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HEADER HYDROLASE 28-JAN-21 7E0N
TITLE CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE CHIMERA
CAVEAT 7E0N THR A 251 HAS WRONG CHIRALITY AT ATOM CB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE,LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS SP. 12AMOR1, BACILLUS
SOURCE 3 OCEANISEDIMINIS 2691;
SOURCE 4 ORGANISM_TAXID: 1629723, 1196031;
SOURCE 5 GENE: A361_02165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MONOACYLGLYCEROL LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.LAN
REVDAT 1 16-MAR-22 7E0N 0
JRNL AUTH D.M.LAN,Y.H.WANG
JRNL TITL CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE CHIMERA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.1_3865
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 107963
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.760
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
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 23.6300 - 4.4500 0.83 7103 126 0.1538 0.1559
REMARK 3 2 4.4500 - 3.5400 0.98 8030 145 0.1322 0.1549
REMARK 3 3 3.5400 - 3.0900 0.99 8026 143 0.1476 0.1806
REMARK 3 4 3.0900 - 2.8100 0.98 7953 144 0.1530 0.1799
REMARK 3 5 2.8100 - 2.6100 0.98 7929 142 0.1541 0.1795
REMARK 3 6 2.6100 - 2.4500 0.97 7871 140 0.1570 0.1658
REMARK 3 7 2.4500 - 2.3300 0.97 7758 139 0.1580 0.1952
REMARK 3 8 2.3300 - 2.2300 0.97 7794 141 0.1577 0.1992
REMARK 3 9 2.2300 - 2.1400 0.97 7766 139 0.1593 0.1979
REMARK 3 10 2.1400 - 2.0700 0.96 7712 138 0.1616 0.1789
REMARK 3 11 2.0700 - 2.0100 0.95 7602 139 0.1655 0.1863
REMARK 3 12 2.0100 - 1.9500 0.92 7305 131 0.1836 0.1891
REMARK 3 13 1.9500 - 1.9000 0.87 6974 119 0.1948 0.2021
REMARK 3 14 1.9000 - 1.8500 0.79 6236 118 0.2086 0.2720
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) : 0.133
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.047
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.05
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 : 0.010 7979
REMARK 3 ANGLE : 1.149 10832
REMARK 3 CHIRALITY : 0.179 1219
REMARK 3 PLANARITY : 0.008 1400
REMARK 3 DIHEDRAL : 14.042 1087
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 1 through 3 or
REMARK 3 resid 5 through 69 or resid 71 through 86
REMARK 3 or resid 88 through 113 or resid 115
REMARK 3 through 219 or resid 221 through 242 or
REMARK 3 resid 244 through 251 or resid 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 1 through 3 or
REMARK 3 resid 5 through 69 or resid 71 through 86
REMARK 3 or resid 88 through 113 or resid 115
REMARK 3 through 219 or resid 221 through 242 or
REMARK 3 resid 244 through 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 1 through 3 or
REMARK 3 resid 5 through 69 or resid 71 through 86
REMARK 3 or resid 88 through 113 or resid 115
REMARK 3 through 219 or resid 221 through 242 or
REMARK 3 resid 244 through 251 or resid 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and (resid 1 through 3 or
REMARK 3 resid 5 through 69 or resid 71 through 86
REMARK 3 or resid 88 through 113 or resid 115
REMARK 3 through 219 or resid 221 through 242 or
REMARK 3 resid 244 through 251 or resid 301))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7E0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115284
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : 0.80200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5XKS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE DIBASIC, SODIUM
