HEADER ELECTRON TRANSPORT 28-APR-15 4ZIZ
TITLE SERIAL FEMTOSECOND CRYSTALLOGRAPHY OF SOLUBLE PROTEINS IN LIPIDIC
TITLE 2 CUBIC PHASE (C-PHYCOCYANIN FROM T. ELONGATUS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-PHYCOCYANIN ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: C-PHYCOCYANIN BETA CHAIN;
COMPND 6 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1
KEYWDS FREE ELECTRON LASER, PHYCOCYANIN, LIPIDIC CUBIC PHASE, ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.FROMME,A.ISHCHENKO,M.METZ,S.ROY-CHOWDHURY,S.BASU,S.BOUTET,P.FROMME,
AUTHOR 2 T.A.WHITE,A.BARTY,J.C.H.SPENCE,U.WEIERSTALL,W.LIU,V.CHEREZOV
REVDAT 8 13-MAR-24 4ZIZ 1 SOURCE
REVDAT 7 27-SEP-23 4ZIZ 1 REMARK
REVDAT 6 14-FEB-18 4ZIZ 1 REMARK
REVDAT 5 22-NOV-17 4ZIZ 1 REMARK
REVDAT 4 08-FEB-17 4ZIZ 1 JRNL
REVDAT 3 14-DEC-16 4ZIZ 1 TITLE JRNL
REVDAT 2 02-SEP-15 4ZIZ 1 AUTHOR JRNL REMARK
REVDAT 1 19-AUG-15 4ZIZ 0
JRNL AUTH R.FROMME,A.ISHCHENKO,M.METZ,S.R.CHOWDHURY,S.BASU,S.BOUTET,
JRNL AUTH 2 P.FROMME,T.A.WHITE,A.BARTY,J.C.SPENCE,U.WEIERSTALL,W.LIU,
JRNL AUTH 3 V.CHEREZOV
JRNL TITL SERIAL FEMTOSECOND CRYSTALLOGRAPHY OF SOLUBLE PROTEINS IN
JRNL TITL 2 LIPIDIC CUBIC PHASE.
JRNL REF IUCRJ V. 2 545 2015
JRNL REFN ESSN 2052-2525
JRNL PMID 26306196
JRNL DOI 10.1107/S2052252515013160
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1894
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 40257
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1838
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 31.5659 - 4.1121 1.00 3042 146 0.1668 0.1906
REMARK 3 2 4.1121 - 3.2649 1.00 2986 142 0.1517 0.2181
REMARK 3 3 3.2649 - 2.8525 1.00 2958 142 0.1862 0.2487
REMARK 3 4 2.8525 - 2.5919 1.00 2963 141 0.1978 0.2378
REMARK 3 5 2.5919 - 2.4062 1.00 2953 142 0.1997 0.2596
REMARK 3 6 2.4062 - 2.2643 1.00 2944 141 0.2201 0.2876
REMARK 3 7 2.2643 - 2.1510 1.00 2949 141 0.2277 0.2916
REMARK 3 8 2.1510 - 2.0574 1.00 2933 140 0.2662 0.3200
REMARK 3 9 2.0574 - 1.9782 1.00 2943 141 0.3025 0.3648
REMARK 3 10 1.9782 - 1.9099 1.00 2943 141 0.3014 0.3109
REMARK 3 11 1.9099 - 1.8502 1.00 2935 140 0.3758 0.3962
REMARK 3 12 1.8502 - 1.7973 1.00 2918 140 0.4387 0.5017
REMARK 3 13 1.7973 - 1.7500 1.00 2952 141 0.5053 0.5005
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) : 33.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 2674
REMARK 3 ANGLE : 1.702 3636
REMARK 3 CHIRALITY : 0.052 402
REMARK 3 PLANARITY : 0.006 470
REMARK 3 DIHEDRAL : 15.529 954
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3417 2.9373 -5.3403
REMARK 3 T TENSOR
REMARK 3 T11: 0.3484 T22: 0.3105
REMARK 3 T33: 0.3388 T12: 0.0007
REMARK 3 T13: 0.0543 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.2804 L22: 0.1370
REMARK 3 L33: 0.1822 L12: 0.0252
REMARK 3 L13: 0.0750 L23: -0.1410
REMARK 3 S TENSOR
REMARK 3 S11: 0.1437 S12: 0.0424 S13: 0.0745
REMARK 3 S21: 0.0435 S22: -0.1523 S23: 0.1921
REMARK 3 S31: -0.0248 S32: -0.0745 S33: -0.0004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8541 -19.5696 -6.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2902 T22: 0.3022
REMARK 3 T33: 0.3083 T12: -0.0062
REMARK 3 T13: 0.0046 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.4318 L22: 1.3783
REMARK 3 L33: 0.2262 L12: -0.6434
REMARK 3 L13: -0.1679 L23: 0.5111
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: 0.0879 S13: -0.0125
REMARK 3 S21: -0.0820 S22: 0.0262 S23: -0.3689
REMARK 3 S31: 0.0191 S32: 0.0733 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9179 -43.4740 -10.1804
REMARK 3 T TENSOR
REMARK 3 T11: 0.3990 T22: 0.2910
REMARK 3 T33: 0.3491 T12: 0.0080
REMARK 3 T13: 0.0435 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0876 L22: 0.1048
REMARK 3 L33: 0.1010 L12: 0.0327
REMARK 3 L13: 0.0607 L23: -0.0086
REMARK 3 S TENSOR
REMARK 3 S11: -0.1131 S12: 0.2553 S13: -0.4566
REMARK 3 S21: -0.1415 S22: -0.0785 S23: 0.0664
REMARK 3 S31: 0.5780 S32: 0.3451 S33: 0.0055
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3362 -24.0539 -6.1646
REMARK 3 T TENSOR
REMARK 3 T11: 0.2707 T22: 0.2714
REMARK 3 T33: 0.2522 T12: 0.0012
REMARK 3 T13: 0.0228 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.9530 L22: 1.7730
REMARK 3 L33: 0.2989 L12: -0.0683
REMARK 3 L13: -0.2329 L23: 0.1085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: -0.0075 S13: 0.0892
REMARK 3 S21: -0.0310 S22: 0.0060 S23: -0.0164
REMARK 3 S31: -0.0093 S32: -0.0587 S33: -0.0006
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8090 11.7950 18.1094
REMARK 3 T TENSOR
REMARK 3 T11: 0.3671 T22: 0.3078
REMARK 3 T33: 0.3347 T12: -0.0544
REMARK 3 T13: -0.0428 T23: 0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.2547 L22: 0.4157
REMARK 3 L33: 0.0779 L12: -0.2403
REMARK 3 L13: 0.0223 L23: 0.0993
REMARK 3 S TENSOR
REMARK 3 S11: 0.0905 S12: 0.0133 S13: -0.1349
REMARK 3 S21: 0.4112 S22: -0.0083 S23: 0.1777
