HEADER METAL TRANSPORT 02-APR-12 4EGW
TITLE THE STRUCTURE OF THE SOLUBLE DOMAIN OF CORA FROM METHANOCALDOCOCCUS
TITLE 2 JANNASCHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAGNESIUM TRANSPORT PROTEIN CORA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN, UNP RESIDUES 1-258;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 243232;
SOURCE 4 STRAIN: DSM 2661;
SOURCE 5 GENE: CORA, MJ1033;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MAGNESIUM TRANSPORTER, MAGNESIUM BINDING, CORA, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GUSKOV,N.NORDIN,A.REYNAUD,H.ENGMAN,A.-K.LUNDBACK,A.J.O.JONG,
AUTHOR 2 T.CORNVIK,T.PHUA,S.ESHAGHI
REVDAT 3 20-MAR-24 4EGW 1 REMARK SEQADV
REVDAT 2 24-JUL-13 4EGW 1 JRNL
REVDAT 1 31-OCT-12 4EGW 0
JRNL AUTH A.GUSKOV,N.NORDIN,A.REYNAUD,H.ENGMAN,A.K.LUNDBACK,A.J.JONG,
JRNL AUTH 2 T.CORNVIK,T.PHUA,S.ESHAGHI
JRNL TITL STRUCTURAL INSIGHTS INTO THE MECHANISMS OF MG2+ UPTAKE,
JRNL TITL 2 TRANSPORT, AND GATING BY CORA
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 18459 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 23091000
JRNL DOI 10.1073/PNAS.1210076109
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21977
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1099
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 42.2921 - 4.9999 0.95 2626 139 0.1571 0.2035
REMARK 3 2 4.9999 - 3.9695 0.95 2605 137 0.1190 0.1598
REMARK 3 3 3.9695 - 3.4680 0.95 2616 138 0.1345 0.2069
REMARK 3 4 3.4680 - 3.1510 0.95 2616 137 0.1505 0.1889
REMARK 3 5 3.1510 - 2.9252 0.95 2590 137 0.1663 0.2100
REMARK 3 6 2.9252 - 2.7528 0.95 2603 136 0.1855 0.2189
REMARK 3 7 2.7528 - 2.6150 0.95 2596 137 0.1951 0.2246
REMARK 3 8 2.6150 - 2.5011 0.94 2611 138 0.2079 0.2683
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 74.29
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.450
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: 0.5000
REMARK 3 OPERATOR: K,H,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4373
REMARK 3 ANGLE : 1.343 5829
REMARK 3 CHIRALITY : 0.084 677
REMARK 3 PLANARITY : 0.005 707
REMARK 3 DIHEDRAL : 21.452 1722
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:37)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7166 -41.8525 -12.6917
REMARK 3 T TENSOR
REMARK 3 T11: 0.5595 T22: 0.2764
REMARK 3 T33: 0.6417 T12: -0.0463
REMARK 3 T13: 0.0135 T23: -0.1963
REMARK 3 L TENSOR
REMARK 3 L11: 3.6006 L22: 3.1001
REMARK 3 L33: 3.2159 L12: -1.4136
REMARK 3 L13: -0.7636 L23: 0.3167
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.1513 S13: -0.6322
REMARK 3 S21: -0.3278 S22: 0.2435 S23: -0.1217
REMARK 3 S31: 0.9058 S32: 0.2772 S33: -0.1893
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 38:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0957 -33.1505 -2.3745
REMARK 3 T TENSOR
REMARK 3 T11: 0.2194 T22: 0.1734
REMARK 3 T33: 0.6291 T12: -0.0937
REMARK 3 T13: 0.0908 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 1.1738 L22: 5.0183
REMARK 3 L33: 2.0465 L12: 2.2087
REMARK 3 L13: 0.3268 L23: 0.2812
REMARK 3 S TENSOR
REMARK 3 S11: -0.0882 S12: -0.2038 S13: -0.4352
REMARK 3 S21: 0.0667 S22: 0.0270 S23: 0.1046
REMARK 3 S31: 0.2484 S32: -0.1349 S33: 0.0258
