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HEADER HYDROLASE 01-JUL-13 4LHE
TITLE CRYSTAL STRUCTURE OF CLOSED FORM OF MONOACYLGLYCEROL LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS;
SOURCE 3 ORGANISM_TAXID: 129908;
SOURCE 4 STRAIN: H-257;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 129908;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: H-257
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.TSURUMURA,H.TSUGE
REVDAT 1 02-JUL-14 4LHE 0
JRNL AUTH T.TSURUMURA,H.TSUGE
JRNL TITL SUBSTRATE SELECTIVITY OF BACTERIAL MONOACYLGLYCEROL LIPASE
JRNL TITL 2 BASED ON CRYSTAL STRUCTURE
JRNL REF J.STRUCT.FUNCT.GENOM. 2014
JRNL REFN ISSN 1345-711X
JRNL PMID 24894647
JRNL DOI 10.1007/S10969-014-9181-2
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 33298
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1684
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 27.3449 - 4.4859 1.00 2848 145 0.2055 0.2180
REMARK 3 2 4.4859 - 3.5631 1.00 2672 161 0.1982 0.2185
REMARK 3 3 3.5631 - 3.1134 1.00 2696 127 0.2194 0.2823
REMARK 3 4 3.1134 - 2.8290 1.00 2676 132 0.2607 0.3028
REMARK 3 5 2.8290 - 2.6264 1.00 2637 154 0.2549 0.3387
REMARK 3 6 2.6264 - 2.4717 1.00 2635 129 0.2644 0.3072
REMARK 3 7 2.4717 - 2.3480 1.00 2613 153 0.2738 0.2915
REMARK 3 8 2.3480 - 2.2458 0.97 2564 124 0.3526 0.4459
REMARK 3 9 2.2458 - 2.1594 0.96 2496 138 0.3565 0.3718
REMARK 3 10 2.1594 - 2.0849 1.00 2625 133 0.2825 0.2936
REMARK 3 11 2.0849 - 2.0197 1.00 2615 147 0.2784 0.3542
REMARK 3 12 2.0197 - 1.9620 0.98 2537 141 0.3019 0.3069
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.76
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 : 0.008 3932
REMARK 3 ANGLE : 1.314 5350
REMARK 3 CHIRALITY : 0.081 598
REMARK 3 PLANARITY : 0.007 691
REMARK 3 DIHEDRAL : 14.947 1428
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4879 3.3286 -10.8167
REMARK 3 T TENSOR
REMARK 3 T11: 0.2951 T22: 0.2309
REMARK 3 T33: 0.2285 T12: -0.0096
REMARK 3 T13: 0.0048 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.7616 L22: 2.4543
REMARK 3 L33: 2.9205 L12: -0.3286
REMARK 3 L13: -0.3143 L23: 0.5325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0792 S12: 0.3961 S13: 0.3473
REMARK 3 S21: -0.4275 S22: 0.0836 S23: -0.0891
REMARK 3 S31: -0.3928 S32: 0.0736 S33: -0.1543
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 70 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7859 4.9379 1.2773
REMARK 3 T TENSOR
REMARK 3 T11: 0.3102 T22: 0.2799
REMARK 3 T33: 0.2585 T12: -0.0661
REMARK 3 T13: -0.0108 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 1.2960 L22: 3.4181
REMARK 3 L33: 3.4375 L12: 0.0772
REMARK 3 L13: 0.8502 L23: -0.9698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0712 S12: -0.2844 S13: 0.2890
REMARK 3 S21: 0.3427 S22: -0.0767 S23: -0.3318
REMARK 3 S31: -0.4704 S32: 0.3260 S33: 0.0107
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 130 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8233 0.8239 -9.1990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3546 T22: 0.4346
REMARK 3 T33: 0.5073 T12: -0.0646
REMARK 3 T13: -0.0000 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.7534 L22: 3.1498