REMARK 3 S31: 0.2198 S32: -0.1957 S33: -0.0012
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 21 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.1592 6.1693 16.8901
REMARK 3 T TENSOR
REMARK 3 T11: 0.4953 T22: 0.3251
REMARK 3 T33: 0.5492 T12: 0.0299
REMARK 3 T13: -0.1889 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3738 L22: 0.0520
REMARK 3 L33: 0.7426 L12: 0.1394
REMARK 3 L13: -0.5269 L23: -0.1965
REMARK 3 S TENSOR
REMARK 3 S11: -0.3792 S12: -0.3104 S13: 0.1269
REMARK 3 S21: 1.1451 S22: 0.4455 S23: -0.5147
REMARK 3 S31: 0.5825 S32: -0.0613 S33: -0.0361
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5865 -19.7956 15.1922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3072 T22: 0.2453
REMARK 3 T33: 0.2301 T12: 0.0060
REMARK 3 T13: -0.0012 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.1417 L22: 0.8834
REMARK 3 L33: 0.1164 L12: 0.2795
REMARK 3 L13: 0.3503 L23: 0.1716
REMARK 3 S TENSOR
REMARK 3 S11: 0.0764 S12: -0.0640 S13: -0.1149
REMARK 3 S21: 0.1611 S22: -0.0893 S23: -0.1642
REMARK 3 S31: -0.0324 S32: 0.0078 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7887 -12.9071 21.4338
REMARK 3 T TENSOR
REMARK 3 T11: 0.4409 T22: 0.3184
REMARK 3 T33: 0.2531 T12: -0.0159
REMARK 3 T13: 0.0336 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 0.4955 L22: 0.5238
REMARK 3 L33: 0.3722 L12: 0.4381
REMARK 3 L13: 0.0494 L23: 0.1541
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.3278 S13: 0.2339
REMARK 3 S21: 0.4092 S22: -0.0394 S23: 0.0879
REMARK 3 S31: 0.0949 S32: -0.0411 S33: -0.0012
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8957 -12.3184 19.8646
REMARK 3 T TENSOR
REMARK 3 T11: 0.4215 T22: 0.2823
REMARK 3 T33: 0.3176 T12: -0.0165
REMARK 3 T13: -0.0600 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.3277 L22: 0.5061
REMARK 3 L33: 0.2669 L12: 0.0779
REMARK 3 L13: 0.1879 L23: 0.0361
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -0.2348 S13: -0.0748
REMARK 3 S21: 0.4648 S22: -0.1645 S23: -0.1378
REMARK 3 S31: 0.0420 S32: 0.0719 S33: 0.0000
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 4ZIZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : CXI
REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.56
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44284
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 31.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 139.4
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 36.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3L0F
REMARK 200
REMARK 200 REMARK: 10 X10X5 UM SIZE CRYSTALS IN TOTAL 6,171
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGCL2 , 17 %PEG 3,350, PH 7,
REMARK 280 BATCH MODE, TEMPERATURE 298K
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 93.19000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.80327
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 20.11333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 93.19000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 53.80327
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 20.11333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 93.19000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 53.80327
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 20.11333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 93.19000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 53.80327
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 20.11333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 93.19000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 53.80327
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 20.11333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 93.19000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 53.80327
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 20.11333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 107.60654
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 40.22667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 107.60654
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 40.22667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 107.60654
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 40.22667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 107.60654
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 40.22667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 107.60654
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 40.22667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 107.60654
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 40.22667
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 60570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -511.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 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 B 309 LIES ON A SPECIAL POSITION.