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 110:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3458 -34.8714 -20.9801
REMARK 3 T TENSOR
REMARK 3 T11: 0.8504 T22: 0.5643
REMARK 3 T33: 0.6512 T12: -0.1306
REMARK 3 T13: 0.1688 T23: -0.1806
REMARK 3 L TENSOR
REMARK 3 L11: 7.4089 L22: 3.8812
REMARK 3 L33: 4.0388 L12: -2.8802
REMARK 3 L13: 2.4109 L23: 0.0964
REMARK 3 S TENSOR
REMARK 3 S11: 0.3715 S12: 1.4215 S13: -0.7678
REMARK 3 S21: -1.1292 S22: -0.1931 S23: -0.1512
REMARK 3 S31: 0.4250 S32: 0.8881 S33: -0.1722
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 134:250)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1383 -12.3774 -8.3838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1869 T22: 0.0856
REMARK 3 T33: 0.5825 T12: -0.0332
REMARK 3 T13: 0.0207 T23: -0.1625
REMARK 3 L TENSOR
REMARK 3 L11: 0.9958 L22: 3.2058
REMARK 3 L33: 1.5563 L12: -0.2011
REMARK 3 L13: -0.1701 L23: 0.7067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: -0.1478 S13: 0.1717
REMARK 3 S21: -0.0997 S22: 0.0698 S23: 0.0251
REMARK 3 S31: -0.2064 S32: 0.0247 S33: 0.0092
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 1:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2178 2.4366 -24.7521
REMARK 3 T TENSOR
REMARK 3 T11: 0.4069 T22: 0.5347
REMARK 3 T33: 0.7562 T12: -0.2080
REMARK 3 T13: -0.1064 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.0539 L22: 2.3052
REMARK 3 L33: 2.3076 L12: 1.1920
REMARK 3 L13: -0.5584 L23: 0.7563
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: -0.2551 S13: 0.4702
REMARK 3 S21: -0.3655 S22: 0.1582 S23: -0.3762
REMARK 3 S31: -0.5581 S32: 0.6674 S33: 0.0835
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 29:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9277 -2.5841 -36.2326
REMARK 3 T TENSOR
REMARK 3 T11: 0.2986 T22: 0.3575
REMARK 3 T33: 0.6895 T12: -0.1351
REMARK 3 T13: 0.0014 T23: -0.0777
REMARK 3 L TENSOR
REMARK 3 L11: 1.7097 L22: 2.3316
REMARK 3 L33: 2.2473 L12: 0.6623
REMARK 3 L13: 0.3182 L23: 0.1178
REMARK 3 S TENSOR
REMARK 3 S11: -0.2979 S12: 0.3086 S13: 0.1872
REMARK 3 S21: -0.1936 S22: 0.1283 S23: -0.0416
REMARK 3 S31: -0.4516 S32: 0.4289 S33: 0.1027
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 110:210)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3153 -14.5558 -27.8229
REMARK 3 T TENSOR
REMARK 3 T11: 0.1891 T22: 0.2769
REMARK 3 T33: 0.4763 T12: -0.0320
REMARK 3 T13: -0.0293 T23: -0.1402
REMARK 3 L TENSOR
REMARK 3 L11: 2.1887 L22: 2.0256
REMARK 3 L33: 1.9487 L12: 0.4115
REMARK 3 L13: -0.5918 L23: -0.0615
REMARK 3 S TENSOR
REMARK 3 S11: 0.0771 S12: -0.3494 S13: -0.0512
REMARK 3 S21: 0.0685 S22: -0.1484 S23: -0.2298
REMARK 3 S31: 0.1110 S32: -0.0348 S33: 0.0756
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 211:250)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0696 -22.9032 -31.9525
REMARK 3 T TENSOR
REMARK 3 T11: 0.2867 T22: 0.3049
REMARK 3 T33: 0.5750 T12: -0.0597
REMARK 3 T13: 0.0300 T23: -0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 2.4912 L22: 1.7341
REMARK 3 L33: 2.8682 L12: 1.2699
REMARK 3 L13: 1.7349 L23: -0.1687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: 0.0149 S13: -0.4122
REMARK 3 S21: -0.1440 S22: -0.0769 S23: -0.2790
REMARK 3 S31: 0.2783 S32: -0.3344 S33: 0.1327
