HEADER OXIDOREDUCTASE, MEMBRANE PROTEIN 12-JUL-14 4QUV
TITLE STRUCTURE OF AN INTEGRAL MEMBRANE DELTA(14)-STEROL REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA(14)-STEROL REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.3.1.70;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOMICROBIUM ALCALIPHILUM;
SOURCE 3 ORGANISM_TAXID: 1091494;
SOURCE 4 STRAIN: DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;
SOURCE 5 GENE: ERG, MEALZ_1312;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MEMBRANE PROTEIN, CHOLESTEROL BIOSYNTHESIS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,G.BLOBEL
REVDAT 4 28-FEB-24 4QUV 1 REMARK
REVDAT 3 28-JAN-15 4QUV 1 JRNL
REVDAT 2 29-OCT-14 4QUV 1 JRNL
REVDAT 1 08-OCT-14 4QUV 0
JRNL AUTH X.LI,R.ROBERTI,G.BLOBEL
JRNL TITL STRUCTURE OF AN INTEGRAL MEMBRANE STEROL REDUCTASE FROM
JRNL TITL 2 METHYLOMICROBIUM ALCALIPHILUM.
JRNL REF NATURE V. 517 104 2015
JRNL REFN ISSN 0028-0836
JRNL PMID 25307054
JRNL DOI 10.1038/NATURE13797
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.5
REMARK 3 NUMBER OF REFLECTIONS : 30541
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1526
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 37.2588 - 6.0931 0.95 3340 182 0.2322 0.2751
REMARK 3 2 6.0931 - 4.8397 0.98 3485 210 0.2235 0.2580
REMARK 3 3 4.8397 - 4.2289 0.97 3429 184 0.1889 0.2538
REMARK 3 4 4.2289 - 3.8426 0.98 3474 165 0.2114 0.2877
REMARK 3 5 3.8426 - 3.5675 0.97 3429 176 0.2397 0.3010
REMARK 3 6 3.5675 - 3.3573 0.89 3145 154 0.2634 0.3098
REMARK 3 7 3.3573 - 3.1892 0.73 2568 125 0.2945 0.3276
REMARK 3 8 3.1892 - 3.0505 0.60 2132 107 0.3149 0.3474
REMARK 3 9 3.0505 - 2.9331 0.49 1710 102 0.2988 0.3629
REMARK 3 10 2.9331 - 2.8319 0.37 1327 68 0.2990 0.3213
REMARK 3 11 2.8319 - 2.7434 0.28 976 53 0.2509 0.3653
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 6736
REMARK 3 ANGLE : 1.646 9216
REMARK 3 CHIRALITY : 0.084 975
REMARK 3 PLANARITY : 0.009 1104
REMARK 3 DIHEDRAL : 16.652 2297
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9950 -6.2620 13.7212
REMARK 3 T TENSOR
REMARK 3 T11: 0.4399 T22: 0.7669
REMARK 3 T33: 0.8130 T12: 0.0621
REMARK 3 T13: -0.1006 T23: 0.4188
REMARK 3 L TENSOR
REMARK 3 L11: 2.0578 L22: 1.1621
REMARK 3 L33: 3.0582 L12: 0.2142
REMARK 3 L13: 0.1193 L23: 0.2509
REMARK 3 S TENSOR
REMARK 3 S11: 0.1819 S12: -0.7167 S13: -1.3086
REMARK 3 S21: 0.3181 S22: 0.1559 S23: 0.1382
REMARK 3 S31: 0.2445 S32: -0.4679 S33: -0.3491
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3106 6.4695 -13.6064
REMARK 3 T TENSOR
REMARK 3 T11: 0.3488 T22: 0.7887
REMARK 3 T33: 0.3986 T12: 0.1652
REMARK 3 T13: -0.1149 T23: 0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 2.9161 L22: 2.6286
REMARK 3 L33: 2.5769 L12: -0.0574
REMARK 3 L13: 0.1889 L23: -0.2693