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 SG CYS A 84 HAC2 CYC A 201 0.88
REMARK 500 SG CYS B 153 HAC2 CYC B 202 0.89
REMARK 500 SG CYS B 82 HAC2 CYC B 201 0.94
REMARK 500 HZ3 LYS A 81 O HOH A 303 1.40
REMARK 500 HH12 ARG B 77 O2D CYC B 201 1.50
REMARK 500 HE ARG B 15 OE1 GLU B 17 1.56
REMARK 500 NH1 ARG A 42 O HOH A 301 2.03
REMARK 500 OD2 ASP B 165 O HOH B 301 2.09
REMARK 500 OD1 ASN A 47 O HOH A 302 2.11
REMARK 500 OD2 ASP B 152 O HOH B 302 2.12
REMARK 500 NZ LYS A 81 O HOH A 303 2.14
REMARK 500 O HOH B 355 O HOH B 357 2.16
REMARK 500 O HOH A 352 O HOH A 379 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 379 O HOH A 379 6555 1.30
REMARK 500 O HOH A 386 O HOH A 386 6555 1.52
REMARK 500 HH11 ARG B 57 O1D CYC A 201 6555 1.58
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 ALA A 75 45.13 -101.00
REMARK 500 THR B 75 150.02 75.98
REMARK 500 CYS B 109 -54.14 -129.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 376 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 377 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B 378 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 379 DISTANCE = 7.73 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CYC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CYC B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CYC B 202
DBREF 4ZIZ A 1 162 UNP P50032 PHCA_THEEB 1 162
DBREF 4ZIZ B 1 172 UNP P50033 PHCB_THEEB 1 172
SEQRES 1 A 162 MET LYS THR PRO ILE THR GLU ALA ILE ALA ALA ALA ASP
SEQRES 2 A 162 THR GLN GLY ARG PHE LEU SER ASN THR GLU LEU GLN ALA
SEQRES 3 A 162 VAL ASP GLY ARG PHE LYS ARG ALA VAL ALA SER MET GLU
SEQRES 4 A 162 ALA ALA ARG ALA LEU THR ASN ASN ALA GLN SER LEU ILE
SEQRES 5 A 162 ASP GLY ALA ALA GLN ALA VAL TYR GLN LYS PHE PRO TYR
SEQRES 6 A 162 THR THR THR MET GLN GLY SER GLN TYR ALA SER THR PRO
SEQRES 7 A 162 GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR TYR
SEQRES 8 A 162 LEU ARG MET VAL THR TYR CYS LEU VAL ALA GLY GLY THR
SEQRES 9 A 162 GLY PRO MET ASP GLU TYR LEU ILE ALA GLY LEU SER GLU
SEQRES 10 A 162 ILE ASN SER THR PHE ASP LEU SER PRO SER TRP TYR ILE
SEQRES 11 A 162 GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU THR
SEQRES 12 A 162 GLY GLN ALA ALA VAL GLU ALA ASN ALA TYR ILE ASP TYR
SEQRES 13 A 162 ALA ILE ASN ALA LEU SER
SEQRES 1 B 172 MET LEU ASP ALA PHE ALA LYS VAL VAL ALA GLN ALA ASP
SEQRES 2 B 172 ALA ARG GLY GLU PHE LEU THR ASN ALA GLN PHE ASP ALA
SEQRES 3 B 172 LEU SER ASN LEU VAL LYS GLU GLY ASN LYS ARG LEU ASP
SEQRES 4 B 172 ALA VAL ASN ARG ILE THR SER ASN ALA SER THR ILE VAL
SEQRES 5 B 172 ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO GLN
SEQRES 6 B 172 LEU ILE GLN PRO GLY GLY MEN ALA TYR THR ASN ARG ARG