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 4EGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21977
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: SAD+MR
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 8000, HEPES-MOPS, ALCOHOL MIX,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 80.64667
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 161.29333
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 120.97000
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 201.61667
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 40.32333
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 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 -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 ILE A 251
REMARK 465 LYS A 252
REMARK 465 MET A 253
REMARK 465 ASN A 254
REMARK 465 GLN A 255
REMARK 465 ILE A 256
REMARK 465 MET A 257
REMARK 465 LYS A 258
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 SER B 0
REMARK 465 ILE B 251
REMARK 465 LYS B 252
REMARK 465 MET B 253
REMARK 465 ASN B 254
REMARK 465 GLN B 255
REMARK 465 ILE B 256
REMARK 465 MET B 257
REMARK 465 LYS B 258
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 OE1 GLU A 85 O HOH A 433 1.83
REMARK 500 O HOH B 420 O HOH B 421 1.90
REMARK 500 OE1 GLU A 155 O HOH A 412 1.91
REMARK 500 OD2 ASP B 38 O HOH B 411 1.95
REMARK 500 NH2 ARG B 171 O HOH B 414 1.98
REMARK 500 O HOH B 424 O HOH B 438 1.99
REMARK 500 O HOH A 403 O HOH A 411 2.02
REMARK 500 OE2 GLU A 155 O6 BU1 A 305 2.02
REMARK 500 O HOH A 416 O HOH A 436 2.04
REMARK 500 OE2 GLU B 39 O HOH B 411 2.05
REMARK 500 OE1 GLU A 71 O5 BU1 A 309 2.07
REMARK 500 OE2 GLU A 129 O HOH A 417 2.07
REMARK 500 NZ LYS B 17 OG SER B 120 2.07
REMARK 500 OD1 ASP B 107 O HOH B 403 2.10
REMARK 500 O LEU B 115 N ILE B 119 2.10
REMARK 500 O HOH A 424 O HOH A 425 2.10
REMARK 500 NE2 GLN B 226 O1 HEZ A 310 2.11
REMARK 500 OG1 THR A 209 O HOH A 402 2.13
REMARK 500 N THR A 210 OD2 ASP A 213 2.14
REMARK 500 O PRO B 65 O HOH B 416 2.14
REMARK 500 OE1 GLU B 175 O HOH B 444 2.16
REMARK 500 OD1 ASP B 170 O HOH B 437 2.16
REMARK 500 NE ARG B 214 O HOH B 404 2.17
REMARK 500 O HOH B 425 O HOH B 426 2.17
REMARK 500 OH TYR A 169 NH1 ARG A 171 2.19
REMARK 500 O HOH A 408 O HOH A 409 2.19
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 OH TYR A 205 OD1 ASP B 60 6545 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 PRO A 16 C - N - CA ANGL. DEV. = 18.9 DEGREES
REMARK 500 PRO A 16 C - N - CD ANGL. DEV. = -19.3 DEGREES
REMARK 500 PRO B 16 C - N - CA ANGL. DEV. = 10.0 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 ILE A 5 70.42 41.59
REMARK 500 VAL A 14 70.43 40.83
REMARK 500 PRO A 16 -164.57 -71.50
REMARK 500 LYS A 17 72.73 65.03
REMARK 500 ASP A 19 12.02 57.00
REMARK 500 GLU A 24 19.59 55.81
REMARK 500 PHE A 73 170.88 175.84
REMARK 500 ASN A 98 -117.27 51.59
REMARK 500 ARG A 125 -128.53 46.33
REMARK 500 TYR A 169 -74.93 -27.33
REMARK 500 TYR A 169 -112.81 25.91
REMARK 500 ASP A 170 73.13 58.15
REMARK 500 ARG A 203 -62.51 -122.52
REMARK 500 ASP B 19 -67.18 -132.40
REMARK 500 ARG B 66 -178.04 -170.92
REMARK 500 GLU B 71 -77.38 -106.60
REMARK 500 ASN B 98 -116.87 49.55
REMARK 500 GLU B 249 165.01 175.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 19 GLU A 20 131.20