REMARK 3 S TENSOR
REMARK 3 S11: 0.3091 S12: 1.4954 S13: -0.3261
REMARK 3 S21: -0.1914 S22: -0.1818 S23: 0.2339
REMARK 3 S31: -0.0846 S32: 0.1055 S33: -0.0522
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 4QUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30541
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 37.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.8
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 28.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : 0.51400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 0.2 M NH4AC, 30% (V/V)
REMARK 280 PENTAERYTHRITOL ETHOXYLATE (15/4 EO/OH), PH 7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 4
REMARK 465 GLU A 5
REMARK 465 SER A 6
REMARK 465 ARG A 7
REMARK 465 ASP A 8
REMARK 465 ASN A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 VAL A 12
REMARK 465 ASP A 13
REMARK 465 ALA A 14
REMARK 465 VAL A 15
REMARK 465 ARG A 16
REMARK 465 GLN A 17
REMARK 465 LYS A 18
REMARK 465 TYR A 19
REMARK 465 GLY A 20
REMARK 465 PHE A 21
REMARK 465 GLY A 22
REMARK 465 LEU A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 LYS A 168
REMARK 465 GLN A 169
REMARK 465 TRP A 170
REMARK 465 GLU A 171
REMARK 465 ARG A 172
REMARK 465 PRO A 173
REMARK 465 THR A 174
REMARK 465 GLY A 175
REMARK 465 ARG A 176
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 GLN B 4
REMARK 465 GLU B 5
REMARK 465 SER B 6
REMARK 465 ARG B 7
REMARK 465 ASP B 8
REMARK 465 ASN B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 VAL B 12
REMARK 465 ASP B 13
REMARK 465 ALA B 14
REMARK 465 VAL B 15
REMARK 465 ARG B 16
REMARK 465 GLN B 17
REMARK 465 LYS B 18
REMARK 465 TYR B 19
REMARK 465 GLY B 20
REMARK 465 PHE B 21
REMARK 465 GLY B 22
REMARK 465 PHE B 23
REMARK 465 PHE B 162
REMARK 465 TRP B 163
REMARK 465 GLY B 164
REMARK 465 LEU B 165
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 LYS B 168
REMARK 465 GLN B 169
REMARK 465 TRP B 170
REMARK 465 GLU B 171
REMARK 465 ARG B 172
REMARK 465 PRO B 173
REMARK 465 THR B 174
REMARK 465 GLY B 175
REMARK 465 ARG B 176
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 SER B 193 CB OG
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 GLY A 158 CD2 PHE A 162 1.93
REMARK 500 O ARG B 328 N ALA B 335 2.14
REMARK 500 O PRO B 92 ND2 ASN B 112 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 LEU A 293 CA - CB - CG ANGL. DEV. = 14.0 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 MET A 99 -158.00 62.79
REMARK 500 ASP A 103 -50.94 75.01
REMARK 500 MET A 130 1.12 -69.78
REMARK 500 ALA A 186 11.40 84.59
REMARK 500 LEU A 187 -125.77 59.55
REMARK 500 ALA A 202 -71.03 -112.40
REMARK 500 ARG A 203 -70.84 -66.52
REMARK 500 HIS A 224 -3.68 -142.38
REMARK 500 VAL A 252 3.48 -69.21
