHANNEL PROTEIN TPC1,
COMPND 6 ATTPC1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: TPC1, CCH1, FOU2, AT4G03560, F9H3.19, T5L23.5;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMD1163;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZ
KEYWDS TWO-PORE CHANNEL, VOLTAGE-GATED, CALCIUM MODULATION, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GUO,W.ZENG,Q.CHEN,C.LEE,L.CHEN,Y.YANG,Y.JIANG
REVDAT 7 06-MAR-24 5E1J 1 LINK
REVDAT 6 20-NOV-19 5E1J 1 REMARK
REVDAT 5 22-NOV-17 5E1J 1 REMARK
REVDAT 4 06-SEP-17 5E1J 1 JRNL REMARK
REVDAT 3 23-MAR-16 5E1J 1 JRNL
REVDAT 2 06-JAN-16 5E1J 1 JRNL
REVDAT 1 16-DEC-15 5E1J 0
JRNL AUTH J.GUO,W.ZENG,Q.CHEN,C.LEE,L.CHEN,Y.YANG,C.CANG,D.REN,Y.JIANG
JRNL TITL STRUCTURE OF THE VOLTAGE-GATED TWO-PORE CHANNEL TPC1 FROM
JRNL TITL 2 ARABIDOPSIS THALIANA.
JRNL REF NATURE V. 531 196 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 26689363
JRNL DOI 10.1038/NATURE16446
REMARK 2
REMARK 2 RESOLUTION. 3.31 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.3
REMARK 3 NUMBER OF REFLECTIONS : 22635
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.325
REMARK 3 R VALUE (WORKING SET) : 0.325
REMARK 3 FREE R VALUE : 0.332
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1741
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 39.7153 - 7.5579 0.96 3339 173 0.2741 0.3110
REMARK 3 2 7.5579 - 6.0056 1.00 3518 178 0.3522 0.4014
REMARK 3 3 6.0056 - 5.2484 1.00 3496 183 0.3748 0.3487
REMARK 3 4 5.2484 - 4.7694 1.00 3480 181 0.3061 0.3344
REMARK 3 5 4.7694 - 4.4280 1.00 3463 204 0.2895 0.3257
REMARK 3 6 4.4280 - 4.1673 1.00 3485 195 0.3236 0.2692
REMARK 3 7 4.1673 - 3.9588 0.97 3354 188 0.3500 0.2987
REMARK 3 8 3.9588 - 3.7866 0.83 2874 165 0.3609 0.3360
REMARK 3 9 3.7866 - 3.6409 0.66 2334 124 0.3632 0.3533
REMARK 3 10 3.6409 - 3.5154 0.49 1734 80 0.3750 0.4133
REMARK 3 11 3.5154 - 3.4055 0.28 970 56 0.3841 0.3778
REMARK 3 12 3.4055 - 3.3080 0.09 331 14 0.3768 0.3570
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.15
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 : 0.006 5097
REMARK 3 ANGLE : 0.854 6894
REMARK 3 CHIRALITY : 0.030 803
REMARK 3 PLANARITY : 0.005 849
REMARK 3 DIHEDRAL : 11.681 1758
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 32:91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.5956 -25.0782 26.0597
REMARK 3 T TENSOR
REMARK 3 T11: 0.6668 T22: 2.0419
REMARK 3 T33: 1.8308 T12: -0.1187
REMARK 3 T13: -0.0527 T23: 0.6279
REMARK 3 L TENSOR
REMARK 3 L11: 1.8221 L22: 0.7825
REMARK 3 L33: 0.1903 L12: -0.9697
REMARK 3 L13: -0.4188 L23: 0.3808
REMARK 3 S TENSOR
REMARK 3 S11: 0.2559 S12: -1.2094 S13: -1.4829
REMARK 3 S21: 0.3226 S22: -0.3980 S23: 0.1199
REMARK 3 S31: 0.3121 S32: -0.0507 S33: 0.1184
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 92:398 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5427 -17.2753 8.2530
REMARK 3 T TENSOR
REMARK 3 T11: 0.4175 T22: 0.5105
REMARK 3 T33: 0.7420 T12: 0.0645