REMARK 3 L33: 1.9416 L12: 1.3395
REMARK 3 L13: 0.1484 L23: -0.4187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.0065 S13: -0.2065
REMARK 3 S21: -0.1741 S22: -0.0278 S23: -0.7313
REMARK 3 S31: -0.2150 S32: 0.6888 S33: 0.0275
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 184 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7201 -9.7677 3.7672
REMARK 3 T TENSOR
REMARK 3 T11: 0.2710 T22: 0.3110
REMARK 3 T33: 0.2902 T12: 0.0234
REMARK 3 T13: -0.0154 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 2.1614 L22: 2.3579
REMARK 3 L33: 4.0939 L12: 0.9244
REMARK 3 L13: 0.1899 L23: 0.1733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: -0.3391 S13: -0.3309
REMARK 3 S21: 0.2872 S22: -0.0430 S23: -0.2275
REMARK 3 S31: 0.4877 S32: 0.4284 S33: -0.0371
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 1 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8018 34.0819 -14.7938
REMARK 3 T TENSOR
REMARK 3 T11: 0.2434 T22: 0.3148
REMARK 3 T33: 0.2517 T12: -0.0246
REMARK 3 T13: 0.0230 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 3.0488 L22: 3.7365
REMARK 3 L33: 2.8703 L12: 0.2875
REMARK 3 L13: 0.5272 L23: 0.0761
REMARK 3 S TENSOR
REMARK 3 S11: 0.0887 S12: -0.3707 S13: -0.1682
REMARK 3 S21: 0.3545 S22: 0.0105 S23: 0.4125
REMARK 3 S31: 0.2101 S32: -0.5384 S33: -0.0898
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESID 110 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5513 20.7737 -13.8367
REMARK 3 T TENSOR
REMARK 3 T11: 0.4632 T22: 0.3660
REMARK 3 T33: 0.5080 T12: -0.0520
REMARK 3 T13: -0.0286 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 3.3205 L22: 1.4256
REMARK 3 L33: 1.4555 L12: 1.4052
REMARK 3 L13: -1.2926 L23: -0.0440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: -0.5636 S13: -0.6623
REMARK 3 S21: 0.1356 S22: -0.1764 S23: -0.2715
REMARK 3 S31: 0.6491 S32: -0.0601 S33: 0.0807
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 180 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7721 29.4786 -25.5606
REMARK 3 T TENSOR
REMARK 3 T11: 0.2191 T22: 0.2324
REMARK 3 T33: 0.2483 T12: 0.0098
REMARK 3 T13: 0.0578 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.4277 L22: 2.9305
REMARK 3 L33: 3.8562 L12: -0.1811
REMARK 3 L13: 0.0945 L23: -0.4687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0057 S12: 0.3205 S13: -0.1113
REMARK 3 S21: -0.3182 S22: -0.0070 S23: -0.3620
REMARK 3 S31: 0.2626 S32: 0.2355 S33: 0.0197
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 4LHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB080632.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-09
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33489
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 27.342
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.61700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.0
REMARK 200 STARTING MODEL: 1R1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULPHATE, 100MM CITRATE,
REMARK 280 0.17M TARTRATE, 20% BENZAMIDINE, PH 5.8, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
