HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-DEC-13 4O1A
TITLE THE CRYSTAL STRUCTURE OF THE MUTANT NAMPT G217R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NAMPRTASE, NAMPT, PRE-B-CELL COLONY-ENHANCING FACTOR 1, PRE-
COMPND 5 B CELL-ENHANCING FACTOR, VISFATIN;
COMPND 6 EC: 2.4.2.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NAMPT, PBEF, PBEF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.OH,M.COONS,B.BRILLANTES,W.WANG
REVDAT 2 28-FEB-24 4O1A 1 REMARK SEQADV
REVDAT 1 22-OCT-14 4O1A 0
JRNL AUTH W.WANG,K.ELKINS,A.OH,Y.C.HO,J.WU,H.LI,Y.XIAO,M.KWONG,
JRNL AUTH 2 M.COONS,B.BRILLANTES,E.CHENG,L.CROCKER,P.S.DRAGOVICH,
JRNL AUTH 3 D.SAMPATH,X.ZHENG,K.W.BAIR,T.O'BRIEN,L.D.BELMONT
JRNL TITL STRUCTURAL BASIS FOR RESISTANCE TO DIVERSE CLASSES OF NAMPT
JRNL TITL 2 INHIBITORS.
JRNL REF PLOS ONE V. 9 09366 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 25285661
JRNL DOI 10.1371/JOURNAL.PONE.0109366
REMARK 2
REMARK 2 RESOLUTION. 1.87 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-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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 82893
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4154
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 46.2649 - 5.7965 1.00 2796 146 0.1659 0.1777
REMARK 3 2 5.7965 - 4.6022 1.00 2753 134 0.1373 0.1414
REMARK 3 3 4.6022 - 4.0209 1.00 2757 136 0.1233 0.1574
REMARK 3 4 4.0209 - 3.6534 1.00 2743 141 0.1257 0.1612
REMARK 3 5 3.6534 - 3.3916 1.00 2699 154 0.1434 0.1670
REMARK 3 6 3.3916 - 3.1917 1.00 2742 124 0.1472 0.1973
REMARK 3 7 3.1917 - 3.0319 1.00 2712 137 0.1469 0.1929
REMARK 3 8 3.0319 - 2.8999 1.00 2747 149 0.1583 0.1987
REMARK 3 9 2.8999 - 2.7883 1.00 2702 168 0.1586 0.2082
REMARK 3 10 2.7883 - 2.6921 1.00 2710 139 0.1571 0.1765
REMARK 3 11 2.6921 - 2.6079 1.00 2742 132 0.1537 0.1887
REMARK 3 12 2.6079 - 2.5334 1.00 2694 155 0.1555 0.2142
REMARK 3 13 2.5334 - 2.4667 1.00 2742 156 0.1573 0.2051
REMARK 3 14 2.4667 - 2.4065 1.00 2699 139 0.1531 0.2335
REMARK 3 15 2.4065 - 2.3518 1.00 2706 141 0.1622 0.2053
REMARK 3 16 2.3518 - 2.3018 1.00 2728 136 0.1592 0.2031
REMARK 3 17 2.3018 - 2.2557 1.00 2700 163 0.1528 0.2047
REMARK 3 18 2.2557 - 2.2132 1.00 2738 142 0.1511 0.1989
REMARK 3 19 2.2132 - 2.1736 1.00 2660 148 0.1499 0.1963
REMARK 3 20 2.1736 - 2.1368 1.00 2738 178 0.1583 0.2219
REMARK 3 21 2.1368 - 2.1023 1.00 2630 169 0.1632 0.2447
REMARK 3 22 2.1023 - 2.0700 1.00 2739 122 0.1698 0.2168
REMARK 3 23 2.0700 - 2.0395 1.00 2733 129 0.1731 0.1868
REMARK 3 24 2.0395 - 2.0108 1.00 2697 151 0.1736 0.2150
REMARK 3 25 2.0108 - 1.9836 1.00 2764 143 0.1734 0.2439
REMARK 3 26 1.9836 - 1.9579 1.00 2715 117 0.1874 0.2362
REMARK 3 27 1.9579 - 1.9334 1.00 2732 131 0.1918 0.2763
REMARK 3 28 1.9334 - 1.9101 1.00 2698 141 0.2011 0.2373
REMARK 3 29 1.9101 - 1.8879 0.75 2018 108 0.2012 0.2624
REMARK 3 30 1.8879 - 1.8700 0.18 505 25 0.2102 0.2719
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.020
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 : 0.007 7764
REMARK 3 ANGLE : 1.028 10504
REMARK 3 CHIRALITY : 0.072 1149
REMARK 3 PLANARITY : 0.005 1332
REMARK 3 DIHEDRAL : 12.612 2866
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 8:487 OR RESID 701:1114 OR
REMARK 3 RESID 601:606 ) ) OR ( CHAIN B AND ( RESID 8:486 OR
REMARK 3 RESID 701:1119 OR RESID 601:606 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6658 1.3476 22.5230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0442 T22: 0.0499
REMARK 3 T33: 0.0461 T12: -0.0014
REMARK 3 T13: -0.0037 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.1252 L22: 0.2242
REMARK 3 L33: 0.1638 L12: 0.0353
REMARK 3 L13: 0.0022 L23: -0.0647
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: -0.0080 S13: -0.0059