REMARK 500 PHE A 263 -130.08 56.28
REMARK 500 THR A 290 52.54 -101.37
REMARK 500 ASP A 325 78.97 -165.39
REMARK 500 ALA A 375 -146.68 62.95
REMARK 500 ILE A 422 -54.11 -129.68
REMARK 500 TYR B 46 30.18 -90.63
REMARK 500 ALA B 56 -60.26 66.77
REMARK 500 MET B 99 -146.39 59.05
REMARK 500 ASP B 103 -55.42 75.22
REMARK 500 ASP B 140 -74.74 -59.76
REMARK 500 LEU B 187 -119.86 63.79
REMARK 500 SER B 193 -6.06 97.19
REMARK 500 ARG B 203 -72.37 -64.82
REMARK 500 HIS B 224 -2.94 -145.71
REMARK 500 THR B 290 54.67 -97.49
REMARK 500 TRP B 331 -151.05 58.63
REMARK 500 ALA B 375 -145.34 64.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NDP A 501
REMARK 610 NDP B 501
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 501
DBREF 4QUV A 1 427 UNP G4SW86 G4SW86_META2 1 427
DBREF 4QUV B 1 427 UNP G4SW86 G4SW86_META2 1 427
SEQRES 1 A 427 MET SER GLU GLN GLU SER ARG ASP ASN ALA ALA VAL ASP
SEQRES 2 A 427 ALA VAL ARG GLN LYS TYR GLY PHE GLY PHE SER TRP LEU
SEQRES 3 A 427 VAL LEU MET ILE ALA LEU PRO PRO LEU VAL TYR TYR LEU
SEQRES 4 A 427 TRP ILE CYS VAL THR TYR TYR GLN GLY GLU LEU VAL PHE
SEQRES 5 A 427 THR SER ASP ALA ALA ALA TRP ARG ARG PHE TRP SER HIS
SEQRES 6 A 427 VAL ALA PRO PRO THR TRP HIS ALA ALA GLY LEU TYR ALA
SEQRES 7 A 427 ALA TRP PHE LEU GLY GLN ALA ALA LEU GLN VAL TRP ALA
SEQRES 8 A 427 PRO GLY PRO THR VAL GLN GLY MET LYS LEU PRO ASP GLY
SEQRES 9 A 427 SER ARG LEU ASP TYR ARG MET ASN GLY ILE PHE SER PHE
SEQRES 10 A 427 LEU PHE THR LEU ALA VAL VAL PHE GLY LEU VAL THR MET
SEQRES 11 A 427 GLY TRP LEU ASP ALA THR VAL LEU TYR ASP GLN LEU GLY
SEQRES 12 A 427 PRO LEU LEU THR VAL VAL ASN ILE PHE THR PHE VAL PHE
SEQRES 13 A 427 ALA GLY PHE LEU TYR PHE TRP GLY LEU ASN GLY LYS GLN
SEQRES 14 A 427 TRP GLU ARG PRO THR GLY ARG PRO PHE TYR ASP TYR PHE
SEQRES 15 A 427 MET GLY THR ALA LEU ASN PRO ARG ILE GLY SER LEU ASP
SEQRES 16 A 427 LEU LYS LEU PHE CYS GLU ALA ARG PRO GLY MET ILE PHE
SEQRES 17 A 427 TRP LEU LEU MET ASN LEU SER MET ALA ALA LYS GLN TYR
SEQRES 18 A 427 GLU LEU HIS GLY THR VAL THR VAL PRO MET LEU LEU VAL
SEQRES 19 A 427 VAL GLY PHE GLN SER PHE TYR LEU ILE ASP TYR PHE ILE
SEQRES 20 A 427 HIS GLU GLU ALA VAL LEU THR THR TRP ASP ILE LYS HIS
SEQRES 21 A 427 GLU LYS PHE GLY TRP MET LEU CYS TRP GLY ASP LEU VAL
SEQRES 22 A 427 TRP LEU PRO PHE THR TYR THR LEU GLN ALA GLN TYR LEU
SEQRES 23 A 427 VAL HIS HIS THR HIS ASP LEU PRO VAL TRP GLY ILE ILE
SEQRES 24 A 427 ALA ILE VAL ALA LEU ASN LEU ALA GLY TYR ALA ILE PHE
SEQRES 25 A 427 ARG GLY ALA ASN ILE GLN LYS HIS HIS PHE ARG ARG ASP
SEQRES 26 A 427 PRO ASN ARG ILE VAL TRP GLY LYS PRO ALA LYS TYR ILE
SEQRES 27 A 427 LYS THR LYS GLN GLY SER LEU LEU LEU THR SER GLY TRP
SEQRES 28 A 427 TRP GLY ILE ALA ARG HIS MET ASN TYR PHE GLY ASP LEU
SEQRES 29 A 427 MET ILE ALA LEU SER TRP CYS LEU PRO ALA ALA PHE GLY