REMARK 3 T13: -0.1590 T23: -0.2070
REMARK 3 L TENSOR
REMARK 3 L11: 3.0025 L22: 1.2835
REMARK 3 L33: 1.2087 L12: 0.0198
REMARK 3 L13: 0.0355 L23: 0.0605
REMARK 3 S TENSOR
REMARK 3 S11: 0.3140 S12: -0.5767 S13: -1.1242
REMARK 3 S21: 0.2691 S22: 0.0045 S23: -0.1441
REMARK 3 S31: 0.4323 S32: -0.2139 S33: -0.0482
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 399:547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7758 0.2121 37.7422
REMARK 3 T TENSOR
REMARK 3 T11: 0.9684 T22: 1.4557
REMARK 3 T33: 0.6085 T12: -0.3414
REMARK 3 T13: -0.3894 T23: -0.3084
REMARK 3 L TENSOR
REMARK 3 L11: 0.2273 L22: 0.3959
REMARK 3 L33: 1.1104 L12: 0.0276
REMARK 3 L13: 0.2685 L23: -0.0526
REMARK 3 S TENSOR
REMARK 3 S11: 0.1712 S12: -0.3113 S13: -0.1339
REMARK 3 S21: 0.3821 S22: -0.0295 S23: -0.1892
REMARK 3 S31: 0.1561 S32: -0.1691 S33: -0.0930
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 548:686 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5933 -9.6206 6.3042
REMARK 3 T TENSOR
REMARK 3 T11: 0.2497 T22: 0.4432
REMARK 3 T33: 0.5208 T12: 0.0548
REMARK 3 T13: -0.1843 T23: -0.3687
REMARK 3 L TENSOR
REMARK 3 L11: 0.5403 L22: 1.1603
REMARK 3 L33: 0.9349 L12: 0.3850
REMARK 3 L13: 0.2034 L23: 0.0463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0847 S12: -0.1640 S13: -0.0888
REMARK 3 S21: 0.1200 S22: 0.0940 S23: -0.6370
REMARK 3 S31: 0.1318 S32: 0.3367 S33: -0.3416
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 5E1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214168.
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 : 5.5-7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34119
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG400, 150 MM BACL2, 100MM HEPES,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 108.62000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 108.62000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 44.21500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.42500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.21500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.42500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 108.62000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.21500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 79.42500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.62000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.21500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 79.42500
REMARK 290 SMTRY3 8 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: 9680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -176.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 BA BA A 801 LIES ON A SPECIAL POSITION.
REMARK 375 BA BA A 803 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 904 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 GLU A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 LEU A 5
REMARK 465 ILE A 6
REMARK 465 GLY A 7