REMARK 3 S21: -0.0178 S22: -0.0057 S23: -0.0114
REMARK 3 S31: 0.0003 S32: 0.0308 S33: -0.0000
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 4O1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97397
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN COOLED DUAL
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82942
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM PHOSPHATE, PH 8.6, 25%
REMARK 280 POLYETHYLENE GLYCOL 3350, 0.2M NACL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
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 53.02400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 ASN A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 THR A 44
REMARK 465 GLU A 45
REMARK 465 ASN A 46
REMARK 465 SER A 47
REMARK 465 LYS A 48
REMARK 465 LEU A 49
REMARK 465 ARG A 50
REMARK 465 LYS A 51
REMARK 465 VAL A 52
REMARK 465 ALA A 488
REMARK 465 ALA A 489
REMARK 465 HIS A 490
REMARK 465 HIS A 491
REMARK 465 LEU A 492
REMARK 465 GLU A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 43
REMARK 465 THR B 44
REMARK 465 GLU B 45
REMARK 465 ASN B 46
REMARK 465 SER B 47
REMARK 465 LYS B 48
REMARK 465 LEU B 49
REMARK 465 ARG B 50
REMARK 465 LYS B 51
REMARK 465 VAL B 52
REMARK 465 GLU B 487
REMARK 465 ALA B 488
REMARK 465 ALA B 489
REMARK 465 HIS B 490
REMARK 465 HIS B 491
REMARK 465 LEU B 492
REMARK 465 GLU B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
REMARK 465 HIS B 496
REMARK 465 HIS B 497
REMARK 465 HIS B 498
REMARK 465 HIS B 499
REMARK 465 HIS B 500
REMARK 465 HIS B 501
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 A 43 CG CD CE NZ
REMARK 470 GLU A 487 CG CD OE1 OE2
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 O2 PO4 B 602 O HOH B 800 2.01
REMARK 500 O HOH B 1031 O HOH B 1036 2.12
REMARK 500 O HOH A 841 O HOH A 846 2.14
REMARK 500 O HOH A 877 O HOH A 1008 2.14
REMARK 500 O HOH B 753 O HOH B 1037 2.14
REMARK 500 O HOH A 966 O HOH A 1041 2.15
REMARK 500 O TYR A 23 O HOH A 1015 2.17
REMARK 500 O HOH A 869 O HOH A 1021 2.18
REMARK 500 O HOH B 909 O HOH B 999 2.19
REMARK 500 O LYS A 255 O HOH A 839 2.19
REMARK 500 O HOH B 957 O HOH B 979 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 983 O HOH B 1055 2646 2.18
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 PHE A 96 124.27 173.49
REMARK 500 TYR A 231 -57.17 -125.06
REMARK 500 PHE A 269 62.63 -112.55
REMARK 500 GLU A 293 -67.43 -133.86
REMARK 500 ASP A 313 17.90 -148.91
REMARK 500 ASP A 416 70.16 -159.79
REMARK 500 TYR B 231 -56.16 -128.09
REMARK 500 PHE B 269 62.24 -115.53
REMARK 500 ASP B 282 97.94 -160.16
REMARK 500 GLU B 293 -66.08 -133.41
REMARK 500 ASP B 313 16.63 -151.75
REMARK 500 ASP B 416 71.24 -160.34
REMARK 500 ASP B 420 87.96 -150.68
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 PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O13 RELATED DB: PDB
REMARK 900 RELATED ID: 4O14 RELATED DB: PDB
REMARK 900 RELATED ID: 4O15 RELATED DB: PDB
REMARK 900 RELATED ID: 4O16 RELATED DB: PDB
REMARK 900 RELATED ID: 4O17 RELATED DB: PDB
REMARK 900 RELATED ID: 4O18 RELATED DB: PDB
REMARK 900 RELATED ID: 4O19 RELATED DB: PDB
REMARK 900 RELATED ID: 4O1B RELATED DB: PDB
REMARK 900 RELATED ID: 4O1C RELATED DB: PDB
REMARK 900 RELATED ID: 4O1D RELATED DB: PDB
REMARK 900 RELATED ID: 4O28 RELATED DB: PDB
DBREF 4O1A A 1 491 UNP P43490 NAMPT_HUMAN 1 491
DBREF 4O1A B 1 491 UNP P43490 NAMPT_HUMAN 1 491
SEQADV 4O1A ARG A 217 UNP P43490 GLY 217 ENGINEERED MUTATION
SEQADV 4O1A LEU A 492 UNP P43490 EXPRESSION TAG