REMARK 500 ASP A 70 GLU A 71 134.88
REMARK 500 ILE A 132 GLY A 133 133.97
REMARK 500 ILE B 132 GLY B 133 130.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 320
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 B 312
DBREF 4EGW A 1 258 UNP Q58439 CORA_METJA 1 258
DBREF 4EGW B 1 258 UNP Q58439 CORA_METJA 1 258
SEQADV 4EGW MET A -21 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -20 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -19 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -18 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -17 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -16 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS A -15 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER A -14 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER A -13 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLY A -12 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW VAL A -11 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW ASP A -10 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW LEU A -9 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLY A -8 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW THR A -7 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLU A -6 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW ASN A -5 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW LEU A -4 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW TYR A -3 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW PHE A -2 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLN A -1 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER A 0 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW MET B -21 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -20 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -19 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -18 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -17 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -16 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW HIS B -15 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER B -14 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER B -13 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLY B -12 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW VAL B -11 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW ASP B -10 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW LEU B -9 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLY B -8 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW THR B -7 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLU B -6 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW ASN B -5 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW LEU B -4 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW TYR B -3 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW PHE B -2 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW GLN B -1 UNP Q58439 EXPRESSION TAG
SEQADV 4EGW SER B 0 UNP Q58439 EXPRESSION TAG
SEQRES 1 A 280 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 280 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE THR VAL
SEQRES 3 A 280 ILE ALA ILE ALA LYS ASP GLY SER ILE VAL GLU PRO LYS