REMARK 465 ARG A 8
REMARK 465 ASP A 9
REMARK 465 SER A 10
REMARK 465 LEU A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 ASP A 17
REMARK 465 ARG A 18
REMARK 465 VAL A 19
REMARK 465 ARG A 20
REMARK 465 ARG A 21
REMARK 465 SER A 22
REMARK 465 GLU A 23
REMARK 465 ALA A 24
REMARK 465 ILE A 25
REMARK 465 THR A 26
REMARK 465 HIS A 27
REMARK 465 GLY A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
REMARK 465 PHE A 31
REMARK 465 GLN A 54
REMARK 465 SER A 55
REMARK 465 SER A 56
REMARK 465 PHE A 57
REMARK 465 GLY A 58
REMARK 465 GLU A 59
REMARK 465 SER A 60
REMARK 465 ALA A 61
REMARK 465 LEU A 174
REMARK 465 SER A 175
REMARK 465 PRO A 176
REMARK 465 LEU A 177
REMARK 465 ALA A 178
REMARK 465 PHE A 179
REMARK 465 ASP A 180
REMARK 465 PHE A 181
REMARK 465 LEU A 182
REMARK 465 PRO A 183
REMARK 465 GLU A 403
REMARK 465 VAL A 404
REMARK 465 PRO A 405
REMARK 465 SER A 406
REMARK 465 LEU A 407
REMARK 465 PHE A 408
REMARK 465 GLU A 409
REMARK 465 HIS A 410
REMARK 465 PHE A 411
REMARK 465 PRO A 412
REMARK 465 GLN A 413
REMARK 465 ILE A 414
REMARK 465 ASP A 519
REMARK 465 GLU A 520
REMARK 465 ASN A 521
REMARK 465 THR A 522
REMARK 465 PHE A 523
REMARK 465 VAL A 591
REMARK 465 ASN A 592
REMARK 465 ALA A 593
REMARK 465 GLY A 594
REMARK 465 CYS A 687
REMARK 465 GLN A 688
REMARK 465 GLY A 689
REMARK 465 GLN A 690
REMARK 465 ASP A 691
REMARK 465 SER A 692
REMARK 465 GLN A 693
REMARK 465 GLU A 694
REMARK 465 LYS A 695
REMARK 465 ARG A 696
REMARK 465 ASN A 697
REMARK 465 ARG A 698
REMARK 465 ARG A 699
REMARK 465 ARG A 700
REMARK 465 SER A 701
REMARK 465 ALA A 702
REMARK 465 GLY A 703
REMARK 465 SER A 704
REMARK 465 LYS A 705
REMARK 465 SER A 706
REMARK 465 ARG A 707
REMARK 465 SER A 708
REMARK 465 GLN A 709
REMARK 465 ARG A 710
REMARK 465 VAL A 711
REMARK 465 ASP A 712
REMARK 465 THR A 713
REMARK 465 LEU A 714
REMARK 465 LEU A 715
REMARK 465 HIS A 716
REMARK 465 HIS A 717
REMARK 465 MET A 718
REMARK 465 LEU A 719
REMARK 465 GLY A 720
REMARK 465 ASP A 721
REMARK 465 GLU A 722
REMARK 465 LEU A 723
REMARK 465 SER A 724
REMARK 465 LYS A 725
REMARK 465 PRO A 726
REMARK 465 GLU A 727
REMARK 465 CYS A 728
REMARK 465 SER A 729
REMARK 465 THR A 730
REMARK 465 SER A 731
REMARK 465 ASP A 732
REMARK 465 THR A 733
REMARK 465 SER A 734
REMARK 465 THR A 735
REMARK 465 ALA A 736
REMARK 465 GLY A 737
REMARK 465 LEU A 738
REMARK 465 VAL A 739
REMARK 465 PRO A 740
REMARK 465 ARG A 741
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 GLN A 32 CG CD OE1 NE2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 PRO A 48 CG CD
REMARK 470 VAL A 49 CG1 CG2
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 ILE A 51 CG1 CG2 CD1
REMARK 470 LEU A 52 CG CD1 CD2
REMARK 470 ASP A 53 CG OD1 OD2
REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 78 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 92 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 92 CZ3 CH2
REMARK 470 SER A 100 OG
REMARK 470 CYS A 101 SG