SEQADV 4O1A GLU A 493 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 494 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 495 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 496 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 497 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 498 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 499 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 500 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS A 501 UNP P43490 EXPRESSION TAG
SEQADV 4O1A ARG B 217 UNP P43490 GLY 217 ENGINEERED MUTATION
SEQADV 4O1A LEU B 492 UNP P43490 EXPRESSION TAG
SEQADV 4O1A GLU B 493 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 494 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 495 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 496 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 497 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 498 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 499 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 500 UNP P43490 EXPRESSION TAG
SEQADV 4O1A HIS B 501 UNP P43490 EXPRESSION TAG
SEQRES 1 A 501 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 A 501 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 A 501 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 A 501 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 A 501 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 A 501 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 A 501 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 A 501 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 A 501 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 A 501 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 A 501 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 A 501 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 A 501 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 A 501 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 A 501 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 A 501 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 A 501 SER ALA HIS LEU VAL ASN PHE LYS ARG THR ASP THR VAL
SEQRES 18 A 501 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 A 501 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 A 501 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 A 501 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 A 501 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 A 501 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 A 501 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 A 501 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 A 501 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 A 501 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 A 501 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 A 501 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 A 501 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 A 501 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 A 501 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 A 501 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 A 501 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 A 501 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 A 501 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 A 501 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 A 501 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS LEU GLU HIS