SEQRES 4 A 280 LEU ASP GLU ILE SER PHE GLU ASP TYR ARG LEU ILE TRP
SEQRES 5 A 280 ILE ASP CYS TYR ASP PRO LYS ASP GLU GLU LEU TYR LYS
SEQRES 6 A 280 LEU SER LYS LYS ILE GLY ILE SER VAL SER ASP LEU GLN
SEQRES 7 A 280 ILE GLY LEU ASP GLU GLN GLU ILE PRO ARG VAL GLU GLU
SEQRES 8 A 280 ASP GLU ASP PHE TYR LEU ILE ILE TYR LYS ALA PRO LEU
SEQRES 9 A 280 PHE GLU GLU ASP ILE THR THR THR SER LEU GLY ILE TYR
SEQRES 10 A 280 ILE LYS ASN ASN LEU LEU LEU THR ILE HIS SER ASP LYS
SEQRES 11 A 280 ILE LYS ALA ILE GLY ARG LEU HIS LYS LEU ILE SER THR
SEQRES 12 A 280 LYS LYS PRO ARG ILE VAL PHE GLU ARG GLY ILE GLY PHE
SEQRES 13 A 280 LEU LEU TYR HIS ILE LEU ASN GLU ILE THR ARG SER TYR
SEQRES 14 A 280 SER ARG ILE LEU MET ASN LEU GLU ASP GLU LEU GLU GLU
SEQRES 15 A 280 LEU GLU ASP LYS LEU LEU ALA GLY TYR ASP ARG GLU VAL
SEQRES 16 A 280 MET GLU LYS ILE LEU GLY LEU ARG LYS THR LEU VAL TYR
SEQRES 17 A 280 PHE HIS LYS SER LEU ILE ALA ASN ARG ASP VAL LEU VAL
SEQRES 18 A 280 LEU LEU LYS ARG LYS TYR LEU PRO ILE THR THR LYS GLU
SEQRES 19 A 280 ASP ARG GLU ASN PHE GLU ASP LEU TYR TYR ASP THR LEU
SEQRES 20 A 280 GLN LEU ILE ASP MET SER ALA THR TYR ARG GLU VAL LEU
SEQRES 21 A 280 THR SER MET MET ASP ILE THR LEU SER LEU GLU ASN ILE
SEQRES 22 A 280 LYS MET ASN GLN ILE MET LYS
SEQRES 1 B 280 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 280 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE THR VAL
SEQRES 3 B 280 ILE ALA ILE ALA LYS ASP GLY SER ILE VAL GLU PRO LYS
SEQRES 4 B 280 LEU ASP GLU ILE SER PHE GLU ASP TYR ARG LEU ILE TRP
SEQRES 5 B 280 ILE ASP CYS TYR ASP PRO LYS ASP GLU GLU LEU TYR LYS
SEQRES 6 B 280 LEU SER LYS LYS ILE GLY ILE SER VAL SER ASP LEU GLN
SEQRES 7 B 280 ILE GLY LEU ASP GLU GLN GLU ILE PRO ARG VAL GLU GLU
SEQRES 8 B 280 ASP GLU ASP PHE TYR LEU ILE ILE TYR LYS ALA PRO LEU
SEQRES 9 B 280 PHE GLU GLU ASP ILE THR THR THR SER LEU GLY ILE TYR
SEQRES 10 B 280 ILE LYS ASN ASN LEU LEU LEU THR ILE HIS SER ASP LYS
SEQRES 11 B 280 ILE LYS ALA ILE GLY ARG LEU HIS LYS LEU ILE SER THR
SEQRES 12 B 280 LYS LYS PRO ARG ILE VAL PHE GLU ARG GLY ILE GLY PHE
SEQRES 13 B 280 LEU LEU TYR HIS ILE LEU ASN GLU ILE THR ARG SER TYR
SEQRES 14 B 280 SER ARG ILE LEU MET ASN LEU GLU ASP GLU LEU GLU GLU
SEQRES 15 B 280 LEU GLU ASP LYS LEU LEU ALA GLY TYR ASP ARG GLU VAL
SEQRES 16 B 280 MET GLU LYS ILE LEU GLY LEU ARG LYS THR LEU VAL TYR
SEQRES 17 B 280 PHE HIS LYS SER LEU ILE ALA ASN ARG ASP VAL LEU VAL
SEQRES 18 B 280 LEU LEU LYS ARG LYS TYR LEU PRO ILE THR THR LYS GLU
SEQRES 19 B 280 ASP ARG GLU ASN PHE GLU ASP LEU TYR TYR ASP THR LEU
SEQRES 20 B 280 GLN LEU ILE ASP MET SER ALA THR TYR ARG GLU VAL LEU
SEQRES 21 B 280 THR SER MET MET ASP ILE THR LEU SER LEU GLU ASN ILE
SEQRES 22 B 280 LYS MET ASN GLN ILE MET LYS
HET HEZ A 301 8
HET HEZ A 302 8
HET HEZ A 303 8
HET HEZ A 304 8
HET BU1 A 305 6
HET HEZ A 306 8
HET PGO A 307 5
HET BU1 A 308 6
HET BU1 A 309 6
HET HEZ A 310 8
HET HEZ A 311 8
HET HEZ A 312 8
HET MG A 313 1
HET MG A 314 1
HET PGO A 315 5
HET PGO A 316 5
HET PGO A 317 5
HET PGO A 318 5
HET BU1 A 319 6
HET PGO A 320 5
HET HEZ B 301 8
HET BU1 B 302 6
HET HEZ B 303 8
HET PGO B 304 5
HET HEZ B 305 8
HET PGO B 306 5
HET MG B 307 1
HET HEZ B 308 8
HET HEZ B 309 8
HET PGO B 310 5
HET PGO B 311 5
HET BU1 B 312 6