REMARK 280 PHOSPHATE MONOBASIC, IMIDAZOLE/HYDROCHLORIC ACID, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 32.39900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.92700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.39900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.92700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 661 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 SER A 252
REMARK 465 SER A 253
REMARK 465 LEU A 254
REMARK 465 GLN A 255
REMARK 465 GLY A 256
REMARK 465 LEU A 257
REMARK 465 GLU A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 SER B 252
REMARK 465 SER B 253
REMARK 465 LEU B 254
REMARK 465 GLN B 255
REMARK 465 GLY B 256
REMARK 465 LEU B 257
REMARK 465 GLU B 258
REMARK 465 HIS B 259
REMARK 465 HIS B 260
REMARK 465 HIS B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 SER C 252
REMARK 465 SER C 253
REMARK 465 LEU C 254
REMARK 465 GLN C 255
REMARK 465 GLY C 256
REMARK 465 LEU C 257
REMARK 465 GLU C 258
REMARK 465 HIS C 259
REMARK 465 HIS C 260
REMARK 465 HIS C 261
REMARK 465 HIS C 262
REMARK 465 HIS C 263
REMARK 465 HIS C 264
REMARK 465 SER D 252
REMARK 465 SER D 253
REMARK 465 LEU D 254
REMARK 465 GLN D 255
REMARK 465 GLY D 256
REMARK 465 LEU D 257
REMARK 465 GLU D 258
REMARK 465 HIS D 259
REMARK 465 HIS D 260
REMARK 465 HIS D 261
REMARK 465 HIS D 262
REMARK 465 HIS D 263
REMARK 465 HIS D 264
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 HOH A 632 O HOH A 636 1.81
REMARK 500 O HOH D 626 O HOH D 746 1.84
REMARK 500 O HOH D 597 O HOH D 721 1.85
REMARK 500 O HOH B 692 O HOH B 721 1.86
REMARK 500 OE1 GLU C 195 O HOH C 401 1.86
REMARK 500 O HOH C 548 O HOH C 681 1.88
REMARK 500 O HOH D 407 O HOH D 695 1.89
REMARK 500 O HOH D 558 O HOH D 623 1.90
REMARK 500 O HOH C 655 O HOH C 718 1.91
REMARK 500 O HOH B 634 O HOH B 653 1.91
REMARK 500 O HOH C 665 O HOH C 692 1.94
REMARK 500 O HOH C 424 O HOH C 677 1.96
REMARK 500 OD1 ASN C 185 O HOH C 402 1.97
REMARK 500 O HOH D 406 O HOH D 644 1.98
REMARK 500 NZ LYS A 155 O HOH A 401 1.98
REMARK 500 O HOH A 586 O HOH A 652 1.98
REMARK 500 O HOH A 434 O HOH A 624 2.00
REMARK 500 O HOH B 455 O HOH B 699 2.01
REMARK 500 O HOH D 680 O HOH D 751 2.02
REMARK 500 O HOH B 455 O HOH B 705 2.02
REMARK 500 OE1 GLU B 156 O3 GOL B 301 2.03
REMARK 500 O HOH B 587 O HOH B 649 2.03
REMARK 500 O HOH A 428 O HOH A 436 2.03
REMARK 500 O HOH B 560 O HOH B 714 2.04
REMARK 500 O HOH C 485 O HOH C 674 2.06
REMARK 500 O THR D 251 O HOH D 401 2.07
REMARK 500 O THR C 251 O HOH C 403 2.08
REMARK 500 O HOH D 486 O HOH D 725 2.08
REMARK 500 O HOH C 409 O HOH C 633 2.11
REMARK 500 O HOH C 618 O HOH C 648 2.11
REMARK 500 O HOH B 470 O HOH B 682 2.14
REMARK 500 OD1 ASN A 185 O HOH A 402 2.14
REMARK 500 O HOH D 520 O HOH D 755 2.14
REMARK 500 O HOH B 662 O HOH B 746 2.15
REMARK 500 OE2 GLU B 45 O HOH B 401 2.16
REMARK 500 O HOH D 730 O HOH D 757 2.17
REMARK 500 O HOH B 621 O HOH B 705 2.17
REMARK 500 O HOH D 485 O HOH D 683 2.18
REMARK 500 O HOH A 568 O HOH A 623 2.18
REMARK 500 O HOH A 523 O HOH A 553 2.18
REMARK 500 O HOH B 410 O HOH B 682 2.18
REMARK 500 O HOH A 636 O HOH A 682 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 O HOH C 641 O HOH C 665 2555 1.93
REMARK 500 O HOH B 568 O HOH B 568 2665 1.97
REMARK 500 O HOH D 440 O HOH D 440 2665 1.97
REMARK 500 O HOH C 641 O HOH C 651 2555 2.09
REMARK 500 O HOH B 540 O HOH B 540 2765 2.14
REMARK 500 O HOH D 632 O HOH D 675 2665 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL C 135 CB VAL C 135 CG2 -0.174
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 ASN A 185 CB - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASN A 185 CB - CG - ND2 ANGL. DEV. = -16.5 DEGREES
