HEADER HYDROLASE/METAL BINDING PROTEIN 11-FEB-14 4OR9
TITLE CRYSTAL STRUCTURE OF HUMAN CALCINEURIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT
COMPND 3 BETA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CATALYTIC SUBUNIT;
COMPND 6 SYNONYM: CAM-PRP CATALYTIC SUBUNIT, CALMODULIN-DEPENDENT CALCINEURIN
COMPND 7 A SUBUNIT BETA ISOFORM;
COMPND 8 EC: 3.1.3.16;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CALCINEURIN SUBUNIT B TYPE 1;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: REGULATORY SUBUNIT;
COMPND 14 SYNONYM: PROTEIN PHOSPHATASE 2B REGULATORY SUBUNIT 1, PROTEIN
COMPND 15 PHOSPHATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM 1;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALNA2, CALNB, CNA2, PPP3CB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CNA2, CNB, PPP3R1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CALMODULIN-BINDING, HYDROLASE-METAL BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.LI,J.WANG,J.W.WU,Z.X.WANG
REVDAT 2 08-NOV-23 4OR9 1 REMARK SEQADV LINK
REVDAT 1 20-MAY-15 4OR9 0
JRNL AUTH S.J.LI,L.MA,J.WANG,C.LU,J.WANG,J.W.WU,Z.X.WANG
JRNL TITL COOPERATIVE AUTOINHIBITION AND MULTI-LEVEL ACTIVATION
JRNL TITL 2 MECHANISMS OF CALCINEURIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50855
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2575
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 47.7931 - 5.8409 0.99 2949 158 0.2010 0.2070
REMARK 3 2 5.8409 - 4.6374 1.00 2813 131 0.1681 0.1718
REMARK 3 3 4.6374 - 4.0515 1.00 2738 161 0.1362 0.1721
REMARK 3 4 4.0515 - 3.6812 1.00 2719 135 0.1723 0.2218
REMARK 3 5 3.6812 - 3.4175 1.00 2719 126 0.1877 0.2282
REMARK 3 6 3.4175 - 3.2160 1.00 2700 142 0.1876 0.2250
REMARK 3 7 3.2160 - 3.0550 1.00 2662 147 0.1893 0.2320
REMARK 3 8 3.0550 - 2.9220 1.00 2636 147 0.1878 0.2019
REMARK 3 9 2.9220 - 2.8096 1.00 2697 133 0.1920 0.2239
REMARK 3 10 2.8096 - 2.7126 1.00 2657 135 0.1942 0.2711
REMARK 3 11 2.7126 - 2.6278 1.00 2665 132 0.1990 0.2536
REMARK 3 12 2.6278 - 2.5527 1.00 2620 151 0.2026 0.2314
REMARK 3 13 2.5527 - 2.4855 1.00 2637 150 0.2026 0.2725
REMARK 3 14 2.4855 - 2.4249 1.00 2613 140 0.2027 0.2457
REMARK 3 15 2.4249 - 2.3697 1.00 2633 142 0.2000 0.2274
REMARK 3 16 2.3697 - 2.3193 1.00 2608 162 0.2068 0.2452
REMARK 3 17 2.3193 - 2.2729 0.99 2637 118 0.2150 0.2281
REMARK 3 18 2.2729 - 2.2300 0.99 2577 165 0.2155 0.2934
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 42.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.22310
REMARK 3 B22 (A**2) : 8.22310
REMARK 3 B33 (A**2) : -16.41150
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 : 0.007 4712
REMARK 3 ANGLE : 1.030 6379
REMARK 3 CHIRALITY : 0.076 683
REMARK 3 PLANARITY : 0.004 841