SEQRES 7 B 172 MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU ARG
SEQRES 8 B 172 TYR VAL THR TYR ALA ILE LEU ALA GLY ASP SER SER VAL
SEQRES 9 B 172 LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR TYR
SEQRES 10 B 172 GLN ALA LEU GLY THR PRO GLY SER SER VAL ALA VAL ALA
SEQRES 11 B 172 ILE GLN LYS MET LYS ASP ALA ALA ILE ALA ILE ALA ASN
SEQRES 12 B 172 ASP PRO ASN GLY ILE THR PRO GLY ASP CYS SER ALA LEU
SEQRES 13 B 172 MET SER GLU ILE ALA GLY TYR PHE ASP ARG ALA ALA ALA
SEQRES 14 B 172 ALA VAL ALA
MODRES 4ZIZ MEN B 72 ASN MODIFIED RESIDUE
HET MEN B 72 16
HET CYC A 201 81
HET CYC B 201 81
HET CYC B 202 81
HETNAM MEN N-METHYL ASPARAGINE
HETNAM CYC PHYCOCYANOBILIN
FORMUL 2 MEN C5 H10 N2 O3
FORMUL 3 CYC 3(C33 H40 N4 O6)
FORMUL 6 HOH *166(H2 O)
HELIX 1 AA1 THR A 3 GLN A 15 1 13
HELIX 2 AA2 SER A 20 ASN A 47 1 28
HELIX 3 AA3 ASN A 47 PHE A 63 1 17
HELIX 4 AA4 PRO A 64 THR A 68 5 5
HELIX 5 AA5 THR A 77 GLY A 102 1 26
HELIX 6 AA6 THR A 104 LEU A 111 1 8
HELIX 7 AA7 GLY A 114 PHE A 122 1 9
HELIX 8 AA8 SER A 125 HIS A 140 1 16
HELIX 9 AA9 THR A 143 LEU A 161 1 19
HELIX 10 AB1 ASP B 3 ARG B 15 1 13
HELIX 11 AB2 THR B 20 GLU B 33 1 14
HELIX 12 AB3 GLU B 33 ASN B 47 1 15
HELIX 13 AB4 ASN B 47 GLN B 63 1 17
HELIX 14 AB5 PRO B 64 GLN B 68 5 5
HELIX 15 AB6 THR B 75 GLY B 100 1 26
HELIX 16 AB7 SER B 102 CYS B 109 1 8
HELIX 17 AB8 GLY B 112 GLY B 121 1 10
HELIX 18 AB9 PRO B 123 ASN B 143 1 21
HELIX 19 AC1 CYS B 153 ALA B 172 1 20
LINK SG CYS A 84 CAC CYC A 201 1555 1555 1.84
LINK C GLY B 71 N MEN B 72 1555 1555 1.38
LINK C MEN B 72 N ALA B 73 1555 1555 1.44
LINK SG CYS B 82 CAC CYC B 201 1555 1555 1.88
LINK SG CYS B 153 CAC CYC B 202 1555 1555 1.86
SITE 1 AC1 26 VAL A 59 THR A 66 SER A 72 GLN A 73
SITE 2 AC1 26 TYR A 74 ALA A 75 GLY A 80 LYS A 83
SITE 3 AC1 26 CYS A 84 ARG A 86 ASP A 87 TYR A 90
SITE 4 AC1 26 TYR A 110 ILE A 118 PHE A 122 LEU A 124
SITE 5 AC1 26 TRP A 128 TYR A 129 HOH A 318 HOH A 336
SITE 6 AC1 26 ARG B 57 ILE B 67 TYR B 74 THR B 75
SITE 7 AC1 26 ASN B 76 HOH B 330
SITE 1 AC2 17 LEU B 66 MEN B 72 ALA B 73 ARG B 77
SITE 2 AC2 17 ARG B 78 ALA B 81 CYS B 82 ARG B 84
SITE 3 AC2 17 ASP B 85 ILE B 88 ARG B 108 THR B 116
SITE 4 AC2 17 LEU B 120 THR B 122 SER B 126 HOH B 316
SITE 5 AC2 17 HOH B 349
SITE 1 AC3 17 LEU A 24 ASP A 28 ARG A 33 GLN A 145
SITE 2 AC3 17 ASN B 35 LYS B 36 LEU B 38 ASP B 39
SITE 3 AC3 17 ASN B 143 ASP B 144 ILE B 148 THR B 149
SITE 4 AC3 17 PRO B 150 GLY B 151 CYS B 153 HOH B 303
SITE 5 AC3 17 HOH B 314
CRYST1 186.380 186.380 60.340 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 0.005365 0.003098 0.000000 0.00000
SCALE2 0.000000 0.006195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016573 0.00000
(ATOM LINES ARE NOT SHOWN.)
END