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM BU1 1,4-BUTANEDIOL
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM MG MAGNESIUM ION
FORMUL 3 HEZ 13(C6 H14 O2)
FORMUL 7 BU1 6(C4 H10 O2)
FORMUL 9 PGO 10(C3 H8 O2)
FORMUL 15 MG 3(MG 2+)
FORMUL 35 HOH *96(H2 O)
HELIX 1 1 LYS A 37 GLY A 49 1 13
HELIX 2 2 SER A 51 LEU A 59 1 9
HELIX 3 3 ILE A 109 LYS A 122 1 14
HELIX 4 4 GLY A 133 LEU A 165 1 33
HELIX 5 5 ASP A 170 LYS A 204 1 35
HELIX 6 6 THR A 210 GLU A 249 1 40
HELIX 7 7 LYS B 37 GLY B 49 1 13
HELIX 8 8 SER B 51 LEU B 59 1 9
HELIX 9 9 ILE B 109 LYS B 122 1 14
HELIX 10 10 GLY B 133 LEU B 165 1 33
HELIX 11 11 ASP B 170 LYS B 202 1 33
HELIX 12 12 THR B 210 GLU B 249 1 40
SHEET 1 A 6 ALA A 6 GLY A 11 0
SHEET 2 A 6 ILE A 29 TYR A 34 -1 O TRP A 30 N ASP A 10
SHEET 3 A 6 LEU A 100 HIS A 105 1 O THR A 103 N CYS A 33
SHEET 4 A 6 THR A 88 LYS A 97 -1 N GLY A 93 O ILE A 104
SHEET 5 A 6 TYR A 74 LEU A 82 -1 N LEU A 82 O THR A 88
SHEET 6 A 6 ARG A 66 GLU A 68 -1 N GLU A 68 O LEU A 75
SHEET 1 B 6 ALA B 6 ALA B 8 0
SHEET 2 B 6 ILE B 29 TYR B 34 -1 O ASP B 32 N ALA B 8
SHEET 3 B 6 LEU B 100 HIS B 105 1 O LEU B 101 N ILE B 29
SHEET 4 B 6 THR B 88 LYS B 97 -1 N LYS B 97 O LEU B 100
SHEET 5 B 6 TYR B 74 LEU B 82 -1 N LEU B 82 O THR B 88
SHEET 6 B 6 ARG B 66 GLU B 68 -1 N GLU B 68 O LEU B 75
CISPEP 1 SER A 12 ILE A 13 0 12.64
CISPEP 2 ILE A 126 VAL A 127 0 -6.15
CISPEP 3 ILE B 13 VAL B 14 0 -22.07
SITE 1 AC1 3 ASP A 219 GLU B 215 ASN B 216
SITE 1 AC2 4 TYR A 137 ASP A 219 ASP B 219 ASP B 223
SITE 1 AC3 8 GLU A 68 GLU A 69 HEZ A 306 BU1 A 308
SITE 2 AC3 8 PGO A 317 HOH A 442 MET B 1 ILE B 2
SITE 1 AC4 4 GLU A 218 SER B 53 GLN B 56 HEZ B 308
SITE 1 AC5 5 GLU A 155 LEU A 158 GLU A 159 TYR A 234
SITE 2 AC5 5 LYS B 117
SITE 1 AC6 7 GLU A 68 GLU A 71 HEZ A 303 BU1 A 308
SITE 2 AC6 7 PGO A 320 HOH A 441 HOH A 442
SITE 1 AC7 3 HEZ A 303 HEZ A 306 HOH A 442
SITE 1 AC8 3 SER A 51 ASP A 54 GLU A 71
SITE 1 AC9 4 LYS A 122 BU1 A 319 HOH A 443 GLN B 226
SITE 1 BC1 5 GLY A 49 ASP A 72 LYS A 97 PGO A 315
SITE 2 BC1 5 PGO A 316
SITE 1 BC2 3 ILE A 13 ARG A 27 HOH A 444
SITE 1 BC3 1 ASP A 163
SITE 1 BC4 2 ASP A 163 HOH A 448
SITE 1 BC5 3 ILE A 126 HEZ A 311 PGO A 316
SITE 1 BC6 6 SER A 45 GLY A 49 ILE A 50 SER A 51
SITE 2 BC6 6 HEZ A 311 PGO A 315
SITE 1 BC7 2 HEZ A 303 ILE B 2
SITE 1 BC8 5 ARG A 181 VAL A 185 HIS A 188 ARG A 235
SITE 2 BC8 5 ASP B 243
SITE 1 BC9 2 PHE A 128 HEZ A 310
SITE 1 CC1 2 GLU A 71 HEZ A 306
SITE 1 CC2 7 GLN A 62 TYR B 205 THR B 209 THR B 210
SITE 2 CC2 7 LYS B 211 ARG B 214 HOH B 407
SITE 1 CC3 4 GLU B 68 GLU B 71 HEZ B 305 HOH B 438
SITE 1 CC4 8 ARG A 145 SER A 148 ARG A 149 MET A 152
SITE 2 CC4 8 ARG B 145 SER B 148 ARG B 149 MET B 152
SITE 1 CC5 4 GLU B 68 GLU B 71 HEZ B 303 HOH B 438
SITE 1 CC6 3 TYR B 169 ASP B 170 GLU B 172
SITE 1 CC7 1 ASP B 163
SITE 1 CC8 5 HEZ A 304 SER B 51 SER B 53 ASP B 54
SITE 2 CC8 5 ARG B 125
SITE 1 CC9 2 TYR A 42 BU1 B 312
SITE 1 DC1 1 LYS B 43
SITE 1 DC2 3 MET B 1 THR B 3 HOH B 447
SITE 1 DC3 3 LEU B 225 ASP B 229 HEZ B 309
CRYST1 68.290 68.290 241.940 90.00 90.00 120.00 P 61 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 0.014643 0.008454 0.000000 0.00000
SCALE2 0.000000 0.016909 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