REMARK 3 DIHEDRAL : 14.328 1777
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 15:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.2884 67.0799 276.1405
REMARK 3 T TENSOR
REMARK 3 T11: 0.6173 T22: 0.4892
REMARK 3 T33: 0.3583 T12: -0.0686
REMARK 3 T13: 0.0984 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 0.7566 L22: 0.9377
REMARK 3 L33: 0.7166 L12: 0.1961
REMARK 3 L13: 0.0085 L23: 0.5423
REMARK 3 S TENSOR
REMARK 3 S11: -0.1347 S12: 0.2439 S13: -0.0601
REMARK 3 S21: -0.7157 S22: 0.1217 S23: -0.3067
REMARK 3 S31: -0.4693 S32: 0.4379 S33: -0.0323
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 52:334)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.7934 62.9337 306.3921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2688 T22: 0.2278
REMARK 3 T33: 0.2345 T12: -0.0199
REMARK 3 T13: 0.0362 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 2.0563 L22: 1.2684
REMARK 3 L33: 3.4376 L12: -0.0589
REMARK 3 L13: -0.4565 L23: -0.3165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0595 S12: -0.1275 S13: -0.1092
REMARK 3 S21: 0.0523 S22: -0.0818 S23: 0.0554
REMARK 3 S31: 0.2285 S32: 0.1023 S33: 0.1225
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 335:387)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1429 41.1617 282.9478
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.4167
REMARK 3 T33: 0.3570 T12: 0.0192
REMARK 3 T13: 0.0921 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 2.5276 L22: 2.9894
REMARK 3 L33: 2.5273 L12: -2.3325
REMARK 3 L13: -2.3586 L23: 2.8907
REMARK 3 S TENSOR
REMARK 3 S11: -0.4756 S12: -0.2583 S13: -0.5933
REMARK 3 S21: 0.3555 S22: 0.2011 S23: 0.4834
REMARK 3 S31: 0.3492 S32: 0.2787 S33: 0.1586
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 416:423)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.5299 37.9477 281.6295
REMARK 3 T TENSOR
REMARK 3 T11: 1.2723 T22: 1.2938
REMARK 3 T33: 0.4514 T12: -0.1724
REMARK 3 T13: 0.1028 T23: -0.1444
REMARK 3 L TENSOR
REMARK 3 L11: 6.5570 L22: 4.4304
REMARK 3 L33: 2.6262 L12: 1.6703
REMARK 3 L13: 4.0466 L23: 0.3145
REMARK 3 S TENSOR
REMARK 3 S11: 0.2720 S12: -0.7823 S13: 0.1176
REMARK 3 S21: 1.4959 S22: 0.2248 S23: 0.1852
REMARK 3 S31: 0.5312 S32: -0.0308 S33: -0.3578
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 478:495)
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0124 44.6898 304.4508
REMARK 3 T TENSOR
REMARK 3 T11: 1.1791 T22: 0.9141
REMARK 3 T33: 1.0061 T12: 0.1081
REMARK 3 T13: 0.1666 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 5.2437 L22: 3.7182
REMARK 3 L33: 4.2417 L12: -1.0522
REMARK 3 L13: 0.4028 L23: 0.8076
REMARK 3 S TENSOR
REMARK 3 S11: -0.1067 S12: -0.2533 S13: -0.6714
REMARK 3 S21: 0.3716 S22: 0.0083 S23: 0.3075