SEQRES 30 A 427 SER PRO ILE PRO TYR PHE HIS ILE VAL TYR PHE THR ILE
SEQRES 31 A 427 LEU LEU LEU HIS ARG GLU LYS ARG ASP ASP ALA MET CYS
SEQRES 32 A 427 LEU ALA LYS TYR GLY GLU ASP TRP LEU GLN TYR ARG LYS
SEQRES 33 A 427 LYS VAL PRO TRP ARG ILE VAL PRO LYS ILE TYR
SEQRES 1 B 427 MET SER GLU GLN GLU SER ARG ASP ASN ALA ALA VAL ASP
SEQRES 2 B 427 ALA VAL ARG GLN LYS TYR GLY PHE GLY PHE SER TRP LEU
SEQRES 3 B 427 VAL LEU MET ILE ALA LEU PRO PRO LEU VAL TYR TYR LEU
SEQRES 4 B 427 TRP ILE CYS VAL THR TYR TYR GLN GLY GLU LEU VAL PHE
SEQRES 5 B 427 THR SER ASP ALA ALA ALA TRP ARG ARG PHE TRP SER HIS
SEQRES 6 B 427 VAL ALA PRO PRO THR TRP HIS ALA ALA GLY LEU TYR ALA
SEQRES 7 B 427 ALA TRP PHE LEU GLY GLN ALA ALA LEU GLN VAL TRP ALA
SEQRES 8 B 427 PRO GLY PRO THR VAL GLN GLY MET LYS LEU PRO ASP GLY
SEQRES 9 B 427 SER ARG LEU ASP TYR ARG MET ASN GLY ILE PHE SER PHE
SEQRES 10 B 427 LEU PHE THR LEU ALA VAL VAL PHE GLY LEU VAL THR MET
SEQRES 11 B 427 GLY TRP LEU ASP ALA THR VAL LEU TYR ASP GLN LEU GLY
SEQRES 12 B 427 PRO LEU LEU THR VAL VAL ASN ILE PHE THR PHE VAL PHE
SEQRES 13 B 427 ALA GLY PHE LEU TYR PHE TRP GLY LEU ASN GLY LYS GLN
SEQRES 14 B 427 TRP GLU ARG PRO THR GLY ARG PRO PHE TYR ASP TYR PHE
SEQRES 15 B 427 MET GLY THR ALA LEU ASN PRO ARG ILE GLY SER LEU ASP
SEQRES 16 B 427 LEU LYS LEU PHE CYS GLU ALA ARG PRO GLY MET ILE PHE
SEQRES 17 B 427 TRP LEU LEU MET ASN LEU SER MET ALA ALA LYS GLN TYR
SEQRES 18 B 427 GLU LEU HIS GLY THR VAL THR VAL PRO MET LEU LEU VAL
SEQRES 19 B 427 VAL GLY PHE GLN SER PHE TYR LEU ILE ASP TYR PHE ILE
SEQRES 20 B 427 HIS GLU GLU ALA VAL LEU THR THR TRP ASP ILE LYS HIS
SEQRES 21 B 427 GLU LYS PHE GLY TRP MET LEU CYS TRP GLY ASP LEU VAL
SEQRES 22 B 427 TRP LEU PRO PHE THR TYR THR LEU GLN ALA GLN TYR LEU
SEQRES 23 B 427 VAL HIS HIS THR HIS ASP LEU PRO VAL TRP GLY ILE ILE
SEQRES 24 B 427 ALA ILE VAL ALA LEU ASN LEU ALA GLY TYR ALA ILE PHE
SEQRES 25 B 427 ARG GLY ALA ASN ILE GLN LYS HIS HIS PHE ARG ARG ASP
SEQRES 26 B 427 PRO ASN ARG ILE VAL TRP GLY LYS PRO ALA LYS TYR ILE
SEQRES 27 B 427 LYS THR LYS GLN GLY SER LEU LEU LEU THR SER GLY TRP
SEQRES 28 B 427 TRP GLY ILE ALA ARG HIS MET ASN TYR PHE GLY ASP LEU
SEQRES 29 B 427 MET ILE ALA LEU SER TRP CYS LEU PRO ALA ALA PHE GLY
SEQRES 30 B 427 SER PRO ILE PRO TYR PHE HIS ILE VAL TYR PHE THR ILE
SEQRES 31 B 427 LEU LEU LEU HIS ARG GLU LYS ARG ASP ASP ALA MET CYS
SEQRES 32 B 427 LEU ALA LYS TYR GLY GLU ASP TRP LEU GLN TYR ARG LYS
SEQRES 33 B 427 LYS VAL PRO TRP ARG ILE VAL PRO LYS ILE TYR
HET NDP A 501 31
HET NDP B 501 31
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
HELIX 1 1 PHE A 23 TYR A 46 1 24
HELIX 2 2 ASP A 55 SER A 64 1 10
HELIX 3 3 THR A 70 ALA A 91 1 22
HELIX 4 4 ASN A 112 MET A 130 1 19
HELIX 5 5 THR A 136 GLN A 141 1 6
