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HEADER HYDROLASE 25-APR-13 4KE8
TITLE CRYSTAL STRUCTURE OF MONOGLYCERIDE LIPASE FROM BACILLUS SP. H257 IN
TITLE 2 COMPLEX WITH MONOPALMITOYL GLYCEROL ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 129908;
SOURCE 4 STRAIN: H-257;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A(+)
KEYWDS ALPHA/BETA HYDROLASE, MONOGLYCERIDE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
REVDAT 1 18-SEP-13 4KE8 0
JRNL AUTH S.RENGACHARI,P.ASCHAUER,K.GRUBER,I.DREVENY,M.OBERER
JRNL TITL CONFORMATIONAL PLASTICITY AND LIGAND BINDING OF BACTERIAL
JRNL TITL 2 MONOACYLGLYCEROL LIPASE
JRNL REF J.BIOL.CHEM. 2013
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 81489
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 43.7488 - 4.4573 0.98 6179 155 0.1397 0.1604
REMARK 3 2 4.4573 - 3.5384 0.98 6061 153 0.1488 0.1773
REMARK 3 3 3.5384 - 3.0912 0.98 6104 152 0.1792 0.2359
REMARK 3 4 3.0912 - 2.8087 0.98 6042 153 0.1930 0.2314
REMARK 3 5 2.8087 - 2.6074 0.98 6014 151 0.1872 0.2384
REMARK 3 6 2.6074 - 2.4537 0.96 5924 148 0.1833 0.2284
REMARK 3 7 2.4537 - 2.3308 0.96 5909 150 0.1826 0.1970
REMARK 3 8 2.3308 - 2.2293 0.90 5517 138 0.2034 0.2738
REMARK 3 9 2.2293 - 2.1435 0.87 5363 136 0.1924 0.2656
REMARK 3 10 2.1435 - 2.0696 0.93 5715 143 0.2039 0.2350
REMARK 3 11 2.0696 - 2.0048 0.90 5532 139 0.2095 0.2556
REMARK 3 12 2.0048 - 1.9475 0.86 5269 133 0.2259 0.2975
REMARK 3 13 1.9475 - 1.8963 0.83 5092 128 0.2704 0.2724
REMARK 3 14 1.8963 - 1.8500 0.77 4769 120 0.2438 0.3056
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.860
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) : -9.43920
REMARK 3 B22 (A**2) : 17.27940
REMARK 3 B33 (A**2) : -7.84030
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.43050
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7951
REMARK 3 ANGLE : 1.043 10811
REMARK 3 CHIRALITY : 0.065 1202
REMARK 3 PLANARITY : 0.005 1391
REMARK 3 DIHEDRAL : 13.402 2855
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
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 : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88070
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 43.737
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 FOR THE DATA SET : 17.9000
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) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
REMARK 200 R SYM FOR SHELL (I) : 0.30200
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC ACID PH 5.2 AND 18% PEG
REMARK 280 3350, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.56250
REMARK 290 SMTRY3 2 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 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 350
REMARK 350 BIOMOLECULE: 3
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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 250
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 250
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 LYS D 155 CD CE NZ
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 ND1 HIS B 61 OE1 GLU B 63 2.09
REMARK 500 ND1 HIS A 61 OE1 GLU A 63 2.16
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 B 20 C - N - CA ANGL. DEV. = 10.3 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 -121.68 -132.60
REMARK 500 THR A 30 -1.04 67.76
REMARK 500 THR A 60 -83.93 -117.71
REMARK 500 SER A 97 -120.92 64.45
REMARK 500 GLU A 195 55.69 -110.60
REMARK 500 TYR A 225 -149.31 -102.86
REMARK 500 ASN B 18 -121.01 -139.15
REMARK 500 THR B 60 -78.95 -118.12
REMARK 500 SER B 97 -122.64 66.02
REMARK 500 GLU B 195 52.55 -113.05
REMARK 500 TYR B 225 -146.62 -101.74
REMARK 500 ASN C 18 -114.53 -131.44
REMARK 500 THR C 30 -3.41 69.85
REMARK 500 THR C 60 -73.85 -123.35
REMARK 500 SER C 97 -118.13 65.79
REMARK 500 TYR C 225 -149.26 -96.18
REMARK 500 ASN D 18 -118.86 -138.40
REMARK 500 THR D 30 -3.89 71.54
REMARK 500 THR D 60 -75.51 -118.12
REMARK 500 SER D 97 -119.27 64.57
REMARK 500 TYR D 225 -145.68 -94.66
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 1QY A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QY B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QY C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QY D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KE6 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE7 RELATED DB: PDB
REMARK 900 RELATED ID: 4KE9 RELATED DB: PDB
REMARK 900 RELATED ID: 4KEA RELATED DB: PDB
DBREF 4KE8 A 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE8 B 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE8 C 1 250 UNP P82597 MGLP_BAC25 1 250
DBREF 4KE8 D 1 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 4KE8 MET A -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY A -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER A -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER A -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER A -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER A -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY A -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 LEU A -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 VAL A -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 PRO A -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 ARG A -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY A -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER A -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS A 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 MET B -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY B -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER B -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER B -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER B -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER B -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY B -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 LEU B -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 VAL B -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 PRO B -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 ARG B -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY B -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER B -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS B 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 MET C -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY C -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER C -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER C -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER C -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER C -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY C -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 LEU C -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 VAL C -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 PRO C -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 ARG C -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY C -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER C -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS C 0 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 MET D -19 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY D -18 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER D -17 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER D -16 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -15 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -14 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -13 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -12 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -11 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D -10 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER D -9 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER D -8 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY D -7 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 LEU D -6 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 VAL D -5 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 PRO D -4 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 ARG D -3 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 GLY D -2 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 SER D -1 UNP P82597 EXPRESSION TAG
SEQADV 4KE8 HIS D 0 UNP P82597 EXPRESSION TAG
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 A 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 A 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 A 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 A 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 A 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 A 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 A 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 A 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 A 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 A 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 A 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 A 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 A 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 A 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 A 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 A 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 A 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 A 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 A 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 B 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 B 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 B 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 B 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 B 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 B 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 B 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 B 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 B 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 B 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 B 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 B 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 B 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 B 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 B 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 B 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 B 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 B 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 B 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 B 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 C 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 C 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 C 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 C 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 C 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 C 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 C 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 C 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 C 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 C 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 C 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 C 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 C 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 C 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 C 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 C 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 C 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 C 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 C 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 C 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