REMARK 500 THR A 251 OG1 - CB - CG2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 VAL C 135 CG1 - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASN C 185 CB - CA - C ANGL. DEV. = -21.8 DEGREES
REMARK 500 ARG D 247 CD - NE - CZ ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG D 247 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG D 247 NE - CZ - NH2 ANGL. DEV. = -7.6 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 THR A 30 -3.79 70.89
REMARK 500 THR A 60 -77.49 -124.08
REMARK 500 SER A 97 -117.29 66.60
REMARK 500 LEU A 128 -64.46 -91.56
REMARK 500 ASP A 137 126.07 -37.37
REMARK 500 TYR A 225 -147.40 -97.90
REMARK 500 THR B 30 -3.69 69.01
REMARK 500 THR B 60 -74.70 -120.56
REMARK 500 SER B 97 -116.67 63.62
REMARK 500 TYR B 225 -148.45 -98.42
REMARK 500 THR C 30 -3.98 71.75
REMARK 500 THR C 60 -76.14 -122.67
REMARK 500 SER C 97 -117.26 66.40
REMARK 500 VAL C 198 -51.16 -121.60
REMARK 500 TYR C 225 -149.59 -98.20
REMARK 500 THR D 30 -5.02 72.12
REMARK 500 THR D 60 -75.27 -123.89
REMARK 500 SER D 97 -117.01 66.32
REMARK 500 TYR D 225 -147.89 -99.45
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 GLU C 250 THR C 251 137.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 185 11.15
REMARK 500 ASN C 185 17.96
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 A 726 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH D 794 DISTANCE = 6.39 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF RESIDUE 1-160 IS GENBANK ENTRY AKM18206.1.
DBREF 7E0N A 1 160 PDB 7E0N 7E0N 1 160
DBREF1 7E0N A 161 256 UNP A0A160MIM0_9BACI
DBREF2 7E0N A A0A160MIM0 159 254
DBREF 7E0N B 1 160 PDB 7E0N 7E0N 1 160
DBREF1 7E0N B 161 256 UNP A0A160MIM0_9BACI
DBREF2 7E0N B A0A160MIM0 159 254
DBREF 7E0N C 1 160 PDB 7E0N 7E0N 1 160
DBREF1 7E0N C 161 256 UNP A0A160MIM0_9BACI
DBREF2 7E0N C A0A160MIM0 159 254
DBREF 7E0N D 1 160 PDB 7E0N 7E0N 1 160
DBREF1 7E0N D 161 256 UNP A0A160MIM0_9BACI
DBREF2 7E0N D A0A160MIM0 159 254
SEQADV 7E0N LEU A 257 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N GLU A 258 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 259 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 260 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 261 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 262 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 263 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS A 264 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N LEU B 257 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N GLU B 258 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 259 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 260 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 261 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 262 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 263 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS B 264 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N LEU C 257 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N GLU C 258 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 259 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 260 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 261 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 262 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 263 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS C 264 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N LEU D 257 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N GLU D 258 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 259 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 260 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 261 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 262 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 263 UNP A0A160MIM EXPRESSION TAG