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 49.87750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.09550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.87750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.09550
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 420 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 THR B 133
REMARK 465 GLY B 134
REMARK 465 GLY B 135
REMARK 465 GLY B 136
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 491 O HOH B 402 2.13
REMARK 500 O HOH A 408 O HOH A 409 2.15
REMARK 500 O TYR B 159 O HOH B 435 2.15
REMARK 500 OD1 ASP A 194 NH1 ARG A 220 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 A 409 O HOH B 417 4454 2.15
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 GLU A 137 N - CA - C ANGL. DEV. = -21.3 DEGREES
REMARK 500 GLY B 19 N - CA - C ANGL. DEV. = -17.9 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 ASN A 18 -80.24 -112.28
REMARK 500 THR A 60 -81.98 -123.87
REMARK 500 SER A 97 -134.43 51.23
REMARK 500 MET A 98 -32.23 -36.54
REMARK 500 ALA A 129 72.23 -113.40
REMARK 500 GLU A 137 -60.03 -102.14
REMARK 500 SER B 2 -155.20 -135.51
REMARK 500 GLN B 4 -18.49 -141.75
REMARK 500 ASN B 18 -77.83 -108.42
REMARK 500 THR B 60 -73.15 -133.47
REMARK 500 HIS B 61 144.18 -170.23
REMARK 500 SER B 97 -133.26 58.20
REMARK 500 LEU B 138 82.56 -156.02
REMARK 500 TYR B 225 -168.75 -100.98
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 CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
DBREF 4LHE A 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4LHE B 1 250 UNP P82597 MGLP_BAC25 1 250
SEQRES 1 A 250 MET SER GLU GLN TYR PRO VAL LEU SER GLY ALA GLU PRO
SEQRES 2 A 250 PHE TYR ALA GLU ASN GLY PRO VAL GLY VAL LEU LEU VAL
SEQRES 3 A 250 HIS GLY PHE THR GLY THR PRO HIS SER MET ARG PRO LEU
SEQRES 4 A 250 ALA GLU ALA TYR ALA LYS ALA GLY TYR THR VAL CYS LEU
SEQRES 5 A 250 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 A 250 GLU ARG THR THR PHE HIS ASP TRP VAL ALA SER VAL GLU
SEQRES 7 A 250 GLU GLY TYR GLY TRP LEU LYS GLN ARG CYS GLN THR ILE
SEQRES 8 A 250 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 A 250 TYR LEU ALA GLU HIS HIS PRO ASP ILE CYS GLY ILE VAL
SEQRES 10 A 250 PRO ILE ASN ALA ALA VAL ASP ILE PRO ALA ILE ALA ALA
SEQRES 11 A 250 GLY MET THR GLY GLY GLY GLU LEU PRO ARG TYR LEU ASP
SEQRES 12 A 250 SER ILE GLY SER ASP LEU LYS ASN PRO ASP VAL LYS GLU
SEQRES 13 A 250 LEU ALA TYR GLU LYS THR PRO THR ALA SER LEU LEU GLN
SEQRES 14 A 250 LEU ALA ARG LEU MET ALA GLN THR LYS ALA LYS LEU ASP
SEQRES 15 A 250 ARG ILE VAL CYS PRO ALA LEU ILE PHE VAL SER ASP GLU
SEQRES 16 A 250 ASP HIS VAL VAL PRO PRO GLY ASN ALA ASP ILE ILE PHE
SEQRES 17 A 250 GLN GLY ILE SER SER THR GLU LYS GLU ILE VAL ARG LEU
SEQRES 18 A 250 ARG ASN SER TYR HIS VAL ALA THR LEU ASP TYR ASP GLN
SEQRES 19 A 250 PRO MET ILE ILE GLU ARG SER LEU GLU PHE PHE ALA LYS
SEQRES 20 A 250 HIS ALA GLY
SEQRES 1 B 250 MET SER GLU GLN TYR PRO VAL LEU SER GLY ALA GLU PRO
SEQRES 2 B 250 PHE TYR ALA GLU ASN GLY PRO VAL GLY VAL LEU LEU VAL
SEQRES 3 B 250 HIS GLY PHE THR GLY THR PRO HIS SER MET ARG PRO LEU
SEQRES 4 B 250 ALA GLU ALA TYR ALA LYS ALA GLY TYR THR VAL CYS LEU
SEQRES 5 B 250 PRO ARG LEU LYS GLY HIS GLY THR HIS TYR GLU ASP MET