SEQRES 39 A 501 HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 501 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 B 501 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 B 501 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 B 501 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 B 501 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 B 501 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 B 501 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 B 501 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 B 501 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 B 501 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 B 501 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 B 501 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 B 501 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 B 501 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 B 501 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 B 501 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 B 501 SER ALA HIS LEU VAL ASN PHE LYS ARG THR ASP THR VAL
SEQRES 18 B 501 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 B 501 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 B 501 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 B 501 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 B 501 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 B 501 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 B 501 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 B 501 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 B 501 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 B 501 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 B 501 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 B 501 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 B 501 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 B 501 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 B 501 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 B 501 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 B 501 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 B 501 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 B 501 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 B 501 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 B 501 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS LEU GLU HIS
SEQRES 39 B 501 HIS HIS HIS HIS HIS HIS HIS
HET PO4 A 601 5
HET PO4 A 602 5
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET PO4 B 601 5
HET PO4 B 602 5
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PO4 4(O4 P 3-)
FORMUL 5 EDO 8(C2 H6 O2)
FORMUL 15 HOH *833(H2 O)
HELIX 1 1 ASN A 10 ALA A 14 5 5
HELIX 2 2 ASP A 16 GLN A 25 5 10
HELIX 3 3 GLY A 61 LEU A 70 1 10
HELIX 4 4 THR A 76 GLN A 92 1 17
HELIX 5 5 ASN A 97 ASP A 109 1 13
HELIX 6 6 ASP A 138 TYR A 142 5 5
HELIX 7 7 TRP A 143 ILE A 148 1 6
HELIX 8 8 ILE A 148 GLN A 154 1 7
HELIX 9 9 SER A 155 GLY A 181 1 27
HELIX 10 10 GLY A 185 TYR A 188 5 4
HELIX 11 11 SER A 200 LEU A 212 1 13
HELIX 12 12 VAL A 221 TYR A 231 1 11
HELIX 13 13 GLU A 246 ALA A 252 1 7
HELIX 14 14 TRP A 253 ASP A 256 5 4
HELIX 15 15 HIS A 257 PHE A 269 1 13
HELIX 16 16 ASP A 282 LYS A 289 1 8
HELIX 17 17 LEU A 295 VAL A 300 1 6
HELIX 18 18 ASN A 316 PHE A 332 1 17
HELIX 19 19 ASP A 357 LYS A 371 1 15
HELIX 20 20 SER A 374 GLU A 376 5 3
HELIX 21 21 GLY A 383 GLN A 388 1 6
HELIX 22 22 ASP A 420 ARG A 424 5 5
HELIX 23 23 GLY A 446 GLU A 451 5 6
HELIX 24 24 SER A 472 ALA A 480 1 9
HELIX 25 25 LEU A 482 GLU A 487 1 6
HELIX 26 26 ASN B 10 ALA B 14 5 5
HELIX 27 27 ASP B 16 GLN B 25 5 10
HELIX 28 28 GLY B 61 LEU B 70 1 10
HELIX 29 29 THR B 76 PHE B 91 1 16
HELIX 30 30 ASN B 97 ASP B 109 1 13
HELIX 31 31 ASP B 138 TYR B 142 5 5
HELIX 32 32 TRP B 143 ILE B 148 1 6
HELIX 33 33 ILE B 148 GLN B 154 1 7
HELIX 34 34 SER B 155 GLY B 181 1 27
HELIX 35 35 GLY B 185 TYR B 188 5 4
HELIX 36 36 GLY B 194 VAL B 198 5 5
HELIX 37 37 SER B 200 LEU B 212 1 13
HELIX 38 38 VAL B 221 TYR B 231 1 11
HELIX 39 39 GLU B 246 ALA B 252 1 7
HELIX 40 40 TRP B 253 ASP B 256 5 4
HELIX 41 41 HIS B 257 PHE B 269 1 13
HELIX 42 42 ASP B 282 LYS B 289 1 8
HELIX 43 43 LEU B 295 VAL B 300 1 6
HELIX 44 44 ASN B 316 PHE B 332 1 17