SEQADV 7E0N HIS D 264 UNP A0A160MIM EXPRESSION TAG
SEQRES 1 A 264 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 A 264 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 A 264 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 A 264 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 A 264 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 A 264 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 A 264 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 A 264 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 A 264 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 A 264 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 A 264 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 A 264 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 A 264 LEU ALA TYR GLU LYS THR PRO VAL LYS SER ILE GLY GLU
SEQRES 14 A 264 ILE THR GLU LEU MET LYS LYS VAL LYS GLY ASP LEU GLU
SEQRES 15 A 264 LYS VAL ASN CYS PRO ALA LEU ILE PHE VAL SER LYS GLU
SEQRES 16 A 264 ASP HIS VAL VAL PRO PRO SER ASN SER GLN GLU ILE TYR
SEQRES 17 A 264 SER SER ILE LYS SER ALA ALA LYS GLU LEU VAL THR LEU
SEQRES 18 A 264 ASP ASN SER TYR HIS VAL ALA THR LEU ASP ASN ASP GLN
SEQRES 19 A 264 ASP ILE ILE ILE GLU ARG THR LEU HIS PHE LEU GLN ARG
SEQRES 20 A 264 VAL LEU GLU THR SER SER LEU GLN GLY LEU GLU HIS HIS
SEQRES 21 A 264 HIS HIS HIS HIS
SEQRES 1 B 264 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 B 264 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 B 264 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 B 264 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 B 264 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 B 264 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 B 264 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 B 264 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 B 264 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 B 264 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 B 264 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 B 264 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 B 264 LEU ALA TYR GLU LYS THR PRO VAL LYS SER ILE GLY GLU
SEQRES 14 B 264 ILE THR GLU LEU MET LYS LYS VAL LYS GLY ASP LEU GLU
SEQRES 15 B 264 LYS VAL ASN CYS PRO ALA LEU ILE PHE VAL SER LYS GLU
SEQRES 16 B 264 ASP HIS VAL VAL PRO PRO SER ASN SER GLN GLU ILE TYR
SEQRES 17 B 264 SER SER ILE LYS SER ALA ALA LYS GLU LEU VAL THR LEU
SEQRES 18 B 264 ASP ASN SER TYR HIS VAL ALA THR LEU ASP ASN ASP GLN
SEQRES 19 B 264 ASP ILE ILE ILE GLU ARG THR LEU HIS PHE LEU GLN ARG
SEQRES 20 B 264 VAL LEU GLU THR SER SER LEU GLN GLY LEU GLU HIS HIS
SEQRES 21 B 264 HIS HIS HIS HIS
SEQRES 1 C 264 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 C 264 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 C 264 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 C 264 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 C 264 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 C 264 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 C 264 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 C 264 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 C 264 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 C 264 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 C 264 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 C 264 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 C 264 LEU ALA TYR GLU LYS THR PRO VAL LYS SER ILE GLY GLU