SEQRES 1 D 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 D 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 D 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 D 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 D 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 D 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 D 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 D 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 D 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 D 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 D 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 D 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 D 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 D 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 D 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 D 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 D 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 D 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 D 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 D 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
HET 1QY A 301 23
HET 1QY B 301 23
HET 1QY C 301 23
HET 1QY D 301 23
HETNAM 1QY TETRADECYL HYDROGEN (R)-(3-AZIDOPROPYL)PHOSPHONATE
FORMUL 5 1QY 4(C17 H36 N3 O3 P)
FORMUL 9 HOH *902(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 ARG A 67 1 7
HELIX 4 4 THR A 69 GLN A 86 1 18
HELIX 5 5 SER A 97 HIS A 110 1 14
HELIX 6 6 ILE A 125 THR A 133 1 9
HELIX 7 7 THR A 164 LYS A 180 1 17
HELIX 8 8 LEU A 181 ILE A 184 5 4
HELIX 9 9 GLY A 202 ILE A 211 1 10
HELIX 10 10 VAL A 227 ASP A 231 5 5
HELIX 11 11 ASP A 233 ALA A 249 1 17
HELIX 12 12 THR B 32 SER B 35 5 4
HELIX 13 13 MET B 36 ALA B 46 1 11
HELIX 14 14 HIS B 61 ARG B 67 1 7
HELIX 15 15 THR B 69 CYS B 88 1 20
HELIX 16 16 SER B 97 HIS B 110 1 14
HELIX 17 17 ILE B 125 THR B 133 1 9
HELIX 18 18 THR B 164 LYS B 180 1 17
HELIX 19 19 LEU B 181 ILE B 184 5 4
HELIX 20 20 GLY B 202 ILE B 211 1 10
HELIX 21 21 ASP B 233 ALA B 249 1 17
HELIX 22 22 THR C 32 SER C 35 5 4
HELIX 23 23 MET C 36 ALA C 46 1 11
HELIX 24 24 HIS C 61 THR C 68 1 8
HELIX 25 25 THR C 69 GLN C 86 1 18
HELIX 26 26 SER C 97 HIS C 110 1 14
HELIX 27 27 ILE C 125 THR C 133 1 9
HELIX 28 28 THR C 164 LYS C 180 1 17
HELIX 29 29 LEU C 181 ILE C 184 5 4
HELIX 30 30 GLY C 202 ILE C 211 1 10
HELIX 31 31 ASP C 233 GLY C 250 1 18
HELIX 32 32 THR D 32 SER D 35 5 4
HELIX 33 33 MET D 36 ALA D 46 1 11
HELIX 34 34 HIS D 61 THR D 68 1 8
HELIX 35 35 THR D 69 GLN D 86 1 18
HELIX 36 36 SER D 97 HIS D 110 1 14
HELIX 37 37 ILE D 125 THR D 133 1 9
HELIX 38 38 THR D 164 LYS D 180 1 17
HELIX 39 39 LEU D 181 ILE D 184 5 4
HELIX 40 40 GLY D 202 ILE D 211 1 10
HELIX 41 41 ASP D 233 GLY D 250 1 18
SHEET 1 A 5 PHE A 14 ALA A 16 0
SHEET 2 A 5 THR A 49 LEU A 52 -1 O LEU A 52 N PHE A 14
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 90 N GLY A 22
SHEET 5 A 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
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 LEU A 221 N VAL A 192
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 GLU B 217 N ILE B 190
SHEET 1 G 5 PHE C 14 ALA C 16 0
SHEET 2 G 5 THR C 49 LEU C 52 -1 O LEU C 52 N PHE C 14
SHEET 3 G 5 VAL C 21 VAL C 26 1 N LEU C 25 O CYS C 51
SHEET 4 G 5 THR C 90 LEU C 96 1 O THR C 90 N GLY C 22
SHEET 5 G 5 GLY C 115 ILE C 119 1 O ILE C 119 N GLY C 95
SHEET 1 H 2 TYR C 141 ASP C 143 0
SHEET 2 H 2 LYS C 161 PRO C 163 -1 O THR C 162 N LEU C 142
SHEET 1 I 2 ALA C 188 SER C 193 0
SHEET 2 I 2 LYS C 216 LEU C 221 1 O LEU C 221 N VAL C 192
SHEET 1 J 5 PHE D 14 ALA D 16 0
SHEET 2 J 5 THR D 49 LEU D 52 -1 O LEU D 52 N PHE D 14
SHEET 3 J 5 VAL D 21 VAL D 26 1 N LEU D 25 O CYS D 51
SHEET 4 J 5 THR D 90 LEU D 96 1 O THR D 90 N GLY D 22
SHEET 5 J 5 GLY D 115 ILE D 119 1 O ILE D 119 N GLY D 95
SHEET 1 K 2 TYR D 141 ASP D 143 0
SHEET 2 K 2 LYS D 161 PRO D 163 -1 O THR D 162 N LEU D 142
SHEET 1 L 2 ALA D 188 SER D 193 0
SHEET 2 L 2 LYS D 216 LEU D 221 1 O LEU D 221 N VAL D 192
LINK OG SER A 97 P1 1QY A 301 1555 1555 1.62
LINK OG SER D 97 P1 1QY D 301 1555 1555 1.58
LINK OG SER B 97 P1 1QY B 301 1555 1555 1.62
LINK OG SER C 97 P1 1QY C 301 1555 1555 1.66
SITE 1 AC1 13 GLY A 28 PHE A 29 SER A 97 MET A 98
SITE 2 AC1 13 ALA A 127 ILE A 128 GLY A 131 LEU A 142
SITE 3 AC1 13 LEU A 170 VAL A 198 HIS A 226 HOH A 548
SITE 4 AC1 13 HOH A 604
SITE 1 AC2 14 GLY B 28 PHE B 29 GLY B 31 SER B 97
SITE 2 AC2 14 MET B 98 ILE B 125 ALA B 127 GLY B 131
SITE 3 AC2 14 LEU B 138 LEU B 142 GLU B 156 VAL B 198
SITE 4 AC2 14 HIS B 226 HOH B 515
SITE 1 AC3 17 GLY C 28 PHE C 29 SER C 97 MET C 98
SITE 2 AC3 17 ALA C 127 ILE C 128 MET C 132 LEU C 142
SITE 3 AC3 17 ILE C 145 GLY C 146 SER C 147 ASP C 148
SITE 4 AC3 17 GLU C 156 VAL C 198 VAL C 199 HIS C 226
SITE 5 AC3 17 VAL C 227
SITE 1 AC4 18 LEU B 168 GLY D 28 PHE D 29 SER D 97
SITE 2 AC4 18 MET D 98 ILE D 125 ALA D 127 ILE D 128
SITE 3 AC4 18 LEU D 142 ILE D 145 GLY D 146 SER D 147
SITE 4 AC4 18 ASP D 148 GLU D 156 LEU D 170 VAL D 198
SITE 5 AC4 18 HIS D 226 VAL D 227
CRYST1 77.015 81.125 85.611 90.00 100.26 90.00 P 1 21 1 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 0.012984 0.000000 0.002350 0.00000
SCALE2 0.000000 0.012327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011871 0.00000
TER 1913 ALA A 249
TER 3827 ALA B 249
TER 5753 GLY C 250
TER 7668 GLY D 250
MASTER 414 0 4 41 36 0 18 6 8645 4 96 84
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