SEQRES 6 B 250 GLU ARG THR THR PHE HIS ASP TRP VAL ALA SER VAL GLU
SEQRES 7 B 250 GLU GLY TYR GLY TRP LEU LYS GLN ARG CYS GLN THR ILE
SEQRES 8 B 250 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 B 250 TYR LEU ALA GLU HIS HIS PRO ASP ILE CYS GLY ILE VAL
SEQRES 10 B 250 PRO ILE ASN ALA ALA VAL ASP ILE PRO ALA ILE ALA ALA
SEQRES 11 B 250 GLY MET THR GLY GLY GLY GLU LEU PRO ARG TYR LEU ASP
SEQRES 12 B 250 SER ILE GLY SER ASP LEU LYS ASN PRO ASP VAL LYS GLU
SEQRES 13 B 250 LEU ALA TYR GLU LYS THR PRO THR ALA SER LEU LEU GLN
SEQRES 14 B 250 LEU ALA ARG LEU MET ALA GLN THR LYS ALA LYS LEU ASP
SEQRES 15 B 250 ARG ILE VAL CYS PRO ALA LEU ILE PHE VAL SER ASP GLU
SEQRES 16 B 250 ASP HIS VAL VAL PRO PRO GLY ASN ALA ASP ILE ILE PHE
SEQRES 17 B 250 GLN GLY ILE SER SER THR GLU LYS GLU ILE VAL ARG LEU
SEQRES 18 B 250 ARG ASN SER TYR HIS VAL ALA THR LEU ASP TYR ASP GLN
SEQRES 19 B 250 PRO MET ILE ILE GLU ARG SER LEU GLU PHE PHE ALA LYS
SEQRES 20 B 250 HIS ALA GLY
HET CL A 301 1
HET SO4 A 302 5
HET CL B 301 1
HET SO4 B 302 5
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *154(H2 O)
HELIX 1 1 THR A 32 SER A 35 5 4
HELIX 2 2 MET A 36 ALA A 46 1 11
HELIX 3 3 HIS A 61 THR A 68 1 8
HELIX 4 4 THR A 69 CYS A 88 1 20
HELIX 5 5 SER A 97 HIS A 110 1 14
HELIX 6 6 THR A 164 LYS A 180 1 17
HELIX 7 7 LEU A 181 ILE A 184 5 4
HELIX 8 8 PRO A 201 ILE A 211 1 11
HELIX 9 9 ASP A 233 HIS A 248 1 16
HELIX 10 10 THR B 32 SER B 35 5 4
HELIX 11 11 MET B 36 ALA B 46 1 11
HELIX 12 12 HIS B 61 ARG B 67 1 7
HELIX 13 13 THR B 69 CYS B 88 1 20
HELIX 14 14 SER B 97 HIS B 110 1 14
HELIX 15 15 THR B 164 LYS B 180 1 17
HELIX 16 16 LEU B 181 ILE B 184 5 4
HELIX 17 17 GLY B 202 ILE B 211 1 10
HELIX 18 18 ASP B 233 HIS B 248 1 16
SHEET 1 A 5 PHE A 14 ALA A 16 0
SHEET 2 A 5 THR A 49 LEU A 52 -1 O VAL A 50 N ALA A 16
SHEET 3 A 5 VAL A 21 VAL A 26 1 N LEU A 25 O CYS A 51
SHEET 4 A 5 THR A 90 LEU A 96 1 O THR A 94 N VAL A 26
SHEET 5 A 5 GLY A 115 ILE A 119 1 O VAL A 117 N VAL A 93
SHEET 1 B 2 TYR A 141 ASP A 143 0
SHEET 2 B 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 C 2 ALA A 188 SER A 193 0
SHEET 2 C 2 LYS A 216 LEU A 221 1 O VAL A 219 N ILE A 190
SHEET 1 D 5 PHE B 14 ALA B 16 0
SHEET 2 D 5 THR B 49 LEU B 52 -1 O LEU B 52 N PHE B 14
SHEET 3 D 5 VAL B 21 VAL B 26 1 N LEU B 25 O CYS B 51
SHEET 4 D 5 THR B 90 LEU B 96 1 O THR B 90 N GLY B 22
SHEET 5 D 5 GLY B 115 ILE B 119 1 O ILE B 119 N GLY B 95
SHEET 1 E 2 TYR B 141 ASP B 143 0
SHEET 2 E 2 LYS B 161 PRO B 163 -1 O THR B 162 N LEU B 142
SHEET 1 F 2 ALA B 188 SER B 193 0
SHEET 2 F 2 LYS B 216 LEU B 221 1 O LEU B 221 N VAL B 192
SITE 1 AC1 3 THR A 32 SER A 35 LEU A 157
SITE 1 AC2 6 GLY A 28 PHE A 29 THR A 30 SER A 97
SITE 2 AC2 6 MET A 98 HIS A 226
SITE 1 AC3 3 THR B 32 GLU B 156 LEU B 157
SITE 1 AC4 7 GLY B 28 PHE B 29 THR B 30 SER B 97
SITE 2 AC4 7 MET B 98 HIS B 226 HOH B 421
CRYST1 99.755 106.191 43.053 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010025 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023227 0.00000
TER 1925 GLY A 250
TER 3831 GLY B 250
MASTER 435 0 4 18 18 0 6 6 3995 2 10 40
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