SEQRES 14 C 264 ILE THR GLU LEU MET LYS LYS VAL LYS GLY ASP LEU GLU
SEQRES 15 C 264 LYS VAL ASN CYS PRO ALA LEU ILE PHE VAL SER LYS GLU
SEQRES 16 C 264 ASP HIS VAL VAL PRO PRO SER ASN SER GLN GLU ILE TYR
SEQRES 17 C 264 SER SER ILE LYS SER ALA ALA LYS GLU LEU VAL THR LEU
SEQRES 18 C 264 ASP ASN SER TYR HIS VAL ALA THR LEU ASP ASN ASP GLN
SEQRES 19 C 264 ASP ILE ILE ILE GLU ARG THR LEU HIS PHE LEU GLN ARG
SEQRES 20 C 264 VAL LEU GLU THR SER SER LEU GLN GLY LEU GLU HIS HIS
SEQRES 21 C 264 HIS HIS HIS HIS
SEQRES 1 D 264 MET THR GLU THR TYR PRO VAL VAL LYS GLY ALA GLU PRO
SEQRES 2 D 264 PHE PHE PHE GLU GLY ASN ASP ILE GLY ILE LEU VAL LEU
SEQRES 3 D 264 HIS GLY PHE THR GLY SER PRO GLN SER MET ARG PRO LEU
SEQRES 4 D 264 GLY GLU ALA TYR HIS GLU ALA GLY TYR THR VAL CYS GLY
SEQRES 5 D 264 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 D 264 GLU LYS THR THR CYS GLN ASP TRP ILE ASP SER VAL GLU
SEQRES 7 D 264 ALA GLY TYR GLU TRP LEU LYS ASN ARG CYS GLY THR ILE
SEQRES 8 D 264 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 D 264 TYR MET ALA GLU HIS HIS PRO GLU ILE CYS GLY ILE ALA
SEQRES 10 D 264 PRO ILE ASN ALA ALA ILE ASN MET PRO ALA LEU ALA GLY
SEQRES 11 D 264 ALA LEU ALA GLY VAL GLY ASP LEU PRO ARG PHE LEU ASP
SEQRES 12 D 264 ALA ILE GLY SER ASP ILE LYS LYS PRO GLY VAL LYS GLU
SEQRES 13 D 264 LEU ALA TYR GLU LYS THR PRO VAL LYS SER ILE GLY GLU
SEQRES 14 D 264 ILE THR GLU LEU MET LYS LYS VAL LYS GLY ASP LEU GLU
SEQRES 15 D 264 LYS VAL ASN CYS PRO ALA LEU ILE PHE VAL SER LYS GLU
SEQRES 16 D 264 ASP HIS VAL VAL PRO PRO SER ASN SER GLN GLU ILE TYR
SEQRES 17 D 264 SER SER ILE LYS SER ALA ALA LYS GLU LEU VAL THR LEU
SEQRES 18 D 264 ASP ASN SER TYR HIS VAL ALA THR LEU ASP ASN ASP GLN
SEQRES 19 D 264 ASP ILE ILE ILE GLU ARG THR LEU HIS PHE LEU GLN ARG
SEQRES 20 D 264 VAL LEU GLU THR SER SER LEU GLN GLY LEU GLU HIS HIS
SEQRES 21 D 264 HIS HIS HIS HIS
HET GOL A 301 6
HET GOL B 301 6
HET GOL C 301 6
HET GOL D 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *1409(H2 O)
HELIX 1 AA1 SER A 32 SER A 35 5 4
HELIX 2 AA2 MET A 36 ALA A 46 1 11
HELIX 3 AA3 HIS A 61 LYS A 67 1 7
HELIX 4 AA4 THR A 69 CYS A 88 1 20
HELIX 5 AA5 SER A 97 HIS A 110 1 14
HELIX 6 AA6 LEU A 128 GLY A 134 5 7
HELIX 7 AA7 VAL A 164 ASP A 180 1 17
HELIX 8 AA8 LEU A 181 VAL A 184 5 4
HELIX 9 AA9 PRO A 201 ILE A 211 1 11
HELIX 10 AB1 VAL A 227 ASP A 231 5 5
HELIX 11 AB2 ASP A 233 THR A 251 1 19
HELIX 12 AB3 SER B 32 SER B 35 5 4
HELIX 13 AB4 MET B 36 ALA B 46 1 11
HELIX 14 AB5 HIS B 61 LYS B 67 1 7
HELIX 15 AB6 THR B 69 CYS B 88 1 20
HELIX 16 AB7 SER B 97 HIS B 110 1 14
HELIX 17 AB8 MET B 125 GLY B 130 1 6
HELIX 18 AB9 ALA B 131 GLY B 134 5 4
HELIX 19 AC1 VAL B 164 ASP B 180 1 17
HELIX 20 AC2 LEU B 181 VAL B 184 5 4
HELIX 21 AC3 PRO B 201 ILE B 211 1 11
HELIX 22 AC4 VAL B 227 ASP B 231 5 5
HELIX 23 AC5 ASP B 233 THR B 251 1 19
HELIX 24 AC6 SER C 32 SER C 35 5 4
HELIX 25 AC7 MET C 36 ALA C 46 1 11
HELIX 26 AC8 HIS C 61 LYS C 67 1 7
HELIX 27 AC9 THR C 69 CYS C 88 1 20
HELIX 28 AD1 SER C 97 HIS C 110 1 14
HELIX 29 AD2 MET C 125 GLY C 130 1 6
HELIX 30 AD3 ALA C 131 GLY C 134 5 4
HELIX 31 AD4 VAL C 164 ASP C 180 1 17
HELIX 32 AD5 LEU C 181 VAL C 184 5 4
HELIX 33 AD6 PRO C 201 ILE C 211 1 11
HELIX 34 AD7 VAL C 227 ASP C 231 5 5
HELIX 35 AD8 ASP C 233 THR C 251 1 19
HELIX 36 AD9 SER D 32 SER D 35 5 4
HELIX 37 AE1 MET D 36 ALA D 46 1 11