HELIX 45 45 ASP B 357 LYS B 371 1 15
HELIX 46 46 SER B 374 GLU B 376 5 3
HELIX 47 47 GLY B 383 GLN B 388 1 6
HELIX 48 48 ASP B 420 ARG B 424 5 5
HELIX 49 49 GLY B 446 GLU B 451 5 6
HELIX 50 50 SER B 472 ALA B 480 1 9
SHEET 1 A 7 LEU A 409 ASN A 412 0
SHEET 2 A 7 CYS A 397 THR A 406 -1 N VAL A 404 O ILE A 411
SHEET 3 A 7 THR A 30 CYS A 39 -1 N TYR A 34 O TYR A 403
SHEET 4 A 7 VAL A 130 ASN A 136 -1 O VAL A 134 N SER A 35
SHEET 5 A 7 ILE A 114 ALA A 118 -1 N GLU A 115 O GLU A 135
SHEET 6 A 7 HIS A 459 LYS A 463 -1 O HIS A 459 N ALA A 118
SHEET 7 A 7 LYS A 466 VAL A 467 -1 O LYS A 466 N LYS A 463
SHEET 1 B 2 GLU A 56 VAL A 58 0
SHEET 2 B 2 VAL A 124 PRO A 126 -1 O ILE A 125 N THR A 57
SHEET 1 C 6 ARG A 217 THR A 218 0
SHEET 2 C 6 LEU A 190 ASP A 192 1 N ASP A 192 O ARG A 217
SHEET 3 C 6 ILE A 378 SER A 382 1 O PHE A 380 N HIS A 191
SHEET 4 C 6 LEU A 348 GLN A 352 1 N GLN A 352 O ALA A 379
SHEET 5 C 6 LEU A 308 ARG A 311 1 N ILE A 310 O ARG A 349
SHEET 6 C 6 VAL A 274 VAL A 277 1 N VAL A 274 O ILE A 309
SHEET 1 D 2 THR A 335 GLU A 336 0
SHEET 2 D 2 LYS A 342 LEU A 343 -1 O LEU A 343 N THR A 335
SHEET 1 E 2 SER A 431 ARG A 434 0
SHEET 2 E 2 PHE A 440 LEU A 443 -1 O VAL A 441 N HIS A 433
SHEET 1 F 7 LEU B 409 ASN B 412 0
SHEET 2 F 7 CYS B 397 THR B 406 -1 N VAL B 404 O ILE B 411
SHEET 3 F 7 THR B 30 CYS B 39 -1 N GLU B 38 O SER B 398
SHEET 4 F 7 VAL B 130 ASN B 136 -1 O VAL B 134 N SER B 35
SHEET 5 F 7 ILE B 114 ALA B 118 -1 N GLU B 115 O GLU B 135
SHEET 6 F 7 HIS B 459 LYS B 463 -1 O VAL B 461 N ILE B 116
SHEET 7 F 7 LYS B 466 VAL B 467 -1 O LYS B 466 N LYS B 463
SHEET 1 G 2 GLU B 56 VAL B 58 0
SHEET 2 G 2 VAL B 124 PRO B 126 -1 O ILE B 125 N THR B 57
SHEET 1 H 6 ARG B 217 THR B 218 0
SHEET 2 H 6 LEU B 190 ASP B 192 1 N ASP B 192 O ARG B 217
SHEET 3 H 6 ILE B 378 SER B 382 1 O PHE B 380 N HIS B 191
SHEET 4 H 6 LEU B 348 GLN B 352 1 N GLN B 352 O GLY B 381
SHEET 5 H 6 LEU B 308 ARG B 311 1 N ILE B 310 O ARG B 349
SHEET 6 H 6 VAL B 274 VAL B 277 1 N VAL B 274 O ILE B 309
SHEET 1 I 2 THR B 335 GLU B 336 0
SHEET 2 I 2 LYS B 342 LEU B 343 -1 O LEU B 343 N THR B 335
SHEET 1 J 2 SER B 431 ARG B 434 0
SHEET 2 J 2 PHE B 440 LEU B 443 -1 O VAL B 441 N HIS B 433
SITE 1 AC1 12 ARG A 40 ARG A 392 SER A 398 LYS A 400
SITE 2 AC1 12 HOH A 748 HOH A 778 HOH A 797 HOH A 811
SITE 3 AC1 12 HOH A 828 HOH A 913 HOH A 927 EDO B 606
SITE 1 AC2 9 ARG A 196 GLU A 246 HIS A 247 ARG A 311
SITE 2 AC2 9 ASP A 313 HOH A 850 TYR B 18 HOH B 817
SITE 3 AC2 9 HOH B 911
SITE 1 AC3 7 HIS A 247 SER A 248 THR A 251 HOH A 738
SITE 2 AC3 7 LYS B 400 CYS B 401 PHE B 414
SITE 1 AC4 8 HIS A 191 VAL A 242 SER A 275 ILE A 351
SITE 2 AC4 8 HOH A 765 HOH A 816 HOH A 966 HOH A1087
SITE 1 AC5 8 ASP A 313 GLY A 353 ASP A 354 HOH A 850
SITE 2 AC5 8 HOH A 860 HOH A1049 PO4 B 601 HOH B 815
SITE 1 AC6 5 PHE A 123 VAL A 124 ARG A 434 ASN A 479
SITE 2 AC6 5 HOH A 836
SITE 1 AC7 10 EDO A 605 ARG B 40 ARG B 392 SER B 398
SITE 2 AC7 10 LYS B 400 HOH B 742 HOH B 815 HOH B 817
SITE 3 AC7 10 HOH B 917 HOH B1014
SITE 1 AC8 10 TYR A 18 HOH A 739 HOH A 748 ARG B 196
SITE 2 AC8 10 GLU B 246 HIS B 247 ARG B 311 ASP B 313
SITE 3 AC8 10 HOH B 747 HOH B 800
SITE 1 AC9 7 LYS A 400 CYS A 401 PHE A 414 HIS B 247
SITE 2 AC9 7 SER B 248 THR B 251 HOH B 747
SITE 1 BC1 9 HIS B 191 ARG B 217 VAL B 242 SER B 275
SITE 2 BC1 9 ILE B 309 ILE B 351 HOH B 730 HOH B 798
SITE 3 BC1 9 HOH B 826
SITE 1 BC2 2 PHE B 123 ASN B 479
SITE 1 BC3 7 PO4 A 601 HOH A 828 HOH A 913 ASP B 313
SITE 2 BC3 7 GLY B 353 ASP B 354 HOH B 800
CRYST1 60.707 106.048 82.482 90.00 96.26 90.00 P 1 21 1 4
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 0.016473 0.000000 0.001807 0.00000
SCALE2 0.000000 0.009430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