REMARK 3 S31: 0.8919 S32: 0.2123 S33: 0.1307
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 4:169)
REMARK 3 ORIGIN FOR THE GROUP (A): 90.0929 34.7893 268.5301
REMARK 3 T TENSOR
REMARK 3 T11: 0.3643 T22: 0.4396
REMARK 3 T33: 0.3630 T12: -0.0513
REMARK 3 T13: 0.0188 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 3.2093 L22: 2.9764
REMARK 3 L33: 2.0703 L12: -2.8340
REMARK 3 L13: -1.9021 L23: 1.5730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.2954 S13: -0.0870
REMARK 3 S21: 0.0470 S22: 0.0490 S23: 0.0503
REMARK 3 S31: -0.0644 S32: 0.1205 S33: -0.0404
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 4OR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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) : 0.97915
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
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 : 50855
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 18.60
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 17.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.842
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1AUI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, PH 5.8, 7% PEG3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 188.48733
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 94.24367
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 141.36550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 47.12183
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 235.60917
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 188.48733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 94.24367
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 47.12183
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 141.36550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 235.60917
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: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 PRO A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 PRO A 13
REMARK 465 PRO A 14
REMARK 465 THR A 388
REMARK 465 GLU A 389
REMARK 465 GLY A 390
REMARK 465 GLU A 391
REMARK 465 ASP A 392
REMARK 465 GLN A 393
REMARK 465 PHE A 394
REMARK 465 ASP A 395
REMARK 465 GLY A 396
REMARK 465 SER A 397
REMARK 465 ALA A 398
REMARK 465 ALA A 399
REMARK 465 ALA A 400
REMARK 465 ARG A 401
REMARK 465 LYS A 402
REMARK 465 GLU A 403
REMARK 465 ILE A 404
REMARK 465 ILE A 405
REMARK 465 ARG A 406
REMARK 465 ASN A 407
REMARK 465 LYS A 408
REMARK 465 ILE A 409
REMARK 465 ARG A 410
REMARK 465 ALA A 411
REMARK 465 ILE A 412
REMARK 465 GLY A 413
REMARK 465 LYS A 414
REMARK 465 MET A 415
REMARK 465 GLU A 424
REMARK 465 GLU A 425
REMARK 465 SER A 426
REMARK 465 GLU A 427
REMARK 465 SER A 428