HELIX 38 AE2 HIS D 61 LYS D 67 1 7
HELIX 39 AE3 THR D 69 CYS D 88 1 20
HELIX 40 AE4 SER D 97 HIS D 110 1 14
HELIX 41 AE5 MET D 125 GLY D 130 1 6
HELIX 42 AE6 ALA D 131 GLY D 134 5 4
HELIX 43 AE7 VAL D 164 ASP D 180 1 17
HELIX 44 AE8 LEU D 181 VAL D 184 5 4
HELIX 45 AE9 PRO D 201 ILE D 211 1 11
HELIX 46 AF1 VAL D 227 ASP D 231 5 5
HELIX 47 AF2 ASP D 233 THR D 251 1 19
SHEET 1 AA1 5 PHE A 14 PHE A 16 0
SHEET 2 AA1 5 THR A 49 GLY A 52 -1 O GLY A 52 N PHE A 14
SHEET 3 AA1 5 ILE A 21 LEU A 26 1 N VAL A 25 O CYS A 51
SHEET 4 AA1 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 AA1 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 AA2 2 PHE A 141 ASP A 143 0
SHEET 2 AA2 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 AA3 2 ALA A 188 SER A 193 0
SHEET 2 AA3 2 LYS A 216 LEU A 221 1 O GLU A 217 N ILE A 190
SHEET 1 AA4 5 PHE B 14 PHE B 16 0
SHEET 2 AA4 5 THR B 49 GLY B 52 -1 O GLY B 52 N PHE B 14
SHEET 3 AA4 5 ILE B 21 LEU B 26 1 N VAL B 25 O CYS B 51
SHEET 4 AA4 5 THR B 90 LEU B 96 1 O THR B 90 N GLY B 22
SHEET 5 AA4 5 GLY B 115 ILE B 119 1 O ILE B 119 N GLY B 95
SHEET 1 AA5 2 PHE B 141 ASP B 143 0
SHEET 2 AA5 2 LYS B 161 PRO B 163 -1 O THR B 162 N LEU B 142
SHEET 1 AA6 2 ALA B 188 SER B 193 0
SHEET 2 AA6 2 LYS B 216 LEU B 221 1 O GLU B 217 N ILE B 190
SHEET 1 AA7 5 PHE C 14 PHE C 16 0
SHEET 2 AA7 5 THR C 49 GLY C 52 -1 O GLY C 52 N PHE C 14
SHEET 3 AA7 5 ILE C 21 LEU C 26 1 N VAL C 25 O CYS C 51
SHEET 4 AA7 5 THR C 90 LEU C 96 1 O THR C 90 N GLY C 22
SHEET 5 AA7 5 GLY C 115 ILE C 119 1 O ILE C 119 N GLY C 95
SHEET 1 AA8 2 PHE C 141 ASP C 143 0
SHEET 2 AA8 2 LYS C 161 PRO C 163 -1 O THR C 162 N LEU C 142
SHEET 1 AA9 2 ALA C 188 SER C 193 0
SHEET 2 AA9 2 LYS C 216 LEU C 221 1 O GLU C 217 N ILE C 190
SHEET 1 AB1 5 PHE D 14 PHE D 16 0
SHEET 2 AB1 5 THR D 49 GLY D 52 -1 O GLY D 52 N PHE D 14
SHEET 3 AB1 5 ILE D 21 LEU D 26 1 N VAL D 25 O CYS D 51
SHEET 4 AB1 5 THR D 90 LEU D 96 1 O THR D 90 N GLY D 22
SHEET 5 AB1 5 GLY D 115 ILE D 119 1 O ILE D 119 N GLY D 95
SHEET 1 AB2 2 PHE D 141 ASP D 143 0
SHEET 2 AB2 2 LYS D 161 PRO D 163 -1 O THR D 162 N LEU D 142
SHEET 1 AB3 2 ALA D 188 SER D 193 0
SHEET 2 AB3 2 LYS D 216 LEU D 221 1 O VAL D 219 N ILE D 190
SITE 1 AC1 10 PHE A 29 GLY A 31 SER A 97 ILE A 145
SITE 2 AC1 10 GLY A 146 GLU A 156 HIS A 226 HOH A 406
SITE 3 AC1 10 HOH A 442 HOH A 492
SITE 1 AC2 8 PHE B 29 GLY B 31 SER B 97 ILE B 145
SITE 2 AC2 8 GLY B 146 GLU B 156 HIS B 226 HOH B 416
SITE 1 AC3 9 PHE C 29 GLY C 31 SER C 97 GLY C 146
SITE 2 AC3 9 GLU C 156 HIS C 226 HOH C 408 HOH C 496
SITE 3 AC3 9 HOH C 527
SITE 1 AC4 10 PHE D 29 GLY D 31 SER D 97 GLY D 146
SITE 2 AC4 10 GLU D 156 HIS D 226 VAL D 227 HOH D 441
SITE 3 AC4 10 HOH D 506 HOH D 516
CRYST1 64.798 99.854 207.236 90.00 90.00 90.00 P 21 21 2 16
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 0.015433 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010015 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004825 0.00000
MTRIX1 1 0.999301 0.034734 -0.013802 31.84990 1
MTRIX2 1 0.035334 -0.998321 0.045894 50.08763 1
MTRIX3 1 -0.012185 -0.046349 -0.998851 104.86780 1
MTRIX1 2 -0.999693 -0.018196 -0.016815 24.42176 1
MTRIX2 2 -0.017453 0.998907 -0.043350 1.23178 1
MTRIX3 2 0.017585 -0.043043 -0.998918 52.55174 1
MTRIX1 3 -0.999980 -0.004835 -0.004080 56.20501 1
MTRIX2 3 0.004860 -0.999970 -0.005969 51.43757 1
MTRIX3 3 -0.004051 -0.005989 0.999974 52.03285 1
TER 1935 THR A 251
TER 3877 THR B 251
TER 5835 THR C 251
TER 7781 THR D 251
MASTER 543 0 4 47 36 0 11 15 9145 4 24 84
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