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 ASP A 103 CG OD1 OD2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 112 CG CD1 CD2
REMARK 470 PHE A 171 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 173 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 ILE A 342 CG1 CG2 CD1
REMARK 470 ARG A 379 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 381 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 400 CG CD OE1 NE2
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 470 GLU A 402 CG CD OE1 OE2
REMARK 470 TYR A 415 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 492 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 492 CZ3 CH2
REMARK 470 PHE A 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 529 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 529 CZ3 CH2
REMARK 470 PHE A 599 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 611 CG CD1 CD2 CE1 CE2 CZ
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 TYR A 63 CD2 PHE A 67 1.85
REMARK 500 OD2 ASP A 337 ND2 ASN A 339 2.01
REMARK 500 O PHE A 195 OG SER A 198 2.03
REMARK 500 OH TYR A 216 O VAL A 657 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 37 CB - CG - CD1 ANGL. DEV. = 11.2 DEGREES
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 GLU A 50 -149.68 -103.92
REMARK 500 ILE A 51 55.20 -159.85
REMARK 500 PRO A 99 72.00 6.65
REMARK 500 ASP A 105 -157.86 -116.83
REMARK 500 TYR A 106 74.95 -119.76
REMARK 500 PRO A 113 -166.53 -105.50
REMARK 500 ARG A 185 -67.24 -92.30
REMARK 500 PHE A 238 53.61 -116.24
REMARK 500 GLN A 243 -151.71 -128.94
REMARK 500 PHE A 248 -58.36 -29.45
REMARK 500 THR A 249 51.06 -116.60
REMARK 500 SER A 250 -131.90 55.24
REMARK 500 ASN A 266 23.84 -148.79
REMARK 500 ARG A 358 -87.50 -121.72
REMARK 500 PRO A 361 -96.33 -98.48
REMARK 500 LYS A 365 -159.62 -131.95
REMARK 500 ASN A 384 -169.49 -104.21
REMARK 500 SER A 417 37.82 -90.04
REMARK 500 ALA A 418 -59.52 -123.58
REMARK 500 SER A 458 47.39 -104.45
REMARK 500 LEU A 534 34.82 -93.65
REMARK 500 PHE A 587 52.31 -100.12
REMARK 500 LEU A 603 -161.33 -115.50
REMARK 500 ALA A 604 -75.49 -65.98
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 810 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 120 OG
REMARK 620 2 GLU A 124 OE1 93.2
REMARK 620 3 GLU A 124 OE2 93.1 55.3
REMARK 620 4 ASP A 170 OD2 141.0 119.3 122.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BA A 804 BA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 239 O
REMARK 620 2 ASP A 240 OD1 80.9
REMARK 620 3 GLU A 457 OE2 46.2 126.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BA A 805 BA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 240 OD2
REMARK 620 2 ASP A 454 OD1 70.3
REMARK 620 3 ASP A 454 OD2 69.7 0.6
REMARK 620 4 GLU A 528 OE1 68.2 2.9 2.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 809 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 335 OD1
REMARK 620 2 ASP A 337 OD1 63.5