REMARK 465 VAL A 429
REMARK 465 LEU A 430
REMARK 465 THR A 431
REMARK 465 LEU A 432
REMARK 465 LYS A 433
REMARK 465 GLY A 434
REMARK 465 LEU A 435
REMARK 465 THR A 436
REMARK 465 PRO A 437
REMARK 465 THR A 438
REMARK 465 GLY A 439
REMARK 465 MET A 440
REMARK 465 LEU A 441
REMARK 465 PRO A 442
REMARK 465 SER A 443
REMARK 465 GLY A 444
REMARK 465 VAL A 445
REMARK 465 LEU A 446
REMARK 465 ALA A 447
REMARK 465 GLY A 448
REMARK 465 GLY A 449
REMARK 465 ARG A 450
REMARK 465 GLN A 451
REMARK 465 THR A 452
REMARK 465 LEU A 453
REMARK 465 GLN A 454
REMARK 465 SER A 455
REMARK 465 ALA A 456
REMARK 465 THR A 457
REMARK 465 VAL A 458
REMARK 465 GLU A 459
REMARK 465 ALA A 460
REMARK 465 ILE A 461
REMARK 465 GLU A 462
REMARK 465 ALA A 463
REMARK 465 GLU A 464
REMARK 465 LYS A 465
REMARK 465 ALA A 466
REMARK 465 ILE A 467
REMARK 465 ARG A 468
REMARK 465 GLY A 469
REMARK 465 PHE A 470
REMARK 465 SER A 471
REMARK 465 PRO A 472
REMARK 465 PRO A 473
REMARK 465 HIS A 474
REMARK 465 ARG A 475
REMARK 465 ILE A 476
REMARK 465 CYS A 477
REMARK 465 LYS A 496
REMARK 465 ASP A 497
REMARK 465 ALA A 498
REMARK 465 VAL A 499
REMARK 465 GLN A 500
REMARK 465 GLN A 501
REMARK 465 ASP A 502
REMARK 465 GLY A 503
REMARK 465 PHE A 504
REMARK 465 ASN A 505
REMARK 465 SER A 506
REMARK 465 LEU A 507
REMARK 465 ASN A 508
REMARK 465 THR A 509
REMARK 465 ALA A 510
REMARK 465 HIS A 511
REMARK 465 ALA A 512
REMARK 465 THR A 513
REMARK 465 GLU A 514
REMARK 465 ASN A 515
REMARK 465 HIS A 516
REMARK 465 GLY A 517
REMARK 465 THR A 518
REMARK 465 GLY A 519
REMARK 465 ASN A 520
REMARK 465 HIS A 521
REMARK 465 THR A 522
REMARK 465 ALA A 523
REMARK 465 GLN A 524
REMARK 465 MET B 0
REMARK 465 GLY B 1
REMARK 465 ASN B 2
REMARK 465 GLU B 3
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 130 156.07 78.19
REMARK 500 ARG A 131 -57.12 74.39
REMARK 500 PHE A 169 -158.06 -85.25
REMARK 500 TYR A 179 -105.48 -133.30
REMARK 500 SER A 266 -152.83 60.95
REMARK 500 ALA A 289 -127.23 -133.12
REMARK 500 HIS A 290 -20.06 76.81
REMARK 500 ASN A 319 51.82 39.37
REMARK 500 ASP A 322 12.97 58.43
REMARK 500 VAL A 421 -172.35 -69.19
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 FE A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 99 OD2
REMARK 620 2 HIS A 101 NE2 108.4
REMARK 620 3 ASP A 127 OD2 95.3 95.6
REMARK 620 4 HOH A 862 O 83.1 96.8 167.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 127 OD2
REMARK 620 2 ASN A 159 OD1 83.1
REMARK 620 3 HIS A 208 NE2 77.0 77.5
REMARK 620 4 HIS A 290 ND1 168.5 99.5 92.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 30 OD1
REMARK 620 2 ASP B 32 OD1 72.3
REMARK 620 3 SER B 34 OG 89.1 74.8
REMARK 620 4 SER B 36 O 73.2 136.8 79.5
REMARK 620 5 GLU B 41 OE2 79.4 79.3 153.8 118.6