HELIX 6 6 GLN A 141 GLY A 164 1 24
HELIX 7 7 TYR A 179 GLY A 184 1 6
HELIX 8 8 LEU A 196 GLY A 225 1 30
HELIX 9 9 THR A 228 HIS A 248 1 21
HELIX 10 10 GLU A 249 THR A 254 5 6
HELIX 11 11 THR A 255 HIS A 260 1 6
HELIX 12 12 GLY A 264 VAL A 273 1 10
HELIX 13 13 VAL A 273 THR A 280 1 8
HELIX 14 14 THR A 280 HIS A 288 1 9
HELIX 15 15 PRO A 294 ARG A 324 1 31
HELIX 16 16 GLY A 350 ALA A 355 1 6
HELIX 17 17 HIS A 357 LEU A 372 1 16
HELIX 18 18 PRO A 373 ALA A 375 5 3
HELIX 19 19 PRO A 379 PRO A 381 5 3
HELIX 20 20 TYR A 382 VAL A 418 1 37
HELIX 21 21 TRP B 25 TYR B 45 1 21
HELIX 22 22 ALA B 56 SER B 64 1 9
HELIX 23 23 THR B 70 ALA B 91 1 22
HELIX 24 24 ASN B 112 MET B 130 1 19
HELIX 25 25 THR B 136 GLN B 141 1 6
HELIX 26 26 GLN B 141 TYR B 161 1 21
HELIX 27 27 LEU B 196 GLY B 225 1 30
HELIX 28 28 THR B 228 HIS B 248 1 21
HELIX 29 29 GLU B 249 THR B 254 5 6
HELIX 30 30 THR B 255 HIS B 260 1 6
HELIX 31 31 GLY B 264 VAL B 273 1 10
HELIX 32 32 VAL B 273 THR B 280 1 8
HELIX 33 33 THR B 280 HIS B 288 1 9
HELIX 34 34 PRO B 294 ARG B 324 1 31
HELIX 35 35 GLY B 350 ALA B 355 1 6
HELIX 36 36 HIS B 357 LEU B 372 1 16
HELIX 37 37 PRO B 373 ALA B 375 5 3
HELIX 38 38 PRO B 379 PRO B 381 5 3
HELIX 39 39 TYR B 382 GLY B 408 1 27
HELIX 40 40 GLY B 408 VAL B 418 1 11
SHEET 1 A 2 THR A 95 GLY A 98 0
SHEET 2 A 2 LEU A 107 ARG A 110 -1 O TYR A 109 N VAL A 96
SHEET 1 B 2 ARG A 190 ILE A 191 0
SHEET 2 B 2 LEU A 194 ASP A 195 -1 O LEU A 194 N ILE A 191
SHEET 1 C 2 TYR A 337 THR A 340 0
SHEET 2 C 2 SER A 344 LEU A 347 -1 O LEU A 346 N ILE A 338
SHEET 1 D 2 THR B 95 GLY B 98 0
SHEET 2 D 2 LEU B 107 ARG B 110 -1 O TYR B 109 N VAL B 96
SHEET 1 E 2 ARG B 190 ILE B 191 0
SHEET 2 E 2 LEU B 194 ASP B 195 -1 O LEU B 194 N ILE B 191
SHEET 1 F 2 ILE B 329 VAL B 330 0
SHEET 2 F 2 LYS B 333 PRO B 334 -1 O LYS B 333 N VAL B 330
SHEET 1 G 2 TYR B 337 THR B 340 0
SHEET 2 G 2 SER B 344 LEU B 347 -1 O SER B 344 N THR B 340
CISPEP 1 GLY A 93 PRO A 94 0 1.28
CISPEP 2 GLY A 104 SER A 105 0 18.92
CISPEP 3 VAL A 423 PRO A 424 0 -8.42
CISPEP 4 GLY B 104 SER B 105 0 2.71
SITE 1 AC1 16 THR A 254 ASN A 316 LYS A 319 ARG A 323
SITE 2 AC1 16 LEU A 345 LEU A 346 LEU A 347 TRP A 352
SITE 3 AC1 16 HIS A 357 ASN A 359 TYR A 360 ASP A 399
SITE 4 AC1 16 CYS A 403 LYS A 406 TYR A 407 TYR A 414
SITE 1 AC2 14 LYS B 319 ARG B 323 LEU B 345 LEU B 346
SITE 2 AC2 14 LEU B 347 TRP B 352 HIS B 357 ASN B 359
SITE 3 AC2 14 TYR B 360 ASP B 399 CYS B 403 LYS B 406
SITE 4 AC2 14 TYR B 407 TYR B 414
CRYST1 74.660 74.615 79.549 66.00 90.37 86.86 P 1 2
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 0.013394 -0.000736 0.000423 0.00000
SCALE2 0.000000 0.013422 -0.005995 0.00000
SCALE3 0.000000 0.000000 0.013768 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