REMARK 620 3 ASP A 337 OD2 105.6 55.5
REMARK 620 4 ASN A 339 OD1 63.0 96.5 85.3
REMARK 620 5 GLU A 341 O 78.9 142.1 147.4 67.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BA A 801 BA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 605 OE1
REMARK 620 2 GLU A 605 OE1 0.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BA A 803 BA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 901 O
REMARK 620 2 HOH A 901 O 92.9
REMARK 620 3 HOH A 902 O 122.0 84.7
REMARK 620 4 HOH A 902 O 84.7 122.0 142.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BA A 803 BA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 903 O
REMARK 620 2 HOH A 903 O 178.5
REMARK 620 3 HOH A 904 O 90.7 90.7
REMARK 620 4 HOH A 904 O 90.7 90.7 0.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 810
DBREF 5E1J A 1 733 UNP Q94KI8 TPC1_ARATH 1 733
SEQADV 5E1J SER A 734 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J THR A 735 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J ALA A 736 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J GLY A 737 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J LEU A 738 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J VAL A 739 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J PRO A 740 UNP Q94KI8 EXPRESSION TAG
SEQADV 5E1J ARG A 741 UNP Q94KI8 EXPRESSION TAG
SEQRES 1 A 741 MET GLU ASP PRO LEU ILE GLY ARG ASP SER LEU GLY GLY
SEQRES 2 A 741 GLY GLY THR ASP ARG VAL ARG ARG SER GLU ALA ILE THR
SEQRES 3 A 741 HIS GLY THR PRO PHE GLN LYS ALA ALA ALA LEU VAL ASP
SEQRES 4 A 741 LEU ALA GLU ASP GLY ILE GLY LEU PRO VAL GLU ILE LEU
SEQRES 5 A 741 ASP GLN SER SER PHE GLY GLU SER ALA ARG TYR TYR PHE
SEQRES 6 A 741 ILE PHE THR ARG LEU ASP LEU ILE TRP SER LEU ASN TYR
SEQRES 7 A 741 PHE ALA LEU LEU PHE LEU ASN PHE PHE GLU GLN PRO LEU
SEQRES 8 A 741 TRP CYS GLU LYS ASN PRO LYS PRO SER CYS LYS ASP ARG
SEQRES 9 A 741 ASP TYR TYR TYR LEU GLY GLU LEU PRO TYR LEU THR ASN
SEQRES 10 A 741 ALA GLU SER ILE ILE TYR GLU VAL ILE THR LEU ALA ILE
SEQRES 11 A 741 LEU LEU VAL HIS THR PHE PHE PRO ILE SER TYR GLU GLY
SEQRES 12 A 741 SER ARG ILE PHE TRP THR SER ARG LEU ASN LEU VAL LYS
SEQRES 13 A 741 VAL ALA CYS VAL VAL ILE LEU PHE VAL ASP VAL LEU VAL
SEQRES 14 A 741 ASP PHE LEU TYR LEU SER PRO LEU ALA PHE ASP PHE LEU
SEQRES 15 A 741 PRO PHE ARG ILE ALA PRO TYR VAL ARG VAL ILE ILE PHE
SEQRES 16 A 741 ILE LEU SER ILE ARG GLU LEU ARG ASP THR LEU VAL LEU
SEQRES 17 A 741 LEU SER GLY MET LEU GLY THR TYR LEU ASN ILE LEU ALA
SEQRES 18 A 741 LEU TRP MET LEU PHE LEU LEU PHE ALA SER TRP ILE ALA
SEQRES 19 A 741 PHE VAL MET PHE GLU ASP THR GLN GLN GLY LEU THR VAL
SEQRES 20 A 741 PHE THR SER TYR GLY ALA THR LEU TYR GLN MET PHE ILE
SEQRES 21 A 741 LEU PHE THR THR SER ASN ASN PRO ASP VAL TRP ILE PRO
SEQRES 22 A 741 ALA TYR LYS SER SER ARG TRP SER SER VAL PHE PHE VAL
SEQRES 23 A 741 LEU TYR VAL LEU ILE GLY VAL TYR PHE VAL THR ASN LEU
SEQRES 24 A 741 ILE LEU ALA VAL VAL TYR ASP SER PHE LYS GLU GLN LEU