REMARK 620 6 GLU B 41 OE1 95.9 125.9 159.3 82.7 46.7
REMARK 620 7 HOH B 353 O 166.8 96.8 80.7 112.6 106.4 96.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 62 OD1
REMARK 620 2 ASP B 64 OD1 72.3
REMARK 620 3 ASN B 66 OD1 80.3 79.5
REMARK 620 4 GLU B 68 O 75.3 143.7 79.2
REMARK 620 5 GLU B 73 OE1 101.4 121.1 159.1 81.2
REMARK 620 6 GLU B 73 OE2 86.5 71.2 150.3 123.0 49.9
REMARK 620 7 HOH B 354 O 164.6 94.5 89.7 114.4 92.1 96.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 99 OD1
REMARK 620 2 ASP B 101 OD1 84.7
REMARK 620 3 ASP B 103 OD1 89.9 75.8
REMARK 620 4 TYR B 105 O 94.3 154.4 78.6
REMARK 620 5 GLU B 110 OE2 95.9 123.2 160.6 82.5
REMARK 620 6 GLU B 110 OE1 95.0 77.7 152.4 127.9 45.6
REMARK 620 7 HOH B 306 O 171.2 86.6 86.3 92.8 90.3 84.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 140 OD1
REMARK 620 2 ASP B 142 OD1 92.0
REMARK 620 3 ASP B 142 OD2 98.6 41.4
REMARK 620 4 ASP B 144 OD1 81.0 80.3 121.7
REMARK 620 5 ARG B 146 O 91.2 147.8 166.7 68.6
REMARK 620 6 GLU B 151 OE1 103.5 132.6 91.6 145.7 77.3
REMARK 620 7 GLU B 151 OE2 86.3 93.2 53.2 165.5 119.1 44.9
REMARK 620 8 HOH B 309 O 155.2 64.4 69.5 87.0 104.5 98.7 102.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ORA RELATED DB: PDB
REMARK 900 RELATED ID: 4ORB RELATED DB: PDB
REMARK 900 RELATED ID: 4ORC RELATED DB: PDB
DBREF 4OR9 A 1 524 UNP P16298 PP2BB_HUMAN 1 524
DBREF 4OR9 B 0 169 UNP P63098 CANB1_HUMAN 1 170
SEQADV 4OR9 MET A -19 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 GLY A -18 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 SER A -17 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 SER A -16 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -15 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -14 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -13 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -12 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -11 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A -10 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 SER A -9 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 SER A -8 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 GLY A -7 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 LEU A -6 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 VAL A -5 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 PRO A -4 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 ARG A -3 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 GLY A -2 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 SER A -1 UNP P16298 EXPRESSION TAG
SEQADV 4OR9 HIS A 0 UNP P16298 EXPRESSION TAG
SEQRES 1 A 544 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 544 LEU VAL PRO ARG GLY SER HIS MET ALA ALA PRO GLU PRO
SEQRES 3 A 544 ALA ARG ALA ALA PRO PRO PRO PRO PRO PRO PRO PRO PRO
SEQRES 4 A 544 PRO PRO GLY ALA ASP ARG VAL VAL LYS ALA VAL PRO PHE
SEQRES 5 A 544 PRO PRO THR HIS ARG LEU THR SER GLU GLU VAL PHE ASP
SEQRES 6 A 544 LEU ASP GLY ILE PRO ARG VAL ASP VAL LEU LYS ASN HIS
SEQRES 7 A 544 LEU VAL LYS GLU GLY ARG VAL ASP GLU GLU ILE ALA LEU
SEQRES 8 A 544 ARG ILE ILE ASN GLU GLY ALA ALA ILE LEU ARG ARG GLU
SEQRES 9 A 544 LYS THR MET ILE GLU VAL GLU ALA PRO ILE THR VAL CYS
SEQRES 10 A 544 GLY ASP ILE HIS GLY GLN PHE PHE ASP LEU MET LYS LEU
SEQRES 11 A 544 PHE GLU VAL GLY GLY SER PRO ALA ASN THR ARG TYR LEU
SEQRES 12 A 544 PHE LEU GLY ASP TYR VAL ASP ARG GLY TYR PHE SER ILE
SEQRES 13 A 544 GLU CYS VAL LEU TYR LEU TRP VAL LEU LYS ILE LEU TYR
SEQRES 14 A 544 PRO SER THR LEU PHE LEU LEU ARG GLY ASN HIS GLU CYS
SEQRES 15 A 544 ARG HIS LEU THR GLU TYR PHE THR PHE LYS GLN GLU CYS
SEQRES 16 A 544 LYS ILE LYS TYR SER GLU ARG VAL TYR GLU ALA CYS MET
SEQRES 17 A 544 GLU ALA PHE ASP SER LEU PRO LEU ALA ALA LEU LEU ASN
SEQRES 18 A 544 GLN GLN PHE LEU CYS VAL HIS GLY GLY LEU SER PRO GLU
SEQRES 19 A 544 ILE HIS THR LEU ASP ASP ILE ARG ARG LEU ASP ARG PHE
SEQRES 20 A 544 LYS GLU PRO PRO ALA PHE GLY PRO MET CYS ASP LEU LEU
SEQRES 21 A 544 TRP SER ASP PRO SER GLU ASP PHE GLY ASN GLU LYS SER
SEQRES 22 A 544 GLN GLU HIS PHE SER HIS ASN THR VAL ARG GLY CYS SER
SEQRES 23 A 544 TYR PHE TYR ASN TYR PRO ALA VAL CYS GLU PHE LEU GLN
SEQRES 24 A 544 ASN ASN ASN LEU LEU SER ILE ILE ARG ALA HIS GLU ALA
SEQRES 25 A 544 GLN ASP ALA GLY TYR ARG MET TYR ARG LYS SER GLN THR
SEQRES 26 A 544 THR GLY PHE PRO SER LEU ILE THR ILE PHE SER ALA PRO
SEQRES 27 A 544 ASN TYR LEU ASP VAL TYR ASN ASN LYS ALA ALA VAL LEU
SEQRES 28 A 544 LYS TYR GLU ASN ASN VAL MET ASN ILE ARG GLN PHE ASN
SEQRES 29 A 544 CYS SER PRO HIS PRO TYR TRP LEU PRO ASN PHE MET ASP
SEQRES 30 A 544 VAL PHE THR TRP SER LEU PRO PHE VAL GLY GLU LYS VAL
SEQRES 31 A 544 THR GLU MET LEU VAL ASN VAL LEU SER ILE CYS SER ASP
SEQRES 32 A 544 ASP GLU LEU MET THR GLU GLY GLU ASP GLN PHE ASP GLY
SEQRES 33 A 544 SER ALA ALA ALA ARG LYS GLU ILE ILE ARG ASN LYS ILE
SEQRES 34 A 544 ARG ALA ILE GLY LYS MET ALA ARG VAL PHE SER VAL LEU
SEQRES 35 A 544 ARG GLU GLU SER GLU SER VAL LEU THR LEU LYS GLY LEU
SEQRES 36 A 544 THR PRO THR GLY MET LEU PRO SER GLY VAL LEU ALA GLY
SEQRES 37 A 544 GLY ARG GLN THR LEU GLN SER ALA THR VAL GLU ALA ILE
SEQRES 38 A 544 GLU ALA GLU LYS ALA ILE ARG GLY PHE SER PRO PRO HIS
SEQRES 39 A 544 ARG ILE CYS SER PHE GLU GLU ALA LYS GLY LEU ASP ARG
SEQRES 40 A 544 ILE ASN GLU ARG MET PRO PRO ARG LYS ASP ALA VAL GLN
SEQRES 41 A 544 GLN ASP GLY PHE ASN SER LEU ASN THR ALA HIS ALA THR
SEQRES 42 A 544 GLU ASN HIS GLY THR GLY ASN HIS THR ALA GLN