SEQRES 25 A 741 ALA LYS GLN VAL SER GLY MET ASP GLN MET LYS ARG ARG
SEQRES 26 A 741 MET LEU GLU LYS ALA PHE GLY LEU ILE ASP SER ASP LYS
SEQRES 27 A 741 ASN GLY GLU ILE ASP LYS ASN GLN CYS ILE LYS LEU PHE
SEQRES 28 A 741 GLU GLN LEU THR ASN TYR ARG THR LEU PRO LYS ILE SER
SEQRES 29 A 741 LYS GLU GLU PHE GLY LEU ILE PHE ASP GLU LEU ASP ASP
SEQRES 30 A 741 THR ARG ASP PHE LYS ILE ASN LYS ASP GLU PHE ALA ASP
SEQRES 31 A 741 LEU CYS GLN ALA ILE ALA LEU ARG PHE GLN LYS GLU GLU
SEQRES 32 A 741 VAL PRO SER LEU PHE GLU HIS PHE PRO GLN ILE TYR HIS
SEQRES 33 A 741 SER ALA LEU SER GLN GLN LEU ARG ALA PHE VAL ARG SER
SEQRES 34 A 741 PRO ASN PHE GLY TYR ALA ILE SER PHE ILE LEU ILE ILE
SEQRES 35 A 741 ASN PHE ILE ALA VAL VAL VAL GLU THR THR LEU ASP ILE
SEQRES 36 A 741 GLU GLU SER SER ALA GLN LYS PRO TRP GLN VAL ALA GLU
SEQRES 37 A 741 PHE VAL PHE GLY TRP ILE TYR VAL LEU GLU MET ALA LEU
SEQRES 38 A 741 LYS ILE TYR THR TYR GLY PHE GLU ASN TYR TRP ARG GLU
SEQRES 39 A 741 GLY ALA ASN ARG PHE ASP PHE LEU VAL THR TRP VAL ILE
SEQRES 40 A 741 VAL ILE GLY GLU THR ALA THR PHE ILE THR PRO ASP GLU
SEQRES 41 A 741 ASN THR PHE PHE SER ASN GLY GLU TRP ILE ARG TYR LEU
SEQRES 42 A 741 LEU LEU ALA ARG MET LEU ARG LEU ILE ARG LEU LEU MET
SEQRES 43 A 741 ASN VAL GLN ARG TYR ARG ALA PHE ILE ALA THR PHE ILE
SEQRES 44 A 741 THR LEU ILE PRO SER LEU MET PRO TYR LEU GLY THR ILE
SEQRES 45 A 741 PHE CYS VAL LEU CYS ILE TYR CYS SER ILE GLY VAL GLN
SEQRES 46 A 741 VAL PHE GLY GLY LEU VAL ASN ALA GLY ASN LYS LYS LEU
SEQRES 47 A 741 PHE GLU THR GLU LEU ALA GLU ASP ASP TYR LEU LEU PHE
SEQRES 48 A 741 ASN PHE ASN ASP TYR PRO ASN GLY MET VAL THR LEU PHE
SEQRES 49 A 741 ASN LEU LEU VAL MET GLY ASN TRP GLN VAL TRP MET GLU
SEQRES 50 A 741 SER TYR LYS ASP LEU THR GLY THR TRP TRP SER ILE THR
SEQRES 51 A 741 TYR PHE VAL SER PHE TYR VAL ILE THR ILE LEU LEU LEU
SEQRES 52 A 741 LEU ASN LEU VAL VAL ALA PHE VAL LEU GLU ALA PHE PHE
SEQRES 53 A 741 THR GLU LEU ASP LEU GLU GLU GLU GLU LYS CYS GLN GLY
SEQRES 54 A 741 GLN ASP SER GLN GLU LYS ARG ASN ARG ARG ARG SER ALA
SEQRES 55 A 741 GLY SER LYS SER ARG SER GLN ARG VAL ASP THR LEU LEU
SEQRES 56 A 741 HIS HIS MET LEU GLY ASP GLU LEU SER LYS PRO GLU CYS
SEQRES 57 A 741 SER THR SER ASP THR SER THR ALA GLY LEU VAL PRO ARG
HET BA A 801 1
HET BA A 802 1
HET BA A 803 2
HET BA A 804 1
HET BA A 805 1
HET BA A 806 1
HET BA A 807 1
HET BA A 808 1
HET CA A 809 1
HET CA A 810 1
HETNAM BA BARIUM ION
HETNAM CA CALCIUM ION
FORMUL 2 BA 8(BA 2+)
FORMUL 10 CA 2(CA 2+)
FORMUL 12 HOH *4(H2 O)
HELIX 1 AA1 GLN A 32 GLY A 46 1 15
HELIX 2 AA2 TYR A 63 TRP A 92 1 30
HELIX 3 AA3 THR A 116 PHE A 137 1 22
HELIX 4 AA4 PRO A 138 SER A 140 5 3
HELIX 5 AA5 GLY A 143 TRP A 148 1 6
HELIX 6 AA6 SER A 150 TYR A 173 1 24
HELIX 7 AA7 PRO A 188 ILE A 199 1 12
HELIX 8 AA8 ILE A 199 PHE A 238 1 40
HELIX 9 AA9 GLN A 243 PHE A 248 1 6
HELIX 10 AB1 THR A 249 THR A 263 1 15
HELIX 11 AB2 ASN A 266 TRP A 271 1 6