SEQRES 1 B 170 MET GLY ASN GLU ALA SER TYR PRO LEU GLU MET CYS SER
SEQRES 2 B 170 HIS PHE ASP ALA ASP GLU ILE LYS ARG LEU GLY LYS ARG
SEQRES 3 B 170 PHE LYS LYS LEU ASP LEU ASP ASN SER GLY SER LEU SER
SEQRES 4 B 170 VAL GLU GLU PHE MET SER LEU PRO GLU LEU GLN GLN ASN
SEQRES 5 B 170 PRO LEU VAL GLN ARG VAL ILE ASP ILE PHE ASP THR ASP
SEQRES 6 B 170 GLY ASN GLY GLU VAL ASP PHE LYS GLU PHE ILE GLU GLY
SEQRES 7 B 170 VAL SER GLN PHE SER VAL LYS GLY ASP LYS GLU GLN LYS
SEQRES 8 B 170 LEU ARG PHE ALA PHE ARG ILE TYR ASP MET ASP LYS ASP
SEQRES 9 B 170 GLY TYR ILE SER ASN GLY GLU LEU PHE GLN VAL LEU LYS
SEQRES 10 B 170 MET MET VAL GLY ASN ASN LEU LYS ASP THR GLN LEU GLN
SEQRES 11 B 170 GLN ILE VAL ASP LYS THR ILE ILE ASN ALA ASP LYS ASP
SEQRES 12 B 170 GLY ASP GLY ARG ILE SER PHE GLU GLU PHE CYS ALA VAL
SEQRES 13 B 170 VAL GLY GLY LEU ASP ILE HIS LYS LYS MET VAL VAL ASP
SEQRES 14 B 170 VAL
HET FE A 601 1
HET ZN A 602 1
HET CA B 201 1
HET CA B 202 1
HET CA B 203 1
HET CA B 204 1
HETNAM FE FE (III) ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 FE FE 3+
FORMUL 4 ZN ZN 2+
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *251(H2 O)
HELIX 1 1 THR A 39 PHE A 44 1 6
HELIX 2 2 ARG A 51 LYS A 61 1 11
HELIX 3 3 ASP A 66 ARG A 83 1 18
HELIX 4 4 GLN A 103 GLY A 115 1 13
HELIX 5 5 PHE A 134 TYR A 149 1 16
HELIX 6 6 CYS A 162 PHE A 169 1 8
HELIX 7 7 THR A 170 TYR A 179 1 10
HELIX 8 8 SER A 180 SER A 193 1 14
HELIX 9 9 THR A 217 ARG A 223 1 7
HELIX 10 10 GLY A 234 SER A 242 1 9
HELIX 11 11 ASN A 270 ASN A 282 1 13
HELIX 12 12 ASN A 319 VAL A 323 5 5
HELIX 13 13 LEU A 352 MET A 356 5 5
HELIX 14 14 ASP A 357 SER A 379 1 23
HELIX 15 15 PHE A 479 ASP A 486 1 8
HELIX 16 16 ARG A 487 ARG A 491 5 5
HELIX 17 17 ASP B 15 ASP B 30 1 16
HELIX 18 18 SER B 38 MET B 43 1 6
HELIX 19 19 LEU B 45 GLN B 49 5 5
HELIX 20 20 LEU B 53 ASP B 62 1 10
HELIX 21 21 PHE B 71 GLN B 80 1 10
HELIX 22 22 ASP B 86 ASP B 99 1 14
HELIX 23 23 SER B 107 GLY B 120 1 14
HELIX 24 24 LYS B 124 ASP B 140 1 17
HELIX 25 25 PHE B 149 GLY B 157 1 9
HELIX 26 26 ASP B 160 LYS B 164 5 5
SHEET 1 A 6 MET A 87 VAL A 90 0
SHEET 2 A 6 ALA A 197 LEU A 200 1 O LEU A 199 N ILE A 88
SHEET 3 A 6 PHE A 204 VAL A 207 -1 O CYS A 206 N ALA A 198
SHEET 4 A 6 SER A 285 ARG A 288 1 O ILE A 287 N LEU A 205
SHEET 5 A 6 LEU A 311 ILE A 314 1 O ILE A 312 N ARG A 288
SHEET 6 A 6 TYR A 297 MET A 299 -1 N ARG A 298 O THR A 313
SHEET 1 B 5 LEU A 153 LEU A 155 0
SHEET 2 B 5 TYR A 122 PHE A 124 1 N PHE A 124 O PHE A 154
SHEET 3 B 5 ILE A 94 CYS A 97 1 N CYS A 97 O LEU A 123
SHEET 4 B 5 ALA A 328 GLU A 334 -1 O LEU A 331 N VAL A 96
SHEET 5 B 5 VAL A 337 PHE A 343 -1 O ASN A 339 N LYS A 332
SHEET 1 C 3 ASP A 243 PRO A 244 0
SHEET 2 C 3 TYR A 267 TYR A 269 1 O TYR A 269 N ASP A 243
SHEET 3 C 3 PHE A 257 HIS A 259 -1 N SER A 258 O PHE A 268
SHEET 1 D 2 SER B 36 LEU B 37 0
SHEET 2 D 2 VAL B 69 ASP B 70 -1 O VAL B 69 N LEU B 37
SHEET 1 E 2 TYR B 105 ILE B 106 0
SHEET 2 E 2 ILE B 147 SER B 148 -1 O ILE B 147 N ILE B 106
LINK OD2 ASP A 99 FE FE A 601 1555 1555 2.23
LINK NE2 HIS A 101 FE FE A 601 1555 1555 2.16
LINK OD2 ASP A 127 FE FE A 601 1555 1555 2.48
LINK OD2 ASP A 127 ZN ZN A 602 1555 1555 2.58
LINK OD1 ASN A 159 ZN ZN A 602 1555 1555 2.22
LINK NE2 HIS A 208 ZN ZN A 602 1555 1555 2.41
LINK ND1 HIS A 290 ZN ZN A 602 1555 1555 2.26
LINK FE FE A 601 O HOH A 862 1555 1555 2.46
LINK OD1 ASP B 30 CA CA B 201 1555 1555 2.53
LINK OD1 ASP B 32 CA CA B 201 1555 1555 2.78
LINK OG SER B 34 CA CA B 201 1555 1555 2.96
LINK O SER B 36 CA CA B 201 1555 1555 2.59
LINK OE2 GLU B 41 CA CA B 201 1555 1555 2.78
LINK OE1 GLU B 41 CA CA B 201 1555 1555 2.78
LINK OD1 ASP B 62 CA CA B 202 1555 1555 2.30
LINK OD1 ASP B 64 CA CA B 202 1555 1555 2.40
LINK OD1 ASN B 66 CA CA B 202 1555 1555 2.58
LINK O GLU B 68 CA CA B 202 1555 1555 2.16
LINK OE1 GLU B 73 CA CA B 202 1555 1555 2.56
LINK OE2 GLU B 73 CA CA B 202 1555 1555 2.65
LINK OD1 ASP B 99 CA CA B 203 1555 1555 2.65
LINK OD1 ASP B 101 CA CA B 203 1555 1555 2.76
LINK OD1 ASP B 103 CA CA B 203 1555 1555 2.82
LINK O TYR B 105 CA CA B 203 1555 1555 2.63
LINK OE2 GLU B 110 CA CA B 203 1555 1555 2.81
LINK OE1 GLU B 110 CA CA B 203 1555 1555 2.88
LINK OD1 ASP B 140 CA CA B 204 1555 1555 2.79
LINK OD1 ASP B 142 CA CA B 204 1555 1555 3.04
LINK OD2 ASP B 142 CA CA B 204 1555 1555 3.17
LINK OD1 ASP B 144 CA CA B 204 1555 1555 2.74
LINK O ARG B 146 CA CA B 204 1555 1555 2.77
LINK OE1 GLU B 151 CA CA B 204 1555 1555 2.83
LINK OE2 GLU B 151 CA CA B 204 1555 1555 2.90
LINK CA CA B 201 O HOH B 353 1555 1555 2.92
LINK CA CA B 202 O HOH B 354 1555 1555 2.59
LINK CA CA B 203 O HOH B 306 1555 1555 2.92
LINK CA CA B 204 O HOH B 309 1555 1555 2.99
CISPEP 1 ALA A 92 PRO A 93 0 2.02
SITE 1 AC1 5 ASP A 99 HIS A 101 ASP A 127 ZN A 602
SITE 2 AC1 5 HOH A 862
SITE 1 AC2 5 ASP A 127 ASN A 159 HIS A 208 HIS A 290
SITE 2 AC2 5 FE A 601
SITE 1 AC3 6 ASP B 30 ASP B 32 SER B 34 SER B 36
SITE 2 AC3 6 GLU B 41 HOH B 353
SITE 1 AC4 6 ASP B 62 ASP B 64 ASN B 66 GLU B 68
SITE 2 AC4 6 GLU B 73 HOH B 354
SITE 1 AC5 6 ASP B 99 ASP B 101 ASP B 103 TYR B 105
SITE 2 AC5 6 GLU B 110 HOH B 306
SITE 1 AC6 6 ASP B 140 ASP B 142 ASP B 144 ARG B 146
SITE 2 AC6 6 GLU B 151 HOH B 309
CRYST1 110.871 110.871 282.731 90.00 90.00 120.00 P 65 2 2 12
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 0.009019 0.005207 0.000000 0.00000
SCALE2 0.000000 0.010415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