HELIX 12 AB3 TRP A 271 SER A 278 1 8
HELIX 13 AB4 TRP A 280 TYR A 294 1 15
HELIX 14 AB5 PHE A 295 ASP A 335 1 41
HELIX 15 AB6 ASP A 343 ARG A 358 1 16
HELIX 16 AB7 LYS A 365 ASP A 373 1 9
HELIX 17 AB8 ASP A 386 PHE A 399 1 14
HELIX 18 AB9 SER A 429 ILE A 455 1 27
HELIX 19 AC1 GLN A 461 GLY A 487 1 27
HELIX 20 AC2 GLU A 489 GLU A 494 1 6
HELIX 21 AC3 GLU A 494 PHE A 515 1 22
HELIX 22 AC4 SER A 525 LEU A 533 1 9
HELIX 23 AC5 LEU A 534 VAL A 548 5 15
HELIX 24 AC6 TYR A 551 LEU A 565 1 15
HELIX 25 AC7 LEU A 565 PHE A 587 1 23
HELIX 26 AC8 LYS A 597 GLU A 602 1 6
HELIX 27 AC9 GLU A 605 LEU A 610 1 6
HELIX 28 AD1 ASP A 615 VAL A 628 1 14
HELIX 29 AD2 TRP A 632 GLY A 644 1 13
HELIX 30 AD3 THR A 645 TRP A 647 5 3
HELIX 31 AD4 SER A 648 ILE A 660 1 13
HELIX 32 AD5 LEU A 662 GLU A 685 1 24
SHEET 1 AA1 2 GLU A 341 ILE A 342 0
SHEET 2 AA1 2 ILE A 383 ASN A 384 -1 O ILE A 383 N ILE A 342
LINK OG SER A 120 CA CA A 810 1555 1555 2.38
LINK OE1 GLU A 124 CA CA A 810 1555 1555 2.36
LINK OE2 GLU A 124 CA CA A 810 1555 1555 2.36
LINK OD2 ASP A 170 CA CA A 810 1555 1555 2.36
LINK O GLU A 239 BA BA A 804 1555 4555 2.75
LINK OD1 ASP A 240 BA BA A 804 1555 4555 2.75
LINK OD2 ASP A 240 BA BA A 805 1555 4555 2.75
LINK OD1 ASP A 335 CA CA A 809 1555 1555 2.36
LINK OD1 ASP A 337 CA CA A 809 1555 1555 2.36
LINK OD2 ASP A 337 CA CA A 809 1555 1555 2.36
LINK OD1 ASN A 339 CA CA A 809 1555 1555 2.38
LINK O GLU A 341 CA CA A 809 1555 1555 2.36
LINK OD1 ASP A 454 BA BA A 805 1555 1555 2.75
LINK OD2 ASP A 454 BA BA A 805 1555 1555 2.75
LINK OE2 GLU A 457 BA BA A 804 1555 1555 2.75
LINK OE1 GLU A 528 BA BA A 805 1555 1555 2.75
LINK OE1 GLU A 605 BA BA A 801 1555 1555 2.75
LINK OE1 GLU A 605 BA BA A 801 1555 4555 2.75
LINK BA B BA A 803 O HOH A 901 1555 1555 2.75
LINK BA B BA A 803 O HOH A 901 1555 4555 2.75
LINK BA B BA A 803 O HOH A 902 1555 1555 2.75
LINK BA B BA A 803 O HOH A 902 1555 4555 2.75
LINK BA A BA A 803 O HOH A 903 1555 1555 2.99
LINK BA A BA A 803 O HOH A 903 1555 4555 2.99
LINK BA A BA A 803 O HOH A 904 1555 1555 2.75
LINK BA A BA A 803 O HOH A 904 1555 4555 2.75
CISPEP 1 CYS A 101 LYS A 102 0 0.47
CISPEP 2 ASP A 103 ARG A 104 0 1.78
CISPEP 3 LEU A 112 PRO A 113 0 -4.47
CISPEP 4 GLN A 242 GLN A 243 0 1.81
CISPEP 5 ARG A 379 ASP A 380 0 6.67
CISPEP 6 ASP A 380 PHE A 381 0 -15.55
CISPEP 7 SER A 459 ALA A 460 0 -1.85
CISPEP 8 GLU A 602 LEU A 603 0 0.11
SITE 1 AC1 1 GLU A 605
SITE 1 AC2 4 HOH A 901 HOH A 902 HOH A 903 HOH A 904
SITE 1 AC3 3 GLU A 239 ASP A 240 GLU A 457
SITE 1 AC4 3 ASP A 240 ASP A 454 GLU A 528
SITE 1 AC5 1 ASN A 339
SITE 1 AC6 4 ASP A 335 ASP A 337 ASN A 339 GLU A 341
SITE 1 AC7 3 SER A 120 GLU A 124 ASP A 170
CRYST1 88.430 158.850 217.240 90.00 90.00 90.00 C 2 2 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 0.011308 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006295 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004603 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
